entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A0A455R4Z0
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ASCI_ACREG
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Terpene cyclase ascI (EC 5.4.99.-) (Ascofuranone/ascochlorin biosynthesis clusters protein I)
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MPQLAGKLILAGLIPLGAWVLHGFASCNGLIQMFEDFGKQTVLSDGVTDYTGAFTGLEGLDRLLRTLLNFFWPVANGHDWALSLHAFMFAGQGVPLLVLNMLEGARPGNKSLVVSYVTVFGILYMVVGLAIMAPLYLFLHLLTSRTATAPSKAKVAVDPNTAKAVGFGVFVGYVLPTIFMSLPHPSLLSTDTKVLSVVFWQAVPLWASVCAYFASTALGQSATSRSSSNLPSALGAVYAASLIIATATHVATFAISANLSDTWSGIFTFLIPPNPFNTDMRISSFLEGATWFLQWDYTMMSLAYMVWAIGIRHGVEVPRSSHHFETLGKIALRSMAKLLVMGPIGAALSLVWERDQLLWQLDSESGEKGEKNRSRRMSRKWMFS
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Epoxide hydrolase part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis. The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units. Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B. Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB. The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group. Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin. The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG. On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring. Finally, ascofuranol is oxidized into ascofuranone by ascJ.
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A0A481NV25
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TYRDC_ENTFC
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L-tyrosine decarboxylase (TDC) (EC 4.1.1.25) (Levodopa decarboxylase) (L-dopa decarboxylase) (EC 4.1.1.-)
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MKDMDIKAVFIGDKAENGPVYKMLLNKMVDEHLGWRENYIPSDMPAISEGDKLTPDYLATRDHMIEVLDEVSQRLRAGSIPWHSAGRYWGQMNAETLMPALLAYNYAMLWNPNNVALESSMATSQMEAEVGQDFASLFNMADGWGHIAADGSIANLEGLWYARCIKSIPLAVKEVLPEKVKNMSEWALLNLSVEEILEMTESFTDEEMDEVKAASSRSGKNIQKLGKWLVPQTKHYSWMKALDICGVGLDQMVAIPVQEDYRMDINALEKTIRELADQKIPILGVVAVVGTTEEGQVDSVDKIIQLREKLKDEGIYFYLHVDAAYGGYARSLFLNEAGEFVPYASLAEFFEEHHVFHHYVTIDKEVYEGFRAISEADSVTIDPHKMGYVPYAAGGIVIKHKNMRNIISYFAPYVFEKSVKAPDMLGAYILEGSKAGATAAAVWTAHRVLPLNVTGYGQLIGASIEAAQRFREFLEQLHFTVKGKTIEVYPLNHPDFNMVNWVFKVQDCTDLNAINELNEKMFDRSSYMDGDVYGERFITSHTTFTQEDYGDSPIRFIERMGLSKEEWQKEQQITLLRAAIMTPYLNDDRIFNFYTKEIAKAMEKKLNEIIK
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Catalyzes the decarboxylation of L-tyrosine to produce tyramine. Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastrointestinal tract (GIT) environments. Therefore, may contribute to the colonization of the human GIT by E.faecium (By similarity). Also involved in drug metabolism, being able to catalyze decarboxylation of levodopa (L-dopa) to dopamine. In gut microbiota this enzyme is in fact exclusively responsible for the decarboxylation of levodopa, and thus reduces in situ levels of levodopa in the treatment of Parkinson's disease. It was shown that abundance of bacterial tyrosine decarboxylase in the proximal small intestine - the primary site of levodopa absorption - contributes to interindividual variation in drug efficacy and can explain the requirement for an increased dosage regimen of levodopa treatment in Parkinson's disease patients.
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A0A482D308
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CS12F_UNCAX
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CRISPR-associated endodeoxyribonuclease Cas12f1 (Un1Cas12f1) (EC 3.1.-.-) (CRISPR-associated endodeoxyribonuclease Cas14a1)
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MAKNTITKTLKLRIVRPYNSAEVEKIVADEKNNREKIALEKNKDKVKEACSKHLKVAAYCTTQVERNACLFCKARKLDDKFYQKLRGQFPDAVFWQEISEIFRQLQKQAAEIYNQSLIELYYEIFIKGKGIANASSVEHYLSDVCYTRAAELFKNAAIASGLRSKIKSNFRLKELKNMKSGLPTTKSDNFPIPLVKQKGGQYTGFEISNHNSDFIIKIPFGRWQVKKEIDKYRPWEKFDFEQVQKSPKPISLLLSTQRRKRNKGWSKDEGTEAEIKKVMNGDYQTSYIEVKRGSKIGEKSAWMLNLSIDVPKIDKGVDPSIIGGIDVGVKSPLVCAINNAFSRYSISDNDLFHFNKKMFARRRILLKKNRHKRAGHGAKNKLKPITILTEKSERFRKKLIERWACEIADFFIKNKVGTVQMENLESMKRKEDSYFNIRLRGFWPYAEMQNKIEFKLKQYGIEIRKVAPNNTSKTCSKCGHLNNYFNFEYRKKNKFPHFKCEKCNFKENADYNAALNISNPKLKSTKEEP
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CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids (Probable). CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), which requires a trans-encoded small RNA (tracrRNA), but not this protein (in vitro) (Probable). Upon expression in E.coli of this protein, a mini CRISPR array and the probable tracrRNA, the protein associates with both RNAs. The mini system is not active in E.coli against phiX174 phage, nor is it active in protection against transformation by foreign plasmids. In vitro the purified protein-tracrRNA-crRNA complex cleaves ssDNA complementary to the crRNA target cleavage requires both tracrRNA and crRNA, but not a protospacer adjacent motif (PAM). The tracrRNA-crRNA can be replaced by a single guide RNA (sgRNA). 2-nucleotide mismatches in the middle of the crRNA:DNA heteroduplex decrease cleavage. Cleavage occurs just downstream of the heteroduplex. Activation of this protein results in non-specific ssDNA degradation in vitro. In vitro and in E.coli (coexpressed with sgRNA) has dsDNA endonuclease activity, recognizing the 5' PAM sequence TTTR both sgRNA and a PAM are required for activity. Cleaves the target strand 24 and the nontarget strand 22 bases upstream of the PAM (respectively), resulting in 5' overhangs. The 2 monomers interact differently with the sgRNA and target DNA. Mutagenesis of a dimeric construct shows that one of the RuvC monomers probably cleaves both DNA strands.
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A0A482N9V7
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ICCA_TALVA
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Hybrid PKS-NRPS synthetase iccA (PKS-NRPS iccA) (EC 2.3.1.-) (EC 6.3.2.-) (Ilicicolin H biosynthesis cluster protein A)
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MAANDSNNQTKPQLPEEPVAIVGSSCRFPGSSNSPSKLWDLLRQPRDVLKEFDPDRLNLKRFYHPDGDTHGSTDVTNKSYLLEEDSRLFDASFFTINPAEAAGMDPQQRILLETVYEAFESAGMTLEQLRGSLTAVHVGTMTNDYAGIQLRDLETIAKYNATGTANSIVSNRISYVFDLKGPSETIDTACSSSLVALHHAARGLLNGDCETAVVAGVNLIYDAASYIAESKLHMLSPDSQSRMWDKSANGYARGEGAAALLLKPLSRALRDGDHIEGVIRATGVNSDGQSPGITMPFAPTQAALIRQTYRRAGLDPVKDRPQYFECHGTGTPAGDPVEARAISEAFEPSADNPIYVGSIKTIIGHLEGCAGLAGVMKVILALKNRTIPPNMLFNELNPAIAPFYGPLQIPKKAMPWPELPENTPIRASVNSFGFGGTNAHVIIESFESSTPSSDSEKCEEGALGPLLFSAGSGASLLHTVQAYVQYLDQNPSVDLRDLSWLLQTRRSTHRVRTHFSGTSSDAILESMIKFVNNNEKTPSTEVGHQPKLINPKEVPGILGVFTGQGAQWPQMGKELIGKSPIFRRTLEDCDATLQALPSSDIPKWSLVKELMANASSSRVAEAAISQPLCTAVQLGLVNMLKASGLNFDAVVGHSSGEIAATYASGIINLQAAIQIAYYRGFHAKLAKGEKGQQGGMLAAGLTLDKAKQLCLREEFVGRLQVAASNAPQTVTLSGDLDAIEEVKKYLDEENVFARQLKVDTAYHSHHMKPCAEPYLKSLLACDIEVRKPTPGQCIWNSSVRGDTGLLKGDLSSLKGPYWVANMVQTVLFSQAVESSIWHGGPWDLAIEVGPHPALKGPTEQTLKAVYGVVPLYTGVLKRGASDVEAFSTAIGVTWSQLGPSFVDFAGYRKTFYESEPPTPKVIKDLPGYSWDHDKVYWRESRISKRYRTGRDQTHELLGRRTPDDNEFELRWRNVLKLSEMPWLRGHEVLEEVLLPGAAYVSIAVEASKHIATSKGKSIELLEVEDVDIQRPVVVPDNKEGVETLFTARLLPGSSSDKVLKALFSYYICNDQSTGTMVHTCSGRLSVHLGEAKEDVLPQRDPVPQNLVNINTDRAYGMFKDIGLNYTGVFRSIKESSRTLQYSAATGIWPEGSLSDKYLVHPAMLDVAFQTLFIARAHPASRLITSALLPSHIERIQVSPSVPILHARENSDEIKADFDCWVVHQTASSLTGDLNIYDKVSGKTFLQVEGLTTKMVGEQDASGDRPVFTKTVWGSDGSLGLDEPERDPVGDAEGLSLAEAAERMALFYMKRVVKEISPEERTKFQWYHQRMFEAFEQHLVNVGSGSHPMLKSEWLSDDSSIMDGLDRIHPTSIDLKLLRACGENMPDVVREKTQLLEVMSKDDMLNRFYMDNCAARINNDIAKVVKQISFKFPRANILEIGAGTGGTTWSILKDINDAYDSYTFTDISSGFFPKAAEKFSDFAHKMIFKTLDVEKQPSEQGFAENSYDVIVAANVLHATRSLETTLRNARSLLRPGGYLILMEITNPESLRTTFIFGGFSGWWLSEEPHRKLGPVVTAMDWDTVLNDTGYSGADMVVHDLAEESKHLTSLIVSQAVDDDFLRLREPLSNLADMSAPTESILVIGGKKLLTSKMVNEINKLLPKSWKRHISSAGSIDDIDINELKPGTEVISLQELDDPLFSTPMTAERMSTIQNLMMSAKTLLWVTTAGKSHAPRASMFHGIARIVPSELQHLQIQVLGLEAGSTPAIATRHCVEAFLRLRGTSDTTREMLWAIEPEVEIMADGQVLIPRVVPDETLNQTYNASRRVVTKTVDATDLAVEAVAGPTKMMLQTAELQAGERKTRIQVKYALHLPAMDGKGIYVVYGQRQDDTSSFVLAVSKSNSSIVDVDSKHAVSVSDNCEPATLNVLATYLIARAIATLSKQAGSVLLSEPEESLAAIVATETAKQGTQAYFLSSKKVSPVEWIKVHANASKRAIQKAVPHDVQLLIDCSGIEASGNAVMASMPLHCVERQLDAHLLFDALESTESKPESLLEEAYQYATQLITQEQVQSECEVFPASDLPLTNMLSLVHKKYVTDWQQRDSLVVSVPPLDLEGIFKADKTYLMVGAAGGLGLSICEWMIRNGAKNLIITSRKPQVDQNMIEEASRVGATVKVMAMDVSSKESVAEVVQQAQEIMPPIAGVCNAAMVLSDKMFLDMDVDQLNGTLAAKVYGTEHLDAVFADAPLDFFIVLSSTATTIGNIGQANYHVANLFMTSLVAQRRARGLAGSVIHIGYVADVGYVTRQDRERQLEQHFRNVRLMALSETDVHHAFAEAVRGGRPGNTVGSPDIIMGLEPASVPLEPERQTLWLSNPCFGHLVPSTLQNDSSQTGGTGNGSSVRRQVEEAQTEDEAVDAVLDGFCAKLEAILQLREGSVKENVQRAVIDLGIDSLVAVEIRTWFLKELGAEVPVVKILGGDTVLQICTTAAKKVMANAMKKKEEDAVAEEGGREAASKKEPAPAASAPTPAPVAPSLLDVPARAFEPDSATISEVGDDSAFSNKGSSSSATGASSPKELSDSESVPDTSKDQSHVRPETVRDERMSPAQARIWFLTKHLDDPSAYNMVFHYRVKGPLKTVRLRHALQVATGHHESLRTLFYSRLEDGQPMQGVMPASAYELKHVPGADEADLKKELALLKAREWDLENGRTFSVSVLSRAADEHDVVFGYHHIIMDVVGWYFFVRDLDRAYRMQPFDKKISGSYVDYSVMQLSQKNTAAASDDLAFWQKEFSTVPDPIPLLPIAAVSARPTDSGRKVSHHEYLELDPAQNLAVKETCEKLRISPFHFHVAVLRALIGGYTNIDDMCIGVVDANRGDERFAQTVGCFVNMLPVRVEAPSDATFADIARSASRKALMAFAHSSAPLDMILDAVKAPRSSETTPLFQVAVNYRTGGVWDLPMGDCQMKLSLTDGKDAENPFDISLGIAETGKGCVIEMHCQKTLYSSDATRTLLNTYLRLVDTFCKNTHVKLKDCVIHDQAKVSEALQIGKGPTTDFGWPSTLSHRVLETCLKSPKNAAIQFKGELLSYEQLASRIHLVAAAIVRAGASKGSRVAVLCEPSADAIISMLATLHIGGVYIPMDVSLPTARHAAMMNGGQPTLLLSHAATKHRVEDLVNETGSTISVLQVDTISSVEEKETVSCAAEPHNNAVLLFTSGSTGTPKGIMLSQANFVNHLALKTDRLQLGQENVLQQSSMGFDMSLIQMFCALANGGCLVIAPSEMRRDPVELTNLVHNSQISLTIATPSEYLAWLRYGTASLKDHTIWRHACMGGEPVSRQLKTEFWRLDLANLQLTNCYGPTEITAAATFETIRLDDQDDDNDRAQHAVGKALPNYSVRILDTAGRPQPVDHIGEICIGGASVALGYLGLPEQTKAKFTVDPVSGERLYLTGDKGKLLSDGTLLCLGRLDGDTQIKHRGLRIELQEVESALIQTANGLFSSAVVSARGSILVAHATISQSQAEPSESDLAKILSRLKLPQYFIPATIGILPTMPTTANGKLDRKAIASLPLPQKVTGEEGPQEKMNIREGELRLLWERVLPDTATTTPLGPSSDFFLCGGNSMLLMKLQAAIKESIGIEISTRVLYQASTLREMALCVDEQREEQADALEQHFDWQAETSLPKWLLDQIEDLPKTTKQPPKPNGIDILMTGATSFIGGRLLRSLVRSPSVRKVHCVAVLADEQDQLYQDEKVKCYTGSLLSSTLGLNNGERDQLARNVDVVIHAGSSGHCLNTYGSLRTPNLVSLQFLASLALPRSIPLLLLSSNRVPLLSGNTALPPTSVAAFPPATDGREGYTATKWASEVFLEKLVGAVQKKAPRPWVASVHRPCVVVSEHAPNSDALNAILRYSASMKCVPHLESATGYLDFASVESIVDSMAESAIEMATGNVTDQPSIRFQHHSGGVKVPIGDFKVHMENVYGGNFEEVHLEEWMHRAAAAGLDPLITAYMEGIIEAGAPIVFPYLGETV
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IccA assembles the backbone of ilicicolin H. The PKS portion and trans-acting enoyl reductase iccB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB since iccA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iccD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. IccA to iccE are sufficient for ilicicolin H biosynthesis and the roles of the remaining enzymes, iccF, iccG and iccH within the pathway have still to be determined (Probable).
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A0A482PDI9
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NLEB_CITRO
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Protein-arginine N-acetylglucosaminyltransferase NleB (Arginine GlcNAcyltransferase NleB) (NleBc) (EC 2.4.1.-) (Non-LEE-encoded type III effector B)
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MLSPLNVLQFNFRGETALSDSAPLQTVSFAGKDYSMEPIDEKTPILFQWFEARPERYGKGEVPILNTKEHPYLSNIINAAKIENERVIGVLVDGDFTYEQRKEFLSLEDEHQNIKIIYRENVDFSMYDKKLSDIYLENIHEQESYPASERDNYLLGLLREELKNIPYGKDSLIESYAEKRGHTWFDFFRNLAVLKGGGLFTETGKTGCHNISPCGGCIYLDADMIITDKLGVLYAPDGIAVYVDCNDNRKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPYYDGVGKGLKRHFNYSSLQDYNVFCNFIEFKHKNIIPNTSMYTNSSW
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Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis. Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins FADD, TNFRSF1A and RIPK1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling. Has preference for host FADD as substrate compared to TNFRSF1A and RIPK1. Also acts on host proteins without a death domain: catalyzes GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2 and TRAF3, leading to inhibit NF-kappa-B signaling and type I interferon production, respectively. Also displays intra-bacterial activity by mediating GlcNAcylation of glutathione synthetase GshB. Catalyzes auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (By similarity).
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A0A494BA31
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B3A4_MOUSE
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Anion exchange protein 4 (AE 4) (Anion exchanger 4) (Solute carrier family 4 member 9)
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MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKLQEVTSLSRQSAALAEDKHHHGPHTPIPELQRTGRLFGGLIQDVRRKACWYTSDFLDALHPQCFSAVFYIYLATVTNAITFGGLLGDATEGAQGVLESFLGTAVAGAAFCLMAGQPLTILSSTGPVLVFERLLFSFSRDYSLDYLPFRLWVGIWVTAFCLALVATEASLLVRYFTRFTEEGFCALISLIFIYDAMGKMLNLIRAYPIQRPGSSAYGCFCQYPGTGGNTSEWTSAKLKDTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDTFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWYVSATVISLAHIDSLRRESKACIPGEAPNFLGIREQRLTGLVVFVLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN
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Electroneutral Cl(-)/HCO3(-) antiporter that favors chloride ion entry and efflux of hydrogencarbonate and sodium ion across the basolateral membrane and may participate in salivary secretion. Also mediates Cl(-)/HCO3(-) exchange activity in the presence of K(+) as well as Cs(+), Li(+), and Rb(+). Does not contribute to Cl(-)/HCO3(-) exchanger in the apical membrane of the upper villous epithelium.
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A0A4P8DY91
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COMTS_KITPR
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Esculetin O-methyltransferase (EC 2.1.1.-) (Bergaptol O-methyltransferase) (EC 2.1.1.69) (Isoscopoletin O-methyltransferase) (EC 2.1.1.-) (Scopoletin O-methyltransferase) (EC 2.1.1.-) (Xanthotoxol O-methyltransferase) (EC 2.1.1.70)
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MTTTELIPPTIQVDEEEEEACMFAMQLASASVLPMVLKSAIELDLLESIAKAGPGAYVSPSELAAKLPSSQPDTPVMLDRILRLLASYSVLKCKVQDLPQGGVERLYALAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNLGMSNHSTITMKKILQTYNGFAGLKTVVDVGGGTGATLNMIISKYPNIKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPEGDAIFMKWICHDWSDAHCLSFLKNCYKALPQNGKVILAECILPEAPDSKLTTKNVIHIDVIMLAHNPGGKERTEKEFEALGKMAGFKSFNKVCCAHNTWIMEFLK
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O-methyltransferase involved in the biosynthesis of methoxylated coumarins natural products such as isoscopoletin, scopoletin, xanthotoxin and bergapten, photosensitizers used for medical purpose such as treating psoriasis and vitiligo or facilitating resistance to microbial infection and other stresses. Catalyzes the methylation of esculetin, bergaptol and xanthotoxol, but seems inactive on scopoletin and isoscopoletin.
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A0A4P8WAE5
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PYIS_MAGGR
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Polyketide synthase-nonribosomal peptide synthetase pyiS (PKS-NRPS pyiS) (EC 2.3.1.-) (EC 6.3.2.-) (Pyrichalasin H biosynthesis cluster protein A) (Pyrichalasin H synthase)
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MAATFSEPVAIIGTGCRFPGQCNTPSKLWELLQTPKDLLKEIPENRFSTEAFYHPQNYHHGTCNVRHSYFLEEDLRGFDAQFFGINPVEAHSVDPQQRLLLETVYESLEAAGLSMKEMQGSDTAVYVGVMSADFTDMIGRDPETFPTYFATGTARSILSNRLSFFFDWRGPSMTIDTACSSSLIEPRTGANKPDCAEQVAGSNLILGSEQYIAESKLQMLSPTGRSRMWDADADGYARGEGVAAIVLKKLSQAIADGDHIECIIRETGANQDGRTPGITMPSATAQEALIRTTYKKAGLDISKRSDRPQFFEAHGTGTPAGDPIEARAVSNAFFGPRSHFSPTSPDDTLFVGSIKTVVGHTEGTAGLAAVIKASLALQAGVVPPNMHLSKLNPKIEPFYGNVQILSEARQWPKLAEGGVRRVSVNSFGFGGANCHAILEAYEPESTLDRRRYNKRTGKCFTPFLFSAATENALAAQLDKYRAHVACGNASAPGDLKKLSLTLSNRRSALPWRAVVPASNSVERLIENLDQCNDFTNETSASSLGTRPRILGIFTGQGAQWPRMGAALIESSPAAAKILARLDESLRLLPIRDRPTWSLREKILEGAESSSVAMAFISQPVCAAVQIMLVDMLRAAGIEFSGVLGHSSGEISAAYAAGYLSSEDAIRAAYYRGFHMKSLTQKKGAMIAVGTSYDDAKELCDLPAFEGRVCVAASNSPFSVTLSGDADAIDEVKALMDEEKKFNRLLQVDRAYHSHHMKACAAAYMASLQQCGVRTLTRTAASSRCQWVSSVYVRHSAELAAEGGLEAKYWASNLTMPVMFTEALQKLLGDCKDGKAYDLAIEVGPHPALKGPAVQTMSEFLGGQSIPYTGVLSRGKDDVESFSTTLGYIWRTLGEGAVDFLGYSRFMNEEQGEATITPLNGLPTYPWDHHRKFWHESRLSRAYRFNKDPVNELLGRQILDGAPDQLRWRNVLKRNELDWLDGHQVQRQTVFPFMGYVSACVEAAMKIRGDANVQSIELQNFKVGQAVAFNDDDSWIEILVVLDSIKESKVKGTKTISAHFAFHSSSNNETVDMTTHAGCDVLVTYGDSISDLLPPPEIQADDEYFMLGVESDRFYNVLDDIGLGYTGPFRALSGLQRKLGKATGRIKNPASSKLWRKPLLVHPAMLDAGIQSIMLAYCYPGDTMMRSIYLPTGIRRLIINPEHCQTFAGEETDVLFQSSASVDDPQGLSGDVSIYAPGGLSCKAIQVEGLQTQPLFNPTEANDLNIFTELVWGVDRPDAKEIVNKVDVQQLDGDLLFSLERVAYYYLRILDKSIPLSQRTGIDWHFGQLFAYVDHVLSRVERGTNRFARKEWQHDTKEIILEILERYPDNIDLRLMRAVGENIAAVIRGEITMLEPMLQNNMLNDFYVVAHGMPRYTKYLASLASQIGHRYPHMHVLEIGAGTGGATKSFLGALDDKFSTYTFTDISSGFFEKARSVFASYSAKMSFKMLNIEKDIGDQGFVEGSYDVVIASLVLHATRNLGQTLRNVRRLLKPGGYLLLLEITENDQMRFGLLFGGLEGWWLGYDDGRALSPCINIEEWEKYLKQTGFSGIDTLMPHDEILPVPLSVIVSQAVDERTELLKQPLQRLDPSTTLVPQLTIIGSGALAEEVHRLLRPFCGRVNVIESLGHMGADQLPVGGAVICLADIQEPVFKSMDADKLRGFQTIFKQSGSALWVTQGTLNGNPYSRMVIGFGRTIVLEMLHLRLQFLDLDHEAPADPTAIVETFIRLHLAENWKNDGVKITPLLHSVEPEMHIDKEGRGFIPRFKLNKKQNDRYNSGRRKIVKEVPLRQQPVELVPPKSEDASWLLAEGKNMPELKGAIDIDVFYTVTRAVEVSGGTFLYAVLGARRDTKEVVLALSPTQASIIRVPQAFIIPAQDSVEYLQLFYTELLARAVLRDVAAGTVVVVLRPTSMLSCAVDRLAADRGARVLHLADEPGSDWDYLHHKSSKVQVQDWVKSRLGTEAPPAVLLLDFGADQFLLAYLLECLPAEVTRAMVGAQSTSSKARMKLGQSEQEIRSFLADVRYALLPAQQTHQSSKGRSSLKVFTLEHLTTNRAGSDVSVVSWPAGTSTIPVQVQPVNSKVTFSNDKTYWLVGLSGTLGLSLCEWMAQQGARYIVITSRNPNVDERWKNKMEKLGIKVEIIANNICDRKSVRSVYSHICQTMPPIGGVAQGAMVLHDTAFSELDLERINKVMQPKVNGSIYLEEIFHNTPLEFFVFFSSMACVTGNPGQSAYAAANMFMSGLAVQRRKRGLNASVVHIGAIFGNGYVTRELSLEQQNFLRKVGNMWLSEQDFRQLFAEAVLAGQPENTGSPELSTGMMTIDNSEGTKENITWFDNPMFQHCIKESTDGKLGGQTAKGRAVPVKTQLLEAINSAEVYEIIHDAFAAKLRSSLQLEDDRPIVDQTADTLGIDSLFAVDIRSWFIKELQLEIPVLKILGGATVGEILETAQQLLPMELLPKMDPNDKSPARKLKAQPDSSPDKAASAERSRAKAQTAIENDGDRKFAATRAESGAKKGETVSKKVEAVTRPSVQWQVPVEPSTAVGDLDDKSFPGEDGVRLRAGSLDTTFTHKSSASSSASILDASEDQSADSVWSLDTVNNELAVSKKTPISFAQSRIWFLEKFLEDPASALNITLTIELDGSLDVDRFGKAVKLVGQRHEALRTRFVHGDDFDAPMQEVLVHSTLSLEQQDIASDAEADEVYRELQKYRYKLGEGENMRIILLKKSNQLFHLVIGYHHINMDGVSLEVVLRELQMAYDSKRLPNFGTILQYPDFAALQQKEYKSGAWQDEIEFWRKEFDGRPPSVLPLLPMAKTRSRTALTSYSSHTAEFSLDQITLAGIQSACESSKATPFQFHLATFYALLSRMVDAADICIGIGSANRHDTAMMQSVGIYLNLLPIVLKSQPNETFASTLKRVRSKVMTAFAHSRVPFDVIVNELGASRATTHNPLFQVLVNYRQGTATRRSFCGCQSEVRSFEQGQAAYDLGLDIIENPGGECKVIMTGQSTLFVPEDMDMLKDMYQRLLLAFSRNQALRLAIPSLYDPEMVKHALRIGRGPSYTHKWPETLIHQIDDIAKQKSHSLAIVDGSGTFLTYAHMSRRTNAIAASLRGIRRGSRVGVHLDPGADWVCSVLAIMRRDAVYLPLDAVSGYSRLSAILQDSKPDLVLVDNSTEKDATAYFSPILAADQIFNIDTVSVTPPETLAIAAKRGSVAALMYTSGSTGVPKGIIMKHESFRNNIEIISEKLGYNNGHTVTLQQSSFNFDMSLGQIFLALSTGGTLHVVPRHLRADPVAISSIIALHGITNTSATPSEFISWVRYGSVEELRNSAWAAVHSGGEPVRDSLKAAFLTVNKPGLRLLDCYGPTEVTFCSHISDVDYGAEETSMNKGLEVLPNYATYIVDSGMKPVPAGVPGEVLIGGAGVVAGYLHTELNTRGFAHDSFASDEFRKQGWEQLHRTGDFGRINKLNGRLLLEGRIADDTQVKLRGLRIDLKEIEAAMVRAAKGDILDCIVSVAQSADVSDEYLVAYATARPDASNHRLEHLMHQLPLPQYMKPATLVLLEKMPTNASGKIDRSAFKSIPLPKATEDNGMQPEVGQDLNDTESRLKQLWEGVLPKHVFSQHKFTAASDFFNVGGSSMLLISLRAKIQDTFAVVVSLFQLFEASTLGDMAALVDELSSGSAEKTAGPNSALDINWEDETAVSPALLGIPVEKKFFTNPEIVVLTGSTGFLGRAILTRLLNDGIVKEIHCFAVREEIPLFDSPKIIVHRGDLTLPGFGLSQKELASIFSKAHAVIHNGADVSFVKSYHSLKPANLEATKQLVDLCLPYQISFHYISTAAVVNLTGEKSWEQRSVGRFPPPAGTDGYIATKWASERYLEKFNDQYGLPIWIHRPSSITGPGAPANDLMANVVEFSRSTAATLNTNSWSGWLDFISVDEAALQIVDEVYEDYSWPGHVKYLYESGERVVALEDMKNVLEREVGSVFEVVDVEEWISRAEKQGFNPLLGEYLKRVANAPLVFPKLIRHEGFF
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, pyiS can also use phenylalanine, tyrosine and even para-chlorophenylalanine as amino acid precursor, which leads to the production of novel cytochalasans, including halogenated cytochalasans. Because pyiS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase pyiC. Reduction by the hydrolyase pyiE leads to 1,5-dihydropyrrolone, which is substrate for dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase pyiF to yield the required isoindolone-fused macrocycle. The tailoring cytochrome P450 monooxygenases piyD and piyG catalyze the hydroxylation at C-18 and C-7, respectivily, whereas the short-chain dehydrogenase/reductase pyiH reduces the carbonyl at C-21 in preparation for the transfer of an acetyl group by the acetyltransferase pyiB. These 3 reactions whose order is not clear yet, lead to the production of O-methylpyrichalasin J, a deacetylated pyrichalasin H. Finally, pyiB to converts O-methylpyrichalasin J into the final product pyrichalasin H via acetylation of C-21.
