accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
P11860
|
PHI3_MYTCA
|
PL-IV
|
Mytilus
|
AKAKRSPRKKKAAVKKSSKSKAKKPKSPKKKKAAKKPAKKAAKKK
|
Involved in nuclear basic protein transition: histones are replaced by spermatid specific proteins which are themselves replaced by protamines in late spermatids.
|
P11860
|
P25824
|
KAD_SCHMA
|
Adenylate monophosphate kinase
|
Schistosoma
|
MTDQKLAKAKVIFVLGGPGSGKGTQCEKLVQKFHFNHLSSGDLLRAEVQSGSPKGKELKAMMERGELVPLEVVLALLKEAMINWLTKIVISLSIRYPRELDQGIKFEKEVCPCLCVINFDVSEEVMRKRLLKRAETSNRVDDNEETIVKRFRTFNELTKPVIEHYKQQNKVITIDASGTVDAIFDKVNHELQKFGVK
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
P25824
|
O49513
|
RAA1E_ARATH
|
Ras-related protein RABA1e
|
Arabidopsis
|
MGAYRADDDYDYLFKLVLIGDSGVGKSNLLSRFTRNEFSIESKSTIGVEFATRSVHVDEKIIKAQLWDTAGQERYRAITSAYYRGAVGALLVYDITRHITFENVERWLKELRDHTDANVVIMLVGNKADLRHLRAVPTEEARSFSERENMFFMETSALDATNVEQAFTHVLTQIYRVMSRKALDGTGDPMSLPKGQTIDIGNKDDVTAVKSSGCCSG
|
Intracellular vesicle trafficking and protein transport.
|
O49513
|
Q6P4S2
|
SHIP1_XENLA
|
SH2 domain-containing inositol 5'-phosphatase 1
|
Xenopus
|
MSYGWYHGNITRSKAEDLLSQAGKDGSYLVRDSESVCRAYALCVLNQNCVHTYRILQNAEHQLSVQASEGVPMRFFTNLVELIEFYRRENVGLVTHLQYPIEKEEEGPEEPDEEQEPAPPNVPPRNFAFTPPSETKECQTAIERAPAANASLLLSETLLQRFQDTDSRCIPEEHLQAICDYFSLHIVSDCDMVRTGSQTLPQFKKLLMTLCTGLHRELTRTLPTLESLQVAIDPQLSPGFKQRSPLPGDSATNNMVNKLTHLTSMVSNLEEKVKTVLMEGAAVKHRRSLIPPIIFEVKADSIGISQKTHLKVDVETGKLIIKKSKDGPDDKFYPSKKILQLIKSQKFPHKLVIVLETEKEKTQRKEYVFADSKKREGFCQLLQQMKNKHSGQSEPDMLSIFIGTWNMGDAPPPKNITPWFQCKGQGKTRDDTADYIEHDIYVIGTQEDPLSEKEWTDTLIHSLREITSVEYKVITTQTLWNIRIVVLAKPEHAHRISHVCTNSVKTGIANTLGNKGAVGASFMFNGTSFGFINSHLTSGSEKKLRRNQNYFNILRFLVLGDKKLSPFNFTHRFNHLFWLGDLNYRLQLPNTEAENIIQKIKQQQHQELLPHDQLNLERRESLIFFQFHEEEITFPPTYRYERGSRERYCYTKQKATGIKYNLPSWCDRILWKSYPQMHILCQSYGCTDDITTSDHSPVFGTFQVGVTSQFVSKNNPGDSGDLEAQGHIELMNCKATLYTKSHTKFYIEFHSPCLENMVKSSEAEDQEGNNGTLVVKFGVLPKLTPIISDLEYLLDQHLLICIKSSDTDESYGEGCIALRKEDTEQQFPFCTILTHHGEETGLFCGEICLPASGGKQREKLYDFVKIEKDETVAQKQLKHPYSQSMEQSRIMKSISEKSAMIARMRAAPETQNSMDHTASVAAISSQAKQSPPTTPPGFRGSEPRQKPGSPVQGRGDTPITSPPRTTLSTQKFSHSNTNRTAPAARPQDSLQITVPSDPHEMVDNPLYGPVNNTLYPPTA
|
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. Able also to hydrolyzes the 5-phosphate of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P3) and inositol 1,3,4,5-tetrakisphosphate. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells.
|
Q6P4S2
|
Q9KRD8
|
METE_VIBCH
|
Methionine synthase, vitamin-B12 independent isozyme
|
Vibrio
|
MTTTHILGYPRIGEKRELKFALEKYWRGEIDQAALKQVGSQIRQKNWALQKEAGLDFVTAGDFAWYDHVLTTTLLLGHVPKRHSHGFPDLDTLFRVGRGQSQNACGCGTGSAASDMTKWFNTNYHYIVPEFSSNDTFNVSWPQLFEEVNEALQAGHDVKPVLLGPISYLYLGKEVEEGFDRLTLLPRLLTAYQAILSKLAKQGVQWVQIDEPILALELEPRWQEAFKLAYQVIRGDVKLLLTTYFDSVLDTLDKIVELPVDGLHVDISAAPAQLETIVNRLPSDWVLSAGVINGRNVWRADLSAILARLQPVKTLLGERLWVASSCSLLHSPVDLDLEGDLSAETRSWFAFAKQKVTEVALLGRALEGDAAAILACDTYSQPIVARKSSHIVNKASVQTRINNITAALAERSAPYIERAHHQAEVLGLPFLPTTTIGSFPQTGEIRTERSAYRQGKLSEQEYVQALKGHIADAVKRQEALGLDVLVHGEAERNDMVEYFAENLAGFQTTQFGWVQSYGSRCVKPAIVVADIEREKPITVEWSTYAQSLTSKQMKGMLTGPVTILCWTFPREDISRQEIAQQLALALRDEVADLQDAGINIIQIDEPAIREGLPLKKRDHQTYLDWAVQAFKISAGSARPETQIHTHMCYSEFNEIIESVAALDADVITIETSRSNMELLKAFEEFNYPNEIGPGVYDIHSPNIPAQAWIEDLLRKAAEKIPAQRLWVNPDCGLKTRNWPEVEAALTNMVNAAKALRAEWQA
|
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
|
Q9KRD8
|
Q8A1E0
|
ISPT_BACTN
|
Isoprenyl transferase
|
Bacteroides
|
MSYIEKIDKNRIPQHIAIIMDGNGRWAKQRGKERTYGHQAGAETVHKIIEDAARLGVKYLTLYTFSTENWNRPQEEVAALMNLLVDSIEEETLMKNNIRFRIIGDIKKLPAEVQEGLSRCIEHTANNTGTCLVLALSYSSRWEMTEAVRQIATLAKTGEISPEQITDEYITAHLTTNFMPDPDLLIRTGGEIRLSNYLLWQCAYSELYFCDTFWPDFDKEEFCKAIYEYQQRERRFGKTSEQIS
|
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
|
Q8A1E0
|
B5RH05
|
TUSC_SALG2
|
tRNA 2-thiouridine synthesizing protein C
|
Salmonella
|
MKRIAFVFSTAPHGSASGREGLDALLATSALTEALGVFFISDGVFQLLPGQKPDAVLARDYIATFKLFDLYDIDQCWICAASLRERGLESVNFVVDATPLEPVALRRELGNYDVILRF
|
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
|
B5RH05
|
Q7NB11
|
POTA_MYCGA
|
Spermidine/putrescine import ATP-binding protein PotA
|
Mycoplasma
|