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A0A4V8GZX0
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TXNA1_OMOSC
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Mu-theraphotoxin-Os1a (Mu-TRTX-Os1a) (Cyriotoxin-1a) (CyrTx-1a) (Mu-theraphotoxin-Cs1a)
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ECKGFGKSCVPGKNECCSGLTCSNKHKWCKVLL
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Potently and reversibly inhibits some human voltage-gated sodium channels (Nav1.1/SCN1A (IC(50)=72.0 nM), Nav1.2/SCN2A (IC(50)=75.5 nM), Nav1.6/SCN8A (IC(50)=115.0 nM), Nav1.7/SCN9A (IC(50)=52.7-129.5 nM), Nav1.3/SCN3A (IC(50)=306.6 nM)). The hNav1.7/SCN9A channel inhibition occurs without any change in steady-state inactivation- and conductance-voltage relationships. On adult mouse DRG neurons, this toxin is approximately 1000-fold more efficient to inhibit tetrodotoxin (TTX)-sensitive than TTX-resistant sodium currents. In vivo, this toxin exhibits analgesic effects in mice pain models.
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A0A4X1UM84
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PCKGC_PIG
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Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (PEPCK-C) (EC 4.1.1.32) (Serine-protein kinase PCK1) (EC 2.7.11.-)
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MPPQLSNGLNHSAKVVRGTLDSLPQAVRDFVESSAKLCQPDQIHICDGSEEENQQLLSHMEEEGVIKRLKKYDNCWLALTDPRDVARIESKTVIITQEQRDAVPIPRSGLSQLGRWMSPEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGSAVLDALGAGEFIKGLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGVTNPEGQKKYFAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDQQGNLRAINPENGFFGVAPGTSVKTNPNAIKTIQSNTIFTNVAETSDGGVYWEGIDQPLAPGIKLTSWKGTEWDPKDGEPCAHPNSRFCTPASQCPIIDPAWEAPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPFAMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKDGRFLWPGFGENCRVLAWMFDRVQGKGGARLTPIGYVPEEAALDLRGLEAIRVSELFQVSKEFWEEEADEIHKYLEEQVNADLPYEIQSEVLALKQRISQM
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Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis. Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (By similarity). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (By similarity). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (By similarity). Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (By similarity). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (By similarity).
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A0A4Y6HUD7
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PALY2_PLEOS
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Phenylalanine ammonia-lyase 2 (EC 4.3.1.24) (PoPAL2)
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MTILSGTTAAPRVNGTTMNGHSKPHTNGVHLNGHAPKATTESPWPQSEEKTLLDKFVEAYYEFESYKSGQTVKVDGKTLSLAGVVAAARHHAKISLDDSASIKDKVVKSRKVIADKVASGASVYGLSTGFGGSADTRTDQPLSLGHALLQHQHVGVLPSSSQPLDVLPLSDPMSATSMPEAWVRAAMLIRMNSLIRGHSGVRWELIEKIAEIFDANITPVVPLRSSISASGDLSPLSYIAGTVVGNPSIRVFDGPAAFGAREMVPSAKALASHGIDPLPLASKEPLGILNGTAFSAAVGALALNEAVHFAMLAQVCTAMGTEALVGTRLSFEPFIHATCRPHPGQIEAARNIYNLLEGTTFASVHHEEVHIAEDQGTLRQDRYPLRTSPQFLGPQLEDILHAYVSVTQECNSTTDNPLIDGETGEIHHGGNFQAMAVTNAMEKTRLALHHIGKLLFAQCTELVNPAMNNGLPPSLAATDPSLNYHTKGIDIATAAYVSELGYLANPVSTHIQSAEMHNQAVNSLALISARATVNSLDVLSLLISSYLYILCQALDLRALQMEFVKGVEEIIREELSLLFASVVSPAELEALTSKVLSAAQTSLDTSGSMDAPARMKKMASTTTIPLFDFLTELTLPDAISSGIAMVSIPSFRSHLASRATALLDQLRRDYLSGQRGAAPASPYLNKTRMVYEFVRLTLGVKMHGSENYARFAKGLGVEDETIGQNISRIHEAIRDGKMQAITVAMFA
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Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and a free ammonium ion. Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids (By similarity).
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A0A4Z3
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A3LT2_RAT
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Alpha-1,3-galactosyltransferase 2 (EC 2.4.1.87) (Isoglobotriaosylceramide synthase) (iGb3 synthase) (iGb3S)
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MALEGLRAKKRLLWRLFLSAFGLLGLYHYWFKIFRLFEVFIPMGICPMAIMPLLKDNFTGVLRHWARPEVLTCTSWGAPIIWDETFDPHVAEREARRQNLTIGLTVFAVGRYLEKYLEHFLVSAEQYFMVGQNVVYYVFTDRPEAVPHVALGQGRLLRVKPVRREKRWQDVSMARMLTLHEALGGQLGREADYVFCLDVDQYFSGNFGPEVLADLVAQLHAWHFRWPRWMLPYERDKRSAAALSLSEGDFYYHAAVFGGSVAALLKLTAHCATGQQLDREHGIEARWHDESHLNKFFWLSKPTKLLSPEFCWAEEIGWRPEIHHPRLIWAPKEYALVRT
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Synthesizes the galactose-alpha(1,3)-galactose group on the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3) by catalyzing the transfer of galactose from UDP-Galactose to its acceptor molecule Gal-beta-1,4-Glc-ceramide. Can also catalyze the addition of galactose to iGb3 itself to form polygalactose structures. Synthesis of iGb3 is the initial step in the formation of the isoglobo-series glycolipid pathway and is the precursor to isogloboside 4 (iGb4) and isoForssman glycolipids. Can glycosylate only lipids and not proteins and is solely responsible for initiating the synthesis of isoglobo-series glycosphingolipids.
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A0A509ADH4
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YOP1_PLABA
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Protein YOP1 homolog (PbYOP1)
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MRMSKLYKNKEKENEKPSNEPPIKQDSLKRMSSKFLGNSLNSFDLSGKLEQVDEYLKKYPFIIEFGYKLGIKPSYIVVFGGSALFISLVLGWGAALICNLVGFAYPAYQSFKAVESQGHAETKLWLTYWVVFSLFFFIEYLIDIILFWIPFYYVIKLLFLLYLYMPQVRGAETVYNYIIRPILLKHEKTIDDTVHKISQTATNHLNQFTGNIAEKLVQEGVRRRNV
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Required to generate and maintain the structure of the tubular endoplasmic reticulum network and the digestive (food) vacuole. Induces high curvature in membranes and causes membrane tubule formation.
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A0A509AFG4
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CDPK3_PLABA
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Calcium-dependent protein kinase 3 (EC 2.7.11.1) (PbCDPK3)
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MNQLCVERNLSISTAYIKSKPKKYIERIKKKKSSNKSIKSQHKFEGSKIANKNNELKDIKSKDPKHYENHINKNTKHKDILLKSKRSDNFKFSRRGFILSFTGNLEDFYNLSEEPLGKGTYGCVYKATDKLLKIQRAVKVVSKKKLKNIPRFRQEIDIMKNLDHPNVIKLLETFEDEEQIYLIMDLCTGGELFDKIIKKGSFVEMYASFIMKQIFSVLNYLHIRNICHRDIKPENFLFYDKSTESLIKIIDFGLAAYFNDIDYEMKTKAGTPYYVAPQVLTGCYDYKCDLWSAGVLFYIILCGYPPFYGESDHEILSMVKKGKYNFKGKEWNNISEEAKDLIKRCLTIDSGKRINASEALKHPWFKKKKGSFNLDVKMDIHVLENFKNYALLLKLQKLAMTIIAQQSNDYDLQQLKTVFLYLDEDGKGNITKNQLKKGLENSGLKLPQNFDVLLDQIDSDGSGRIDYTEFLAAALDRKHLSKKLIYCAFRVFDVDNDGEITTAELAHILYNGNKKGSITQKDVNQVKKMIQEVDKNNDGKIDFYEFCEMMKLKY
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Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). In the mosquito midgut, regulates the gliding motility of the ookinete which is essential for the ookinete to invade the midgut epithelium. However, another study showed that while required for ookinete invasion of the midgut epithelium, is not required for ookinete gliding motility.
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A0A509AH51
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EIK2_PLABA
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Eukaryotic translation initiation factor 2-alpha kinase 2 (PbeIK2) (eIF2alpha kinase 2) (EC 2.7.11.1)
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MLNMVDQKKGINNGSSTGVINNINGKIKNEFIFMYLIAAGGFSCVYKIKKKKSNKFYALKKIKFSANESNYEKKVLLNLREIECLRKLKNHPNIVSMNDFWLEVVQTLSKSKRERRGRRKEQQREQMGDKRREKRQQQRREKRKEQNTNTKKRVLITLSDHKKKKLKHLSCPENALNISNITNNERNVLKKDNWKNLILLKNFKKEKHNYNFNHQIELNKYNIMCLWKILNQMCVCKNEKKNIESLLPEQLIKNFKNFLFEKYILAIYDDCSYLNNKNNKTFIFFNNNLGNILHYLWWSYLGKNGKEKKNDIFKLLKYVSDNIIKDNTNLYNIILEFRHSLIELSRFPSNELGNVILNMRIPPNGSCELSEYISNMAKINKLEIYRNKNTLEKFIFKINCNNFDVYKMWINFKNDIIYEGKDVYKEHRKINLKRKIIKKKDIWIKGKKEKHLKNTIGNKCIKKINIYYEKPIHVFVYKSLTYKRQKHHKLWRKHYNNKKNWKYCLNKHENSKKYILFSKICRLMKTQMNKFKREEKFEKKKKIAITNIKVNYNDFEQDISSFNIQIYNKKNKNQLINRIKEQYEQLSISLNPYKLTYENENILRYNEHNYLFGLKNDNEKENIYNAIYFLNFYIWIRREINEYAIISKKRQICQNSRNYQSKKKFYIKRHNQKTYFFENIIFYHYIIMLFLDIEKYKNKFVSLFQYNLYRKLLKISKRIVLMLHRIETNVICIFLLKHFEDYFIRKGIHIVQDKSDRSNKGDEIGIHKMVKIWKSMIAISLIFGKKMYKKKKNIFNFFIELFLNNIQINIFKKFEILYLIIYFYNYFEKSKQFDIEGIGDIIYVWLSLINLFYDDKGKCIKILSKIFAKLNKKLYYVYWGKLYIIMNWTTIVDTIFIRNVLSINREGNYYWVIIVLKMINYFVNVAYTLTRMDIFFIKVMIKFYTRIGSAAATNSVSKNSYNEIFNNIFTLNFMNYIIYNSYFENEKKNYDIYTKYAILFIYCFIIQAYYFDTLFNIRSLESNEIANNLFPGYNYSYKNILLFYERLGRVIKNSNNTKICKYMWRKFINMWSNSIVIKENIISCLTTSRHIYFNILMNFMKIYCLDNILHIKKKKKKMNTPIVLTSKNDLKKWKDCELTKNPKSVKKGILIKKKNRNNNKKYKKKLKETHFIYNIKKVLFKKLVNINIETILYEQNGQCYILVFGSVIKKKNGQIKVKDTKIVRDINIIRDYRIYFYNYLEYFYKNNAHISDNINLIYARKWPYNNKNAVKQFCPYFDKIKDGNRKDIVSLYGNKILVKQNFSKIGNKIKNKKNNLCKKKMRTQKSIYNSNYWREKKENKLLNGNVNIIKKYKSEKIKKKELENFFDNIVYSSENDDFKIIFENATNSNACSTVDLASPNELNTKRNNINKKLKFFKHKKNSKKQKNYKNHKSHKKIFFKSVNNANRFFVTNVEPNPIMSNNHQIADSNDIYNNFSIQKKYEYNHKNCGNIYNTKDCDENDSSYICFLINEHEGQVLSHRHKELYKNMLGMERGNILYRDNACKLKDDFSCLHDQCDNSMIKACGTNELIKESTKIKRENMDKINKMNEVNQHISLETLKYKCSFKKIDKNLIQNKKKIIIRKICQINKTFYFKYNKINDKKRIYFDSVLCKSERHKTYKKRNENIKVILLKTLKGESNEYVLTTYLTEIYSDNINDPFENSRKKINSNEIFYQKTFDMYCIEDEGEVYEEQKRVNKNNKKKKYINEMIKMDTIRTDFEDNFTNSYNKKCNILKMASNINNKNNSGKKERDIKRQFLITNKKKHENNIKIFYNLFKLEESNVNSNPQTNPYYETVIHDNEDNIFYCLYKYIQQQVYRYCNCDIDEYTSNCIDKNVNKWEWYGFIKENENYDKIKTEINSNSFYNCREKHNICNSYNSVYQLEFRKLGNASKEKNFEEKKKIIKIEFRKSFNNFKLPSLLCILKWDNFFKPHFIIRCDNFLHTYNIYFDFFILLMNLFHKGEGSNLYRFNSNKSIIYNPYLSHQIYMVTKYFISNVHKINNKLPIHLENDILEIYSYNRFLTIPNKCSFKNCGNDNNNYDQRSKKHYFTKCGILNTEKVKPSKKRRIGWDGQRQRKRKDIINTLNEENQNMFCKNKEKKEENYKKIDTNISQFSEKNPVSNIDNEKNKQNFIKNKKYKFNLYIRMEYCKDTIENYINRRTRINIKRNIEIINMIIMGLNYIHNNNIMHRDLKPSNIFISNNDIVKIGDFGLASYDYLDDHKINTTKEEEIQKDLIINKNCDKIFFCNKKKLFSNYNSVFPLENGQISDVHNTKGDYNESSISKSKKFAIQNKNRNLRSCKRIFQWWSTIGELNILSKNRRRLTKFKSGSNTIHIRKSTLDENIIVRHANKCHNLSFSQNREHIDRNRMKKCNIIKNHIIKSNKSEKMNISMNVFLRCTKTRRYFTDEDKSVETRKKCSKTSEEENGNICDTKKKKNDIGEKMDKNKIAAQKKKKKKENKHPIGRRSTNSSISSAIVVKRNAYCRLEIEKYFLSKSFQNCRSNKKKKYINIKTIKNKFCSASNKNFGAKWMRIYRKGLHHDDIQEKSADQTTEQMGGCNKTVASDFSSNLKNKKESINHTLGIGTKLYSAPEQLEGNKYTKSVDIFSLGLIIIDLFIKTETNMERTQILCNARERILPDLLIKKHPNVASLCKKMLSLDYKSRPTSAQLYNKIISAGDIFLPDKCP
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Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.
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A0A509AHB6
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CDPK1_PLABA
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Calcium-dependent protein kinase 1 (EC 2.7.11.1) (PbCDPK1)
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MGCNQSKSANDVRGNKVNHVNSKKKNNKREDTNDGEEIAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCKEKNGHSEKAIKVIKKSQFDKGRYSDDNKNIEKFHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKNSLLNIKIVDFGLSSFFSKDYKLRDRLGTAYYIAPEVLKKKYNEKCDVWSCGVIMYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISDEAKELIKLMLTYDYNKRCTAEEALNSRWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNVLRNFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRRAFNLFDTDKSGKITKEELANLFGLTSISEKTWNDVLGEADQNKDNMIDFDEFVSMMHKICDHKTF
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Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK4 and CDPK5. In the mosquito midgut and during the last stage of male gamete exflagellation, may play a role in the rupture of the host erythrocyte membrane. In the mosquito midgut, required for the differentiation of the zygote into the ookinete by promoting the translational activation of a subset of repressed mRNAs these mRNAs are kept repressed in the zygote by the DOZI- or CITH-containing mRNP complexes. Dispensable during the asexual blood stage.
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A0A509AKL0
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KGP_PLABA
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cGMP-dependent protein kinase (EC 2.7.11.12) (PbPKG)
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MDDDEIIPKKNHPSNERNKKKAILSHEDFTGEDSLMENHLELRDKLTEDIVTIKASLKNNLVCSTLNENEILALSNYMQFFVFKSGDMVIKQGEKGSYFFIINSGKFDVYVNDKKVKTLTKGSSFGEAALIHNTQRSATIKAGTNGTLWGVQRSTFRATLKQLSNRNFNENRSFIDSVSVFDMLTEAQKNMITNACVIQNFKPGETIVKQGDYGDVLYILKDGKATVYINDEEIRVLEKGSYFGERALLYDEPRSATIIAKEVTSCASICRKLLNVVLGNLQVVLFRNIMTEALQQSEIFKQISPDQLNDLADTAIVRDYPANYNILHKDKIKSVKYIIVLEGKVELFLDDESIGILTRGKSFGDQYVLNQKQKFKHTLKSLEVCKIALITESCLADCLGNNNIDASIDYNNKKSIIKKMYIFRYLTDKQCNLLIEAFKTTRYEEGDYIIQEGEVGSRFYIIKAGEVEIVKNNKRLRTLGKNDYFGERALIYDEPRTASVISTVNNLECWYVDKSVFLQIIEGPMLAHLEERIKMQDTKVEMSELLTERIIGRGTFGIVKLVLHEPTKIRYALKCVSKKSIIELNQQNNIKLEREITAENDHPFIIRLVRTFKDSKYFYFLTELVTGGELYDAIRKLGLLSRSQAQFYLGSIILAIEYLHERSIVYRDLKPENILLDKQGYVKLIDFGCAKKIHGRSYTLVGTPHYMAPEVILGKGYGCTVDIWAFGVCLYEFICGPLPFGNDQEDQLEIFRDILTGQLTFPDYVTDTDSINLIKRLLCRLPQGRIGCSINGFKDIKENSFFADFDWDRLAGRLLEPPLISKSETYAEDIDVKQIEQEEEDNANTEIDDENWDIDF
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Serine/threonine protein kinase which acts as a downstream effector of the second messenger cGMP (By similarity). Controls the release of Ca(2+) from intracellular stores by regulating phosphoinositide biosynthesis. Ca(2+) signals are essential for merozoite and sporozoite invasion and egress from host hepatocytes and erythrocytes, and, in the mosquito vector, for gametocyte activation, and ookinete and sporozoite motility. During the host liver stage, regulates the initial invasion of host hepatocytes by sporozoites by regulating sporozoite motility and microneme exocytosis. Following parasite development in the hepatocytes, required for the release of merosomes, a vesicle containing the mature merozoites. During the asexual blood stage, required for the progression from schizont to the ring stage following merozoite invasion of host erythrocytes and for merozoite egress (By similarity). Regulates merozoite egress by promoting the release of exonemes and micronemes which contain proteins essential for egress (By similarity). Phosphorylates CDPK1 predominantly at the late schizont stage phosphorylation at 'Ser-64' regulates CDPK1 protein-protein interaction and phosphorylation at 'Thr-231' may regulate CDPK1 kinase activity (By similarity). In the mosquito vector, required for the initiation of gametogenesis induced by xanthurenic acid, specifically the gametocyte differentiation from the crescent-shaped form to the spherical form. Required for the gliding motility of ookinetes to reach and penetrate the midgut epithelium by promoting Ca(2+)-mediated activation of CDPK1 and CDPK4. Also required for microneme secretion in ookinete by promoting Ca(2+)-mediated activation of CDPK3.
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A0A509AMC3
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PK4_PLABA
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Eukaryotic translation initiation factor 2-alpha kinase PK4 (eIF2alpha kinase PK4) (EC 2.7.11.1) (Protein kinase PK4) (PbPK4)
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MYNKGINICLNEDNKCIILLHIIFNKCIVSFVASHILVEGKICFLNRIKNSKIFRRFGNINNHRRNNVKEYYKFVGRINKGKEKRNKCRIKLHRFYEYAKSYILKQIKWVLNKSKYIYFNIIYHLKTICYLKNAFFLQYTQRKYFSQNIENYIINSLPKHIQSFNPIKWSYYNNNEYASNYIIINNLNFIKYKNKYEKQYDIEMEEDINCKGANDIFYNSYNYCNNNNSNSKCDEKIEKNIVDKNIENKYNIKEYDKTNKSILFPIEEEFKKIIQIENNIERNYMVPNESNKNILYNIKNILEKIRNIEAISNINNYIDMKNTIESYKLNPDKCKEILHKDKDFRNKSKLCLSCFHNIIHKIIYYSKMENISFSDMYKQLLTNYNNTSCEYCNLINNSINSNNDFLSLYNDKNMYNWKNCEKNKFETLENEISCWNFNSSYGNHFQHIQKNSKIYRRILNEENEKAFNNIVGRNEMENDELYKRIHTENNYANQFTENNVDFGVYSDLREYNNGNEKYMLDENEMDQIIDEEVKKQEKNQNLNNMDFNNVNKKYNQLKDDNIIIFNKNNMHNNLYSNGLNDSNLEKNNILFPYEKYNNLDKNEMNLTKYSQNKQFYGQYKYDEAIYKYDLIVLDTSGYIYKVSTDGTYHWKYRIVKNIQYYINYEEENKIENYYNAFKKNNGKINMTHKDILRKNDYEQYHKLKLRAMKKLQYNNFIDVFNSNYKKNYPTYLNEQITEKDDIYKKKNYNYEKSKKKSKNKNAMKKLLSDYSGDLFYVDENNEAIPININIKDVVNNSPFKSTLFPNILFIGSRQSSIVNLDFDTGYVIKKYEENYDDLVKEKQKALPNKYEKFINKNSNVLHDKLEKYLDHSIDINDKNYYVNEEKDDLDKDYTIIDGKVAENNQQLDNIDLYNNEIETENNNGINHLLLIDGKGQIEEQSPNNGNKIIKGDVSNMTDECGTENCLSKHSKEEIEIANNKFNKNNKDKLLIQRTKIKNKKHFLMGKWYMNISNNNLLNINSSVLGINKKKRNSKKGENRNKKRKTQKRQLQISLVKWVIKAVDETSLKQKWITSWVDVGSIFITDSHKQDLSFINSLIDIDGNKLILRTLENNKVNKPYNNTISKNIEDAERNELEFASENYKNDIPNEIDEHNNKMGRNMNKLNSNIKSKIFIFSKEISSVFALQYKSKTNIFTLDTILKQNEKLFPEYDNIKPYSYNLLNLKNNSNALLLPFSSSNDYLKNNDKKNLPWNFNYDENGTNANNSIAFQNYNNFIVQRLNNISINITSIEKDLRYLLLSIIFVFDKHKKIPMNYIFQMKTLLHEYQKTKQKFMICLRGLNHNKNINIFSNHNDIRDTDIKHYGYNDYDYINKEMDAIDEPIHICEYTNKFIDLSFEGKEKCIDYCSMLNIWDKIFNNYTNHDDCLLLSNLYRILNSTYPLTNKDFNRIIDGIFLKNNESMLIKRRRKPNEGSRNHDLTEFSSQKHKKSWYWNIFYAITLVIVIPFIFIYRLFKKQTNNKNNNKIIMRKKKITDYDEDSNDTYDDELLNIDKVLLKRNKRKLANILKENGISSLNKTELEKYMKKSLKKAQDIEQLTLVDILARHARDSDSDSNFYDIHDGKYNLYPYYYSGQESKYSLPNMHYIDLSKSNSGETNKYDLNGNNLFYMHRRRAASQDVTYKQSFIVKKRVRSNYKLGNKYNKRNYTDYEKDKKNSSIKERNINEKAFDKSDFINFLKNFNKKFMKKNPFVDHLMKNNKTDSNNEFNNDNKEKSKYLYNEKYNLNSADEENKSPYAKKYSDEKKNRSKSSKYIENTQSNNNDNTNGNMNVGNHINNDKMNNKGSSARNLSIIQTSHIPYDAPLADFLENGRFTRTFQNISLIGQGGFGSVYKVSHRLEPGSPTYAVKFIYLKVSSLDNVNSRRYFREIAANRDIYSKHVVRYYTWWCEEPQFLPMDIIPKEIQNTLKKNKDPFKKVCNKNKKDNDYSSDCTVSSGENNKFDLKNYKKVITKKNSPKLKFYSDNDTPYNKRKNINQKNSFLNDKNLSDNIYIIENNKKKKKKKKKKKKIIYKEKKKGNIGINEDNKYSTFYEQNNPNNFSSTLQEYDPFGYGYLSENERDLIVFADNDESNGSGHSKKNDNDERKSLNNQNGIYNTGGDISKNGNVIHDDSNMLACQQSDKNSMTIKNTQGTSINGTINRNTISDETGTQGTNNNPKYSIDYHIDAIVKPKGESFTWVEKSPSNKYKKDSLDIINRNRKLIEEKNKKEKGQEKEKYKLKMNGELEKKENANKIKYYKKKNVGPEFSIVLLLQMEFCKGFTLRRWLDRSSRSDKPLYFTYGDKNTNHPLEFDLFKQLIKGLKDIHSTCFIHRDLKPENIFVDLDTYILKIGDLGLVRFIEEKKRENDLNNIDNFKDNIYTEINHNTITSQISLKGQMIGTPGYTAPEGGALCDEKADIYSAALILLELLCPRFNTIMERYKTLNDFRNYYTVPDYVKIHLNPWYILMLQMSKPNPADRPSAADLYNKIKVLLDPHLTDFTFSFNDINNDDLEYTGNRNVINSTNPNGDIKENVNQNNLVDDKGNNNIINGNEVDH
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During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.
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A0A509APX1
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GCYB_PLABA
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Guanylate cyclase beta (PfGCbeta) (EC 4.6.1.2) (Guanylyl cyclase beta)
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MKETDKIKSEVLNLMQLDGKREHINKNNKLYRKVIINPTSEDDLQKFCKNYFRIYQFSLYNFIRRLISLDAVIVYTLFMTVYIFSEISQGITKKYLFVDTAISLFLNIGILVVIESLFELKLLKDIKNANSQHYLRIVPKMSYFEKVMTKDIKVGNIIRVFQGEEFPADVVILYSKKNTNAVVDSFKIDGLYNKSIKYPVEKYKIDRDYLKMLSEINGVIKCELPNKNVFCFQGTYKLDKHPRSLHLSYENFALQSSILKGAEYIDGVVVYTGADTKKNLNIPRKIEENMTFCIKMNNVVYYLIFMYILFVLLSIIIKAIFYRKGKLLENSNDTFFTVLEDFIGLYILVLPVMLYSEKSLIYIIQSLKIERDTRMNKDENSNNTKVFNKNKNDALGTVDIIATARNGVLVNKKEILVSCTINNVLYSKKKFIISDEFLKLPSLNILDAERTNVSELLNLDERIFKDPENIFFPSRDFNNFLKILGNNTNPIYDPINGDFSKILKEIYRNYLNEEFLYKKIKLSSSVKSLLDNGYNQFLEDCESSYDCKEIIEDGLKNNEQSEKIEEFILGICACNRIIIYNEKFGDIEMKDNINEKSTSEHMNYDKDREVENIESENKYAVDSDGEENMNTIEHEDICLFNTSKNIGFHIYCYKKCLFFYNLKNICKEYYIICFHDFLRSNNYTMCILKNKKELDKGILYIRGYDFNILPYLCKNKNDINKIKKTIKIHTANYLKVILICKKNITNEDIAKYIYLKSVRSKFSFKFFDIIKTFFLYDLECIGIIGLKNDLNDGVVETFNDINNFDIRSWIFTNDSSKNTYLTALQCNLITPNSNLFIINFLNPDHSDEETVANYLFNNFLFSMENMKSRSYAIAINEMSLKNIMRSRYALKVFLCIIMRATVVLFCKLNNETKGKIISKFLSYTTPKLTVLGVGSTLNDAYLLKNTTISVCLTLNKQVNALYSISDYAMEEFKYVGELLILGRLNRFSLCRAFLWIIYLKVMIGSFYFFHNFDNFFSGSSISSILYSQTAFAIFHYSLIVAFASYEIDIPYKFIRNFPYIYQLARRKYFLNNTIIFLNIVESIFSSFISYYILRGNLFNLITHRKFTFHIFVLNFFLISEKILLFSKTWHIFFFIMTIIIVSILFIYINIYTLVDCLITGKCEFSLFDPEDSYFWISLLPILYINFIIDKFMKFVKNKIYPDITYHLSNTLKIETQEKFATNNKREEVITDKNIEKLAPVPKSYIIKEDNAYYGKSKKNKYIFDTLRKIIDIKIKYRNQQLNLEYKTYEKRNKLKLRIIILLLFIIFLITFTIQIIISKFIEKKLHSLSYLTVIYYIVAVLYLIKILIRNKTNYTYFYIIGKLLLVIGYLLEISENSVNNIINMLVTYSFTVCYIFFISFKILEGLVMCIIILSIAIWVYYHKNNNLNAMCTDFCDNPYTSLDNLEYINISCICKQQIFTFLICTLSFTLICLFMKYYEIYYLKKKFLTRYKQKVNLGKQIEILHTMLPSFLVEYLLVSDPKADGIMVGKNISGEDRGIISVIFCDIDDFQTMVSTLEPHTLVQTLDNLYLYFDKCIKYFNCIKIETVFESYLAASGLSEKKNNCVHKIKYDTKCAIKMAIAQLSAKYYISYKVLDTLSNNKDSNSIFPIESKYIYKNISLRIGIHTGKAISGVIGSVKPQYSLFGDTVNTASRMKSTSLKDHIHVSYDTYKYLKDDKTLVWKERSIFIKGKGEMKTYLLVDILDNSKKDHTKALEESTSSIFRSNDEIVNKSELITKEKEFDKIEMPDKSEIIDETKKIFKKSEKPSTKKKKIKKENAKEKNINIKMKEMGEILNNYDKEKVYNCNKSDDGSNSIGQNDFLYSTKNYNYKKSKYLDLERLSTNKSFRRNVLAYNFESPINLPPKIGDNTKRNYDSDNFFTSPYIIDKNEKDEIRDTTNKALYIKKSKNIINRMREDSIDFKDEFSKENDKIKEYIKERITYRQKVTPNYFNFNNMSKYSNAFKKKKKKKKDIQKKYTYRQKTSFYNFLNKNDIINYNYSSEFEYFIDPKMKNKKPINFNNLFAKIYKKKLSLLNIKNEPINIKKKNIKNKSRDRIIFSSRRDEEHDDNQKMNKKLFSRTYAQKAEQTSHENIFTEMINDNFLKKEDKEQCEIRNENRCPTVFLIKRNKTTININKNRVLKRIFKDIITRKKIKRNRILKNKKLNYVNKNDNLGKKYEILNNICLVHKRAMTFVQYNTEDEEKKRTKRFHKNDEIFGSDMNISRNLNGSNSNIQNINRRSKNKAEDDLFIRNKVNLNNIKNNINLRKNIYKTDERGMQYNDLKGYDKKKNTEENNEDKEKKIEYDSNENIKNGFPKNEDKMIMKKRMISKRISFYSLKEYEKGDSFKSYDNSSCGIKSKKTNSIISDEEMNEYFNYNTEFNSNRNKNKQNKEFSLASKVNNIFKNIFKKNYISDKLKSGKYNTMSNSKSGQTNITTDNKKSQIKKNGDVNKANTNVSNKNSDFVTNFDNYNKNILKKLTSTLQINRKTSYFNRFYYKFKDEELEEEYTREYYQEIINIDLTKKLIIIFVISELILSLCNVIELSYYENKETPNDFIVIIWLIRSIYLFTITFIWLLLKTKLKEYKDNSSKMMWTTFILNIFLSSWGIIMIDLACIHYSNLVGNSRERSIFFMKDATELIISMQLIFVKNMLFKHKFFFFVFFFVFLMYSFFKLFVIHVCELRICCSILLILSINILYFWYSEYLDRTQYIIKRKRNRMERTSHDFLTRILPRQVLEEYQNDNLQLTYKHEKIAFLFADIVGFTKWSKTAAPKNVLKLLQKLISKIDKDTIKLGLYKLFTIGDAYVATSQPNASITDQTEAADGIISIFKLAKLILHNINTIKIQFNKHDFNMRIGLHYGSCVGGIIGSVRIRYDMWGLDVLIANHIESNGIPGEIVCSEQFKNFFLENEPHAKLNFWHYKTISINDKDIKIYVVEDKNYEEDYDPKIINYETLLKLREQNKVKG
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Catalyzes the synthesis of the second messenger cGMP from GTP (By similarity). Probably by regulating cGMP production, required for ookinete gliding motility, which is necessary for the ookinete to traverse the midgut epithelium of the mosquito.
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A0A509AQ68
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ENO_PLABA
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Enolase (EC 4.2.1.11)
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MAHVITRINAREILDSRGNPTVEVDLETTLGIFRAAVPSGASTGIYEALELRDNDKSRYLGKGVQQAIKNINEIIAPKLIGLDCREQKKIDNMMVQELDGSKTEWGWSKSKLGANAILAISMAICRAGAAANKTSLYKYLAQLAGKNTEKMILPVPCLNVINGGSHAGNKLSFQEFMIVPVGAPSFKEAMRYGAEVYHTLKSEIKKKYGIDATNVGDEGGFAPNILNAHEALDLLVASIKKAGYENKVKIAMDVAASEFYNIETKTYDLDFKTPNNDKSLVKTGQELVDLYIELVKKYPIISIEDPFDQDDWENYAKLTEAIGKDVQIVGDDLLVTNPTRIEKALEKKACNALLLKVNQIGSITEAIEACLLSQKNNWGVMVSHRSGETEDVFIADLVVALRTGQIKTGAPCRSERNAKYNQLFRIEESLGANGSFAGDKFRLQLN
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Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (By similarity). In addition to glycolysis, involved in various processes such as parasite development and invasion. Plays an essential role during ookinete invasion of the mosquito vector midgut by mediating the interaction of the ookinete with the midgut epithelium and, further, by binding to mammalian host plasminogen in the blood meal, whose conversion to active plasmin promotes the invasion process.
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A0A509AQE6
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CDPK5_PLABA
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Calcium-dependent protein kinase 5 (EC 2.7.11.1) (PbCDPK5)
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MCEHKANNKNDGEFVNLKEKNENNHCGNTKSTIADCDDDYSIITLCTKCLSTKTEVNKNKIILDSKALKDSRTKRRSSVNINIDILNNNLNLSPYFDRSQIVQETILMNNDDLEKLYELDKYKLGKGSYGNVVKAINKKTGQAKAIKIIDKKRINNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCTGGELFDKIVKHGSFSEYETYKIMKQIFSALAYCHSKNIIHRDLKPENILYVDSSDDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILKGKYDKKCDIWSSGVIMYILLCGYPPFNGKNNDDILKKVKKGEFVFDSNYWSKISLDAKELICECLNYNYKERIDVHKIVNHKWFIKFKNYNHITINKHLSKELIEKFKKFHKLCKIKKLAITCIAYQLNKKKFGKMKKTFEAFDHNGDGVLTISEIFQCLKVGDNEIDRDLYYLLKQLDTDGNGLIDYTEFLAACLDHSILEQDAVCRNAFKIFDANGDGIITKDELLNVLSFSNDQMPFSKEIIENVIKEVDANNDGYIDYDEFYKMMSGRQS
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Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase (By similarity). Plays a central role in host erythrocytes and hepatocytes infection cycles. During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK1 and CDPK4. Involved in merosome egress from host hepatocytes, probably together with CDPK4. Required for the release of hepatic merozoites from merosomes in the host blood stream. During the asexual blood stage, required for merozoite egress from host erythrocytes by triggering microneme secretion (By similarity). Phosphorylates transporter NPT1 at late schizont stage (By similarity).
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A0A517FNB9
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C9B52_PARPY
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Cholesterol 22-monohydroxylase CYP90B52 (EC 1.14.14.-) (Cytochrome P450 CYP90B52) (PpCYP90B52)
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MEGLLLLLPTAIIALYLYISLIRRSRKKHNLPPGSDGWPFLGETFSYLKPHSAISIGRFMEDHISRYGKIYRSNLFGEPTIVSADAELNRFVLQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRMISLNFMSAARLRTRLMPEVERQTLLVLRSWREGSTFSAQEEAKKFTFNLMAKHIMSMDPGEPETEMLRREYITFMKGVVSAPLNFPGTPYWKALKSRSSILAVIERKMEERIGRRDRGDGGVEDDDLLGWAMNQSNLLKEQILDLLLSLLFAGHETSSMALALAIYFLESCPEAVRDLRDEHLAISMSGKEGECGLSWDQYKQMEFTHCVINESLRLGNVVRFVHRKAIQDVQYKGYDIPCGWKVLPVFAAVHLDSTLYSDPHRFNPWRWQSSSSKTTAANFMPYGGGLRLCTGSELAKLEMAVFLHHLVLNYQWKLAEPEQAFAYPFLDFPKGLQIKVRAIT
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Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation.
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A0A517FNC5
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C90G4_PARPY
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Cholesterol 16,22-dihydroxylase CYP90G4 (EC 1.14.14.-) (Cytochrome P450 CYP90G4) (PpCYP90G4) (Protein DWARF 4 homolog) (PpDWF4) (Steroid 22-alpha-hydroxylase CYP90G4) (EC 1.14.14.-)
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MAPVVILFFLFPTLLVLVVAVLGLRGGDDSWKKRGLKVPPGSMGWPLLGETIAFRRLHPCTSLGEYMEEHVNKYGKIYRSNLFGAPTIVSADAELNRFVLMNDERLFEPCFPKSVADILGHTSMLVLTGEMHRYMKSLSVNFMGIARLRNNFLGDSELYITQNFNRWKENIPFPAKEEACKVTFNLMVKNILSLNPGEPESEHLRKLYMSFMKGVVAIPLNLPGTAYKKAIQSRATILKMIEKLMEERIRNKKAGTDKIGEADLLGFILEQSNLDAEQFGDLLLGLLFGGHETSATAITLVIYFLYDCPKAVDHLREEHLGIVRAKKARGEPPALTWDDYKQMEFSQCVVSETLRLGNIIKFVHRKAKTDVQFKGYDIPKGWSVIPVFAAAHLDPSVYENPQKFDPWRWQTISTGTARIDNYMPFGQGLRNCAGLELAKMEIVVFLHHLTLNFDWEMAEPDHPLAYAFPDFPKGLPIKVRRLALK
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Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones. During the 5,6-spiroketalization of cholesterol, catalyzes the hydroxylation of cholesterol to form 16S,22S-dihydroxycholesterol and, possibly, the subsequent conversion of 16S,22S-dihydroxycholesterol into 16-oxo-22-hydroxy-cholesterol and 16-hydroxy-22-oxo-cholesterol. 16-hydroxy-22-oxo-cholesterol submit a spontaneous reaction leading to the production of furostanol-type steroid diastereomers, precursors of diosgenin.
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A0A517FNC6
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C9B51_TRIFG
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Cholesterol 22-monohydroxylase CYP90B51 (EC 1.14.14.-) (Cytochrome P450 CYP90B51) (PpCYP90B51)
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MSDSDITFYCLSSILSVLLIFIFILIKRKQAKPKLNLPPGKMGWPFLGETIGYLKPYSATTLGEFMDQHIARYGKIYKSKLFGEPAIVSADAGLNRFILQNEGKLFECSYPRSIGGILGKWSMLVLVGDMHRDMRLISLNFLSHARLRTHLLKEVEKHTRLVISSWKENSTFAAQDEAKKFTFNLMAEHIMSLQPGKIETEKLKKEYVTFMKGVVSAPLNFPGTAYWKALKSRGTILKFIEGKMEERIKRMKEGNENLEEDDLLNWVLKHSNLSTEQILDLILSLLFAGHETSSVSIALAIYFLPGCPQAILQLREEHKEIARAKKQAGETELTWEDYKKMEFTHCVVNETLRLGNVVRFLHRKALKDVRYKGYDIPCGWKVLPVIAAVHLDPLLFDQPQHFNPWRWQNNGNCPNFSGASSNSNNIFLPFGGGPRLCAGSELAKLEMAVFIHHLILNYHWELTDNNDQAFAYPFVDFPKGLQIRVQSHSLI
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Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation.
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A0A5B8NIM2
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CMU_ERYQU
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Chorismate mutase (EC 5.4.99.5) (EqCMU)
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MDAAVDLLDPSKALNLKHIRQQLIRMEDTITFQLIERVQFPLNRTVYEPGAVKIPNSNLSFLDWTLREREKTDSLIRRYQSPDEHPFFPDALLKPILQPLIYPKILHRNNINLNDKIKKYFTDQVLPSICHDFGREDRGEQAENYGSTVTADIQCLQTLSRRIHFGKWVAESKYIDDPQGFAKLIKAGDRQAIGKAITKPAVELQVLERIRLKSRTYSTDPCESDDPEPKINVDAVVAMYRDCVIPLTKEVEIDYLMQRLSD
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Catalyzes the Claisen rearrangement of chorismate to prephenate. May function both as an effector during plant infection and in the fungal tyrosine and phenylalanine biosynthesis pathways. During infection it channels chorismate into the phenylpropanoid pathway, thereby decreasing the synthesis of the plant immune signal salicylic acid (Probable). Within fungal cells, it acts at the first branch point in the aromatic amino acid pathway where it steers biosynthesis towards phenylalanine and tyrosine, and away from tryptophan (Probable).
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A0A5C2A2T2
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COP1_CONPU
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Conodipine-P1 (Cdpi-P1) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A2) (PLA2) [Cleaved into: Conodipine-P1 alpha subunit; Conodipine-P1 beta subunit]
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MKLLAPVLWAMAALGVTWLVAVDSKESCTKHSNGCSTPLRLPCQEYFRPACDIHDNCYHCGTIFGISRKECDDAFLKDMNTLCKKLGSNSATCPARGKREVTSHRATSIAHSRLWKTALDQKSFLNRKARQAILLTPNSCLYWANNFYMAVHVFGARSYSRTTDPKDCQGLKHCLPNH
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Catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
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A0A5E4M3Q4
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SYD9_CAEEL
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Zinc finger protein syd-9 (Synapse defective protein 9)
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MSVCVSPLVQATILMTEESLTCPQCPKSFSSTKLLQQHQQMFHTDKSVLLSLKSTDAPVGMDRAFICETCGKAFRFRSNLAEHRSVHTALKPYVCKFCGKSSRLKGNLTKHILKHHKKEQNEAIAKDDIIVKKAPKIVTKDNGPTTNGSTPTTSTATPSVITVSSALASSNGHNNNNNNHAVNNNLRTIKMELEDPDYNLIAKSAPTPVVSKIVATHTVTPRSRPTPKDIKEILETIAPSVGVSETPEEMCLLPKDASSESDRSVLISLGFDFGSTLSLNHQQLQQVVRELKGELSISPDTVQSDHSDDFEQDSPPPMAIANISTVGGEATLAAMIVAATNASGQRGDGTPDSTDTQKGCSPQRELSPESDPSTSSGDSCPSPPKMLHCKECGTLVRKSSHLPIHMTMSHGYPPPLVAAPVEEKPAPEQPVNASSLHNELRVISNAICELKAQQAATPRVEQALTYIDSRVGKLERSLETALNSIYTLVQLQTGMTSSVNRLREDSTKNFSDLKTRMEMSLSPIKPFQQRFSRERSSSSSVERSPSRERSRSPL
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Plays a role in regulating synaptic function, probably by modulation of endocytosis. May be dispensable in muscle for normal locomotion. May be involved in post-transcriptional mRNA processing, in parallel with unc-75.
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A0A5F8MPU3
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CTSRT_MOUSE
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Cation channel sperm-associated targeting subunit tau (CatSper-tau) (C2 calcium-dependent domain-containing 6)
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MELPPPGNRRVSINNPQETSGRVPTTSAGFPTQSSKISLKRSTYAYRPSMMSNRSSGGQSLLPSSILQKTSLNPPGSLQSKPSNLSSVHYADEEGKPLTDKNKDKDKGRGKGKGTGTRLLTMLRKTLQGSQSDEMAIANQTPNLIPFGDVVGCLAIHIKSCRQFSQRFLGQQRFNLFMRVSINNIVKCTKIRHLKAVNNEKNLVLRFGEMKYFSVQVPRRQDDERNFIYLELMHDGGDPESPPIPLGGAESHLYEVIQKGCFTEVMHLMHKNSSICRVEVEFMFSYGNFGYGFSHQLKPLQKAIEPSMFMNIAPPPERTDPVTNVITPQRVEYPAFLSPEFNVSIGVPEASHATVVQLEKLREKPRERLERMKEEYKNMSTWIEKADYLRNLINPKMTKRDNKGSSIPSESNSSALEELERTTYDIHHRKYEAISNEYGDKEGRVIPVLKVLDQNYSEVFLPKSSDSTPLEDVLLPPIHSLQIVEENEMPHLPKTSEPEDRPHEERKSIVFSSDEELMPKHPSILKISSSQQENRRKMEKSPHFSDVLIIPDKPFEDLNTNKKGRPPIELRKSWERHPTDVACSLRKVAFAQKDYTIPVCKAETTEFKPKHQFQKLSKSGLDPFLRNINSKMSFRKKKDHDDGYRNLSTSSAEILEHEDQDPPYPGHSGSAGSDATWAENPSPVTVQMVNRDSLPPDLITATIVISDRKNKLSLDSVFNSANSLNTKSIFASDNPVVSLTKLSDSDNKLITDSSFNTTKPSNRRLSKDSNFNTTKPSDRKLSSDPSSNTTKPSDTKLFSDPSSNKLSQGPSSNASQLSGSNRLSHNPSINGNKSSYTSDLNKVSRDPSIVSTISSDPNKLSRDPSFVLAKSSDPNKLSHYPSIISAKSSDPNKLSHDPSFVSARSSDPNKLSHDPSIISARSSDPIKLSRDPSFVSARSSDPNKLSHDPSIISARSSDPNKLSRDPSINSTKLSDPSKLSRDPSIFSTKSSDPNKLYRVPSIISGMSSNPKLSRDPSIISGMSSDPKLSRDPSIISAKSSDPNKLSHDPSIISGMSSNPNKLSHDPSIISMKLSDMSKLSRESSINASKSSDTNQLSYDPNIISAKSLDSNNSSASSSPTVNSDTTTNAAEPSGTKNMLDPVVSTIDSSDKQSKLEWLPNVQGASSVTENINTHRSSNSVNFTSDIDILKQSIVLKSILSKNLQDLSDELFSKSELYTNDEGYSPPPSVHSRPSDSTDDRVLGKVQDLNSWRSSKDLLNSQVLLSPVVKNSPQDLLPEGEPGKSSDIEDYVSEKLLEAAGRNFPMNRKSSFKKKHLVSEESSSEHVLSGSIYEYVIKQIFTAPIFSQLGIGIKSSSEARMDSQNQLLTPWERSVTSHIINYEEKDSDVNLSQSKSIISQIIQSFPVNTLLESGVIKVIELDKEHQNSLLDSQTTSSTEQYSDSRSQIKLLSRQNTSSINPLDSSVSGAEYTEDCQSISTQESKYPVRDTKSDSPNDTEEMELDSNLESSSSSLDKVKDTDTAKLKNILKNIFSIFFKYNQSERRQQPEKDSESLIKHSSSSGSEHLEKTQENFNKADKKVDRKPILNPKLRMFLEKLSETEVKNLKSELSKHIQHYLVERLTESGHITKEDLPTIYHKLYLMNEKVELKEQTPFQEKYSETVKEIMSFVNNFNHHFIDKHLETKLRGFLSEILQNYFLKNLSVSNLFNETDAMALHASMSPVRSKSELGQDIADGNFGSSLKINMQYPVTKSLQHYLQDLSENELLSLKTDLSKYLQVLFIEKLYKSGLVSERQLKGISQEIISLHSPSIPLKHIKTNLPFRNESYFMREDSEEQMKYLKNGQNAALHVLLKDKCGETELSRKKERESSFSQILKENLPAIWEQKNIYTREEETLNLIQMQSFLNKNNQANPLTRSPERPSDISLKKQKKDHGFMQFTQVEGSVYKTEIQDPYSWDSRSKTIQSKPCLEKTLKMKLLDKRENNNFYKLTAQEKLDTEFSSYLKLPNCKIPKEKEPISRLSFPTWKTNTFIHVKPEIGEQSKLDHYYQRLKGNNNNNKKHLVTFAQFKNEMETLYRNPYEACNEKRAKISESQSFKYKEKEKSSRPFFFPEVLKRENTKSKRKERDHATKPKKSFHKIVRLLPATLPTTRPHLRKSAPRNLLHWTARRTIHDCLDRFDDLHAPTVKCPKKSKSGARLLGKSPEDSHNQAKHCARPYTAPEPNKRRESAAWKFASPRMVSAGLLHLYVTPAYGIRKVRSKRKLKEDIEKRPLISEIIQMLDNAE
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Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CatSper complex targeting and trafficking into the quadrilinear nanodomains. Targets the preassembled CatSper complexes to elongating flagella, where it links the channel-carrying vesicles and motor proteins.
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A0A5K1K8H0
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CDPK5_PLAF7
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Calcium-dependent protein kinase 5 (EC 2.7.11.1) (PfCDPK5)
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MKETEVEDMDTNRKDGKIKKKEKIVNMKNEEVKSTTKSTLADSDEDYSIITLCTKCLSKKLEDNKNRIILDSKAFKDNRLKGRCSVSSNEDPLDNKLNLSPYFDRSQIIQEIILMNNDELSDVYEIDRYKLGKGSYGNVVKAVSKRTGQQRAIKIIEKKKIHNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCDGGELFDKIVKYGSFSEYEAYKIMKQIFSALYYCHSKNIMHRDLKPENILYVDNTEDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILRGKYDKRCDIWSSGVIMYILLCGYPPFNGKNNDEILKKVEKGEFVFDSNYWARVSDDAKDLICQCLNYNYKERIDVEQVLKHRWFKKFKSNNLIINKTLNKTLIEKFKEFHKLCKIKKLAVTCIAYQLNEKDIGKLKKTFEAFDHNGDGVLTISEIFQCLKVNDNEFDRELYFLLKQLDTDGNGLIDYTEFLAACLDHSIFQQDVICRNAFNVFDLDGDGVITKDELFKILSFSAVQVSFSKEIIENLIKEVDSNNDGFIDYDEFYKMMTGVKE
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Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels probably in part downstream of cGMP-activated PKG kinase. Plays a central role in host erythrocytes and hepatocytes infection cycles. During the liver stage, involved in sporozoite motility and thus in sporozoite invasion of host hepatocytes, probably together with CDPK1 and CDPK4 (By similarity). Involved in merosome egress from host hepatocytes, probably together with CDPK4 (By similarity). Required for the release of hepatic merozoites from merosomes in the host blood stream (By similarity). During the asexual blood stage, required for merozoite egress from host erythrocytes by triggering microneme secretion. Phosphorylates transporter NPT1 at late schizont stage.
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A0A5K7RLP0
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MEIOS_MOUSE
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Meiosis initiator protein
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MLGSDKFSCFSDQHRARSPSPTDRKDKKNHTNKLRELALLIPVTMKTRDKKYTKKEILLRVLHYIQYLQRNIDMTKALLKLHSSNGKGRFVGPGLNPSAGQTQQQHSTPSSSQKPSLWSTSSKPRKKKFTRVSEHPSWPYNPRRSLALDQAENPNTIHPGLKEENEECATYPGVLSPSTYPTTEPSVSEGDGQGAQLVFLDMAQNIFAYDILSDHAVEVQGGEPNADIKVQRSFFLTRAQPCVSSCRQKLFLCTSSEADKEAPDSDPWLPVWTSEDSPNGSPLALGSSQINTWHVADYLNEILGVSSSLFSSPSKILPDHVLEDGTYFLTEGLLESSPATCEVESPQEKEVSSEGPTGPPNFQSSVSLDHCYLSLSENVKVLSNCGSSSESTDTESLWGQEEVRGVATYPRRTGVFSLAQPSVLQQANPEGLQTSSDEDRDYTWTPTGQSSGLPVASKKIKKVQASQGPVKPKDSRKACPGQVKKKCVNGFIMFCRMNRKQYIRACPGTASTAATKDLAQLWRGMTLEEKKPYCTKARRFSRQNNRIVKQENSSSEDDDGETPKPFYQLLAEKAQVSLGLTSLPTPNCQ
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Gatekeeper of meiotic initiation in both male and female germ cells. In complex with STRA8, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis. Temporal expression of MEIOSIN is required for meiotic entry decision.
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A0A5P3XKQ1
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PMP1_PARBF
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Paraclostridial mosquitocidal protein 1 (PMP1) [Cleaved into: Paraclostridial mosquitocidal protein 1 light chain (LC) (EC 3.4.24.69); Paraclostridial mosquitocidal protein 1 heavy chain (HC)]
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MLQIRVFNYNDPIDGENIVELRYHNRSPVKAFQIVDGIWIIPERYNFTNDTKKVPDDRALTILEDEVFAVRENDYLTTDVNEKNSFLNNITKLFKRINSSNIGNQLLNYISTSVPYPVVSTNSIKARDYNTIKFDSIDGRRITKSANVLIYGPSMKNLLDKQTRAINGEEAKNGIGCLSDIIFSPNYLSVQTVSSSRFVEDPASSLTHELIHALHNLYGIQYPGEEKFKFGGFIDKLLGTRECIDYEEVLTYGGKDSEIIRKKIDKSLYPDDFVNKYGEMYKRIKGSNPYYPDEKKLKQSFLNRMNPFDQNGTFDTKEFKNHLMDLWFGLNESEFAKEKKILVRKHYITKQINPKYTELTNDVYTEDKGFVNGQSIDNQNFKIIDDLISKKVKLCSITSKNRVNICIDVNKEDLYFISDKEGFENIDFSEPEIRYDSNVTTATTSSFTDHFLVNRTFNDSDRFPPVELEYAIEPAEIVDNTIMPDIDQKSEISLDNLTTFHYLNAQKMDLGFDSSKEQLKMVTSIEESLLDSKKVYTPFTRTAHSVNERISGIAESYLFYQWLKTVINDFTDELNQKSNTDKVADISWIIPYVGPALNIGLDLSHGDFTKAFEDLGVSILFAIAPEFATISLVALSIYENIEEDSQKEKVINKVENTLARRIEKWHQVYAFMVAQWWGMVHTQIDTRIHQMYESLSHQIIAIKANMEYQLSHYKGPDNDKLLLKDYIYEAEIALNTSANRAMKNIERFMIESSISYLKNNLIPSVVENLKKFDADTKKNLDQFIDKNSSVLGSDLHILKSQVDLELNPTTKVAFNIQSIPDFDINALIDRLGIQLKDNLVFSLGVESDKIKDLSGNNTNLEVKTGVQIVDGRDSKTIRLNSNENSSIIVQKNESINFSYFSDFTISFWIRVPRLNKNDFIDLGIEYDLVNNMDNQGWKISLKDGNLVWRMKDRFGKIIDIITSLTFSNSFIDKYISSNIWRHITITVNQLKDCTLYINGDKIDSKSINELRGIDNNSPIIFKLEGNRNKNQFIRLDQFNIYQRALNESEVEMLFNSYFNSNILRDFWGEPLEYNKSYYMINQAILGGPLRSTYKSWYGEYYPYISRMRTFNVSSFILIPYLYHKGSDVEKVKIINKNNVDKYVRKNDVADVKFENYGNLILTLPMYSKIKERYMVLNEGRNGDLKLIQLQSNDKYYCQIRIFEMYRNGLLSIADDENWLYSSGWYLYSSGWYLDNYKTLDLKKHTKTNWYFVSEDEGWKE
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[Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice. [Paraclostridial mosquitocidal protein 1 light chain]: Neurotoxin that cleaves A.gambiae syntaxin 1a, probably hydrolyzing the '240-Glu-|-His-241' bond. Does not cleave A.gambiae n-synaptobrevin or SNAP-25, nor human syntaxin 1A. [Paraclostridial mosquitocidal protein 1 heavy chain]: Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of PMP1 light chain (LC) into host cytosol. Composed of 3 subdomains the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD), called HCN and HCC.