MEDKVFIQLRNVNKTFDDGFVAVRNLNLDINKSEFVTLLGPSGCGKTTTLKLLAGFEQPTYGQIKINGIDIKDMPVHKRPFATVFQDYALFPNMTVYNNVCYGLKIMRVPKENTDPKLAVEAENIKKEAEKKAAAKIKDLSRKKNDLSNKLDKIRKEYEKNDWMLENDEMRFAQYQEELIKLEAQLSEAYEQSEINKLNQEIVELKTNYQKKIPIDNRYDKVLKELENADGWTSYWETYPIMKKEHFENKVLTRRLTKKEIEERANNMIKLVGLTGKEDKYPSELSGGMQQRVALARALVIEPETLLLDEPLSALDAKVRKQLQNELKRIHKELNITFILVTHDQEEALSLSDKIVVMSQGDIEQVGKPNAIYDSPINEWTAKFIGAANIFDGKYLGDYKIELNSGDIIDTDEEYEFKKGDNVRVLIRPEDFDVVEKDQGFFNVEVIKTSYKGVLWEVECLMSDKTKIKVDNIDEVKVGAIVGLKFDEMDVHMMRKEEEDV
|
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
|
Q7NB11
|
Q02LM8
|
KYNB_PSEAB
|
N-formylkynurenine formamidase
|
Pseudomonas
|
MTSLRYWDISPALDPSTPTWPGDTPFQQEWAARLDEQCPVNVGRITLSPHTGAHVDGPLHYRADGLPIGQVPLDIYMGPCRVIHCIGANPLVTPEHLAGQLDDLPSRVLLRTFERVPANWPEGFCAIAPATIECLAERGVRLVGIDTPSLDPQHSKTLDAHHAVGRHGMAILEGVVLDDVPAGDYELLALPLKFTHLDASPVRAVLRALPTAE
|
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
|
Q02LM8
|
B4TUC9
|
NADE_SALSV
|
NH(3)-dependent NAD(+) synthetase
|
Salmonella
|
MTLQQEIIQALGAKPHINPEEEIRRSVDFLKAYLKTYPFLKSLVLGISGGQDSTLAGKLSQMAIAELREETGDNALQFIAVRLPYGVQADEQDCQDAIAFIQPDRVLTVNIKGAVLASEQALREAGIELSDFVRGNEKARERMKAQYSIAGMTHGVVVGTDHAAEAITGFFTKYGDGGTDINPLHRLNKRQGKQLLAALGCPEHLYKKVPTADLEDDRPSLPDEAALGVTYDNIDDYLEGKTLDPAIAKTIEGWYVKTEHKRRLPITVFDDFWKK
|
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
|
B4TUC9
|
B0TBM6
|
BCHL_HELMI
|
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
|
Heliomicrobium
|
MIIAVYGKGGVGKSTTTSNLAVAIAKTGRRVLQIGCDPKSDSTFTIAGRMIPTVVEILDKFNYHYESIEPDDLVVQGYAGVCVVETGGPPAGSGCGGYVVGETVKLLEKLDIMRQYDVILFDVLGDVVCGGFATPLQYADLACIVSSNDFDALFAANRICESIVEKNASGYDVKLAGVIGNRCDQVDLLETFTRRIEAPLMGVVPRNEEVRQSRVKGYTLFELEEMGEPVSEMTGEFRKMAAYLLSQPDGVVPNAVGTREMFELFRGEDLPWKGSNGKTAASTPSVP
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
|
B0TBM6
|
A4FWK8
|
RPO10_METM5
|
DNA-directed RNA polymerase subunit N
|
Methanococcus
|
MIFPIRCFSCGAVISEVYEEYRTRLKNGENPEEILNDLEVKKYCCRRMFASHRLDNDRELFDDIVEYK
|
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A4FWK8
|
A0A286LEZ9
|
PSIR_PSICY
|
Psilocybin cluster transcription regulator
|
Psilocybe
|
MAPTTPATHDPALSHGAPPTQGSQAPANAAPNLTPADISGMQLNGLDQSQIMNLLRSLPGMFTGAKIPDQGQGNPKEDAAQTLSNLAQASSPFGGQHLPIHYQTGAAGGLPGINDPGPSTHPRGPPNLGQLSAVAMQAAPATIQHQDQQQSGRQEDGEQAGNTSIDSPSAKDGENGTGEFNQTSTSTPSGGRRGGRSATMGSDEWSRQRKDNHKEVERRRRGNINEGINELGRIVPSGSGEKAKGAILSRAVQYIHHLKENEARNIEKWTLEKLLMDQAMGDLQAQLEEIKRLWEEERMARTRLEAELEVLRNMNGVSTAGAGSGAAKDESAAGTKRRSTDGADAAGTNVEGGNNDNAEGERDGKRQRTE
|
Transcription factor that may regulate the expression of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product.
|
A0A286LEZ9
|
P45483
|
FTSZ_BORBU
|
Cell division protein FtsZ
|
Borreliella
|
MKDYNMIDSHTRRFDSTTNPTILKVIGAGGGGSNAVNRMIEYGVRDVEFIVANTDLQALQTSIAPIKIALGAKVTAGLGAGGKPEIGQAAAEEDIDVIRNHLSGADMVFITAGMGGGTGTGAAPVIAQVAKELGILTVGVVTKPFKFEGPKKLRLAEQGINNLRKSVDTLIIIPNQKLLTVVDKRTTIKDAFKRADDVLRMGVQGIAGLIIEHGEVNIDFADVKSIMQGQGDALMGIGYGKGENRAVDAATSAISNPLLEEVRIEGSKGLLVNVTGGDDFSLLELEEIMGIITVSVDDEATVIYGHAINSNLEDEIYVTVVATGFASKKQKEISSTPENNTLSSKEFDTLMSGNQNAPSGSYEQQDSSFAAKSKNVNYFDDDIDVPTFLRNLNKKSSDD
|
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
|
P45483
|
Q88VR2
|
END4_LACPL
|
Endonuclease IV
|
Lactiplantibacillus
|
MLRLGSHVSMKAPDMLLGSANEAASYGANTFMIYTGAPQNTRRKPIDELKIDEAQPIIEAHDLRQIVVHAPYIINLGNTKKPGYFEFATDFLYQEIQRADAVGATQLTLHPGAHIGAGANVAITQIIKGLNAVIRPEQHVQIALETMAGKGTEVGRTFEELAQMIDGVTYNEKLSVTFDTCHTSDAGYAIKDDFDGVLNEFDHVIGLDRLKVIHLNDSKNPQGAHKDRHTNIGMGTIGFDTLNKVAHHPQLPDISKILETPYVGEDKKHQLPPYKYEIAMLRAGQFNPHLIEDIEQQR
|
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
|
Q88VR2
|
Q5HRM9
|
MCSB_STAEQ
|
Protein-arginine kinase
|
Staphylococcus
|
MMSNIHTNISEWMKMSEETPVIISSRIRLARNLENHVHPLMFPSEQEGYRVINEVQDALSNLTLNRLDTMDQQSKMKLVAKHLVSPELVKQPASAVMLNDDESVSVMINEEDHIRIQALGTDLSLKDLYQRASKIDDELDKALDISYDEHLGYLTTCPTNIGTGMRASVMLHLPGLSIMKRMNRIAQTINRFGFTIRGIYGEGSQVYGHIYQVSNQLTLGKTEEDIIDNLTEVVNQIINEEKQIRERLDKHNSVETLDRVYRSLGVLQNSRIISMEEASYRLSEVKLGIDLNYILLENFKFNELMVAIQSPFLIDDDDNRTVNEKRADLLREHIK
|
Catalyzes the specific phosphorylation of arginine residues in proteins.