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A0A5S9I252
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TATC6_HYPAT
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Terpene cyclase 6 (EC 4.2.3.-) (EC 4.2.3.104) (EC 4.2.3.137) (EC 4.2.3.157) (EC 4.2.3.182) (EC 4.2.3.57) (Sesquiterpene synthase 6)
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MGQPTTTSLFMRDVMFHRMTGTSQAVNDVATLSGERREIIRRALNKKILVPNILELMPAWPSEFQPNIDEVNVEIDEWLKTVNVAKEKKLKHRARGNYTLLAGIYYPHCRKEKMLALSQFLYWIFFWDDEIDTGGELTEDREGTILCCAETNKCINDCLGPEPNYTPPPGSRGTVEMLYPILRDLRAGLSPVSTMRLKQELHDYVNGVKNQQKVRQEDHLPNPWDHFQMRVDDVGVIPSITQNEYAMDFTLPDWIRRHEAMEEIVLQCTKLTILLNEILSLQKEFRVSQLENLCLLFMNTYDMSIEQSIHKVLGLLKDHYKICIEAEARLPWSTTDEKLNNNIREYIRGCQRLATGTACWSYNCERYFKLSQLNDQQELLLDLSRT
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Terpene cyclase that is able to convert FPP into a mixture of sesquiterpene hydrocarbons and alcohols. The main product is trichobrasilenol. Additionally, side products include alpha-humulene, caryophyllene, 2-epi-caryophyllene, african-3-ene, african-1-ene, isoafricanol and pristinol. Does not accept GPP, GGPP, and GFPP as substrates.
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A0A5S9MMK5
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FPEB1_CAEEL
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FLYWCH-type zinc finger-containing protein peb-1 (Pharyngeal enhancer binding protein peb-1)
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MMTTTVQKNCWRLDQTMLGLEKPGSSDISSSSTDTSAISPISVSSMPLSPDKEKKKISFVRYNPDIPQIVTSFKGYQKLMYQGYRYNIYQIAPERNFKSWRCVCAKKMHDGQWCKCRAETTMDNKNACTKGSHNHPPRHHVAEIEFIKSQLYSAALENPDHDAGDLVNQASMYLSDGVMFDNKESIKKSLVVARNKDGKPKKPRSKRMMKFEVDDDDENEYKMPKLETDISCFLPFINNMVKVEPPFSHTPTIQIPQPIPTPIQHQQQEQSNLLQPATLNGMNNPWMGMEDHLAMIWAANAMLNPGLDVLSTIAALSKHQQHVQGPSPQQAATAPTTASLSSNLSVSSFTPQMPKEASIAIPAPLQVLNLKDLKPLPPLANIQTSPVIQAANLLLPVAALKKDSSTQTTEEIKVSQCLTSGCGCRVIRICCCDEGVCRRTAAC
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Putative transcription factor. Binds to specific sequence motif 5'-[TC][AGT]TGCC[GA][AT]-3' in regulatory elements of target genes such as myosin myo-2. May modulate gene expression, perhaps acting in opposition to transcription factor pha-4. Involved in morphogenesis, perhaps especially in formation of the pharynx. Plays roles in molting, feeding and morphology.
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A0A6B7FMR5
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VMMP3_VIPAA
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Disintegrin-like/cysteine-rich protein MPIII-3 (D'C protein MPIII-3) (Metalloproteinase-like protein of class P-III MPIII-3) (Snake venom metalloproteinase precursor-derived protein MPIII-3) (SVMP precursor-derived protein MPIII-3) (Snake venom metalloproteinase-like) (SVMP-like) (Vaa-MPIII-3) (VaaMPIII-3)
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MIQVLLVIICLAVFPYQVSSIILESGNINNYEVVYPQKVTALPKGAIQQLEQKYEDAMQYQFKVKGEPVVLHLEKNKDFFPEDYSETHYSPDDREITTNPPVEDHCYYYGHIQNDADSTASISACNGLKGYFTLRGVTYLIEPLKIPESEAHAIYKYENVEKEDEDPKKCEFRRAGTECRPARSECDVAEYCTGQSAECPTDVFHSNGKPCLNNFGYCYNGNCPIMYHQCYALFGPNATVGQDGCFEWNKKGESYFYCRKENDVPIPCAPEDIKCGRLFCELIKNTCKYDYSEDPDYGMVDHGTKCGDGKVCINRHCVDVTTAY
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Abolishes platelet aggregation induced by collagen, ADP (IC(50)=292 nM) and arachidonic-acid. The inhibition of collagen-induced platelet aggregation may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. The inhibition of ADP- or arachidonic-acid-induced platelet aggregation may be due to it acting as an antagonist of the ADP receptors or thromboxane-prostanoid receptors of the platelets, respectively. Does not interact with integrins alpha-IIb (ITGA2B) or beta-3 (ITGB3) nor platelet glycoproteins VI (GP6) or IX (GP9) in vitro, however, the detection is dependent on experimental conditions and may happen in vivo. Able to bind to platelet glycoprotein Ib alpha chain (GP1BA) receptor in vitro, although this interaction may have pathologically only limited effect in vivo as it is not able to abolish the von Willebrand factor (vWF)-dependent platelet agglutination induced by ristocetin. Does not affect blood coagulation.
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A0A6B9HER0
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PIPCL_PIPNI
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Piperic acid--CoA ligase (PipCoA ligase) (EC 6.2.1.-)
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MEKSGYGNDGIYRSLRPPVLFPNDPNLSVTSYLFQRSDAYPDRLALADANSGETLNFAQFKAMVQRVSHGLSRLGIKKGDVVLIFSPNSIYFPVCFLAIVALGAVVTTGNPQYTSAEITKQANDSKPKLVITVPQLWDKVNHLGLPAVFLGSKISGDGTIAPSNRNINGTVTYFSNLVELGGHVSEFPPVSIKRSDIAALLYSSGTSGTSKGVILTHRNLISTACMTTSDQEFDGEDPNVFLCFLPMSHVFGLVIICYSQLMRGNSVVSVEKFDLEMVLRSVGKYRVTYLCVVPPVMIALAKQNWGKIYDLSSLKRIICGSAPLGKEVIEECAKNYPHVPIIQGYGLTESCGIASLEIPEGVREYGSSGILFPAVEAKIVHVENLTPLPPNQLGEIWIRGPNMMQGYLNNPQATKLTIDEQGWVHTGDLGYFNGEGRLSVVDRIKELIKCKGFQVAPAELEGLLLSHQEILDAVVIPYPDAEAGEVPIAYVVRALSSTLDEEAVKKFIAEQVAPFKRLRKVTFVNSVPKSASGKILRRELIAKVRSKI
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Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Acts as a carboxylate--CoA ligase that catalyzes exclusively the formation of piperoyl--CoA from piperic acid and CoA. Can also use the synthetic substrate 5-phenylpentanoic acid to form the corresponding CoA ester.
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A0A6J4B487
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LUC5_FUSSX
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Hybrid PKS-NRPS synthetase LUC5 (EC 2.3.1.-) (EC 6.3.2.-) (Lucilactaene biosynthesis cluster protein 5)
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MGAPNSTREPIAIVGTACRFPGGANTPSKLWDLLCEKRDVQTRIPPERFNPDAFYHRNGEKSGCTDVKKAYLLTEDIRAFDASFFKINPREAEAMDPQQRLLLETVYEATEAAGLPYEDLKGSNTAVYVGSMTGDYHEMLLRDPQDMPKYMATGTARSILSNRVSYFFDWKGPSMTIDTACSSSLVAVHEAVTALRLGVSNIACAAGTNLILGPEMMISESKLHMLSPTGRSKMWDASANGYARGEGTAAIMMKTLSQALSDGDHVYGIIRETGVNSDGHTNGITLPSSESQKTLIRQTYANAGLDLIKERCQFFEAHGTGTPAGDPIEARAIHEAFFEDAAGSSDQMFVGSVKTAIGHLEGCAGLAGLIKALEAVRRGVIPPNQLFENLNPALKPFAGNLSIPTETLPWPEVAPGTPRRASVNSFGFGGTNAHAIIESFDNTPQPAPTGGIISYPLVLSANSEKSLRRQISQLHDTLQNAGEGEVQDTLYTLAQRRSQLPARTYFSGHTQEELLKKLSAASAEDATITVASQEVTNQNSRILGVFTGQGAQWPTMGREILKSSAFAGDLITRLETSLASLQEPPTWTLSEQILADPESSRLGEAAVSQPVCTAVQLMLVELLRQAGITFSTVIGHSSGEIAAAYAAGFLTPEDAIRIAYCRGVCAKLAGGEEGQKGSMMAVGLSYEEAACFCEDHFPGCIDVAASNAPSSATLSGDKDAILEAKALLDEQGTFARVLKVDTAYHSRHMQPCAEPYMALLRESNIQLLPGDDSCEWFSSVIGERMSSFTHGQLLTGEYWVENMVKPVLFTLASELAADSKLPCHVALEVGPHPALKGPFSQTYKRATGSQLPYQGALTRNVHDVEALSDALGFIWARLGKSAVNFASHAELFSVSKTSFSTNLPSYPWDHSQSFWKESRKSANFRQRTSPPHPLLGTRSTEDATQDLRWLNILHLDDAPWLEGHKVEGLVVYPAAAYLVMAMESAKSIDETKTIQLVELFDVQILSAIQLSQDSQGVETLFTLEIDDVNSTAATARWSLFTSMVGRGSNWKCNAKGHLRVDFGSEAQDSLLPSRDPPVASLTSVNIERFYTSLAEIGLGYTGAFKHLATVQRQSGFATAKASQMNTDFSAMIHPALLDSAFQSLFAAYCWPDDGSLAAPFVPTFFKSLRIVSLDHIENGQELTIDSYLTDTNDREITADLDIFTSDSEKPLLQLQGLTCTSLLRPGPSNAKELYTQTKWEVDISCAVASLDVQQHDAAEDLDLVDLCERLSYYYLRELNRKVDRSEVPAMDWHFQRIFEWIDYLFPIIEAGKHTTIRKEWSADEGSWLLEQASKFPGQVDLLLIRAVGENLTEVVRKETTMLEHMVRNDVLNRFYKFGLGFQRANGYLSRISKQIAHRYPQMKILEIGAGTGGATKGILESLGTTFESYTFTDISTGFFEAAAEAFEPWVSKIIFKPLNVENDPVEQGFLEAQYDFIVASNVLHATKSLSTTMRNVRRLLKPGGQLLLLEVTSDIVRVRLMMSGLSGWWLGGDDGRRYAPTITVPEWDSLLRSTGFSGVDHTVNDFYDPSKYMTSVMLSQAVDDHHVDILRKPLNSALGWLPQRCITIIGGKNNEIAQQVSKTLLSMKSASLDLINHVDSFEQLASTPELPLRAVLILEDLDEPVLKSLTSEKLAGLQRTINDSRQILWVSKGCQKDEPYANMSTGLCRSLASEYPHIQLQHIDMETGLDSLAVSRIVEALIRIVYKASLKQDDDLLWSHEAELILEDEGRWLIPRILPDDKLNDHLNAGKMKVKTNASLADTPVEIQQAGSQWVISQTVPSLPISDNTDHIRIKASYSTLHAVRVRGSRVYLSYGHRVTGSTTPVIAFSETAGSIISVPESQVFDVPQGFDIDQSASLRSLVLTAIVESVLAECDHGAAIIVHEADNYLGAAFETKCREIGLKLVRTTSKSDHKDDAIFIHPLAPERVVKKALPHVEVAVVVDLSGRDYSVVDSPLRRHVPSTTKFLELSDLIGSVTCGLRDVNIQCVQDAIESSFKSPSDGPVVNISEVSGLQASETSYATVVDWSIEKPVSVQVQPLQANRLLRSDRTYLLAGCTGGLGKALCRWMVAAGVRHLALTTRNVEAIDKVWLEGLQLQGADVRLFQVDVGDKAALERAHAQVTAEMPPICGVANAAMVLSDRSFGELKVGDFDKVFGPKVRGTQNLHELFQDEPLDFFIMFSSLASVVGNRGQANYAAANLFMTAVAEQRRAKNLAASVIHIGMILGVGYVSSTGAYEATLRQYNYMPISEPDFLNMFSEAILVGQPGSSHAPELITGLNRYSLQEDAPKFFWHENMRFSHHTLEEQHQESTSTTKASISQRLAQVQTPAEMLEVVEEEFCTKLERMLQAESGTIKVSQPLMSLGVDSLIAAEIRSWFFKELDVDMPVLEILNTASVAEICSTAVASLATLAPQEQTETTTLVTSEAVQSLNAVSGNGSSSSRAPTEFNSSTLKSGAQSTQGTSVSGDKDTNSVDGSAKVERNGPLSFAQERIWFLQQYLQDATTFNVTMAYRITGPLRVNDLESAFQKVIQRHESLRTGFHMDPETTVPTQIVYEQSPFGLEQRNDSDITKEFEELQNTHYDLENGRVLKAIVLTKPDTDEHILLVGFHHIALDGFSAQILVRDLAIAYAGGNLAPLDKGYLDFAVDQRAAVYPAETLQYWKTEFETLPPALPVFDFAETKTRLPLTDYKTRVSERTLQPDVAGKAKSAARALAATPFHVYLAALQVLLSDFASTQDVCIGITDANKNDAAHMDTIGFFVNLLPLRFQLSASQTLAELVSNTKAKANGALTHSRLPFDVLLDELKIPRSTSHSPLFQVVLNFKMGSTQKVPLADCQAEVIDFKDVNNPYDLAFDIETYPDGSTSISVKSQEYLYTKNELDLILESYINLLSLFEKDSSKTLGEVSQCTPDEAQKTLTLGRGERIPSPSFDTLSHYFEDWVKRQPDAIAIRDDQGTTLSYSQLKSFVNNIAATLEKSGLTPGARVGVYCEPSIFIIASLLAIAEVGGVYVPLDPQNPIKRLQLIVDDCEPEILLFDESTKELAPKLQTNASLINIYNVRRLPSSAAITNRAQGAGMAYMFYTSGTTGVPKGVALTHANLVHHIDSITHFYDIKRGTMLQQAPLGFDMSLTQMSLSTMLGGTLVVASSEARKDPLQLAKLMLSERVTHTFMTPTLAVALIHHGYEYLVKCVGWEFSLLSGEAFRTHVISEFQRLGLPQLKLFNGYGPTEITINSSSGLNELDLAAPRDTRNPTIGFTLPNYSCYILDEDLKPVRPGHAGELFVGGAGIAVGYLRRDELNKERFLSDPFASSEDVARGWARMYRTGDKAKFLPDGRIVFLGRIAGDSQIKLRGFRIELEDIANTIVKSSGGVVSEAAVSFRQGVNGPDDGAFLVAFAIISQAHRPENPSSFLKQLLKDLSLPRYMIPAKIVQVEHLPMGPTGKLDQNALDVMPIPQDENVHEETLTTTQERLRALWFESLPAVAPDAFIGSETDFFEAGGNSLRIVMLREHIAREFGVMVSVFDLFQASTLGGMAAKIDGSTGADNQPIIWEEETRVDIPSGLETPDEPAILDGDELEVALTGATGFLGLAILRSLLKDERISRVHCLAVRSPSKARDEVFKSPRVVVYHGDLSSPRLGLSEDEFGTLSKKFDIIIHNGAEVSFLKSYQALKKANVSSTKELAQLASGRQIPFHFVSTGGVVNLTDHDGLPEISVSGFKPPIDGTEGYAASKWASEVILESHAERAHLPVWIHRPANVTGAAAPATDLMGSILQYSTTMQSLPEISNWKGSFDFVPVEQVADEIAASIHESRSSEPVYRHHCGDQKISVSELSAHLEAGIGAKMEIIGVDDWLARARSTGIDETTALLVEKMLSGENGGTVPWLRKGE
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of the mycotoxin lucilactaene and the lucilactaene-related compound NG-391 that act as cell cycle inhibitors with potent growth inhibitory activity against malarial parasites, moderate growth inhibitory activity against cancer cells, and no activity against bacteria and fungi. The hybrid PKS-NRPS synthetase LUC5 is responsible for the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate prelucilactaene B, as an alcohol with an open ring structure. Lucilactaene and NG-391 lack the 7-methyl group present in fusarins which is inserted in fusarins by the C-methyltransferase (CMeT) domain of the fusarin synthetase FUS1, suggesting that the CMet domain of LUC5 does not methylate this position. Within the pathway, both the cytochrome P450 monooxygenase LUC2 and the hydrolase LUC6 function in parallel in modification of prelucilactaene B. LUC6 may catalyze the 2-pyrrolidone ring formation to form prelucilactaene C from prelucilactaene B, followed by C-15 hydroxylation by the same enzyme to give prelucilactaene D, which is then converted to prelucilactaene E by epoxidation, and finally to prelucilactaene F by cyclization. Prelucilactane D, prelucilactaene E, and prelucilactaene F can be converted to dihydrolucilactaene, NG391, and lucilactaene, respectively, via C-20 methyl group hydroxylation by the cytochrome P450 monooxygenase LUC2. However, LUC2, unlike FUS8 in fusarin C biosynthesis, is not enough for the full oxidation of the C-20 methyl group into carboxylic acid, which is a prerequisite for the final methylation step. The aldehyde dehydrogenase LUC3 is involved in the biosynthesis by further oxidation of the C-20 alcoholic analog prelucilactaene G into a carboxylic derivative. This unidentified carboxylic derivative may be converted to demethyllucilactaene. As the last step, the methyltransferase LUC1 methylates the hydroxyl group at C-21 of demethyllucilactaene to generate lucilactaene (Probable).
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A0A6M7H989
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DLMIS_ECO57
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D-lyxose/D-mannose isomerase (EC 5.3.1.15) (EC 5.3.1.7)
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MKRSAINDILGHTRQFFSQHDVHLPPFASFSPAQWQQLDTAAWEEVFDLKLGWDVTAFGRNNFAAHGLTLFTLRNGSAKGMPYVKCYAEKIMHVRDAQVTPMHFHWRKREDIINRGGGNLIVELWNADSNEQTADSDITVVIDGCRQKHTAGSQLRLSPGESICLPPGLYHSFWAEAGFGDVLVGEVSSVNDDDHDNHFLQPLDRYNLIDEDEPAQLVLCNEYRQFR
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Sugar isomerase that catalyzes the reversible isomerization of D-lyxose to D-xylulose, and D-mannose to D-fructose. Shows similar activity toward D-lyxose and D-mannose with a turnover and catalytic efficiency for D-lyxose as a substrate only 1.1- and 1.3-fold higher than those for D-mannose, respectively. Shows weaker activity with L-gulose, D-talose, L-ribose and L-allose. Overexpression enables cell growth on the rare pentose D-lyxose as the sole carbon source.
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A0A6P3CW73
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CYCTI_TITOB
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Cyclotide trypsin inhibitor TopI1
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MKFIIVLLLLTALTLTSIPVIEGILKRCKTYDDCKDVCKARKGKCEFGICKCMIKSGK
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First cyclic scorpion trypsin inhibitor (Kd~0.5 nM). Does not inhibit chymotrypsin.
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A0A6P3HVI0
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SL9B2_BISBI
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Sodium/hydrogen exchanger 9B2 (Na(+)/H(+) exchanger NHA2) (Na(+)/H(+) exchanger-like domain-containing protein 2) (NHE domain-containing protein 2) (Sodium/hydrogen exchanger-like domain-containing protein 2) (Solute carrier family 9 subfamily B member 2)
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MRNQDKRAAHKDSEPSTEVNHTASSYQGRQQETGMNLRGIDGNEPTEGSNLLNNNEKMQGTPAEPNHLQRRRQIHACPPRGLLARVITNVTMVILLWAVVWSVTGSECLPGGNLFGIIMLFYCAIIGGKLFGLIKLPTLPPLPPLLGMLLAGFLIRNVPVISDNIQIKHKWSSALRSIALSVILVRAGLGLDSNALKKLKGVCVRLSLGPCLIEACTSAVLAYFLMGLPWQWGFMLGFVLGAVSPAVVVPSMLLLQEGGYGVEKGIPTLLMAAGSFDDILAITGFNTCLGMAFSTGSTVFNVLKGVLEVIIGVVTGLVLGFFIQYFPSSDQDNLVWKRAFLVLGLSVLAVFSSTYFGFPGSGGLCTLVTAFLAGRGWASTKTDVEKVIAVAWDIFQPLLFGLIGAEVLITALRPETIGLCVATLGIAVLIRILVTYLMVCFAGFNIKEKIFISFAWLPKATVQAAIGSVALDTARSHGEKQLEGYGMDVLTVAFLSIIITAPVGSLLIGLLGPRLLQKAEQNKDEEDQGETSIQV
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Electroneutral Na(+) Li(+)/H(+) antiporter that extrudes Na(+) or Li(+) in exchange for external protons across the membrane. Uses the proton gradient/membrane potential to extrude sodium (By similarity). Contributes to the regulation of intracellular pH and sodium homeostasis (By similarity). Also able to mediate Na(+)/Li(+) antiporter activity in kidney (By similarity). May play a physiological role in renal tubular function and blood pressure homeostasis (By similarity). Plays an important role for insulin secretion and clathrin-mediated endocytosis in beta-cells. Involved in sperm motility and fertility. It is controversial whether SLC9B2 plays a role in osteoclast differentiation or not (By similarity).
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A0A6P6W6H5
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TPS1_COFAR
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Limonene synthase, chloroplastic (EC 4.2.3.-) (Alpha-pinene synthase, chloroplastic) (EC 4.2.3.-) (Beta-farnesene synthase, chloroplastic) (EC 4.2.3.47) (Beta-myrcene synthase, chloroplastic) (EC 4.2.3.15) (Beta-pinene synthase, chloroplastic) (EC 4.2.3.-) (Sabinene synthase, chloroplastic) (EC 4.2.3.-) (Terpinolene synthase, chloroplastic) (EC 4.2.3.113)
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MAIINLPVPTNSSSEVNKHNHLRSCLPSGRATFTTLSAAAMRSATMAAANVREQSGQKQQLINRRSGNYEAPLWEFDYIQSLKNEYAGDIYVSRANELKEQVKMMLDEEDMKLLDCMELVDGLERLGLAYHFEGRINRLLSSDYKAIHEGNHQRNKEDLYAAALEFRIFRQNGFNVPQDIFNDFITEDGEFDESLSEDTMGLLSLYEASFLSLEGEATLDLAREFTTKHLNNYLGKENTDQNLRILVYHALELPLRWRAPRIEARWYIDAYERSPNVNPTLLELAKIDFNIVQAIHQQDLKHVSWWWKNIRIAEKLTFIRDRIVENFFWAIGAVFEPQYGSCRRMLTKVFALITMIDDIYDVYGTLEELELFTDAVDRWDVKAIDQLPDYMRVGYLGFFNSINEMAYDALKEQGVHIVEYLRKVWADLCKAYLQEAKWYYAGYTPTVEEYLENAWVSMSVPVMLMHAYAGVTNPMNKEAMDVLDTHDIVRCSSYLLRFADDLGTSPGEMKRGDVPKLVQCYMKEAGCSEEESREHVWFLLRETWKKMNKDSEWAESPFSKTFVTAAKNFGRVALVMYQYGDGHGLHSNPEAKDRILASLFSPVPPA
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Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products, constituent of coffee beverage aroma. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into limonene, beta-pinene, sabinene and beta-myrcene, and, as minor products, alpha-pinene and alpha-terpinolene. Can also, with a low efficiency, use farnesyl pyrophosphate (FPP) as substrate to produce beta-farnesene. Not able to use geranylgeranyl pyrophosphate (GGPP) as substrate.
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A0A7J6K7I9
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WNG2_TOXGO
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Serine/threonine-protein kinase WNG2 (EC 2.7.11.1) (Rhoptry kinase family protein ROP34) (With-No-Gly-loop kinase 2)
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MMFPAVAAPPRRLPGERLQRSQNPVETSWLSFRILATRGPCVTSTFLFLTVAFLGLSWVSVAVAAHAEHPEDSATNFLFSFAENSLANREPPEDSAARPSSRSGGAERRRLDSLIPGFLKRRRIFKQLRPVDEFQLREFQEASSKVKAQFFSAGHSKVTFVDRPSAALLSFLHLEEEDVPYGVVIKAIPYDAFDFYESVAEPYIHRMFDDPRKFPYVVPVLAALRSTSKRVLYLVLPLYRELPETVDEEARSLDFVLLLAEMAMAVCQLHERNLAHRDLKEDNFLVSPEGHIVVSDLATLDITDNKSFLIGTSGYMPPETRSSYLLRKGYKRSRYGEKTDVYSLGVAFRHLAFMLEGLGVQVPHRTQLAKLIKKMTSPDPEKRPLIGEVMEDPFFASVDFRLVRQRAGKHPFKKLPGADLLAERQRARLEAREKADAAAKAADNAEVPAAKSPAGKTGGAGTLSGDRDRAGSGEKPAERAEEEKGRGRGAQTHEGNHDRTDDAGREELREGPGDQKPSGEENREGGQPPGQREEQREGTGLEEGFNKEDAQES
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Probable serine/threonine-protein kinase.
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A0A7J6K7Y0
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WNG1_TOXGO
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Serine/threonine-protein kinase WNG1 (EC 2.7.11.1) (Rhoptry kinase family protein ROP35) (With-No-Gly-loop kinase 1)
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MPEQDLASGFLLRFQNARPVCLSVGSFVSFRTVQPRKMRDRGWRCVWHRMAGVGALFGIFGVLCTVEAGATVAAPQVETGPLLSVRAPRSPLHLRDVDAPEVTHASSEGSPQFESSLSQQRLRRPADRGEAHNGEEPRKDAATQTVRGYGGQSTEPPPASIVPVSSEAPQDGAEQRQASSAAESLAGLDPDAGDTGLRSQEMDEEGSGAAQDMERAHAAQPTVSTWDDAHLVQVSTSHPDMFPVDGSFSKKQEGRRERRLAVRGDDSFARGHNRDRDASNGRSILRRAPGWAKIAALATGLLVSAFGYSSYKHGGPRVALRIHKLHLKRKLPISWRRYLNNLPVLDERLFPEFEDILPWLRRGARLVKRVPHVSEALADFIGLDEETRRTGIVIKVKSSTDAEARRLVYEVNAHANMVPDNPFFLPIIGAYQGASKRAVYMILPRARADVADYVRARPYDVDVRLAAAEMVYSNYILHTHGFLHRDIKAHNYFVTFDGHVVLADFEGVGVLQQRTPVVGTRGYFAPELSRATDHTEKSDVFALGQTLKRLVKYMRPTVRVPHLRELWALTKRMTAKDPEERPTLKQVMEDPYFDGIDFERLEAKDQGVPFRGDFSIDDPDAGGKMYIPPSKEQDHEQENE
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Serine/threonine-protein kinase which, at the tachyzoite stage, phosphorylates several parasitophorous vacuole (PV)-resident proteins such as GRA2, GRA6 and GRA7. By phosphorylating GRA2 and GRA6, regulates the formation of a functional intravacuolar network (IVN) IVN is composed of membranous tubules that bud from the PV membrane into the vacuolar lumen. Plays a role in the establishement of chronic infection in the host by controlling cyst formation in the host tissues.
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A0A7L8UVC9
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FFSA_ASPFV
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Polyketide synthase-nonribosomal peptide synthetase ffsA (PKS-NRPS ffsA) (EC 2.3.1.-) (EC 6.3.2.-) (Cytochalasans biosynthesis cluster protein ffsA)
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MATTTAPTTQGHNQPSREPIAIVGSACRFPGGASSPSKLWKLLEHPRDVLKEIPPDRFSVDGFYHPDNMHHGTSNVRHSYILDDDIRVFDAQFFGIKPVEANSIDPQQRLLMETVYEGIESAGLQLNKMKGSQTGVYVGLMSNDYADMLGNDQESFPTYFATGTARSIVSNRVSYFFDWHGPSMTIDTACSSSLVAMHQAVQYLRSGDGSDVAIAAGTNILLNPDQYIAESKLKMLSPDGRSQMWDEKANGYARGDGIAVVVLKTLSQALRDGDHIECIVRETHINQDGKTKGITMPSATAQTALIRSTYKNAGLDITKPSDRPQFFEAHGTGTPAGDPIEAEAIHTAFFGYKGLSKEIEPLSVGSIKTIIGHTEGTAGLAAVLKASLALQAGVIPPNLLFDKVNPKVKPFYGNLQIQTQAKSWPSLAPGAVRRASVNSFGFGGANAHAILEAYEPSSTPTVGTPANVFTALNVSAMSETALRGTLKKYVEYLKEEPSVDLRSLALTVNTRRSTFPVRTSVFGTSVEELSQRLSERSEAEGKTLTPVAPTSLSSSPKILGVFTGQGAQWKQMGAVLLATSPRVVAILDQLEKSLAELPDGPSWSIKGEILADEDSRVNEAVISQPLCTAVQIVLVDLLQSAGVQFHTVVGHSSGEIGAAYAAGYLSASDAIRIAYYRGLHLYLAQGPNGQQGAMMAVGTSFEDAQELCDLPAFRGRISIAASNSSASVTLSGDLNAIEWAKDVFDDEKKFARLLKVDKAYHSHHMLACSDAYRKSMTDCGITVLQPARNGTTWISSVYGEDALDYRHEMNAEYWISNMVSPVLFSQAIEFAMADQGPFDIGIECGPHPALKGPALQVIQEMLGSSIPYTGLLSRGRPDTQALAEGISYLWQALGADVVNYTSFDRFIAGPDASEPQVLANLPSYAWDHDRAFWHESRQYWANRTKEDPPHEILGTKCPDGTDQQHRWRNMLRPREIPWIAGHQIQEQMVFPAAGYVSAAIEAVQMVTRGQSLGAIEIEDFVIGQAIAFNDEYASVETQFTLTDISVEKDIWSASFFFYSASPKSSRSLDLNASGKLKVTLGEPKDDFLPPHLSPEFNMIDVDSERFYDALKKLGFGYTGPFKALGSLKRRMGVATGTITNPTSTDPAHDLLLHPATFDNAIQSIILAYCYPNDGRLWSVQLPTGIKKIKINPVLCNRYAGKKALLCFKASTSDDRSAEIGGDVDIYDEQGNNALMQLEGLQTKPLANATAANDSPLFLETIWDIESPSREAAVADRPDMQPKTELSFDVERVAFFYLRHLDSVATREEREKAESHHKIFFEYIDHTVANVKSGTAQFAKREWMYDTHDEILDIISKYPDSLDMKLMHAVGEHLLPVIRGETTMLEYMREDNLLNDFYVHAIGFDEYTENLAQQVSQFSHRYPHMNILEIGAGTGGATKRIFSKLGKRFGSYTYTDISAGFFEKTRETFREYEHMMTFKALNIEKDPVEQGFTEQSYDLVVASLVLHATHEMETTMRNVRRLLKPGGYLIMLELGDYIEMRTGLIFGSLPGWWMGYDDGRKLSPCMSEEDWSVCMQKTGFSGVDAIVPRQSELPISLAVLTGQAVDDHVNFLRDPLTPGSIDFVESNLTIIGGTTSKVSAMVEEAAKSLGRFYEKIVTATSLAELDTTEVPFMGSVLFLTDLDEPIFENVTEDALTALKQLFKQSRTCLWVTQGARDDNPFQNMSVGLGRVVKLEMTHLRLQSLDFDVETEPSAPTIMQRLLQFEAMAQWEQSGESKDLLWSVEPEIGYDHGKAIIPRLMPNPVRNARYNSSRRLITKYMEPTSANLSLRWSGKSYDIHEGEPSGATSLVMDGRVQLEVSHSTLDAIGVTATDYAYLVLGKNVKSQQQVIALTPKSDSIVRVFDSWTVPYSMAEDDALRLLPVVYTNLMALSVISRLSSGETLVLVEPEEAFAQTLSRLATERAISVVTLTSRMDVKNSDWIYLHVNSPKRLVRSTVPRNASWVIADRDQGGLAANVLQCLPANCKILATESLTSKQPKLDTFSSMAFIPSILRTAFVRAHDIKATLELPSVVAAADISSDNQPSTEATFFSWTASPSVPVQVTPVDHGTLFSSEKTYWLVGLSGGLGLSLCDWMVKHGAKYIVITSRNPQVDARWEQHMKAQGAVVRVYANDITDRESVSSVCKKIRDELPPVGGIAQGAMVLADTMFVDMDLPRVQKVVGPKVNGSIHLHEMFVEVDLEFFVFFSSMAYVTGNQGQSIYAAANAYMTALAAQRRKRGLAGSAINIGTIIGNGYVTRQLTIAQQEYLTHMGNVFMSEQDFHQIFAEAVVAGRPTSKDIPEIMTGLRLAHLDDSDKVTWFHNPKFSHCVLWPEEQGGKAVMSKQNVTVRAQLLLATTADEAREIIEESLAAKLRSSLQIDATVSVINMNADQLGLDSLVAVDIRSWFIKELNVEMPVLKILGGYTVAEMVAAAQEKLSPSLIPNLGKEVDPSLKAVVKAQVEKPVAAAEEKPIVTEKAEYADFDDENEEEGIPTEDSLPEITVSDESSELSDREPAKFNFNGPGFKKVGFSPGPQTPLSEDDRSKWSSYGSPFDSDSDNASIRKSRTSAATSVTALDEYFSKPDHTIFERTLPMSFGQTRFWFLKFYMEDQTTFNITTSISLAGKLDVGRFSRAVHHLGRRHEALRTAFFTDSNNQPMQAVLKEPVLRLEHARGEANVASEYRRIKNHQYDIGRGETMKITLLSLSEKLHQLIIGYHHINMDGISLEVIIRDLQQLYDGKSLAPVSIQYPDFSIMQYKEHSSGQWDDELTFWKSEFADIPEPLPILPPSTKAVRTPLSIYSSNTVKFEVGAELSSQIENACKRTKTSPFNFYLATFKVLLYRLAEGKATDICIGMADGGRNNDLVSQSVGFFLNLLPLRFKQQSSQMFSDALKEARSKVITALANSKVPFDVLLNEVNAPRTATLSPLFQAFINYRQGVQEKRQFCGCESEATKFDGSQTAYDLSLDILGNPGSGIVYLAGQSSLYSQSDVETIAQSYYALLKAFAKNPALRISRPSLYDPQAVDHALAKGKGPTNVGTWPETLVHRVDEIVKAHGSKVALKSATAKLTYTQMAERVNAIASTLQSNGINKCSRVGVFQDPSTDFFCTILAVLRIGAVFVPLEPRLTAPRLATMVQDSDLNAIVYDKANQKTLAELGSNSKKINVSLVLAKSSAVVSNQATPGATAIILYTSGSTGKPKGILLSHSAWRNQIESSSRAWEVPTGTGVHLQQSSWSFDISISQTFVALANGASLIITPKTMRGDSSAITKTIVSDQVTHVQATPSELSSWLRFGDLAALRASKWQFAMTGGERMTPALIDGFRKLAKNDLKLFNAYGPAETTLAVGSSEVDYMTSDDLDTPFTLFPNYSVYILDGQKQPVPAGIPGEVYIGGAGVAQGYLNQDSLTAKRFLPDTFGTTEYTHFGWTKMHRSGDRGHLSEDGHLVLEGRIDGDTQVKLRGIRIDLQDIESAMVQQANGALTEAVVSVCKLQETEYLVAHVVISPTFTGNTESFLDQLRASLPVPQYMQPAIAVTLDALPVNHSGKVDRKAIAALPILPKATQPGATSQPRDSTEKLKDIWTQVLGQGMTSLHHIDAQSDFFHVGGSSLALVEVQAKIKTIFQVEVSLVQLFENPTLGAMARMVDPTAFSAPVNANLTIPAEVATAISAPTTSINTAPKEIDWEEETALTDDFYDIEIDPTPKDQGLPYKTVVITGATGFLGKALLRRMLDDNHIDKIHAITLRRSRSDLPGIFSDPKVHLHRGDLNAPRLGLSETAAAEIFAETDAVIHNGADVSFMKTYRTLSKTNVGSTRELVKLCLPHRIPIHYISSASVVHLSGLESYGEASVSSFEPPQDGTDGYTASKWASERFLERVSEKFSVPIWIHRPSSITGEDAPTLDLMTNMLSFSKKLRKAPTSPAWQGTLDFVDVEKVATEIVEEVKNDSAHPGGLVKYMYESGDLEIAVDDMKGSLERETGQAFQTLSLEEWTKAAAEEVTNELGICCSK
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of the cytotoxic leucine-containing cytochalasans, including aspochalasin C, aspochalasin E, TMC-169, flavichalasine F, aspergillin PZ, aspochalasin M and flavichalasine G. The first step in the pathway is catalyzed by the hybrid PKS-NRPS ffsA that utilizes 8 units of malonyl-CoA to iteratively assemble the octaketide chain before addition of L-leucine by the C-terminal NRPS modules. Because ffsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase fssC (Probable). The methyltransferase (MT) domain of ffsA catalyzes the alpha-methylation at C10 and C14 using S-adenosyl-L-methionine as the methyl-donating cosubstrate (Probable). Reduction by the hydrolyase ffsE, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ffsF then yield the required isoindolone-fused macrocycle (By similarity). A number of oxidative steps catalyzed by the tailoring cytochrome P450 monooxygenase ffsD, the FAD-linked oxidoreductase ffsJ and the short-chain dehydrogenase/reductase ffsI, are further required to afford the final products (Probable).
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A0A7T9QPQ1
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C719A_PIPNI
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Piperic acid synthase CYP719A37 (EC 1.14.19.-) (Cytochrome P450 719A37) (PnCYP719) (NADPH--cytochrome P450 reductase) (CPR) (P450R) (EC 1.6.2.4)
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MESGSSIDLSPLDLVAAILQGKADASSLLSLTRSTVSDGNGDLLVLLATSAALLVGLVAALVWRRSAAARTAEPPKPLLAKKEAEPEVDDGKRKVTVFFGTQTGTAEGFAKAFAEEAKARYEKAAFRILDLDDYAADDDEYEEKMKEETLAFFFLATYGDGEPTDNAARFYKWFAEGKDTGNFFEKMQYGVFGLGNRQYEHFNKIAKVVDELLAEQGAKRLVPLGLGDDDQCIEDDFTAWRELIWPELDQLLRNEDDVSGASATYTAAIPEYRVVFYDHEDSRIQEKKNANGYANGHASYDIQHPCLANVAVRRELHTPASDRSCTHLEFDVSGLGLHYETGDHVGVYAENCIETVEKAECLLGLSPATIFSLHTDQVDGTPLSGSFLPPPFPSPCSLRTALAKYADLLSSPKKAALVALASYASEPSEAKRLQFLASPSGKDEYSQWIVANQRSLLEVMAEFPSAKPPLGVFFGAIAPRLQPRYYSISSSPKVAPTRIHVTCALVYEPTPTGRIHKGVCSTWMKNAVPQEESSNCSSAPISVRQSNFKLPMDTSLPVIMIGPGTGLAPFRGFLQERLALKDAGFNLGPAVLFFGCRNRKMDFIYENELNEFVEAGVLSDLIVAFSREGPTKEYVQHKMAEKAVDIWNMISQGGYVYVCGDAKGMARDVHRALHTIVQEQGSMDSSKVESYVKNLQMEGRYLRDVW
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Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Catalyzes the conversion of feruperic acid (5-(4-hydroxy-3-methoxyphenyl)-2,4-pentadienoic acid) to piperic acid. Inactive toward ferulic acid and feruperine.
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A0A7U9P668
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CDAS_GEOTM
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Cyclomaltodextrinase (CDase) (EC 3.2.1.54) (Cyclomaltodextrin hydrolase, decycling)
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MRKEAIHHRSTDNFAYAYDSETLHLRLQTKKNDVDHVELLFGDPYEWHDGAWQFQTMPMRKTGSDGLFDYWLAEVKPPYRRLRYGFVLRAGGEKLVYTEKGFYHEAPSDDTAYYFCFPFLHRVDLFQAPDWVKDTVWYQIFPERFANGNPAISPKGARPWGSEDPTPTSFFGGDLQGIIDHLDYLADLGITGIYLTPIFRAPSNHKYDTADYFEIDPHFGDKETLKTLVKRCHEKGIRVMLDAVFNHCGYEFGPFQDVLKNGAASRYKDWFHIREFPLQTEPRPNYDTFAFVPQMPKLNTAHPEVKRYLLDVATYWIREFDIDGWRLDVANEIDHQFWREFRQAVKALKPDVYILGEIWHDAMPWLRGDQFDAVMNYPLADAALRFFAKEDMSASEFADRLMHVLHSYPKQVNEAAFNLLGSHDTPRLLTVCGGDVRKVKLLFLFQLTFTGSPCIYYGDEIGMTGGNDPECRKCMVWDPEKQNKELYEHVKQLIALRKQYRALRRGDVAFLAADDEVNHLVYAKTDGNETVMIIINRSNEAAEIPMPIDARGKWLVNLLTGERFAAEAETLCVSLPPYGFVLYAVESW
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Hydrolyzes alpha-, beta- and gamma-cyclodextrins with the highest activity with alpha-cyclodextrin (cyclomaltohexaose). Pullulan is the preferred substrate from linear substrates. Maltose is a major product of these reactions. Is also able to hydrolyze maltotriose and acarbose, and transglycosylate their hydrolytic products. Major reaction products of maltotriose and of acarbose are maltose and glucose, and glucose and pseudotrisaccharide, respectively. No activity with glucose or maltose as substrate.
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A0A858E6N7
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GGDPS_MELLI
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Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
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MKPLPSTNGKVNGNGKHHDSSLSSTSSTSSSSSSDTQFNISDRYGDFLHRLDTLDTWPKSNEQILLEPYTYLNNIPGKEIRSMMIDAFNHWLQIPRPALEIIKKIVGQLHTASLLMDDVEDDSDLRRGVPVTHKIYGIPQTINTANYVYFLAYQELSKLKPCLSSNASTDLWSLVNDELLQLHRGQGMDLYWRDSLTCPTEEEYLQMVNNKTGGLFRIAIKLMIALSPLTETPDYLPLVNLVGIIFQIRDDLLNLSSVYTKNKGFCEDLTEGKFSFPIVHSIRADSSNHQLMNILRQKPTDIGTKTFAVSYMKDQTKSLQYTREVLTCLEEQAIEEVTRLGGNPALESIFELMHVLPSPPATDQH
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Geranylgeranyl pyrophosphate synthase that catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Does not show any monoterpene nor sesquiterpene synthase activity.
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A0A8B7DWS6
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ACTL1_HYDVU
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Hydra actinoporin-like toxin 1 (HALT-1) (Alpha-pore-forming toxin) (alpha-PFT) (DELTA-hydritoxin-Hma1a) (DELTA-HYTX-Hma1a)
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MLLYICLVNLLLPLSVGAASGAALGVIAKVGVDAALQQIDDVWKGKTVRYWKCAVENRSSKTLYALGTTQESGSMTTVFADIPPKSTGVFVWEKSRGAAKGAVGVVHYKYGNKVLNIMASIPYDWNLYKAWANVHLSDHKESFSDLYKGKNGAKYPTRAGNWGEVDGTKFFLTEKSHAEFKVIFSG
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Pore-forming protein that forms hydrophilic pores and causes cytolysis. Compared to equinatoxin-2 (AC P61914), it reveals lower cytolysis activity (5-12-fold difference, tested on erythrocytes), a larger pore size (probably 2-3 nm) and different affinity to membrane lipids (100-fold lower affinity to sphingomyelin). Binds to sulfatides (SFT) as well as to the two sphingolipids, lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). It seems to bind more strongly to LPA than to S1P and SFT. Shows cytolytic activity on HeLa cells, with a different potency than its paralogs (from most potent to less potent: HALT-4>HALT-6~HALT-1>HALT-3>HALT-7>HALT-2). Pore formation is a multi-step process that involves specific recognition of membrane lipid by a protein aromatic residues rich region, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers (By similarity). In vitro, binds to the folate receptor alpha (FOLR1), a GPI-anchored membrane protein that plays a major role in the uptake of folate/folic acid into cells via endocytosis, suggesting a possible involvement of this receptor in the mechanism of HALT-1-induced cell lysis. In vivo, does not cause visible paralysis in larvae of the blowfly Sarcophaga faculata, the most common arthropod prey of Hydra.
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A0A8I3NFE2
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SHIP2_CANLF
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Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
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MASACGAPGPGGAGPGGALGSPAPAWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEREREPDPPDDRDVSDGEDEKPPLPPRSGSTSISAPVGPGSPPAAPETPTTPAAESAPNGLSTVSHEYLKGSYGLDLEAVRGGASNLPHLTRTLATSCRRLHSEVDKVLAGLEILSKVFDQQSSPMVTRLLQQQNPAQTGEQELESLVLKLSVLKDFLSGIQKKALKVLQDMSSTAPPAPPQPAIRKAKTVPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFTHDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDEPDMISVFIGSWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDREWLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLSAFDISLRFTHLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPTYRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSPVFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKSFENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVALKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKSKAPSVSRGSQDPRSGNRKPAPAEASCPLSKLFEEPEKPPPTGRPPAPPRAASREEPLTPRLKAEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPPATKNKVAITVPAPQLGRHRPPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGRSGGEARGPPPPKAHPRPPLPPGPSPTSTFLGEVASGDDRSCSVLQMAKTLSEVDYAPAGPGRSVLLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCPQGGRAGGLGEAGMGAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
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Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (By similarity). Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear (By similarity). While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking (By similarity). Confers resistance to dietary obesity (By similarity). May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling (By similarity). Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation (By similarity). Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading (By similarity). Required for HGF-mediated lamellipodium formation, cell scattering and spreading (By similarity). Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation (By similarity). Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth (By similarity). Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A) (By similarity). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems (By similarity). Involved in EGF signaling pathway (By similarity). Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3 (By similarity). Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity (By similarity). Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1 (By similarity). In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling (By similarity). Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly. Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2. Promotes formation of apical membrane-initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity).
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A0A8I3NQW8
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ASTER_CANLF
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PAT complex subunit Asterix (Protein WDR83OS homolog)
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MSTNNMSDPRRPNKVLRYKPPPSECNPALDDPTPDYMNLLGMIFSMCGLMLKLKWCAWVAVYCSFISFANSRSSEDTKQMMSSFMLSISAVVMSYLQNPQPMTPPW
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Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. Within the MPT complex, the PAT subcomplex sequesters any highly polar regions in the transmembrane domains away from the non-polar membrane environment until they can be buried in the interior of the fully assembled protein. Within the PAT subcomplex, WDR83OS/Asterix binds to and redirects the substrate to a location behind the SEC61 complex.
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A0A8I3P7X4
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CCD47_CANLF
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PAT complex subunit CCDC47 (Coiled-coil domain-containing protein 47)
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MKASLAFCVVLLVFGSVSEAKFDDFEDEEDIVEYDDNDFAEFEDVTEDSVTESPQRVITTEDDEDETTVELEGQDENQEGDFEDADTQEGDTESEPYDDEEFEGYEDKPDTSSSKNKDPITIVDVPAHLQNSWESYYLEILMVTGLLAYIMNYIIGKNKNSRLAQAWFNTHRELLESNFTLVGDDGTNKEATSTGKLNQENEHIYNLWCSGRVCCEGMLIQLRFLKRQDLLNVLARMMRPVSDQVQIKVTMNDEDMDTYVFAVGTRKALVRLQKEMQDLSEFCSDKPKSGAKYGLPDSLAILSEMGEVTEGMMDTKMVHFLTHYADKIESVHFSDQFSGPKIMQEEGQPLKLPDTKRTLLFTFNVPGSGNTYPKDMEALLPLMNMVIYSIDKAKKFRLNREGKQKADKNRARVEENFLKLTHVQRQEAAQSRREEKKRAEKERIMNEEDPEKQRRLEEAALRREQKKLEKKQMKMKQIKVKAM
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Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. Within the MPT complex, the PAT subcomplex sequesters any highly polar regions in the transmembrane domains away from the non-polar membrane environment until they can be buried in the interior of the fully assembled protein. Within the PAT subcomplex, CCDC47 occludes the lateral gate of the SEC61 complex. Involved in the regulation of calcium ion homeostasis in the ER (By similarity). Required for proper protein degradation via the ERAD (ER-associated degradation) pathway (By similarity). Has an essential role in the maintenance of ER organization during embryogenesis (By similarity).
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A0A8I3PDQ1
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CASL_CANLF
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Enhancer of filamentation 1 (CRK-associated substrate-related protein) (CAS-L) (Neural precursor cell expressed developmentally down-regulated protein 9) (NEDD-9) (p105)
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MWARNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPIQETPSGQDQPTSGLMHQTFGQQKLYQVPNPHSAPRDTIYQVPPSYQHQGIYQVPTSHGIQEQDVYQVPPSVQRSIGAANGPHLSKKVVTPVRTGQGYVYEYPSRHQKDIYDIPPSHTTQGVYDIPPSSVKVPVFSLPVGEIKPQGVYDIPPTKGLYAIPPSACRDEAGLREKEYDFPPPMRQAGRLDVRPEGVYDIPPTSTKPTGKDLHIKYNCDAPGAAELATRRHQSVLLNHAPSQLGQSPGAQNDAYDVPRGVQFLEPPAETSEKANPEERDGVYDVPLHNPPDAKGSQDVVDGMNRLSFSSTGSTRSNMSTSSTTSKESSVSASPSQDKRLLLDPDTAIERLHRLQQTLEVGVSSLMALVTTDWRCYGYMDRHINEIRTSVDKVELFVRDYLHFARGAVANASCLPELTLHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAVNKPQNKCDDLDRFVMVAKTVPDDAKQLTTTINTNAEALFRPGPGSSHVKSGSENIMNSTEYPHAASQMPLLHPGDHKAQGLNKPLPPSLGKDQPPDCSSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIIKQNKLQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNSSVGAQDRQLLCFYYDQCETHYISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVAAQDICHKVMNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF
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Negatively regulates embryonic fibroblast migration (By similarity). May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRKl and SHPTP2 to the tyrosine phosphorylated form (By similarity). Promotes adhesion and migration of lymphocytes as a result required for the correct migration of lymphocytes to the spleen and other secondary lymphoid organs (By similarity). Plays a role in the organization of T-cell F-actin cortical cytoskeleton and the centralization of T-cell receptor microclusters at the immunological synapse (By similarity). Negatively regulates cilia outgrowth in polarized cysts. Modulates cilia disassembly via activation of AURKA-mediated phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (By similarity). In conjunction with NKX2-5, positively regulates transcription of genes such as COL3A1 and MMP2, resulting in increased pulmonary endothelial fibrosis in response to hypoxia (By similarity). Positively regulates RANKL-induced osteoclastogenesis (By similarity). Required for the maintenance of hippocampal dendritic spines in the dentate gyrus and CA1 regions, thereby involved in spatial learning and memory (By similarity).
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A0A8I3PI99
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TMCO1_CANLF
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Calcium load-activated calcium channel (CLAC channel) (GEL complex subunit TMCO1) (Transmembrane and coiled-coil domain-containing protein 1)
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MSTMFADTLLIVFISVCTALLAEGITWVLVYRTDKYKRLKAEVEKQSKKLEKKKETITESAGRQQKKKIERQEEKLKNNNRDLSMVRMKSMFAIGFCFTALMGMFNSIFDGRVVAKLPFTPLSYIQGLSHRNLLGDDTTDCSFIFLYILCTMSIRQNIQKILGLAPSRAATKQAGGFLGPPPPSGKFS
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Calcium-selective channel required to prevent calcium stores from overfilling, thereby playing a key role in calcium homeostasis (By similarity). In response to endoplasmic reticulum (ER) overloading, assembles into a homotetramer, forming a functional calcium-selective channel, regulating the calcium content in endoplasmic reticulum store (By similarity). Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. Within the MPT complex, the GEL subcomplex may mediate insertion of transmembrane regions into the membrane.
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A0A8I3S724
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AURKA_CANLF
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Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A)
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MDKSKENCIAGPVKTAIALGDGPKRVLVTQQVPSQNPLSANSGQAQRVLCPSNSSQRVPPQTQKLVSSHKPAQNLKQKQLQATGVPRPASRSLNNTQKSEQPSSSAPGNNSEKELATKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILAIKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGAVYRELQKLSKFDEQRTATYITELADALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEASTYQETYKRISRVEFTFPDFVPEGARDLISRLLKHNPSQRPTLKDVLEHPWIMANSSKPSSSQKSKDSTSKQS
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Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (By similarity). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (By similarity). Required for initial activation of CDK1 at centrosomes (By similarity). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (By similarity). Regulates KIF2A tubulin depolymerase activity (By similarity). Important for microtubule formation and/or stabilization (By similarity). Required for normal axon formation (By similarity). Plays a role in microtubule remodeling during neurite extension (By similarity). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (By similarity). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (By similarity). Inhibits cilia outgrowth. Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (By similarity). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (By similarity).
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A0A8I3S9V6
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RCAF1_CANLF
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GEL complex subunit OPTI (Obligate partner of TMCO1 insertase) (Rab5-interacting protein) (RIP5) (Respirasome Complex Assembly Factor 1) (RCAF1)
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MSGGRRKEEPPQPQLANGALKVSVWSKVLRSDAAWEDKDEFLDVIYWFRQIIAVVLGVIWGVLPLRGFLGIAGFCVINAGVLYLYFSNYLQIDEEEYGGTWELTKEGFMTSFALFMVIWIIFYTAIHYD
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Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. Within the MPT complex, the GEL subcomplex may mediate insertion of transmembrane regions into the membrane. In addition to its role in multi-pass membrane insertion, RAB5IF/OPTI also acts as an assembly factor for mitochondrial respiratory complexes (By similarity).
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A0A8I5ZNK2
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OXSR1_RAT
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Serine/threonine-protein kinase OSR1 (EC 2.7.11.1) (Oxidative stress-responsive 1 protein)
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MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKERVAIKRINLEKCQTSMDELLKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKGGVLDESTIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPSLDTGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFLQEKILQRAPTISERSKKVRRVPGSSGRLHKTEDGGWEWSDDEFDEESEEGKAAISQLRSCPTQQHCLCLLQLFSAADPMGTLLQVPEQISAHLPQPASQMPTQPAQVSLLPPAEPAKPAQARSSGERSQETKVPISLVLRLRNSKKELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVEEPQSNRSVTFKLASGVEGSDIPDDGKLIGFAQLSIS
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Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif (By similarity). Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity (By similarity). Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases (By similarity). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4 (By similarity). Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1 (By similarity). Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation (By similarity). Phosphorylates RELL1, RELL2 and RELT (By similarity). Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT (By similarity).