|
Q5HRM9
|
A7MXU9
|
HEM3_VIBC1
|
Pre-uroporphyrinogen synthase
|
Vibrio
|
MTQSTPIRIATRKSPLALWQAHFVKDALQAAHPGLEVELVTMVTKGDIILDTPLAKVGGKGLFVKELEVAMLEGRADLAVHSMKDVPVDFPEGLGLVTICEREDPRDAFVSNTYNNIDELPQGAVVGTCSLRRQCQLKEYRPDLVIKELRGNVGTRLGKLDAGEYDAIILAAAGLKRLELEERIRSFIEPEQSLPAVGQGAVGIECRVDDERLLKLLEPLNHQDTADRVRCERAMNLTLEGGCQVPIGSYSLLDGDNIWLRALVGEPDGSLIVRGEIRGHRNDAEALGVQLANELLENGARDILTKLYADHE
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
A7MXU9
|
C5DBT1
|
GET2_LACTC
|
Golgi to ER traffic protein 2
|
Lachancea
|
MSEISDAEKRRILREKRQQKFNKGGASSRLAKITGQTENSFLSTESPLDSRESTYPAQETKAPAGNEDSTKQMDELLAKATSKTTSKASSPPGSAEQQNGNPELDLFAQIAKLQQNANNETVSTDPSGTPDIFAQLMASMQQDEAKGGSPGATAQQPIDPAIVEAHNIAVNKLKSYTILVKWLFFLLPYLYYITHSARDPFQHNAVNYVLDRSNFFTVFTTFEIVALSVYYQLLMSAEKSHNVNTLDNNSKILKLVSMVPPGLVPIPNLRGKVAQALQYWDVVSMYLTDLCFAIVLAGLFQYYHSM
|
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET1, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER.
|
C5DBT1
|
Q6GHY0
|
MNTH_STAAR
|
Divalent metal cation transporter MntH
|
Staphylococcus
|
MNNKRHSTNEQLSLDEINNTIKFDHRSSNKQKFLSFLGPGLLVAGGYMDSGNWITSMQGGAQYGYTLLFGNLISRLSAMLLQSMTVRLGIATGMDLAQMTRHYLSRPIAIIFWIIAELAIIATDIAEVIGSAIALNLLFNIPLIVGALITVLDVFLLLFIMKYGFRKIEAIVGTLIFTVLFIFIFEVYISSPQLNAVLNGFIPHSEIITNNGILYIALGIIGATIMPHNLYLHSSIVQSRTYSRHNNEEKAQAIKFATIDSNIQLSIAFVVNCLLLVLGASLFFNSNADDLGGFYDLYHALKTEPVLGATMGAIMSTLFAVALLASGQNSTITGTLAGQIVMEGFLRLHIPNWLRRLITRSLAVIPVIVCLIIFKGNAAKIEQLLVFSQVFLSIALPFCLIPLQLATSNKDLMGPFYNKTWVNIISWTLIIILSILNVYLIVQTFQELQG
|
H(+)-stimulated, divalent metal cation uptake system.
|
Q6GHY0
|
P50478
|
AMPH_CHICK
|
Amphiphysin
|
Gallus
|
MADMKTGIFAKNVQKRLNRAQEKVLQKLGKADETKDEQFEEYVQNFKRQEAEGSRLQRELRAYLAAIKGMQDASKKLTESLHEVYEPDWYGREDVKMIGEKCDELWEDFHQKLVDGSLLTLDTYLGQFPDIKTRIAKRSRKLVDYDSARHHLEALQSSKRKDEGRITKAEEEFQKAQKVFEEFNTDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIALLCHKLYEVMTKLGDQHADKAFTIQGAPSDSGPLRIAKTPSPPEEVSPLPSPTASPNHMLAPASPAPARPKSPTQLRKGPPVPPLPKLTPTKELQQENIINLFDDNFVPEINVTTPSQNEIPETKKVESLLDLDFDPFKPEVVSTGVTHSPMSQTLPWDLWTTTSELVQPASSTAFNGFAQDTTAFAVQSNENVTETLTEAEEAPLGELKVEETPTAAVVEKEAILAEPDEPTEQAAESIEAGDKETTGIAEKESEVVSAAGGAVAVEDSVVVAAGAGEGAVRTEQEAAAEGDKPQGEEKDVDVSQEKVSSIPSVVIEPASNNEGEGEEHHVIMNESKDAAAEMGTQGTDSETSQIGSEQKATEEIQTTPSQDQPASAGDTASDMPPGFLFKVEVLHDFEAANSDELNLKRGDIVLVIPSETTADQEAGWLTGIKESEWLQYRDANSYKGLFPENFTRHLE
|
May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.
|
P50478
|
Q92X16
|
PDXA2_RHIME
|
Putative D-threonate 4-phosphate dehydrogenase
|
Sinorhizobium
|
MSKIIGITMGDPCGVGPEITVRSLAEMSAADREATRIYGNLATLEAAREALGLSVDLQPYVVDLTVEGAPLPWGSLSAVAGDAAFRFIERAVRDAEAGNIGCIVTAPINKEALNMAGHHYDGHTGMLRSLTGSSAAYMLLASERLKVIHVSTHVSLKEAIGRATTERVLATIRAGNAHLKRIGYEHPRIAVAGINPHCGENGLFGTEDDDQIGPAVAAAREEGIDVQGPISADTVFHRAYSGGFDLVVAQYHDQGHIPIKLVAFDTAVNVSVDLPIDRTSVDHGTAFDIAGKGIANHGNLNSAIAYARKLVAGQASRKAAS
|
Catalyzes the NAD-dependent oxidation and subsequent decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone phosphate (DHAP).
|
Q92X16
|
Q60BS1
|
TRMD_METCA
|
tRNA [GM37] methyltransferase
|
Methylococcus
|
MRFDIVTLFPEMVRDAARYGVTGRALAAGKVSLEVWNPRDFTRDRHRTVDDRPYGGGPGMVMKVEPLRDAIRAAKGQATPGARVVLMSPQGTRLDQAAVRRFAAAPGLILVAGRYEGVDERLIETEIDEEWSIGDYVLSGGELPALVVFDAVVRLLPGVLGDAESAEQDSHAEGLLDHPHYTRPERVAGRDVPAVLQSGNHAAIGRWRLKQALGKTWLKRPDLLACRVMTPEQLELLDEFKREFELQKNRG
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q60BS1
|
Q9DEX1
|
CAO1A_XENLA
|
Protein Xdsg
|
Xenopus
|
MELILYVCKKVNIMENISQPQLPMGVSFLNVAHTYVPNTKVECHYTIPFGMKSSTRDWIGIFKVNTSSIRDYETFVWAVPPENAGERSISHCSVQFQAYYLPHPGEQQYHFRYVDQCGSVRGCSEAFVFGEPQPMEEMVTLEDEDSCLDMLLIVPKATFLQNQLEMAQKERNDLMRARLALEEEVISKEKRICYLEAALDISEKTCFSLKEQCEDLVTREQIAIGERNLLNCQEAELRERILQLESEIQSMNKKMQENDRVLEGTVAIKFSLETEKGELKQRLGETTVEIERYQLQVDSLREKLRSSQDMLSSSQQKALLMGEELASMSSIRDCTISDLHKSRLETADLAIKVSDLSVKFKEGMGQWWQEKTALNHSMEAKRDQIVNLKAEKLSLDNSLQEERSQRHALQCKLNQETDARQVQLSENRRELSELKSALKVTQMEKEQLIEERQEIHQYVRRLEERLDKLADEKWKEDKMLMEDKTDSSPPTLSVDLSDSDDESPGDEGVSQQLGPCSLDEQDLSLNLPVFPCEPQKVVINQPAPIACQLQPLPEDNPDSW
|
May function as a coactivator for aryl hydrocarbon and nuclear receptors.
|
Q9DEX1
|
Q09437
|
CD111_CAEEL
|
Cyclin-dependent kinase 11.1
|
Caenorhabditis
|
MSDHLGSSHDEGELSDESHKKSQRASSSDEPNPAKSNKGLESKMRESILSRLSKRKNSESDDDTTEQRFSIQPKNAQKAKEDRYRDKERDKKREKDKRDDRRDVRGPDARQKDRDFKGRQERSGRDQKVHEHRHHHHHRKHETDGHRTNRSNRDRSSERDSEKHKRHIDRHKKSSTTSPDNDKSPHKKSKHTDVPADAKLFDRILDPNYKKKDDDVLVIEDVEMSPIEILEEKEEKEIVEFTIDSPAGPKKYSKFESDPESDHDDTKPKSPGKAEDDDDVIEVLDDALHSDDDADSDEDKYLKTPEDREWEEMTETEQRLHKEAMKKRASMKQKTLIAQLPVFYPGLMGCRNIDEYECVNRVDEGTFGVVYRGKDKRTDEIVALKRLKMEKEKEGFPITALREINMLLKAGNHPNIVNVKEILLGSNMDKIYMAMEFVEHDMKSLLDTMSRRNKRFSIGEQKTLLQQLLSGIEHMHKLWILHRDLKTSNLLMSHKGILKIADFGLAREYGDPLKKFTSIVVTLWYRSPELLLGTRLYSTPVDMWSVGCIMAEFILLKPLFPGRGELEQIKKIFMEMGTPTESIWPGVTELDGWKALTFEKYPYNQLRKRFLAGRLLNDTGFKLLNGLLTLDPKNRFSATQALDHEWFTEEPYPVPPEEFPTFPAKSEQNKAPPPAKQKQQENRISHVDPETAKLLKQFEVRPEQVKPGGFSLKFDPTRF
|
Probable cyclin-dependent kinase whose activity is most likely regulated by the cyclin cyl-1/Cylin-L . Important for normal oocyte and sperm development; probably required during multiple stages of gametogenesis . Plays a role in the activation of RAS-ERK signaling in the germ line . Also acts partially redundantly with cdk-11.2 to ensure embryonic viability .
|
Q09437
|
C0HL90
|
LEC2_SOLFI
|
Lectin SfL-2
|
Solieria
|
GRYTVQNQWGGSSAPWNDAGVFVLGGRANQNVMAIDVSSSDGGKTLTGTMTYSGEGPIGFKGTRRGESNNYEVENQWGGSSAPWHPAGTFVIGSRSGQAVVAMNVTSHDGGKTLSGHMTYENEGPIGFKGTQAEGDTYNVENQWGGSSAPWNKAGVWALGSRASQGVVKLDVSSSDGGKTLTGTMQYQNEGPIGFRGTLTGANNYKAENQWGGSSGAWNPAGLWLIGDRHNQNIIGVKVTSDDNGKTLEGTCTYYREGPIGFKGVAN
|
Lectin specific for high mannose N-glycans, recognizes the branched moiety of these glycans. Does not recognize other types of N-glycans or monosaccharides.
|
C0HL90
|
Q1D768
|
RL16_MYXXD
|
50S ribosomal protein L16
|
Myxococcus
|
MLQPARTKYRKMHKGRMPGSAHRGSDMTYGEYGLMSLQPGWITSRQIEAARIAMTRHVKRGGKIWIRIFPDKPITKKPAETRMGTGKGGVEYYVAVVKPGRILYEMEGMTPEVATGALKLAQAKLPVLTKIVKRADLSL
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q1D768
|
B3DVR2
|
NADD_METI4
|
Nicotinate mononucleotide adenylyltransferase
|
Methylacidiphilum
|
MIKKTTSFRLAIFGGSFDPIHYGHLICAMDCLEQISLNKIIFMPCSRSPFKKQNPVASALQRLEMIQLAIKPFKNFEVSSFEVQSPAPSYSIRTVQEFHKLYPHAELFWIIGSDQVPGLPRWKDYAELIQIVKFIVVSRSNYYPYEKRDYLVPLPKIRYVDISSTEIRERVKKELPIFHLLPQAVFQYIKENSIYIPNRTVHEK
|
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
|
B3DVR2
|
Q8DCU4
|
PURA_VIBVU
|
IMP--aspartate ligase
|
Vibrio
|
MANNVVVLGTQWGDEGKGKIVDLLTEDAKYVVRYQGGHNAGHTLVIDGVKTVLHLIPSGILRDNVKCVIGNGVVLSPEALIKEMKPLEERGIPVRERLFISEACPLILPYHVAMDQAREIARGKKAIGTTGRGIGPAYEDKVARRGLRVGDLFDMEAFAEKLKEVMEFHNFQLVNFYKAEAVSYEEVLEQARGYAELLTSMVIDVTDELDAARKRGDKIMFEGAQGTLLDIDHGTYPYVTSSNTTAGGVAAGSGFGPRYLGYILGIAKAYCTRVGAGPFPTELYDGQEKQDPVGKHLGTVGHEFGATTGRLRRTGWFDAVAMRRAIQINSVSGFCLTKLDVLDGLKELKICTGYQMEDGSVLEVSPMAAEAFEKVTPIYETMPGWSENTFGAKSLEDLPQAAINYIKRIEELTGVPVDIISTGPDRNETIVKVHPFES
|
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
|
Q8DCU4
|
O47040
|
PSAI_PICAB
|
Photosystem I reaction center subunit VIII
|
Picea
|
MIIPNLPSFFVPLVGLLLPAITMVIFHLYIQNDDIF
|
May help in the organization of the PsaL subunit.