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A0A8M1NHK4
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RBM47_DANRE
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RNA-binding protein 47 (RNA-binding motif protein 47)
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MTAEDSASAVAMSNPSPSSSSKSSSGHPQHHCTVPEGVAGAPNEAALVSLMERSGYGMVQENGQRKYGPPPGWQGTSPPRGCEIFVGKIPRDVYEDELVPVFESVGRIYEMRLMMDFDGKNRGYAFVMYTQKHEAKRAVRELNNFEIRPGRLLGVCSSVDNCRLFIGGIPKTKKREEILEEVSKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETSEEILRQTFGQFNPGCVERVKKIRDYAFVHFASRDDAVVAMDNLNGTEIEGSRIEVTLAKPVDKEQYTRYQKASKGTAAATTVESTQQSYVYQCDPYTLAYYGYPYNTLIGPNRDYFIKGTVRGRGRAGASSRGPGPRGSYLGGYSAGRGIYSRYHEGKTKLPDKPYEIMSNLELAAVNPVGIKPGTMALPALGAQYPTVFSAAPATKLMEEGKIHPVEHLINPLALQHDPTAASATAAVIPAVSTPPPFQGRPITPVYAMAHNIQRIPAAAASLYGAGYMPIAAHANTATLAALQKNAAVAAAYGGYAGYMPQAFPAATFQMPIHDVYQTY
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Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing (By similarity). Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation.
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A0A8M2
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L14AA_XENLA
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Protein LSM14 homolog A-A (RNA-associated protein 55A-A) (RAP55A-A) (xRAP55) (xRAP55A)
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MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDEIFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSSASSFQSVSSYGPFGRMPAYSQFNTGPLVGPQFGAVGVGSSLTSFGAETTSSTSLPPSSAVGTSFTQEARTLKTQSSQGQSSSPLDSLRKSPNIEQAVQTAAAPHAPSTATVGRRSPVLSRPVPSSIQKTAESPEQRKGELHKMQRPDIDQLKNDKNDPSKRQPVLSALQPRRGRGGNRGGRGRFGVRRDGPMKFEKDFDFESANAQFNKEEIDREFHNKLKIKDDKPEKPVNGEDKTDSVVDTQNSEGNAEEEEVLAGGVCYYDKTKSFFDNISCDDNRDRRQTWAEERRINVETFGLPLRSNRGRGGFRGRGGGMGFRGGRGRGGERRGAPGGGGFGPARGFRGGFRGGRGGREFADYEYRKDNKVAA
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RNA-binding component of messenger ribonucleoprotein complexes (mRNPs), storage particles that mask maternal mRNAs from the translational apparatus during oocyte maturation. Acts as a repressor of mRNA translation. Probably involved in the storage of translationally inactive mRNAs in the cytoplasm in order to prevent their degradation.
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A0A8M9PFP2
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CSTN3_DANRE
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calsyntenin-3
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MARMSFLSFLLFCLTSVAHGNKANKHKPWIETEYQGIVMENDNTVLLNPPLFALDKDAPLHYAGEICGFRVHNGPGGSGSAQFEAVVLDRSTGEGLVRSKEPLDCESQKEHSFTIQAYDCGEGPDGTNSKKSHKATVHVRVNDVNEFSPVFVERRYEASVPEGRLFDRIVRVEAVDADCSPQYSQICFYDIITPNVPFTIDNDGNIKNTEPLDSKRQRVHSFWVTAFDCGKNRAQADAQVIVTVKPSCKPGWIGWTKRIEYTPGSGSIPLFPNLHLETCEETVWNIQATVELQTSHIGKGCDRDSYSDRSVRRLCGAVRGEVDLLPPPSPATNWTAALPTLPSSDSSLVFSFNGSTHVAVVPDSVASAVSGDHFTLQLWMRRGGASTQPPANQARGTRKEEETIVCSTVKNDDSYSHYSLSVHGCRLSLFYWPDVSAARPVKFLWKLEQVCDSEWHHLSLSVQFPSVTLYVDGVTFDPALIHDNGAIPNPAPHQRLVIGACWEPEEKPKDIVNNTMPENKDTGKFVSGYKGLLSGVTVRPGNVEPHSVVECLYACREGLDFGDLETLGSGMKVHVNPSQSVLVLEGDDIESFNRAVQQVTYRNSLRFATPGVRPLKLTTSLRCFSEESCLSLRQLEGYLVVLQPDAPQISLSGVGPHLARPAAEFEGPQGVPLFPELRIVCSLSHAVNTAAQGMEGGALMSDAVAHTLDGCEVQPLGEELNTEREELLVDMESLRERGLDIINTTAYIAITGAESISVYEDVLRSIHYRLAKGSARFERRFRLSCSEMNGRYTSNELTLEVNFLHSLDSLYHPSHLLASQQQFLHPSHHTGELSGHTLPNPHRNSVVPGAATVIIMVCVGFLVVMVILGVFRIRSIHRRGEGARGGGKEGGNQWDDSALTIIVNPMETYENRMGITTDMEGECEDEEEVVDSPDDTSDDQRIIIKKEGRDSAPRRY
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Synaptic adhesion molecule. Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with presynaptic neurexins (By similarity).
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A0A8V1ABE9
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DSD1_CHICK
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D-serine dehydratase (EC 4.3.1.18)
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MWLGALLDTLPTPALTIDRTTAHRNAERMRERCRALGVRLRPHVKTHKTLEGGLLATGGTRRGIAVSTLAEARFFADGGFDDILLAYPVPTARLEECAGLARRLDAFHVLLDRPEALASLRQRPLGHGKRWLVWLKLDCGNGRAGVRPTDPAALELAQAIANDAPEEVTLVGVYAHCGNTYGCSGADTIQAIARTTTNAVLSFVAALRQAGVPCPQASIGSTPSCSHPIPEMSQLTELHPGNYIFYDLQQTQLGSCQPQDVAIRVLTRVIGHYAHRGQLLVDCGWAALSLHGAGAGQGPQGCAAIDGHPELRLVGLTQEHGLLEHAGGQMDFGRFPVGSVLALIPYHACATAAMHPVYYVHEEGKVVALWHPVRGW
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Catalyzes the conversion of D-serine, an allosteric activator of the N-methyl-D-aspartate (NMDA) receptor for L-glutamate, to pyruvate and ammonia.
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A0AAR7
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CCAMK_LOTJA
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Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase (LjCCaMK) (EC 2.7.11.17)
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MGYDQTRKLSDEYEISEILGRGGFSVVRKGTKKSGNEKTQVAIKTLRRLGSSPSGTGGGQKSTATVMGFPSLRQVSVSDALLTNEILVMRRIVENVSPHPNVIDLYDVCEDSNGVHLVLELCSGGELFDRIVAQDKYAETEAAAVVRQIAAGLEAVHKADIVHRDLKPENCLFLDSRKDSPLKIMDFGLSSVEEFTDPVVGLFGSIDYVSPEALSQGKITAKSDMWSLGVILYILLSGYPPFIAQNNRQKQQMIINGNFSFYEKTWKGITQSAKQLISSLLTVDPSKRPSAQELLSHPWVRGDKAKDEQMDPEIVSRLQSFNARRKLRAAAIASVWSSTIFLRTKKLRSLVGTYDLKEEEIESLRIHFKKICGNGDNATLSEFVEVLKAMKMPSLIPLAPRIFDLFDNNRDGTIDMREILCGFSSLKNSKGDDALRLCFQMYDTDRSGCITKEEVASMLCALPEECLPADITEPGKLDEIFDLMDANSDGKVTFEEFKAAMQRDSSLQDMLLSSLRPS
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Calcium- and calmodulin-dependent protein kinase necessary and sufficient for dedifferentiation of root cortical cells into nodule initials. Not required for calcium spiking. Acts as central regulator of the nodule organogenesis program. Required for root hair curling and infection thread (IT) formation upon rhizobial infection, and arbuscule formation during arbuscular mycorrhiza (AM) fungal infection. Phosphorylates the downstream target IPD3, a protein required for root infection by symbiotic rhizobia and AM fungi. Phosphorylates the downstream target CIP73, a protein required for root nodule organogenesis.
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A0AUJ5
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POLG_BVY3
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Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]
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MPTRYRGADRYGNLGYDKVLQSKADAAKRRGLLFDHGSETYECPRCGEIWRNLDDYMAEGGKMHPKKCLPEECDSDEEQISSCNAALIHEKWGDLDSDTSSKLSEFYKEPSILTYTTRTHCVVEKMRSMTAPQCIEDIVGVRLHGRTAWFFSKDPTLQYGHHPIYYDTHPWNDELDKYLGGAKYNTALVQVYDGTRDLPYHKDDEPCYDITNNPIRTVNVTGTGDLCISKDKRRLYETIPMTSGTVITFPATMQENFYHAVRNPSAGRISITFRNQIRTVERQVAHSANKRWVPIVEARVTTNESRRGDNKQFQEAQSKLQTKTTINFGEFAAEVDGYYPTLSQDHKPALPKIIPELGLPTVDFIYVGNMRVPIDFKKNNVPAIVDTARHVAKIIDSQALTSEPIKVFTEQREVVGNVVTCTGTGFSVADAKEAKALLNGLMYNRASNLFICPSCSDAAVLPEALLTLEHKRSCELASMKKISLARNMQVHVKQEAVARLISQQNSISVPIATLSSCVRGSADTTQVSLHIDEEDSIVDAIHLPNDFITCDHEHAFETDSASDNDVETMKKSEKRRKRRKRNPPPVRQVITRAPVSNIICDVILTCLETQIPVEFIGKSCITFKPVRVGPVHTVGIQLKHQLHKTGFEVDDLPDRETTSDIILAATRALRRLRHAHSNAQQVHNSDITFGTSGAILPWSWLAHDVIVEGPVQDSLVVRGRNVVSGHVTNALNLQQDCLADDYLQYSEELQPLHDDLSELKPLNVINNELIRQNMHITTLYSNMSKLQNDALATKAEMKLPLFGVAQLVVNQLKYNTTTHEWGERGDYVRKFVGKFFADFPTTQVPKQYMTRTTNGHIRITAYKALSLTSDPEIMMSRRMTQPMLTTAKQADCVFQSTTGATCTSASCTTNSSGVVLSNKCADPAPNTLRVRTMWDDIIIELPLQGGRVHVPLEGLCFSTIFLHMYLLVPDESVKLFHRTVTERAMPSLGQWPTLRHLATWVLNLVAMFPVLSTTPMPEILVHHESQSVHIPDCLGTATSGYHRLNIVTPYDFIIFATEIGRNGCQEYRVGGFAHDIKYTVSLMQDKRKLLHELMLTPTWAFYALSSPTLLKILYRSGALKRTYEHAVMANHNAVDLVHELNFLPERVSRAQTLQDEITAWEANVGRVLQQVDGYLTRNHDPPLQRWYADASARLQHLKIDVDLLKNGFRSSQREHVEKKEQLLCDSFERLYNEQNSSLESLKTRCGMGSARALIKPSGKCESPEPAKQLSCKDLICSTKDKYALMLYTQADALKRKIVAGSQSAFTTVCAGVAYRATKVMLRTPFNLLNALNTYSLLIAAVNVMVLVQNYRRDQRKRAQYVNNLETQSMIRHYFAHLEQYIVNYVPRDEQFEVIKAKFDEEFPEYNVMFKEVYKERIQFQSADEGKNMCKIFASAILVMMVFDAHRADLMYKSFSQVRALFNTLYDSGNPFNIIFQAERTIAPTMDVIIQEPKPAIPSTSSCTFETWFRNCVNANNVIPVIPECDLLDFTRDTASSVVATLTSSVKREFVIRGFVGSGKSTYLPHLLTKHGKVLLCEPVRVLASNVFEALSGSPFYQSPTLLMRGTTKFGSGKITVATSGYAANYYNANRHRLNEFAYIIFDESHQHTAHNFLLRSILDVIGYEGTVLHVSATPIGKEIPFRTMHPVEVVNMSTLSFEDFAIGQRKQVRCDVFNKGANILVYVASYNDVDRMSTLLLERGLRVKKIDARTVANVNNITCDGSDGEPLYLVATNIVENGVTLNVDVVVDFGLCVKPVINALQRRVDYVKTPITWGQRIQRNGRVGRYKNGFCLNVGDVYKTPPIISEDVALESALMCFAANVPPIFDNVDPALFGQVTRPQVQTAQMFELPIYITTPMISDAGALQSDIYQVIKKFVLREGSIQLTQDATYLSNMSNWKTIADYFPDISDTHAMRHEKVPFFVKDFGENSYIALAEAIRKARNKSLGARGKLYGDVDATALLLQTDPGSLDRSIMIVETELVAQRSKLEDLNHHVHESTGMFQRYVSHLNHCLRGRYQTDQIQKNIEVLSNMRSTLVGYRQVVDKVEPEEIPHFVQQNPNITMIIDFQSDRTKADGFVKHGINGIYNYTKIASDTFSLLLIACVVIYYVVQYFFREMKSHITFEASGSRRNRLHLRDNKLIKGGYTWAGPSDDMEREFGPEYALKRDKFSEKKARKHMRERIQPRTNMGVKLAPFQVFYGFDVADYDVLQLFDPITGVKIDMDPRATAKEITEEVEDTPFNKEVWSDTHMPEKIQATFVKKGGVNREDVLKQVRVDMTTHNPTMVTGSGGIMGYPEHKGDFRQTGPPKFSIVPEGRSTIKSGNNIAPFISAMGTIKNVYMNGDFDTLACTQIGNKLVVNAHIFMEPVKKQELILQHGVYELPNNGTINIKHVPGIDMVIQTLPMDVPLARQIKAYRGPIPGELIRLLKIERNTKTNSTSLSDPGTARVGPGTIWYHNITTKHGDCGSLVLSEKDNKIVGIHTGQQDGTNLNLFAPITKDAIVAIETVLPGELNDWVFTPDMLDVGSNNAIRKQASDPFPVVKKLLEGITFQNNRTTTTDSVSNTAILPARKYWVASDLPVNIKYQCDMPTFFNTRHTYEGESQPFMAYLRECGDAETFFRPLLSHYIPSNLNGDAFKKDFFKYGKPVPVGLVHGPSFKIASDRVIKRFERVGYERHSIPFEFDAEAIRDDLNKHAAMGAQYVGKKEQHLDGISEEQFCDEFVASCCRLANNCDGVWKGSLKAELRSKEKVQENKTRVFTSAPYDVLLGGKACVMHFNKKFYANNTKGPWTVGINKLGLGWHRLLKSLPEGFVYGTGDGSQFDSSLTPLLINEVCRIRMYFMQDDELGQAMLRGLYRQIIWTLISMPDGSVVRKAKGNPSGQPSTVDDNTIMVMLAVEYVFAYLGITQEEMDTIFKYYANGDDLIFAIHPDRESILNEFTHLFAHLGLNYIFEDRTRNRAELEYMSLTGIEREGFYIPKLSRERISSIVQWRRKGDTRAMFDALNAAILESWGYDDLTYWLRKYYEWLIINRYDIDLPEGEKLPYHTETAVETLYTCDDNTTVYDGRYDFEVPTDASGGVFIIDFQSSSGTDTPPVIPPATSEPALQPVLTRQTSRPPTPPNTILTGQQQQQLMPKSSQPYQLEPLLAPTGVQQPTFGTFGMPQAQQTTTEPVVAAARVRGKQKEGDTSLSQVRDHRRLSPERIVRHDDDLAPPNESTSGESSHYDELTLPDVPRDKRKGLGARLKGKPIITQTQIYNYRPAFGSIHNNKATDIELEAWKKQIADYFQVDDVSTLILGFMAYVIENGTSPEIFTNQKFVMATSSGEQREYPLAPFRSRSVELRKIMRRFSEEAIDYIQIQREHNPQYVPRQAVVRNVKRAIYFPYCFDFIDETILTPDALEIVHQMKAAALESASSKVLGLDGGSARAIDTERHTTEDATARTHNLRGAAMMA
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[Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. [Viral genome-linked protein]: Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity). [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication. [Capsid protein]: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
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A0AV02
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S12A8_HUMAN
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Solute carrier family 12 member 8 (Cation-chloride cotransporter 9)
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MTQMSQVQELFHEAAQQDALAQPQPWWKTQLFMWEPVLFGTWDGVFTSCMINIFGVVLFLRTGWLVGNTGVLLGMFLVSFVILVALVTVLSGIGVGERSSIGSGGVYSMISSVLGGQTGGTIGLLYVFGQCVAGAMYITGFAESISDLLGLGNIWAVRGISVAVLLALLGINLAGVKWIIRLQLLLLFLLAVSTLDFVVGSFTHLDPEHGFIGYSPELLQNNTLPDYSPGESFFTVFGVFFPAATGVMAGFNMGGDLREPAASIPLGSLAAVGISWFLYIIFVFLLGAICTREALRYDFLIAEKVSLMGFLFLLGLYISSLASCMGGLYGAPRILQCIAQEKVIPALACLGQGKGPNKTPVAAICLTSLVTMAFVFVGQVNVLAPIVTINFMLTYVAVDYSYFSLSMCSCSLTPVPEPVLREGAEGLHCSEHLLLEKAPSYGSEGPAQRVLEGTLLEFTKDMDQLLQLTRKLESSQPRQGEGNRTPESQKRKSKKATKQTLQDSFLLDLKSPPSFPVEISDRLPAASWEGQESCWNKQTSKSEGTQPEGTYGEQLVPELCNQSESSGEDFFLKSRLQEQDVWRRSTSFYTHMCNPWVSLLGAVGSLLIMFVIQWVYTLVNMGVAAIVYFYIGRASPGLHLGSASNFSFFRWMRSLLLPSCRSLRSPQEQIILAPSLAKVDMEMTQLTQENADFATRDRYHHSSLVNREQLMPHY
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Cation/chloride cotransporter that may play a role in the control of keratinocyte proliferation.
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A0AV96
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RBM47_HUMAN
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RNA-binding protein 47 (RNA-binding motif protein 47)
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MTAEDSTAAMSSDSAAGSSAKVPEGVAGAPNEAALLALMERTGYSMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPVDKEQYSRYQKAARGGGAAEAAQQPSYVYSCDPYTLAYYGYPYNALIGPNRDYFVKAGSIRGRGRGAAGNRAPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEIPTVNPVAIKPGTVAIPAIGAQYSMFPAAPAPKMIEDGKIHTVEHMISPIAVQPDPASAAAAAAAAAAAAAAVIPTVSTPPPFQGRPITPVYTVAPNVQRIPTAGIYGASYVPFAAPATATIATLQKNAAAAAAMYGGYAGYIPQAFPAAAIQVPIPDVYQTY
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Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing. Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules. Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10. Also involved in the alternative splicing of several genes including TJP1. Binds the pre-mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs. Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity).
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A0AVF1
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IFT56_HUMAN
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Intraflagellar transport protein 56 (Tetratricopeptide repeat protein 26) (TPR repeat protein 26)
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MMLSRAKPAVGRGVQHTDKRKKKGRKIPKLEELLSKRDFTGAITLLEFKRHVGEEEEDTNLWIGYCAFHLGDYKRALEEYENATKEENCNSEVWVNLACTYFFLGMYKQAEAAGFKASKSRLQNRLLFHLAHKFNDEKKLMSFHQNLQDVTEDQLSLASIHYMRSHYQEAIDIYKRILLDNREYLALNVYVALCYYKLDYYDVSQEVLAVYLQQIPDSTIALNLKACNHFRLYNGRAAEAELKSLMDNASSSFEFAKELIRHNLVVFRGGEGALQVLPPLVDVIPEARLNLVIYYLRQDDVQEAYNLIKDLEPTTPQEYILKGVVNAALGQEMGSRDHMKIAQQFFQLVGGSASECDTIPGRQCMASCFFLLKQFDDVLIYLNSFKSYFYNDDIFNFNYAQAKAATGNTSEGEEAFLLIQSEKMKNDYIYLSWLARCYIMNKKPRLAWELYLKMETSGESFSLLQLIANDCYKMGQFYYSAKAFDVLERLDPNPEYWEGKRGACVGIFQMIIAGREPKETLREVLHLLRSTGNTQVEYMIRIMKKWAKENRVSI
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Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium. Required for transport of specific ciliary cargo proteins related to motility, while it is neither required for IFT complex B assembly or motion nor for cilium assembly. Required for efficient coupling between the accumulation of GLI2 and GLI3 at the ciliary tips and their dissociation from the negative regulator SUFU. Plays a key role in maintaining the integrity of the IFT complex B and the proper ciliary localization of the IFT complex B components. Not required for IFT complex A ciliary localization or function. Essential for maintaining proper microtubule organization within the ciliary axoneme.
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A0AVI4
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TM129_HUMAN
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E3 ubiquitin-protein ligase TM129 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TM129)
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MDSPEVTFTLAYLVFAVCFVFTPNEFHAAGLTVQNLLSGWLGSEDAAFVPFHLRRTAATLLCHSLLPLGYYVGMCLAASEKRLHALSQAPEAWRLFLLLAVTLPSIACILIYYWSRDRWACHPLARTLALYALPQSGWQAVASSVNTEFRRIDKFATGAPGARVIVTDTWVMKVTTYRVHVAQQQDVHLTVTESRQHELSPDSNLPVQLLTIRVASTNPAVQAFDIWLNSTEYGELCEKLRAPIRRAAHVVIHQSLGDLFLETFASLVEVNPAYSVPSSQELEACIGCMQTRASVKLVKTCQEAATGECQQCYCRPMWCLTCMGKWFASRQDPLRPDTWLASRVPCPTCRARFCILDVCTVR
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E3 ubiquitin-protein ligase involved in ER-associated protein degradation, preferentially associates with the E2 enzyme UBE2J2. Exploited by viral US11 proteins to mediate HLA class I proteins degradation.
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A0AVK6
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E2F8_HUMAN
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Transcription factor E2F8 (E2F-8)
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MENEKENLFCEPHKRGLMKTPLKESTTANIVLAEIQPDFGPLTTPTKPKEGSQGEPWTPTANLKMLISAVSPEIRNRDQKRGLFDNRSGLPEAKDCIHEHLSGDEFEKSQPSRKEKSLGLLCHKFLARYPNYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLNKTLGTLKSIGEENKYAEQIMMIKKKEYEQEFDFIKSYSIEDHIIKSNTGPNGHPDMCFVELPGVEFRAASVNSRKDKSLRVMSQKFVMLFLVSTPQIVSLEVAAKILIGEDHVEDLDKSKFKTKIRRLYDIANVLSSLDLIKKVHVTEERGRKPAFKWTGPEISPNTSGSSPVIHFTPSDLEVRRSSKENCAKNLFSTRGKPNFTRHPSLIKLVKSIESDRRKINSAPSSPIKTNKAESSQNSAPFPSKMAQLAAICKMQLEEQSSESRQKVKVQLARSGPCKPVAPLDPPVNAEMELTAPSLIQPLGMVPLIPSPLSSAVPLILPQAPSGPSYAIYLQPTQAHQSVTPPQGLSPTVCTTHSSKATGSKDSTDATTEKAANDTSKASASTRPGSLLPAPERQGAKSRTREPAGERGSKRASMLEDSGSKKKFKEDLKGLENVSATLFPSGYLIPLTQCSSLGAESILSGKENSSALSPNHRIYSSPIAGVIPVTSSELTAVNFPSFHVTPLKLMVSPTSVAAVPVGNSPALASSHPVPIQNPSSAIVNFTLQHLGLISPNVQLSASPGSGIVPVSPRIESVNVAPENAGTQQGRATNYDSPVPGQSQPNGQSVAVTGAQQPVPVTPKGSQLVAESFFRTPGGPTKPTSSSCMDFEGANKTSLGTLFVPQRKLEVSTEDVH
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Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene.
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A0AVT1
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UBA6_HUMAN
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Ubiquitin-like modifier-activating enzyme 6 (Ubiquitin-activating enzyme 6) (EC 6.2.1.45) (Monocyte protein 4) (MOP-4) (Ubiquitin-activating enzyme E1-like protein 2) (E1-L2)
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MEGSEPVAAHQGEEASCSSWGTGSTNKNLPIMSTASVEIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNRAEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPIKFISADVHGIWSRLFCDFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLNGSIQQITVISPFSFSIGDTTELEPYLHGGIAVQVKTPKTVFFESLERQLKHPKCLIVDFSNPEAPLEIHTAMLALDQFQEKYSRKPNVGCQQDSEELLKLATSISETLEEKPDVNADIVHWLSWTAQGFLSPLAAAVGGVASQEVLKAVTGKFSPLCQWLYLEAADIVESLGKPECEEFLPRGDRYDALRACIGDTLCQKLQNLNIFLVGCGAIGCEMLKNFALLGVGTSKEKGMITVTDPDLIEKSNLNRQFLFRPHHIQKPKSYTAADATLKINSQIKIDAHLNKVCPTTETIYNDEFYTKQDVIITALDNVEARRYVDSRCLANLRPLLDSGTMGTKGHTEVIVPHLTESYNSHRDPPEEEIPFCTLKSFPAAIEHTIQWARDKFESSFSHKPSLFNKFWQTYSSAEEVLQKIQSGHSLEGCFQVIKLLSRRPRNWSQCVELARLKFEKYFNHKALQLLHCFPLDIRLKDGSLFWQSPKRPPSPIKFDLNEPLHLSFLQNAAKLYATVYCIPFAEEDLSADALLNILSEVKIQEFKPSNKVVQTDETARKPDHVPISSEDERNAIFQLEKAILSNEATKSDLQMAVLSFEKDDDHNGHIDFITAASNLRAKMYSIEPADRFKTKRIAGKIIPAIATTTATVSGLVALEMIKVTGGYPFEAYKNCFLNLAIPIVVFTETTEVRKTKIRNGISFTIWDRWTVHGKEDFTLLDFINAVKEKYGIEPTMVVQGVKMLYVPVMPGHAKRLKLTMHKLVKPTTEKKYVDLTVSFAPDIDGDEDLPGPPVRYYFSHDTD
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Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Required for UBD/FAT10 conjugation. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility.
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A0AVX7
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CHP3_CHICK
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Calcineurin B homologous protein 3 (Tescalcin) (TSC)
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MGSAQSVPPEMRALAERTGFTSEQIEQLHRRFKQLNHNRKTIRKEDFDTIPDLEFNPIRARIVHAFFDKRNLRKAPAGLAEEINFEDFLTIMSYFRPIEMDMDEERLESFRKEKLKFLFHMYDADYDGIITLQEYKNVLDELMSGNPHLEKESLRAIAEGAMLEAASACMARTGPDEVYEGITFEDFLKVWKGIDIETKMHVRFLTMEAIAHCY
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Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Promotes the induction of hematopoietic stem cell differentiation toward megakaryocytic lineage. Essential for the coupling of ERK cascade activation with the expression of ETS family genes in megakaryocytic differentiation. Also involved in granulocytic differentiation in a ERK-dependent manner. Inhibits the phosphatase activity of calcineurin (By similarity).
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A0FGR8
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ESYT2_HUMAN
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Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)
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MTANRDAALSSHRHPGCAQRPRTPTFASSSQRRSAFGFDDGNFPGLGERSHAPGSRLGARRRAKTARGLRGHRQRGAGAGLSRPGSARAPSPPRPGGPENPGGVLSVELPGLLAQLARSFALLLPVYALGYLGLSFSWVLLALALLAWCRRSRGLKALRLCRALALLEDEERVVRLGVRACDLPAWVHFPDTERAEWLNKTVKHMWPFICQFIEKLFRETIEPAVRGANTHLSTFSFTKVDVGQQPLRINGVKVYTENVDKRQIILDLQISFVGNCEIDLEIKRYFCRAGVKSIQIHGTMRVILEPLIGDMPLVGALSIFFLRKPLLEINWTGLTNLLDVPGLNGLSDTIILDIISNYLVLPNRITVPLVSEVQIAQLRFPVPKGVLRIHFIEAQDLQGKDTYLKGLVKGKSDPYGIIRVGNQIFQSRVIKENLSPKWNEVYEALVYEHPGQELEIELFDEDPDKDDFLGSLMIDLIEVEKERLLDEWFTLDEVPKGKLHLRLEWLTLMPNASNLDKVLTDIKADKDQANDGLSSALLILYLDSARNLPSGKKISSNPNPVVQMSVGHKAQESKIRYKTNEPVWEENFTFFIHNPKRQDLEVEVRDEQHQCSLGNLKVPLSQLLTSEDMTVSQRFQLSNSGPNSTIKMKIALRVLHLEKRERPPDHQHSAQVKRPSVSKEGRKTSIKSHMSGSPGPGGSNTAPSTPVIGGSDKPGMEEKAQPPEAGPQGLHDLGRSSSSLLASPGHISVKEPTPSIASDISLPIATQELRQRLRQLENGTTLGQSPLGQIQLTIRHSSQRNKLIVVVHACRNLIAFSEDGSDPYVRMYLLPDKRRSGRRKTHVSKKTLNPVFDQSFDFSVSLPEVQRRTLDVAVKNSGGFLSKDKGLLGKVLVALASEELAKGWTQWYDLTEDGTRPQAMT
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Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding this occurs most likely via the AP-2 complex. Promotes the localization of SACM1L at endoplasmic reticulum-plasma membrane contact sites (EPCS).