|
O47040
|
B9JH39
|
DNLJ_AGRRK
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Agrobacterium tumefaciens complex
|
MSSEQKPVEDLTEEEAAAALAYLAAEIARNDALYHGNDAPEISDAEYDALKRRNDAIEARFPALVRADSPSRRVGAAPSETFMPVVHARPMLSLDNTFSQEDVQDFVAGVYRFLGRLPDQSIAFTAEPKIDGLSMSIRYENGRMVSAATRGDGTTGENVTANIRTIKEIPQTLPAGAPAVVEIRGEVYMAKSDFLALNAQMEAEGKQSYVNPRNTAAGSLRQLDAKVTASRKLKFFAYAWGEMSDMPADTQFGMVQAFGEWGFPVNPLMKRLNSVADILAHYDEIGLQRPDLDYDIDGVVYKVDSLELQARLGFRSRSPRWATAHKFPAEQALTRLLDIDIQVGRTGALTPVARLEPITVGGVVVTNATLHNADYIKGIGNKGEPIRDGRDIRIGDMVIVQRAGDVIPQIVDVVLEKREASSVAYEFPKTCPVCGSHAVRDINEKTGKVDAVTRCTGGFICRAQATEHLKHFVSRNAYDIEGLGSKQIDFFFESDDPALQVRTAPDIFTLERRQQSSLSKLENIDGFGKVSVSKLYAAINERRDIALHRFIFALGIRHVGETTAKLLARSYGTYEAFEAGMKEAAPLAGDAWNDLNNIEGVGEVVARAVVEFYKEPRNVEVISKLLDEVRPQEAEQPTTSGSPVVGKTVVFTGSLEKFTRDEAKAKAESLGAKVSGSVSKKTDIVVAGPGAGSKLDKAREFNVQVMTEDEWLELIGG
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
B9JH39
|
O26343
|
RFCS_METTH
|
MthRFC small subunit
|
Methanothermobacter
|
MIIMNGPWVEKYRPQKLDDIVGQEHIIPRLKRYVEEKSMPNLMFTGPAGVGKTTAALALAREILGEYWRQNFLELNASDARGIDTVRTSIKNFCRLKPVGAPFRIIFLDEVDNMTKDAQHALRREMEMYTKTSSFILSCNYSSKIIDPIQSRCAIFRFLPLKGHQIIKRLEYIAEKENLEYEAHALETIVYFAEGDLRKAINLLQSAASLGEKITESSIYDVVSRARPKDVRKMIKTILDGKFMEARDMLREIMVLQGISGEDMVTQIYQELSRLAMEGEVDGDRYVGLIDAIGEYDFRIREGANPRIQLEALLARFLEHA
|
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. The complex possesses DNA-dependent ATPase activity which is further stimulated by PCNA. In conjunction with PCNA stimulates DNA synthesis by PolB, relieving inhibition by replication protein A (RPA).
|
O26343
|
A2RCQ1
|
DPO4_STRPG
|
DNA polymerase IV
|
Streptococcus
|
MLIFPLINDTSRKIIHIDMDAFFAAVEERDNPALKGKPVVIGKDPRETGGRGVVSTCNYEARKYGIHSAMSSKEAYERCPKAIFISGNYEKYRTVGDQIRRIFKRYTDLVEPMSIDEAYLDVTDNKLGIKSAVKIAKLIQHDIWKEVGLTCSAGVSYNKFLAKLASDFEKPHGLTLVLKEDALCFLAKLPIEKFHGVGKKSVEKLHDMGIYTGQDLLAVPEMTLIDHFGRFGFDLYRKARGISNSPVKSDRIRKSIGSERTYAKLLYQETDIKAEISKNAKRVAALLQDHKKLGKTIVLKVRYADFTTLTKRVTLPELTRNAAQIEQVAGDIFDSLSENPAGIRLLGVTMTNLEDKVADISLNL
|
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
|
A2RCQ1
|
Q2FEZ8
|
COAW_STAA3
|
Pantothenic acid kinase
|
Staphylococcus
|
MKVGIDAGGTLIKIVQEQDNQRTFKTELTKNIDQVVEWLNQQQIEKLCLTGGNAGVIAENINIPAQIFVEFDAASQGLGILLKEQGHDLADYIFANVGTGTSLHYFDGQSQRRVGGIGTGGGMIQGLGYLLSQITDYKQLTDMAQHGDRNTIDLKVRHIYKDTEPPIPGDLTAANFGHVLHHLDADFTPSNKLAAVIGVVGEVVTTMAITVAREFKTENIVYIGSSFHNNALLRKVVEDYTVLRGCKPYYVENGAFSGAIGALYLEK
|
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
|
Q2FEZ8
|
P46600
|
HAT1_ARATH
|
Homeodomain-leucine zipper protein HAT1
|
Arabidopsis
|
MMMGKEDLGLSLSLGFAQNHPLQLNLKPTSSPMSNLQMFPWNQTLVSSSDQQKQQFLRKIDVNSLPTTVDLEEETGVSSPNSTISSTVSGKRRSTEREGTSGGGCGDDLDITLDRSSSRGTSDEEEDYGGETCRKKLRLSKDQSAVLEDTFKEHNTLNPKQKLALAKKLGLTARQVEVWFQNRRARTKLKQTEVDCEYLKRCVEKLTEENRRLEKEAAELRALKLSPRLYGQMSPPTTLLMCPSCERVAGPSSSNHNQRSVSLSPWLQMAHGSTFDVMRPRS
|
Probable transcription factor.
|
P46600
|
A0AKK8
|
PDXS_LISW6
|
Pdx1
|
Listeria
|
MEKKVGTDRVKRGMAQMQKGGVIMDVVNAEQAKIAEDAGAVAVMALERVPSDIRAAGGVARMADPRIVEEVMNAVSIPVMAKARIGHITEARVLEAMGVDYIDESEVLTPADDEFHLLKSDFTVPFVCGCRDIGEALRRIGEGAAMLRTKGEPGTGNIVEAVRHMRQVNGQIRQIVGMTDDELMVAAKNFGAPYELVKEIKSLGKLPVVNFAAGGVATPSDAALMMELGADGVFVGSGIFKSDNPAKFASAIVQATTYYTDYELIGKLSKELGSPMKGIEMSRLNPEDRMQDRSV
|
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
|
A0AKK8
|
A0A089FRP6
|
PRLG_FUNXX
|
Pyrrolocin biosynthesis protein G
|
Fungi
|
MSSTDAEAKNEEAVDWEGPDDPENPRNWNQGAKMTHVLLVSSFTLYSNLAAVMFAPGAQDLVAEFGITSTIVASLTVSIYILGYVFGPFLLASMSEIYGRLIIYHICNAVYIAFTIGCALSTDTAMFLVFRFICGCAASAPMAIGGGTIADLHKPEERGKAMALFGLGPLLGPVIGPVVGGFVTQFLGWRWTFWLVLILAGVVSLLALVLMRETFEPVLLTRKAAELRKSTGNYRLQARTYNKDLTPAQLLARATIRPTKMLLMSPIVFLLSVYCAFMFGLTYLLFTTFPAVFEETYGFAADVSGLAYLGLGVGMIISIGLFAVLSDKLLHQPHGGTIARPELRLILMIWSSPLVPIGFFWYGWSAKYEVHWIVPILGTSVIGLGAFLILMPAQLYLVDAFGTEAAASALAANTVLRSLFGAVLPLAGPSLYDSLGLGWGNSLLAFIGLAFAPVPFFFYKYGERLRVRFPVNS
|
Efflux pump that might be required for efficient secretion of pyrrolocin or other secondary metabolies produced by the pyrrolocin gene cluster .