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A0FGR9
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ESYT3_HUMAN
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Extended synaptotagmin-3 (E-Syt3) (Chr3Syt)
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MRAEEPCAPGAPSALGAQRTPGPELRLSSQLLPELCTFVVRVLFYLGPVYLAGYLGLSITWLLLGALLWMWWRRNRRGKLGRLAAAFEFLDNEREFISRELRGQHLPAWIHFPDVERVEWANKIISQTWPYLSMIMESKFREKLEPKIREKSIHLRTFTFTKLYFGQKCPRVNGVKAHTNTCNRRRVTVDLQICYIGDCEISVELQKIQAGVNGIQLQGTLRVILEPLLVDKPFVGAVTVFFLQKPHLQINWTGLTNLLDAPGINDVSDSLLEDLIATHLVLPNRVTVPVKKGLDLTNLRFPLPCGVIRVHLLEAEQLAQKDNFLGLRGKSDPYAKVSIGLQHFRSRTIYRNLNPTWNEVFEFMVYEVPGQDLEVDLYDEDTDRDDFLGSLQICLGDVMTNRVVDEWFVLNDTTSGRLHLRLEWLSLLTDQEVLTEDHGGLSTAILVVFLESACNLPRNPFDYLNGEYRAKKLSRFARNKVSKDPSSYVKLSVGKKTHTSKTCPHNKDPVWSQVFSFFVHNVATERLHLKVLDDDQECALGMLEVPLCQILPYADLTLEQRFQLDHSGLDSLISMRLVLRFLQVEERELGSPYTGPEALKKGPLLIKKVATNQGPKAQPQEEGPTDLPCPPDPASDTKDVSRSTTTTTSATTVATEPTSQETGPEPKGKDSAKRFCEPIGEKKSPATIFLTVPGPHSPGPIKSPRPMKCPASPFAWPPKRLAPSMSSLNSLASSCFDLADISLNIEGGDLRRRQLGEIQLTVRYVCLRRCLSVLINGCRNLTPCTSSGADPYVRVYLLPERKWACRKKTSVKRKTLEPLFDETFEFFVPMEEVKKRSLDVAVKNSRPLGSHRRKELGKVLIDLSKEDLIKGFSQWYELTPNGQPRS
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Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. {ECO:0000250, ECO:0000269|PubMed:23791178}.
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A0FI79
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INP5E_PANTR
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Phosphatidylinositol polyphosphate 5-phosphatase type IV (72 kDa inositol polyphosphate 5-phosphatase) (Inositol polyphosphate-5-phosphatase E) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase) (EC 3.1.3.86)
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MPSKAENLRPSEPAPQPPEGRTLQGQLPGAPLAQRAGSPPDVPGSESPALACSTPATPSGEDPPARAAPIAPRPPARPRLERALSLDDKGWRRRRFRGSQEDLEARNGTSPSRGSVQSEGPGAPAHSCSPPCLSTSLQEIPKSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVAGSSPRLPSLLPPRPPPALSLDIASDSLRTANKVDSDLADYKLRAQPLLVRAHSSLGPGRPRSPLACDDCSLRSAKSSFSLLAPIRSKDVRSRSYLEGSLLASGALLGADELARYFPDRNVALFVATWNMQGQKELPPSLDEFLLPAEADYAQDLYVIGVQEGCSDRREWETRLQETLGPHYVLLSSAAHGVLYMSLFIRRDLIWFCSEVECSTVTTRIVSQIKTKGALGISFTFFGTSFLFITSHFTSGDGKVAERLLDYTRTVQALALPRNVPDTNPYRSSAADVTTRFDEVFWFGDFNFRLSGGRTVVDALLCQGLVVDVPALLQHDQLIREMRKGSIFKGFQEPDIHFLPSYKFDIGKDTYDSTSKQRTPSYTDRVLYRSRHKGDICPVSYSSCPGIKTSDHRPVYGLFRVKVRPGRDNIPLAAGKFDRELYLLGIKRRISKEIQRQQALQSQNSSTICSVS
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Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), phosphatidylinositol 4,5-bisphosphate(PtdIns(4,5)P2) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Specific for lipid substrates, inactive towards water soluble inositol phosphates (By similarity). Plays an essential role in the primary cilium by controlling ciliary growth and phosphoinositide 3-kinase (PI3K) signaling and stability (By similarity).
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A0FIN4
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IRF1_PIG
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Interferon regulatory factor 1 (IRF-1)
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MPITRMRMRPWLEMQINSNQIPGLIWINKEEMIFQIPWKHAAKHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTKNQRKERKSKSSRDAKCKAKKKSCGESSPDTFSDGLSSSTLPDDHSSYTAQGYIGQDLDIEQALTPALSPCAISSTLPEWRIPVEIVPDSTSDLYNFQVSPMPSTSEAATDEDEEGKLTEDIMKLLEQSGWQQTNVDGKGYLLNEPGAQPTAVYGDFSCKEEPEVESPGGYTGLISSDLKNVDTSWLDNLLTPVRLPSIQAIPCAP
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Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses (By similarity). Regulates transcription of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage (By similarity). Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon-stimulated response element (ISRE) in their promoters (By similarity). Binds to a consensus sequence in gene promoters (By similarity). Its target genes for transcriptional activation activity include: genes involved in anti-viral response, such as IFN-alpha/beta, RIGI, TNFSF10/TRAIL, ZBP1, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin antibacterial response, such as GBP2, GBP5 and NOS2/INOS anti-proliferative response, such as p53/TP53, LOX and CDKN1A apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8 immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB DNA damage responses and DNA repair, such as POLQ/POLH MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA metabolic enzymes, such as ACOD1/IRG1 (By similarity). Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4 (By similarity). Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53 (By similarity). Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells (By similarity). Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development (By similarity). Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells (By similarity).
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A0FKE6
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TD1_SOLLC
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Threonine dehydratase 1 biosynthetic, chloroplastic (EC 4.3.1.19) (SlTD1) (Threonine deaminase 1)
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MEVLRFTAVKSLNSCVRPEFTAMSSVIVPISTVKVSGTRKSKKKALICAKATEILSSPATVTEPLKAEPAEAPVPLLRVSPSSLQCEPGYLLPNSPVLGTGGVTGYEYLTNILSSKVYDVAYETPLQKAPKLSERLGVNVWLKREDLQPVFSFKIRGAYNMMAKLPKEQLEKGVICSSAGNHAQGVALSAQRLGCDAVIVMPVTTPDIKWKSVKRLGATVVLVGDSYDEAQAYAKKRAESEGRTFIPPFDHPDVIVGQGTVGMEINRQLKDNIHAIFVPVGGGGLIAGIAAYLKRVAPDIKIIGVEPLDANALALSLHHGQRVMLDQVGGFADGVAVKVVGEETYRLCEELIDGVVLVGRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKGENVVAITSGANMNFDRLRLVTELADVGRQREAVLATFMPEDPGSFKKFAEMVGPMNITEFKYRYNSDKERALVLYSVGLHTILELEGMVERMESADLQTINLTDNDLVKDHLRHLMGGRTNVHNELLCRFTFPEKPGALMKFLDAFSPRWNISLFHYRAQGDTGANVLVGIQVPPDEVVEFEGRADSLGYEYAMESLNEAYQLIMH
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Has a housekeeping role in isoleucine biosynthesis (Probable).
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A0FKN5
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S26A5_CHICK
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Prestin (Solute carrier family 26 member 5)
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MEDAQESGECLVQNQKYCVERPIYNQEILQGQLHKRERTPQSLRQKIEHSCRCSSKKAKSHLYSFLPILKWLPRYPVKEYLLGDIISGISTGVMQLPQGLAYALLAAVPPVFGLYSSFYPVFLYTFFGTSKHISIGTFAVISMMVGGVAVRQVPDEVISVGYNSTNATDASDYYSLRDDKRVQVAVTLAFLSGIIQLCLGFLRFGFVAIYLTEPLVRGFTTAAAVHVFTSQLKYLLGVKTSRYSGPLSVVYSLVAVFSKITTTNIAALIVGLTCIALLLIGKEINLRFKKKLPVPIPMEIIVVIIGTGVSAGMNLTESYGVDVVGKIPQGLSAPAVPEIQLIPAIFIDAVAIAIVGFSMAVSMAKIFALKHGYTIDGNQELIALGICNSVGSFFQSFPITCSMSRSLVQESTGGKTQIAGALSSIMVLLVIVAIGYLFEPLPQTVLAAIVMVNLKGMFKQFADVAHFWRTSKIELAIWVVAFVASLFLGLDYGLLTAVAFAMITVIYRTQRPQYRILGQIPDTDIYCDVEEYEEVKEYPGIKIFQANTSLYFANSESYTSALKKKTGVDPCAILAARRKAQKKHAREIKKANKVKKKAVLKLVNSSTNDVEASVKHEIANDGLPANGKFAFVDAGVQDGSPDELEHFVEPKTNVHSLILDFAPVNFVDSVGAKTLKSVIKEYNEVGVCVCIASCSGPVMNELTRLNFFDNTVTRELLFHSIHDAVLACQGKDRSASQTALDH
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Electrogenic antiporter that exchanges sulfate or oxalate for chloride ion in a strictly coupled manner with a 1:1 stoichiometry. Adopts a dynamic conformation, which alternates between the exposure of the central binding site to the extra- and intracellular solutions leading to an inward-to-outward conformational transition during the transport cycle.
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A0JJU1
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TENS_BEABA
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Tenellin synthetase (TENS) (EC 2.3.1.-) (EC 6.3.2.-) (Hybrid PKS-NRPS synthetase tenS) (Tenellin-type 2-pyridones biosynthesis cluster protein S)
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MSPMKQNESESHSVSEPIAIIGSAYRFPGGCNTPSKLWDLLRQPRDILKEIDPERLNLRRYYHPDGETHGSTDVANKAYTLEEDISRFDASFFGISPLEAASMDPQQRTLLEVVYESTETAGIPLDKLRGSLTSVHVGVMTTDWAQMQRRDPETMPQYTATGIASSIISNRISYIFDLKGASETIDTACSSSLVALHNAARALQSGDCEKAIVAGVNLILDPDPFIYESKLHMLSPDARSRMWDAAANGYARGEGAAAVVLKTLGHALRDGDRIEGVIRSTFVNSDGLSSGLTMPSSAAQTALIRQTYRKAGLDPVRDRPQFFECHGTGTKAGDPVEARAISDAFLPPSHRTNGAATTVDAPLYVGSIKTVVGHLEGCAGLAGLVKVLLSLKHGIIPPNLWFDKLNPEIARYYGPLQIPTKAIPWPKLAPGTPLRASVNSFGFGGTNAHAIIERYDASQSYCSQWRRNMTEEKTIARTQNNESIEIPVPLVLTAKTGRALWRTVDAYAQHLRQHPKLRVTNLSQFMHSRRSTHRVRASFSGASREELVENMAKFVQAHAADAKSPASQNRIGYSPLHIDPKEAPGILGVFTGQGAQWPAMGRDMMHQSPLFRKTIADCESVLQALPAKDAPVWSLSEELKKDASTSRLGEAEISQPLCTAVQLALVNVLLASGVHFDAVVGHSSGEIAATYASGIINLEAAMQIAYYRGLYAKLARGETDAAGGMMAAGLSMNDAVKLCRLPEFEGRIHVAASNAPQSVTLSGDKEAIKAAKAKLDADGVFARELKVDTAYHSHHMLPCAEPYLKALLACDIQVSAPTTTPGRKCMWSSSVRGDAELLRHDRNLDSLKGPYWVANMVQTVLFSRAVQSTIWHGGPFDLAVEVGPHPALKGPTEQTLKAVYGSAPLYTGVLSRGANDAVAFSTAIGNIWSHLGPAFVDITGYQSIFSSTCEGHGGGSAAPFISDLPLYPWDHDEEYWRESRISRRHRTGKDESHELLGRRTPDDNEREIRWRNLLKVSELPWTQGHRVLGEVLLPGAAYISMAIEAGRRLALDQGREARLLEVSDVDILRPVVVADNKEGTETLFTVRLLDEYASTGKKSDELITASFSFYIYNSPASTSIVHTCEGRIAVQLGAKLGSEAGANSMPQLPHREPSISNLQQLDCEKLYSVFETIGLEYSGAFRRIVSSSRCLGHATATASWPTTDLNDCYLIHPAILDVAFQTIFVARAHPDSGQLSSALLPSRIERVRVVPSLAMGSKLQNNENFNAAIDSWALNQTASSLTGNINVYDAESGRALIQVEGFEVRAVGEPDASKDRLLFYETVWGRDISIMGLSDPIRDETSDAMVHNLSEAIERVSLFYVRQLMGELSTADRRQANWYHTRMLAAFDYHLAKVHEETHLHLRPEWLADDWAVIQTIDEAYPDAVELQMLHAVGQNVADVIRGKKHLLEVLRVDNLLDRLYTEDKGMHMANLFLANALEEITFKFPRCKILEIGAGTGATTWAALSAIGEAFDTYTYTDLSVGFFENAVERFSAFRHRMVFRALDIEKDPASQSFDLNSYDIIIATNVLHATRNLGVTLGNVRALLKPGGYLLLNEKTGPESLRATFNFGGLEGWWLAEEKERQLSPLMSPDGWDAQLQKASFSGVDHIVHDVQEDQQDKQQNSMIMSQAVDDTFYARLSPLSEMANLLPMNEPLLIIGGQTTATLKMIKEIQKLLPRQWRHKVRLIASVDHVEAEGLPAHSDVICLQELDRGLFTTAMTSKCLDALKTLFINTRNLLWVTNAQNSSSMTPRASMFRGITRVLDGEVPHIRTQVLGIEPRETPSATARTLLEAFLRLRSDDGRHAGNVDEDGADGSSQQVLWLHEPEAELLSNGTMMVPRVKARKSLNDTYLASTRAISTTVDARCVSVQAVAGPAKMLLRPVEDFAGEHAISNQTSDSKVHIQVESTLHIPEALDGTCLYLVCGWTRTAETSVPVIALSANNASMVAVESKAVAMIDEVDVKPETLLRVFQHMAMQALDSAVKRHGQGQSTALIYGADEELAKLTSERFAVRESKVYFASSRTFAPGDWLKVQPLLSKFALSQMIPADVEVFIDCLGDTESFDACRTLQSCLSTTRTVQHRLDACLLSQMSRCSPDALVDAYSYAKTQSNAEFSWNGYVKTFTAAELAGKLSHSLIHSVYMTNWQKKDSILVTVPPLQTRGLFKSDRTYLMVGAAGGLGTSICRWMVRNGARHVVVTSRNPKADPEMLNEAERYGAAVQVVPMDACSKDSVQTVVDMIRATMPPIAGVCNAAMVLRDKLFLDMNVDHMKDVLGPKMQGTEHLDSIFAQEPLDFFVLLSSSAAILNNTGQSNYHCANLYMDSLVTNRRSRGLAASIIHVGHVCDTGYVARLVDDTKVQMSLGTTRVMSVSETDVHHAFAEAVRGGQPDSRSGSHNIIMGIEPPTKPLDLTKRKPVWISDPRLGPCLPFSTLENQMMASEQAAAASAVDSLAQQVSEATTDEEAAVAALKGFATKLEGILLLPLGSIGEDSAGRPVTDLGIDSLVAVEIRTWFLKQLRVDVPVMKILGGSTVGQLSALAAKLARQDAKKRAQLEEPSGNQPVALPSPPPKDKAGGLNKNGKSPKLPEIAQVDTVVERMEPLVLEASDRGGSSTANLTTSSSVSELDDSLHESTLQSSDNNGESTPSKSSNCNSDSGSDNQAPKEIPSNGFFTQPAATARPNVLREAPMSPAQSRIWFLSKHIAEPDAYNMVFHYRVRGPLSMVRLRHALQTVTNHHECLCMCFYASADNGQPMQGLLASSAFQMTHVPGGEEQDVQRELRKLKTRVWSVESGQTLELVVLGPRPGTAAAAEEEEEEFSLLFGYHHIVMDAISFYIFLADLDKAYRMLPLDKASAGSHLDLAAHQRQQERAGAWEESLEFWRAEFETIPEMLPSLSVALPTLHRGAVGTHRVLRELAHEQGGDAAIKKMCKHLRVSPFNLHIAVLQVVIARLASIEDVCVGIVDANRSDSRASRMVGCFVNMLPVRSRILPTATLADVARAASSKALAAFAHGQVPLDSILDKVKAPRPAGSTPLFQVALNYRPAAAIASKQALGGECEMELLADDFKDAENPFEISVLVSEMSGGRIAVEVVCQKSRYTMQATEALLDAYLNVLAGFLSDSAQSVGDCVVHDQSKVEHALDLGRGAQKSFGWPRTLSERVMSICQQHSTKSAIKDGRNELSYAQLASRVNRTASAILGTGCSVGSRIAVLCNPSIDAIVAMLAILHIGGVYVPLDTSLPEARHQSLASNCTPSLIISHAATRERAHKLSAAISAPGHEPARELTLDDLSPPEETGYMAPLNAEPNAPAILLYTSGSTGTPKGVLLTQANFGNHIALKTDILGLQRGECVLQQSSLGFDMSLVQVFCALANGGCLVIVRQDVRRDPVELTTLMTQHKVSLTIATPSEYLAWLQYGSDALAQATSWKNLCMGGEPIPPLLKDELRRRLERKDLVVTNCYGPTETTAAISFQSVALDSEHGHELPGESELAQYAVGKALPNYSIRIRDSAGGAWLPVNHTGEIVIGGAGVALGYLDMPEETRARFLQTPGEEDGMMLYRTGDKGRLLSDGTLLCFGRITGDYQVKLRGLRIELGEVEAALLQASHGLIHTAVVSRRGDVLVAHCARSHESSRETTGGGEQQDATAILRRVSELLPQYSVPAAIALLPSLPTNANGKLDRKAIAALPLSPQDEAAAATSPSNNNINNNTPSGGGGEKMTVRQGELRLLWERVLPRDAATTTTNSVRITPESDFFLRGGNSLLLMKLQAAIRESMGVRVSTKALYQASTLSGMARCVAEQRSDDDEAEEDIDWAAEVAVPPSMLAQIEKLQHSSASSSSSSSSSSSAGSSSTQRPRKTSGLEILLTGATGFLGGQLLERLVQSPRVSTVHCVAVPVDEQSLLEPFLQQQADGTRRKVRCYIGNLAAPALGLTAADQTALSQTADVIVHAGSMGHCLNTYATLAAPNFASTRHLCSLALSRSPPIPLAFASSNRVALLTGSTAPPPASAAAFPPPPGAQGFTASKWASEAFLEKLAASIMTSKTKSTTTTTTTTVPWRVSIHRPCALISDRAPNSDALNAILRYSTSMRCVPSLPEHRAEGYLDFGQVDKVVEEMVGDILGLADERQQEGPAVVYRHHSGGVKVPIHEFREHMESVYGGRFESVELGQWIVRAVDAGMDPLISAYLETFLEGDASMVFPYMGEQAV
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.
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A0JLT2
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MED19_HUMAN
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Mediator of RNA polymerase II transcription subunit 19 (Lung cancer metastasis-related protein 1) (Mediator complex subunit 19)
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MENFTALFGAQADPPPPPTALGFGPGKPPPPPPPPAGGGPGTAPPPTAATAPPGADKSGAGCGPFYLMRELPGSTELTGSTNLITHYNLEQAYNKFCGKKVKEKLSNFLPDLPGMIDLPGSHDNSSLRSLIEKPPILSSSFNPITGTMLAGFRLHTGPLPEQCRLMHIQPPKKKNKHKHKQSRTQDPVPPETPSDSDHKKKKKKKEEDPDRKRKKKEKKKKKNRHSPDHPGMGSSQASSSSSLR
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Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
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A0JMD4
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TPC2_DANRE
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Two pore channel protein 2 (Two pore calcium channel protein 2) (Voltage-dependent calcium channel protein TPC2)
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MEEEPLLAGSINQGSGDYGAHSESCLHYPDEHTPRSRRLSYSVTDDSCNVEEDADADLYVQQAVVFIEDAIKYRSINHRVDSGSLRLYRWYYSNLCQWGLGLTIAVVLALAFIERPSSLTYTSDIRVKPKPWEPPCGMTEGIEIVCLCIFILDVTAKGYLIGWEEFRMNKWLLAYLIVITASVIDWMLSISMLCDENLRVRRLIRPFFLLQNSSLMKKTLKCIKRTLPEIASVILLLALHICLFTMIGMLIFAKSDDPKQNGEWQTYFRNLPKALSSLLVLLTTANNPDVMIPAYSLNRGYSIFFILFSVFGTYLLMNLMTAIIYNQFRGYLLMSVQTSIIRRRLGIRAAFEVLCCPGRGHTSTQAEGHVERVAVSMFLKVMERVHMKSYCRQAIVKAARRFPDGFISGEDFQRLFNELDKDFVKEHPPKPEYSSSGLQHIQYVYSHYYISVLGNAVALANVICICTVLVLNAEKSASEKNYFYMEIINCIFILYYLIEMLLKIVAFGWKGYLSYRNNIFDGFLTVLLLAIQIVIFITFKIPYVDVDPVPRHVMALWEMIRLVNMLIVFRFLRIIPEIKLMAVVASTIVDLVKNLRAFAGILLVVYYMFAVLGIWLFQGAISPPSNMSLVSNSSLENITGPYSMECGTFEQLEYWPNNFDDFASSLILLYNIMVVNNWHVFTDAYARYTTDWSLVYFVVWWLTSSVMWVNLFVALILENFTYKWDRSNGLSVEDVERIAYQSTVQLMFKEHVKEPTEEELLAQLHQHPHLHLSW
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Intracellular channel initially characterized as a non-selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid adenine dinucleotide phosphate), it is also a highly-selective Na(+) channel activated directly by PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate). Localizes to the lysosomal and late endosome membranes where it regulates organellar membrane excitability, membrane trafficking, and pH homeostasis.
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A0JMQ9
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ZRN1B_DANRE
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Ubiquitin thioesterase zranb1-B (EC 3.4.19.12) (Zinc finger Ran-binding domain-containing protein 1-B)
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MTDLGLKWSCEYCTYENWPSAIKCTMCRAQRHNAPIITEEPFKSSSSLDPSLCTTQGGSTLLICPDSSARPRVRIADELPETSSKWSCHMCTYLNWPRAIRCTQCLSQRQQGSQQHSPLSPSETPQTSGSRPSPVTSDPCEEYNDRNRLNMHAQRWPCSACTYENWPKSLRCVVCDHPKPSGSPETPQQDSEAESATSPSIVNEQERENVRTAGGGGGGSRGRLRKLSPPMCKGQAEVKIELASGAVGSDNEQEADFKKLKQIRNRMRRSDWLFLNACAGVVEGDLAAVEAYKSSGGDIARQLTADEVRILNRPSAFDAGFTLVHLAIRFQRQDMLAVLLTEVSQQTAKCIPALVCPELTEQIRREVAAALHRRKGEFPCYFFTDLVTFTLPADIEDLPPNVQEKLFDEVLDRDVQKELEEESPIINWSLELGTRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKSLNDSLHDCSHWFYTRWKEWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHVFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYDNRGAGANLNTDDDVTVTFLPLVDSERKLLHIHFLSAQEMGTEEQQERMLRQWMDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDGYRQLAACPTLSDGEEEEEDEDE
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Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates apc protein, a negative regulator of Wnt-mediated transcription (By similarity). Acts as a regulator of autophagy by mediating deubiquitination of pik3c3/vps34, thereby promoting autophagosome maturation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the stress fiber dynamics and cell migration (By similarity).
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A0JN54
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DGKA_BOVIN
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Diacylglycerol kinase alpha (DAG kinase alpha) (EC 2.7.1.107) (Diglyceride kinase alpha) (DGK-alpha)
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MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAEYLQGDAIGYEGFQQFLKIYLEVDNVPDHLSQALFQSFQTGYYIEDTVREDVVCLSDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDRIIIQMMRMAEYLDWDVSELRPILQEMMKEIDYDGSGSVSLAEWLRAGATTVPLLVLLGLEMTLKDNGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYIVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLVGLHCVWCHLEIHDDCLPAMGHECDCGLLRDHILPPSSIYPSVLASGQERKTSKISQKTMDDLSLSTSEALRIDPVSNTHPLLVFVNPKSGGKQGERVLWKFQYLLNPRQVFNLLKDGPEPGLRFFRDVPDYRILVCGGDGTVGWILESIDKANLPFVPPVAVLPLGTGNDLARCLRWGGGYEGQNLGKILKDLETSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVLNIPSTHGGSNLWGDTKRPHGDIHGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLEGAIEIGQIYTKLKNAGHRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHRNQMPMLVGPPPRSSNFFGFLC
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Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group. Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol.
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A0JNB0
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FYN_BOVIN
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Tyrosine-protein kinase Fyn (EC 2.7.10.2) (Proto-oncogene c-Fyn) (p59-Fyn)
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MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHGAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL
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Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity).
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A0JNC1
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CDS2_BOVIN
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Phosphatidate cytidylyltransferase 2 (EC 2.7.7.41) (CDP-DAG synthase 2) (CDP-DG synthase 2) (CDP-diacylglycerol synthase 2) (CDS 2) (CDP-diglyceride pyrophosphorylase 2) (CDP-diglyceride synthase 2) (CTP:phosphatidate cytidylyltransferase 2)
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MTELRQRVAREPEAPPEDKESESEAKADGETASDSESRVEAVTQPPSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMMIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLTGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSGLFRLQEYNIPGVIQSIIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLVQQFLTLRPDQQLHIFNTLKSHLTDKGMLTAATEDK
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Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (By similarity). Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (By similarity). Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (By similarity).
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A0JNC3
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INSI1_BOVIN
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Insulin-induced gene 1 protein (INSIG-1)
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MPRLDDHLWRGPCAKGTKHRSHPRASARGLVAKAGEMINSSGSGPSLLAAHGALGTDPAHGPQSAGVGGQGSSSHVNSWHHHLVQRSLVLFSVGVVLALVLNLLQVQRNVTLFPDEVIATIFSSAWWVPPCCGTAAAVVGLLYPCIDSHLGEPHKFKREWASVMRCVAVFVGINHASAKLDFANNVQLSLTLAALSLGLWWTFDRSRSGLGLGITIAFLATLITQLLVYNGVYQYTSPDFLYIRSWLPCIFFSGGVTVGNIGRQLAMGVPEKPHSD
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Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Binds oxysterol, including 25-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi. Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG1 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2. Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligases AMFR/gp78 and/or RNF139. Also regulates degradation of SOAT2/ACAT2 when the lipid levels are low: initiates the ubiquitin-mediated degradation of SOAT2/ACAT2 via recruitment of the ubiquitin ligases AMFR/gp78.
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A0JNC4
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ELOV7_BOVIN
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Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
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MAFSDLTSRTVRLYDNWIKDADPRVEDWLLMSSPLPQTIILGFYVYFVTSLGPKLMENRKPFELKKVMITYNFSIVLFSVYMFYEFIMSGWGTGYSFRCDIVDYSQSPTALRMVRTCWLYYFSKFIELLDTIFFILRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHAFLNTAVHVVMYSYYGLCALGPDYQKYLWWKKYLTSLQLIQFVLITIHISQFFFMEDCKYQFPVFQYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTVKHGICKNKDH
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Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03207}.