|
A0A089FRP6
|
P00533
|
EGFR_HUMAN
|
Receptor tyrosine-protein kinase erbB-1
|
Homo
|
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA
|
(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.
|
P00533
|
Q8XQB8
|
NOSZ_RALSO
|
N2O reductase
|
Ralstonia
|
MMSKHPHSPSTPQDETPSVPGRRRFMNSAALAGLATVVACTDKGAPAGSAAATGVAATAEEHTVAGLHPKPGQLDTYYGLWSGGHTGDMRVMGMPSGREIHRIPMFVPDALVGWGITNESKKVMGTRPDGRLKYTVGDTHHVHASYKDGNYDGRYAWINDKINSRLGRVRLDYFICDKITELPNVQGFHGIFPDKRDPVDPQINYTTRVFCGGEFAIPLPNTAGIDDPAKYRSLFTCVDAESMEVRWQVLIDGNCDLVATSYDGKLAATNQYNTEMGAHYEDMMSAERDACLFFNVARIEAAVKAGRFKTIGDSKVPVVDGTHAANQDPKTALTAYVSVPKNPHGVNASPDQKYFICAGKLSPTATVIELARVLDWFDGKLAKIDDAIVAEVELGLGPLHTAFDGRGNAYTTLFLDSQIVKWNIDAAIRFHKGDKNAKYVVDRLDVHYQPGHLNASQSETVAADGKFLAVGCKFSKDRFLPVGPLHPENEQFIDISGDKMVLLQDHPIRSEPHDFIIFKRELLHPKQIYSLDDFPLATKDPKQSGVVRNGKKVTVRLTSQAPSYSLREFKLKKGDEVTLILTNLDKVEDLTHGFAIPKYDINFIVNPQETASVTFIADKPGVFWCYCTHFCHALHLEMRSRMIVEA
|
Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.
|
Q8XQB8
|
A0PM48
|
MFTB_MYCUA
|
Peptide chaperone MftB
|
Mycobacterium
|
MRGLLTVPAPAQAAAGAGAFDPDRGWRLHAQVAVRPEPFGALLYHFGTRKLSFLKNRTILAVVRSLADHPDVRSACRAAGVDDSEHAPYLHALSVLAGSHMLVPQEADQ
|
Peptide chaperone involved in the biosynthesis of the enzyme cofactor mycofactocin (MFT). Binds MftA and MftC with high affinity, and is essential for MftC activity on MftA, likely via the formation of a ternary complex.
|
A0PM48
|
B8GQD7
|
LEUD_THISH
|
Isopropylmalate isomerase
|
Thioalkalivibrio
|
MKPLTTVDGLVLPLDRSNVDTDAIIPKQYLKSVKRTGFGPNLFDDWRYLEPGEPGMDHSARKPNPDFVLNAPRYQGAEILLARKNFGCGSSREHAVWALTDYGIRVVIAPSFADIFFGNSFKNGLLPIVLDEAVVDRLFQEVEATEGYRLKVDLAEQTVTTPSGEAFPFEVGEFHKYCLLNGLDDIGLTLQHADEIRAYEQRRRAEAPWLFR
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
B8GQD7
|
Q2LSK9
|
CHED1_SYNAS
|
Probable chemoreceptor glutamine deamidase CheD 1
|
Syntrophus
|
MGDVIVSISDFRVSNNVGDILVTYALGSCIAVAIYDPKVKVGGLLHYMLPDSSLDVDKAKTTPGMFADTGIPLLFKACYSLGAQKKSMIVKVAGGASILDDTNFFRIGQKNIMMARKMFWKNNVLINGEDTGSNCNRTVRLEIKTGKVFVKSSGGPLREL
|
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
|
Q2LSK9
|
A1TE06
|
ISPH_MYCVP
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
|
Mycolicibacterium
|
MPPTVNMGIPGASRTALGSVAGDVTGKRVLLAEPRGYCAGVDRAVETVERALEKHGAPIYVRHEIVHNRYVVDTLAKAGAIFVEQTDEVPEGAIVVFSAHGVAPTVHEEAAARHLRTIDATCPLVTKVHNEAKRFARDDYDILLVGHEGHEEVVGTAGEAPDHVQVVDNPDAVDKVTVRDPNKVIWLSQTTLSVDETMETVRRLREKFPTLQDPPSDDICYATQNRQVAVKAMAPECELVIVVGSKNSSNSVRLVEVALGAGASAAHLVDYADDIDPAWFDGVTTVGVTSGASVPEILVRGVLDRLAEHGYDVVQPVTTANETLVFALPREIRPARQ
|
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
|
A1TE06
|
Q9HK20
|
DCDA_THEAC
|
Diaminopimelate decarboxylase
|
Thermoplasma
|
MGIYDIFDDESARSISGMSIDEMAKKYGTPVIIYSRARIVSNIRRIREAYENRVRMLYSVKANDNPRIIEIMHQESIGSDSASPMEIMMSIFSGIPPEDILYSPNNASEYDLNFALDRGIAINFNTFTQYRKMREKPERISFRINPGFGMGEFAGTTTGGARTKFGIDPDAAILAYRKAREDGIREFGIHMMIGSNNRDHVKIAEAYSNFFRIADRIGREAGVSFQFADVGGGLGIPYVQGENELDIAALGSAVLKEFDRYHFGDLVLEPGRYLVGDAGIIVGTVNDVHNGFAGTDIGMNLNIRPALYGARHTIIPVGERVEGEKITVTGQICENTDRIGDTAWRLSEGDRIMVLDAGAYVYSMSSRYNGRPRPPEIMIMEDGKDVMIRRREDFSDFIATVV
|
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
|
Q9HK20
|
O74919
|
RNC1_SCHPO
|
RNA-binding protein that suppresses calcineurin deletion 1
|
Schizosaccharomyces
|
MAYNHFSIPKNIEEKENSFFDVTFQDEPDETTSTATGIAKVSIPTPKPSTPLSTLTNGSTIQQSMTNQPEPTSQVPPISAKPPMDDATYATQQLTLRALLSTREAGIIIGKAGKNVAELRSTTNVKAGVTKAVPNVHDRVLTISGPLENVVRAYRFIIDIFAKNSTNPDGTPSDANTPRKLRLLIAHSLMGSIIGRNGLRIKLIQDKCSCRMIASKDMLPQSTERTVEIHGTVDNLHAAIWEIGKCLIDDWERGAGTVFYNPVSRLTQPLPSLASTASPQQVSPPAAPSTTSGEAIPENFVSYGAQVFPATQMPFLQQPKVTQNISIPADMVGCIIGRGGSKISEIRRTSGSKISIAKEPHDETGERMFTITGTHEENEKALFLLYQQLEMEKDRRSH
|
Binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression suppresses the Cl(-) sensitivity of calcineurin deletion.