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A0JNH9
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APLF_BOVIN
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Aprataxin and PNK-like factor (EC 3.1.1.-) (Apurinic-apyrimidinic endonuclease APLF)
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MSGGFELQPQDGGPRVALAPGETVIGRGPLLGLHRNPCYYQSSEKSQLLPLKTNIWCWLNPGDHFSLLVDKYIFCVLSTHSEMEMECTLRNSQMLDEDDILNEIPKSSSADLPDKTPSAPRRERSTETAKPQAAANNMSFIGESRDLSKQQPNPSERKRILPAWMLTENSSDQNLSVISGGNNVTWESEKERVCKDKTQVNITQPGKKRLISSGSSESTSAKQDTGKKCKNDDQEESIISSKEMPQSFSAAMLHNTEIDNTKTNPQRSKVPVEALGKVSEHKIITKGSSNEDSTARSCSESYSSTQSKSFCDKPQKSHPEPSSNPPSPECVQAKATDSVPNGSEENKVQRTSCMYGANCYRKNPVHFQHFSHPGDSDYGGVNITCQDEADDRPECPYGASCYRKNPQHKIEYRHSTFPVRSISDEDDNVGQPNEYNLNDSFIDDEEEEYEPTDEDSDWEPEKEDLEKEDMEGLLKEAKKFMKRKK
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Histone chaperone involved in single-strand and double-strand DNA break repair. Recruited to sites of DNA damage through interaction with branched poly-ADP-ribose chains, a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions (By similarity). Following recruitment to DNA damage sites, acts as a histone chaperone that mediates histone eviction during DNA repair and promotes recruitment of histone variant MACROH2A1 (By similarity). Also has a nuclease activity: displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage (By similarity). Together with PARP3, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). Also acts as a negative regulator of cell pluripotency by promoting histone exchange. Required for the embryo implantation during the epithelial to mesenchymal transition in females (By similarity).
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A0JNI4
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SRR_BOVIN
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Serine racemase (EC 4.3.1.17) (EC 4.3.1.18) (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (L-serine ammonia-lyase) (L-serine dehydratase)
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MCDQYCISFADVEKAHINIRDFIHLTPVLTSSILNQITGRNLFFKCELFQKTGSFKIRGALNAIRGLISAHPEEKPRAVVAHSSGNHGQALSFAARLEGIPAYVIVPETAPNCKKLAIQAYGASIVYSEQSEESRENITKRIAEETEGIMVHPNQEPAVIAGQGTIAMEVLNQVPLVDALVVPVGGGGMLAGIAVTVKALRPSVKVYAAEPLNADDCYQSKLKGELTPNPYPPETIADGIKSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGVAVVLSQHFRTVPAEVKNICIVLSGGNVDLTSLTWVKKQDEKAAP
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Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine (By similarity).
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A0JNK3
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HTRA2_BOVIN
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Serine protease HTRA2, mitochondrial (EC 3.4.21.108)
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MAALRAGRGAGWSLRGWRALWGGRWGKGPLLTPDLRALLTSGTPDPRTRVTYGTPSFRARLSVGVPEPRTCLRSRTSDLRARLIAGTPDPRTPEDSGTPGTRLRVWLAVALGAGGAVLLLFWGGGRGPPAVLASVLGSPPTSPRSQYNFIADVVEKTAPAVVYIEILGRHPFSGREVPISNGSGFVVAADGLIVTNAHVVADRRRVRVRLPSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPAKDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTSGISFAIPSDRLREFLHRGEKKNSWFGISGSQRRYIGVMMLTLTPSILAELQLREPSFPDVQHGVLIHKVILDSPAHRAGLRPGDVILAIGEQLVQNAEDIYEAVRTQSQLAVRIRRGQETLTLYVTPEVTE
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Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis (By similarity).
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A0JNM1
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OSTB_BOVIN
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Organic solute transporter subunit beta (OST-beta) (Solute carrier family 51 subunit beta)
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MNYSEKLTGAPPMTEVPLELLEEMLWFFRVEDATPWNCSMFVLAALVAIISFILLGRNIQANRNQKKLPPEKQTPEVLYLAEGGNKDDKNLTSLTETLLSEKPTLAQGEMEAKCSDVPRVHLPDPQEPES
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Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. The Ost-alpha/Ost-beta complex efficiently transports the major species of bile acids (taurocholate). Taurine conjugates are transported more efficiently across the basolateral membrane than glycine-conjugated bile acids (By similarity). Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols (By similarity). Able to transport eicosanoids such as prostaglandin E2 (By similarity). Modulates SLC51A glycosylation, membrane trafficking and stability activities (By similarity).
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A0JNT9
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BICL1_MOUSE
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BICD family-like cargo adapter 1 (Bicaudal D-related protein 1) (BICD-related protein 1) (BICDR-1) (Coiled-coil domain-containing protein 64A)
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MSAFCLGLAGRASAPAEPDSACCMELPAGAGDAVRSPATAAALVSFPGGPGELELALEEELALLAAGERSSEPGEHPQAEPESPVEGHGPPLPPPPTQDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQLQDELERQQLHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLSYRQLQGKVEELTEERSLQSSAATSTSLLSEIEQSMEAEELEQEREQLRLQLWEAYCQVRYLCSHLRGNDSADSAVSTDSSMDESSETSSAKDVPAGSLRTALNDLKRLIQSIVDGVEPTVTLLSVEMTALKEERDRLRVTSEDKEPKEQLQKAIRDRDEAIAKKNAVELELAKCKMDMMSLNSQLLDAIQQKLNLSQQLEAWQDDMHRVIDRQLMDTHLKEQSRPAAAAFPRGHGVGRGQEPSTADGKRLFSFFRKI
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Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Predominantly recruits 2 dyneins, which increases both the force and speed of the microtubule motor. Component of secretory vesicle machinery in developing neurons that acts as a regulator of neurite outgrowth. Regulates the secretory vesicle transport by controlling the accumulation of Rab6-containing secretory vesicles in the pericentrosomal region restricting anterograde secretory transport during the early phase of neuronal differentiation, thereby inhibiting neuritogenesis.
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A0JNU3
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LPP60_MOUSE
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60 kDa lysophospholipase (EC 3.1.1.5) (Lysophospholipase-transacylase) [Includes: L-asparaginase (EC 3.5.1.1) (L-asparagine amidohydrolase); 1-alkyl-2-acetylglycerophosphocholine esterase (EC 3.1.1.47) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase)]
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MARAMGPERRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLKTLHMFHDEEYAQAHSLPEDTLVLPPASPDQRIIYTVLECQPLFDSSDMTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQPGLSLNDRKKLLAKDLRGEMTLPATDVLLQDGMLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSFKDSVCAQPQPH
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Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities (By similarity). Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3) transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer) (By similarity). Mediates the synthesis of 1-arachidonoyl species of phospholipids by transferring the arachidonoyl residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-acyl lysophospholipid (By similarity).
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A0JNW5
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BLT3B_HUMAN
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Bridge-like lipid transfer protein family member 3B (Syntaxin-6 Habc-interacting protein of 164 kDa) (UHRF1-binding protein 1-like)
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MAGIIKKQILKHLSRFTKNLSPDKINLSTLKGEGELKNLELDEEVLQNMLDLPTWLAINKVFCNKASIRIPWTKLKTHPICLSLDKVIMEMSTCEEPRSPNGPSPIATASGQSEYGFAEKVVEGISVSVNSIVIRIGAKAFNASFELSQLRIYSVNAHWEHGDLRFTRIQDPQRGEVLTFKEINWQMIRIEADATQSSHLEIMCAPVRLITNQSKIRVTLKRRLKDCNVIATKLVLILDDLLWVLTDSQLKAMVQYAKSLSEAIEKSTEQRKSMAPEPTQSSTVVASAQQVKTTQTSNAPDVNDAIVKLFNDFDVKETSHHLVISHLDLHICDDIHAKEKESNRRITGGAMQLSFTQLTIDYYPYHKAGDSCNHWMYFSDATKTKNGWANELLHEFECNVEMLKQAVKDHNVGSPPKSPTHASPQHTQTEKDYPLKGTCRTPSVLSQQSKAKLMSSSVVVRLADFNIYQVSTAEQCRSSPKSMICCNKKSLYLPQEMSAVYIEFTEYYYPDGKDFPIPSPNLYSQLNALQFTVDERSILWLNQFLLDLKQSLNQFMAVYKLNDNSKSDEHVDVRVDGLMLKFVIPSEVKSECHQDQPRAISIQSSEMIATNTRHCPNCRHSDLEALFQDFKDCDFFSKTYTSFPKSCDNFNLLHPIFQRHAHEQDTKMHEIYKGNITPQLNKNTLKTSAATDVWAVYFSQFWIDYEGMKSGKGRPISFVDSFPLSIWICQPTRYAESQKEPQTCNQVSLNTSQSESSDLAGRLKRKKLLKEYYSTESEPLTNGGQKPSSSDTFFRFSPSSSEADIHLLVHVHKHVSMQINHYQYLLLLFLHESLILLSENLRKDVEAVTGSPASQTSICIGILLRSAELALLLHPVDQANTLKSPVSESVSPVVPDYLPTENGDFLSSKRKQISRDINRIRSVTVNHMSDNRSMSVDLSHIPLKDPLLFKSASDTNLQKGISFMDYLSDKHLGKISEDESSGLVYKSGSGEIGSETSDKKDSFYTDSSSILNYREDSNILSFDSDGNQNILSSTLTSKGNETIESIFKAEDLLPEAASLSENLDISKEETPPVRTLKSQSSLSGKPKERCPPNLAPLCVSYKNMKRSSSQMSLDTISLDSMILEEQLLESDGSDSHMFLEKGNKKNSTTNYRGTAESVNAGANLQNYGETSPDAISTNSEGAQENHDDLMSVVVFKITGVNGEIDIRGEDTEICLQVNQVTPDQLGNISLRHYLCNRPVGSDQKAVIHSKSSPEISLRFESGPGAVIHSLLAEKNGFLQCHIENFSTEFLTSSLMNIQHFLEDETVATVMPMKIQVSNTKINLKDDSPRSSTVSLEPAPVTVHIDHLVVERSDDGSFHIRDSHMLNTGNDLKENVKSDSVLLTSGKYDLKKQRSVTQATQTSPGVPWPSQSANFPEFSFDFTREQLMEENESLKQELAKAKMALAEAHLEKDALLHHIKKMTVE
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Tube-forming lipid transport protein which mediates the transfer of lipids between membranes at organelle contact sites. Required for retrograde traffic of vesicle clusters in the early endocytic pathway to the Golgi complex.
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A0JP82
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TET3_XENTR
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Methylcytosine dioxygenase tet3 (EC 1.14.11.80)
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MDTQPAPVPHVLPQDVYEFPDDQESLGRLRVSEMPAELNGGGGGGSAAAFAMELPEQSNKKRKRCGVCVPCLRKEPCGACYNCVNRSTSHQICKMRKCEQLKKKRVVPMKGVENCSESILVDGPKTDQMEAGPVNHVQEGRLKQECDSTLPSKGCEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPTIPNHAANNNSNLEDAKNLVAFSAVAEAMSTYGMPASGTPSSVSLQLYEKFNYETNRDNSGHLEGNAPSCPEDLNTLKAALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSTVKGSQESPFPNLGQVSKELVQKQYPKEQVLNLENKNSTCPSGNLPFSQNALSLAKEKNISLQTAIAIEALTQLSSALPQTNNECPNAPSQPLINPHDQLTHFPSAKGNQLPMLPVARNELFQNQQSQLYTGKNALPVPQSPRQTSWEQNKKSSYQEGQYIPENLSHSSSVLPSDASTPQKPEFLQQWVQNADLLKSPSDPMTGLKQLLGNTDEYIKSVFKGPEALPNKKNVKPKHTIKSIKKESTEFLKMSPDQQLSQLLQTNEFHRNTQAALQQHLHHKRNLFVDPNAMEACTQEQQNWWVPSSQQAPVSKTTEKPVKERKKRRQSPSQKQVEPKPKPQRKQVQIKKPKVKEGSAVFMPVSQISLDTFRRVEKEENQGKEMDAENSLPNNVQTELLESQSLQLTGSQANPDDRKTVNTQEMCNENQSNIGKANNFALCVNRANSFVAKDQCPTPSTHDTSSSSGQGDSANQHTNVSDVPGQNDLSCLDDKLEDLIRQFEAEFGEDFSLPGSAVPSQNGEGPPKQTPSGDPQFKLPFPSQLLPPENSTKPATHSNPALSNNPVSREVSNNLDSLFSSKSPKQIKIESSGAITVVSTTCFYSEENQHLDGTPTKSDLPFNPTLSGFLDSPLKYLTSPTKSLIDTPAKKAQAEFPTCDCVEQINEKDEGPYYTHLGSGPTVASIRELMEERFGQKGDAIRIEKVIYTGKEGKSSRGCPIAKWVIRRQSEDEKLMCLVRQRAGHHCENAVIIILIMAWEGIPRSLGDSLYNDITETITKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGENPKEEDGLKDNFQNLATKVAPVYKMLAPQAYQNQVNNEDIAIDCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRMIGRVAEDEQLHVLPLYKVSTTDEFGSEEGQLEKIKKGGIHVLSSFPREVRKLSEPAKSCRQRQLEAKKAAAEKKKLQKEKLVSPDKTKQEPSDKKTCQQNPGVPQQQTKPCIKVEPSNHYNNFKYNGNGVVESYSVLGSCRPSDPYSMNSVYSYHSFYAQPNLPSVNGFHSKYALPPFGFYGFPNNPVVPNQFMNYGTSDARNSGWMNNCFEKKPELQSLADGMNQSYGSELSEQSFRRSSEVPHHYSLQNPSSQKSVNVPHRTTPAPVETTPYSNLPCYNKVIKKEPGSDPLVDSFQRANSVHSHSPGVNHSLQASDLPISYKANGALSSSGRTNAESPCSMFMPNDKNGLEKKDYFGVHSNAPGLKDKQWPPYGTDVSVRQHDSLDSQSPGKVWSSCKLSDSSAALPSSASTQDKNWNGRQVSLNQGMKESALFQEKLWNSVAASDRCSATPSDRSSITPCSELQDKNWGSFPNPTVNSLKTDSSQNHWDPYSLDDNMDDGQSKSVKEEDDEEIWSDSEHNFLDENIGGVAVAPGHGSILIECARRELHATTPLKKPNRCHPTRISLVFYQHKNLNQPNHGLALWEAKMKQLAERARAREEEAAKLGIKQEVKSLGKKRKWGGAATTETPPVEKKDYTPTRQAATILTDSATTSFSYAYTKVTGPYSRFI
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Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development. Conversion of 5mC into 5hmC probably constitutes the first step in cytosine demethylation. Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes, including pax6, rax, sox9 and six3. May also contribute to the regulation of target genes in ways that do not require its enzyme activity.
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A0JPF9
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ISPD_DANRE
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D-ribitol-5-phosphate cytidylyltransferase (EC 2.7.7.40) (2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase-like protein) (Isoprenoid synthase domain-containing protein)
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MGTVTIQLSCLRHIRKLCFSCPWEGRRLFKMLLQFHHETQRPLDPGCLLPQDAERSADQPGRAVVDFPVAAVLPAGGSGERMGLTTPKQFCSIFNRPLISYTIQAFERLPWIVMVVVVVAKDNHDLMLNIVRKFNHTKVKVVHGGTTRHRSIYNGLQAFSDSTDSSTPKPKVVIIHDAVRPFVEEDLLLKITLAAKEQGASGAIRPLVSTVIATTSESYLDHSLERAKYRASEMPQGFLYDIIFQAYQRCSEFDLEFGTECLHLALQYCGTNARLIEGPPTLWKVTYKRDLAAAEAIIKETLSVSACIIAEAEEEAVELAKTLQKNLNMMETDVIPCGKESNVQYLSKTRNFIHISASASSSLWVLEMVKCFEDIDHARLYPVVIVWVQLSMTKQSADSQETDEFMALASEVKQRNVLLYGIKIDHSKELEQWQRSLERLGQITLVLIRDRNMALTGQMLHV
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Cytidylyltransferase required for protein O-linked mannosylation. Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate (By similarity). CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). Shows activity toward other pentose phosphate sugars and mediates formation of CDP-ribulose or CDP-ribose using CTP and ribulose-5-phosphate or ribose-5-phosphate, respectively (By similarity). Not involved in dolichol production (By similarity).
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A0JPL0
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ZN382_RAT
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Zinc finger protein 382 (KRAB/zinc finger suppressor protein 1) (KS1) (Multiple zinc finger and krueppel-associated box protein KS1)
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MNCHSVPLQGPVSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFISVGFHITKPDMIRKLEQGEELWTERMFPSQSYLEDEEVLVKFRDYQDKPPTSIVIINHKKLIKERNNVYEKTLGNNHIISKTLFEYKSDGKVLKNISDFISRDINPVMGTLGDSSEWEESVLTSEQEKTHPVPTLYKQIGRNLSSSLELAQHQKTQIPEQRFECDECDSSFLMTEVAFPHDRAHRGVRDFNCSKDEIAFFEKSDLGIHPHNLMEKKCSTYNKYGKLLCRKSVFVMHPRSQVDERPFQCPYCGNSFRRKSYLIEHQRIHTGEKPYICSQCGKAFRQKTALTLHEKTHTDGKPYLCVDCGKSFRQKATLTRHHKTHTGEKAYECTQCGSAFGKKSYLIDHQRTHTGEKPYQCAECGKAFIQKTTLTVHQRTHTGEKPYMCSECGKSFCQKTTLTLHQRIHTGEKPYVCSDCGKSFRQKAILTVHYRIHTGEKSNGCPQCGKAFSRKSNLIRHQKTHTGEKPYECHECGKFFSCKSNLVAHQKTHKAETVRFQ
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Functions as a sequence-specific transcriptional repressor.
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A0JPN2
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S39A4_RAT
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Zinc transporter ZIP4 (Solute carrier family 39 member 4) (Zrt- and Irt-like protein 4) (ZIP-4)
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MMLPKSLTQGLLLAMLVGTAAMVQPYHLLSLLTSGQGALDRTALDGLLNTLVARVHCTDGPCEKCLSVETALALGKPDKPQLAPESVLESRYITYLSAAAALYLNDPEKTCKDIRAGLLASHVDDYLAKLESPEAMTLGLSQLLQKIEAHDASQPTREETCVDVPQLLEEAEEAGVSRSPGLVLTALLDHVLNGSCFQGLPSPQYFVDFVFRQLSSKPRNITLPELEDLMHHLGVGGEDHSDHGDHVDHSHLDREANHQDSELHATHNSSSSVWDTLCLSAKDVMAVYGLSEEAGVSPQAWAQLTPALVQQQLSEACSSSPIIHVQDQLSQAERYLYGSLATLLICLCAVFGLLLLTCAKCSTATHYIMQTFLSLAVGALTGDALLHLIPKVLGLHTHSGEVHSHEEESIGGQSTWRLLAVLGGFYIFFLFESFFNLLLPRDQDHEKDGPCSHGGHSHGISLQLSPSNLRQSKQPHESSRSDLVTEETPELLNPDTRRLRAELRMLPYLITLGDAVHNFADGLAVGAAFSSTWKTGLATSLAVFCHELPHELGDFAALLHAGLTVKRALLLNLASALTAFAGLYVALAVGVGEEGETWILAVATGLFLYVALCDMLPAMMNVRDQRPWLLFLLHNVGLLGGWTILLLLSLYEDSITF
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Selective transporter that mediates the uptake of Zn(2+). Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability. Exhibits also polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(2+) but at higher concentrations (By similarity).
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A0JPN4
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ZC12A_RAT
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Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A)
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MSDPCGKKLVQEISPTMSLWGLEDRHSCQGQPQPDQDPVAKEASASELQMKVDFFRKLGYSSSEIHSALQKLGVQADTNTVLGELVKHGSATERECQASTDPCPQPPLVPRGGSTPKPSTVEPSLPEEDKESSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGVVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLPSEHRKQPCPYGRKCTYGIKCRFFHPERPSRPQRSVADELRANALLSPPRTPVKDKSSQRPSPASQPNSMSLEAEPGSPDGKKLGTRSSPGPHQEGSTQTCAPAGRSLPVSGGSFGPTEWLPHTLDSLPYTSQECLDSGIGSLESQMSELWGLRGGSPGESGPTRGPYTGYQTYGSKLPAAPAFSPFRQAIGTGHFSVPTDYVPPPPTYPAREYWSEPYPLPPPTPVLQEPQRPRPRASGDPWGRVSDLAKERAGVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHLSE
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Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay. Modulates the inflammatory response by promoting the degradation of a set of translationally active cytokine-induced inflammation-related mRNAs, such as IL6 and IL12B, during the early phase of inflammation. Prevents aberrant T-cell-mediated immune reaction by degradation of multiple mRNAs controlling T-cell activation, such as those encoding cytokines (IL6 and IL2), cell surface receptors (ICOS, TNFRSF4 and TNFR2) and transcription factor (REL). Inhibits cooperatively with ZC3H12A the differentiation of helper T cells Th17 in lungs. They repress target mRNA encoding the Th17 cell-promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The cooperation requires RNA-binding by RC3H1 and the nuclease activity of ZC3H12A (By similarity). Together with RC3H1, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR (By similarity). Self regulates by destabilizing its own mRNA. Cleaves mRNA harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-dependent manner (By similarity). Plays a role in the inhibition of microRNAs (miRNAs) biogenesis (By similarity). Cleaves the terminal loop of a set of precursor miRNAs (pre-miRNAs) important for the regulation of the inflammatory response leading to their degradation, and thus preventing the biosynthesis of mature miRNAs (By similarity). Also plays a role in promoting angiogenesis in response to inflammatory cytokines by inhibiting the production of antiangiogenic microRNAs via its anti-dicer RNase activity (By similarity). Affects the overall ubiquitination of cellular proteins. Positively regulates deubiquitinase activity promoting the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains on TNF receptor-associated factors (TRAFs), preventing JNK and NF-kappa-B signaling pathway activation, and hence negatively regulating macrophage-mediated inflammatory response and immune homeostasis (By similarity). Induces also deubiquitination of the transcription factor HIF1A, probably leading to its stabilization and nuclear import, thereby positively regulating the expression of proangiogenic HIF1A-targeted genes. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (By similarity). Prevents stress granules (SGs) formation and promotes macrophage apoptosis under stress conditions, including arsenite-induced oxidative stress, heat shock, and energy deprivation. Plays a role in the regulation of macrophage polarization promotes IL4-induced polarization of macrophages M1 into anti-inflammatory M2 state. May also act as a transcription factor that regulates the expression of multiple genes involved in inflammatory response, angiogenesis, adipogenesis and apoptosis (By similarity). Functions as a positive regulator of glial differentiation of neuroprogenitor cells through an amyloid precursor protein (APP)-dependent signaling pathway (By similarity). Attenuates septic myocardial contractile dysfunction in response to lipopolysaccharide (LPS) by reducing I-kappa-B-kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial pro-inflammatory cytokine production (By similarity).
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A0JPQ4
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TRI72_RAT
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Tripartite motif-containing protein 72 (Mitsugumin-53) (Mg53)
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MSTAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPADDGTVACPCCQASTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKAQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGEAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPELEELTFDPSSAHPSLVVSASGRRVECSEQKAPPAGEDTCQFDKTVAVVAKQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLTFYDASNTDALTPLFSFHERLPGPVYPMFDVCWHDKGKNSQPLLLVGPDSEQA
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Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).
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A0JQ18
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SOP14_ARATH
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Serine rich endogenous peptide 14 (AtSCOOP14) (Phytocytokine SCOOP14) (Precursor of serine rich endogenous peptide phytocytokine 14) (Secreted transmembrane peptide 2)
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MAAKTSNLVALLLSLFLLLLSISSQVGLGEAKRNLRNNLRLDCVSHPSPPPPHRSMAPPIFVPPSTSHKGQGP
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Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation. Inhibits root growth and regulates root meristems. Prevents general growth and development. Exhibits antibacterial effects against Pseudomonas syringae pv. tomato DC3000, Ralstonia solanacearum, Bacillus subtilis and Agrobacterium tumefaciens, thus being an antimicrobial peptide (AMP).
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A0KEL1
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FADB_AERHH
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQGETLTVSYLEDGIAELRFDAPGSVNKLDRATLLSLSEAIAALQQERELKGLILTSGKDAFIVGADITEFLELFDLPQADLLGWLKKANDIFSAIEDLPVPTLSAIKGHALGGGCETILSTDFRLADTSAKIGLPETKLGIMPGFGGTVRLPRVIGADNALEWITTGKDYRADDALKVGAIDAVVAPDALQSAAVQMIKDAVKGKLDWQGRRAAKKAPLRLSKLEAMMSFTTAAGMVAAVAGKHYPAPMTAVKTVEAAAGMSRDEALAVEAQGFIKLAKTDVAKALVGIFLNDQHIKALAKKAAKQAAKATSHAAVLGAGIMGGGIAYQSASKGIPAVMKDINEKALALGMGEATKLLNGQLEKGRIDGIKMGQVLSAITPTLSYDNVKHVDVVVEAVVENPKVKAAVLGEVEGIIGEDAVLASNTSTIPISLLAKELKRPQNFCGMHFFNPVHRMPLVEIIRGEQTSDETINRVVAYAAAMGKSPVVVNDCPGFFVNRVLFPYFFGFNKLVADGADFAAVDKVMEKEFGWPMGPAYLLDVVGIDTGHHAGDVMAQGFPARMSKEGRTAIDVMYEVNRFGQKNGKGFYAYEQDKKGKPKKVADAASYELLAPIAKPKQDFDKDAIIARMMIPMINEVVLCLEEGIVATPAEADIALVYGLGFPPFRGGVFRYLDTIGLDRYVAMADQYADLGPLYRVSDKLREMAAQGKTFY
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A0KLG5
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BSR_AERHH
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Broad specificity amino-acid racemase (EC 5.1.1.10) (Broad spectrum racemase)
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MHKKTLLATLILGLLAGQAVAAPYLPLASDHRNGEVQTASNAWLEVDLGAFEHNIQTLKDRLGDKGPKICAIMKADAYGHGIDLLVPSVVKAGIPCIGIASNEEARVAREKGFTGRLMRVRAATPAEVEQALPYKMEELIGSLVSAQGIADIAQRHHTNIPVHIALNSAGMSRNGIDLRLADSKEDALAMLKLKGITPVGIMTHFPVEEKEDVKMGLAQFKLDSQWLLEAGKLDRSKITIHAANSFATLEVPDAYFDMVRPGGLLYGDSIPSYTEYKRVMAFKTQVASVNHYPAGNTVGYDRTFTLKRDSWLANLPLGYSDGYRRALSNKAYVLIQGQKVPVVGKTSMNTIMVDVTDLKGVKPGDEVVLFGRQGEAEVKQADLEEYNGALLADMYTIWGYTNPKKIKR
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Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes ten of the 19 natural chiral amino acids known, including both non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino acids (His, Lys and Arg). Is not active on negatively charged (Glu and Asp) or aromatic (Tyr, Trp and Phe) amino acids and displays minimal activity towards beta-branched aliphatic (Ile, Val and Thr) substrates. Enables bacteria to produce and release extracellular non-canonical D-amino acids (NCDAAs) that regulate diverse cellular processes (By similarity).
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A0KR50
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FADB_SHESA
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIQVELLEDNIAKLCFNAPGSVNKFDRETLASLDAALDSIKQQSNIQALVLTSGKDTFIVGADITEFLGLFAQDDAVLLSWIEQANAVFNKLEDLPFPTASAIKGFALGGGCETILATDFRIADTTAKIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITTGKDQRPEDALKVGAVDAVVAPEALEAAAIQMLKDAVAEKLDWQARRQRKMSPLTLPKLEAMMSFTTAKGMVFAVAGKHYPAPMAAVSVVEQAATKGRSDALQIEHQAFIKLAKTDVAKALIGIFLNDQLVKGKAKKAGKLAKDVKSAAVLGAGIMGGGIAYQSASKGTPIVMKDIAQPALDLGLGEAAKLLSAQVARGRSTPEKMAKVLNNITPALDYAPVKHADVVVEAVVEHPKVKAQVLAEVEQYVSEDAIIASNTSTISINLLAKSMKKPERFCGMHFFNPVHKMPLVEVIRGEHSSEETIASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFNGLLAEGGDFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMAEGFPDRMGKSGNDAIDVMFENKRLGQKNGKGFYAYSVDSRGKPKKDVDPTSYELLKAAFGEQKAFDADEIIARTMIPMIIETVRCLEEGIVASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRALAANNGSYYQA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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