|
O74919
|
Q9Y227
|
ENTP4_HUMAN
|
Uridine-diphosphatase
|
Homo
|
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGRLTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDIRQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTAGMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHIEDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKNLLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTPDMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPPIHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASHADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPLRDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAALWMEEGLPAQNAPGTL
|
Has a broad substrate specificity with the ability of cleaving all nucleotide di- and triphosphates with the exception of adenosine di- and triphosphate (ADP and ATP). Preferentially hydrolyzes CTP, UDP, CDP, GTP and GDP. Can use either Ca(2+) or Mg(2+) equally.
|
Q9Y227
|
Q8DDQ8
|
ENGB_VIBVU
|
Probable GTP-binding protein EngB
|
Vibrio
|
MSVKIHYQNTHFITSAPDIRHLPADEGIEIAFAGRSNAGKSSALNRLTNQKNLAKTSKTPGRTQLINLFKVTEGCHIVDLPGYGFAQVPLEMKNKWQKSLGEYLQKRECLKGLVVLMDIRHPMKDLDQQMIFWAIESRIPVQVLLTKADKLKSGARKAELLKVRKLAETFGGDVQVDVYSSLKGLGVDQLRAKLDTWFAPALAHLLEDEEGSNSAE
|
Necessary for normal cell division and for the maintenance of normal septation.
|
Q8DDQ8
|
A8AI19
|
MTOX_CITK8
|
N-methyl-L-tryptophan oxidase
|
Citrobacter
|
MKYDLIIIGSGSVGAAAGYYATRAGLKVLMTDAHMPPHQQGSHHGDTRLIRHAYGEGEKYVPLVLRAQTLWEELSTHNEDPIFVRSGVINLGPADSPFLANVAHSAQQWQLNVEQLDAAAIMARWPEIRVPDNYIGLFEMDSGFLRSELAIKTWVRLAEEAGCAQLFNCPVTALHHDNDGVTVETADGEYRAKKVLISAGTWVQALVPELPIQPVRKVFAWYQADGRYSMKNNFPAFTGELPNGDQYYGFPAENDALKIGKHNGGQLIHSPEERKPFAAVASDGSEAFPFLRTILPGIGCCLNGAACTYDNSPDEDFIIDTLPGHDNTLIVTGLSGHGFKFASVLGEIAADFAQGKSPAFDLTPFKLNRFTQ
|
Catalyzes the oxidative demethylation of N-methyl-L-tryptophan.
|
A8AI19
|
A1DFN5
|
HSE1_NEOFI
|
Class E vacuolar protein-sorting machinery protein hse1
|
Aspergillus subgen. Fumigati
|
MFRAQQNAFDDAVAKATDENLTSENWEYILDVCDKVAAEESGAKDAVAAMIKRLAHRNANVQLYTLELANALAQNCGPKIHRELASRSFTDALLRLANDRNTHQQVKPKILERMQEWAQMFANNPDFGIMEQAYMKLKTQNPNLQPPSKPGKREITEADRQKEEEELQMALALSIREKPSAAPEPKAEPSTSASVPASQTQAATSQAVPPGTSAATVSRVRALFDFQPSEPGELQFRKGDIIAVLESVYKDWWKGSLRGQTGIFPLNYVEKLPDPTVEELQREAQMEAEVFGQIKNVEKLLTLLSTRSSELNVQDNEEITALYHSTLSIRPKLIELIGKYSQKKDEFTQLNEKFIKARRDYESLLEASMSHPAQPQYGRPGQTPYGYPGPAAPLGYPQGPPQSDPQRYFSPRPQDQTHMYPPTSHSPDPRGRTPPAGPSFPQHQQPPPDSYQPVHHRPESTYDNPQELGTSVYDSPVEHPSSSQRLPYPPSGAPVPPGVHQQFQHQQQEYPPSGYPPEDASKPPTAGFASQPPQQTLQQPPYPTAPVAHQPPPSHQPPPVPSTASKPTPYPSLTPGTPSGGEYQAYNPSQAGAANSNPNSYYR
|
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
|
A1DFN5
|
Q28V47
|
GREA_JANSC
|
Transcript cleavage factor GreA
|
unclassified Jannaschia
|
MEKIPMTPKGLEAMNGELKQLKSVERPAIIKAIAEAREHGDLSENAEYHSAKEKQSFIEGRIKELEGSISLAQVIDPATLSGAIKFGATVDLVDEETEEEKTYMIVGEAEADIEKGLLNIKSPLARALIGKEEGDSVEVRTPGGAKGFEIVKISYV
|
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
|
Q28V47
|
Q759M1
|
SIP5_ASHGO
|
Protein SIP5
|
Eremothecium
|
MGNVPGKLEAEEYGAMNGRRGGSQKQFRSLSQSSTASSGSAAADSGRSRRATSLVGNLLSSGGVSRAESYGGSAYRRRVAREKDRLREQHALRLVVRSEETVDGGYLAPYGSYRLEKLDYDAPVVQGLIVERRLAPFYTPLQDFDEGWTREELVRVVDSLLLHAPFEEEPEEFEGVPLGNLGVADIDALVDKTLSRREQRRQRSKIFRARLHRKRILWQEEENSKFLELKLEARRTGVSSACLPSDDAKWDLYRNGAECPICFLYFPEPMNVSRCCLQPICTECFVQIKRQEPHFSHDEVDPAQPDEDKDPDLLISTPASCPFCATPNFGVTYKPPADRILGIQGGPPSSYVSACSDPPHHHTEPPPRRTSVAHDHSSVVTSDMIRPDWETELIKERTKLARRAANATAIHVSNRLVDPGHTRGYSNSFASASSTYASNSSMTADFEEEMIRHVMRLSLLDQQPNATSISPGPVDR
|
May negatively regulate the SNF1 kinase.
|
Q759M1
|
O78713
|
NU1M_ZAGBR
|
NADH dehydrogenase subunit 1
|
Zaglossus
|
ILLAVAFLTLIERKILGYMQFRKGPNIVGPHGLLQPIADAVKLFIKEPLRPMTSSIYMFILAPILALSLALTIWVPLPMPLPLIDLNLGLLFVLSVSGLSVYSILWSGWASNSKYALTGALRAVAQTISYEVTLAIILLSIMLINGSFTLTTLNLTQEFMWLVVPTWPLMLTRFISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFAMFFLAEYANIIIMNALTVILFFGAYHLIFLPELSTINFMIKTMMLTSLFLWIRASYPRFRYDQLMHLLWKNFLPITLVTCLWFIMLPLALSWIP
|
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
|
O78713
|
O78937
|
CYB_TAXTA
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Taxidea
|
MTNIRKTHPLAKIINNSFIDLPAPSNISTWWNFGSLLGVCLIIQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFLHVGRGLYYGSYMFPETWNIGIILLLTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIILALAAIHLLFLHETGSNNPSGIPSNSDKIPFHPYYTIKDILGALLMALLLMVLVLFSPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILILAIIPLLHTSKQRSMMFRPLSQCMFWLLVADLLILTWIGGQPVEHPYITIGQLASILYFTILLALMPTISIIENNLLKW
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Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
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O78937
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Q1AZC4
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LEUC1_RUBXD
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Isopropylmalate isomerase 1
|
Rubrobacter
|
MEKKKPRTLVEKIWERHVVRRAEGEPDLLYVDLHMVHEVTSPQAFEALRLAGRRVRRPDLTVATMDHNVPTTDVRLGVRDRVSARQMEALRKNCEEFGIQLHEWGSPGQGIVHVIGPEMGLTQPGMVIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTIPQRRPKTMAITVEGEAPPDVTAKDIMLGILHRIGTGGGVGHAIEYRGEAIRNLSMEGRMTICNMTIEGGGRAGMVAPDEKTYSYIEGRPHAPKGRAWEEALEYWQSLPTDEGATFDKEVVIDAAELVPYVSWGTTPAQTVPLDGEVPEPQNEGHERALRYMGLRPGTPIREIEVDTVFIGSCTNARIEDLRAAARVLEGHKVKEGIRAMVVPGSMRVKKQAEEEGLDEIFKKAGFEWRNAGCSMCLGMNPDILSPGERCASTSNRNFEGRQGKGGRTHLVSPVVAAATAVMGRFASPSELGVPVEVG
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Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
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Q1AZC4
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Q2NIN4
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TILS_AYWBP
|
tRNA(Ile)-lysidine synthetase
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Candidatus Phytoplasma asteris
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MENIKLACSLETNQTYIIAVSGGVDSMALLHYLVAQKIKLQVVHFNHLTNSNTWKNKELVKNYCLQNSLGFHYFELNCPQKNFQAQARLLRQQKLMQIAAKHRTPFILTAHHLDDLAETILQKISRSSTLLGYSGMQIQTSWTDFIFLKPFLYIPKAKIISYAAFYKIPFLEDYTNQKLTYQRNQIRHQVIPYLKTQTSFLQNIQKYQQTLLQAYNFIRKQTLLFLTKHTNHSCNQPNSIALAPFLNLDLVIQKDIILLLLEQKNITQSFIFIQNIIKGINNPYKPNLSWHLNSDWHLIKDYKHIKLMNPALPLPFALTKPLLCVSTCNLCLVCVCPLIETLNYNSQKVSFPLKVRLRQPKDTLKFSFGTKKLKKFLIEKKVPLTQRNNLWLVVDNLDNILFIPQLYTNLTLGNQFRIYLAFKNFFTSSNCFSQTN
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Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
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Q2NIN4
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Q04JX1
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AROE_STRP2
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Shikimate dehydrogenase (NADP(+))
|
Streptococcus
|
MKLDGYTRLAAVVANPIKHSISPFIHNRAFEATATNGAYVAWEIEASDLVETVANIRRYQMFGINLSMPYKEQVIPYLDKLSDEARLIGAVNTVVNENGNLIGYNTDGKGFFKCLPSFTISGKKMTLLGAGGAAKSILAQAILDGVSQISVFVRSVSMEKTRPYLDKLQEQTGFKVDLCALEYVSELQARIAESDLLVNATSVGMDGQSSPVPENIVLPETLLVADIIYQPFETPFLKWARSQGNPAVNGLGMLLYQAAEAFQLWTGKEMPTEEIWQSLTEKYQ
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Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
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Q04JX1
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Q5HEE4
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LEU1_STAAC
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Alpha-isopropylmalate synthase
|
Staphylococcus
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MSSHIQIFDTTLRDGEQTPGVNFTFDERLRIALQLEKWGVDVIEAGFPASSTGSFKSVQAIAQTLTTTAVCGLARCKKSDIDAVYEATKDAAKPVVHVFIATSPIHLEHKLKMSQEDVLASIKEHVTYAKQLFDVVQFSPEDATRTELPFLVKCVQTAVDAGATVINIPDTVGYSYHDEYAHIFKTLTESVTSSNEIIYSAHCHDDLGMAVSNSLAAIEGGARRIEGTVNGIGERAGNAALEEVALALYVRNDHYGAQTALNLEETKKTSDLISRYAGIRVPRNKAIVGQNAFSHESGIHQDGVLKHRETYEIMTPQLVGVSTTELPLGKLSGKHAFSEKLKALGYDIDKEAQIDLFKQFKAIADKKKSVSDRDIHAIIQGSEHEHQALYKLETLQLQYVSSGLQSAVVVVKDKEGHIYQDSSIGTGSIVAIYNAVDRIFQKETELIDYRINSVTEGTDAQAEVHVNLLIEGKTVNGFGIDHDILQASCKAYVEAHAKFAAENVEKVGN
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Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
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Q5HEE4
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B6YXF3
|
KPTA_THEON
|
Probable RNA 2'-phosphotransferase
|
Thermococcus
|
MFPGRRKVSKLMAYILRHSPEEFGLRPDVEGFVPLSELVEALKTIYPDVTEEFVREIVARDAKGRYEIQGDRIRARYGHSFPVSLDHEEDTESRFLYHGTPRRNLESILREGLKPMRRQFVHLSTSKSEAIKTGRRHGRDVVLLVIDAECLRKKGLKVYKAGKNVRIVEKVPPECITLEV
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Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase.
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B6YXF3
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B2GUZ5
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CAZA1_RAT
|
CapZ alpha-1
|
Rattus
|
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYDDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEDVDGGLKSWRDSCDSALRAYVKDHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSVTVSNEVQTAKEFIKIIESAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
|
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions.
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B2GUZ5
|
Q1C5I5
|
RLMN_YERPA
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tRNA m2A37 methyltransferase
|
Yersinia
|
MSEQLLTASTPIDAAPLSDNTVQTTAPATSKINLLDLNRQQMREFFAEMGEKPFRADQVMKWMYHYCYDDFEQMTDINKGLRAKLQRVAEIRAPEVAEEQRSVDGTIKWAIKVGDQQVETVYIPEADRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIIGSLKSTGTRPITNVVMMGMGEPLLNLNNVVPAMDIMMDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPTDDIRDEIVPINRKYNIETFLAAVRRYLDKSKANGGRVTVEYVMLDHINDSTEQAHQLAECLKDTPCKINLIPWNPFPGAPYGRSSNSRVDRFSKVLMEYGFTTIVRKTRGDDIDAACGQLAGEVIDRTKRTLKKKMAGEPIAIKTV
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Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
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Q1C5I5
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Q9EPC5
|
RET7_MOUSE
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Cellular retinoic acid-binding protein IV
|
Mus
|
MPADLSGTWNLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIQTCSSLRNYLVKFKVGEEFEEDNKGLDNRKCTSLVTWENDKLTCVQRGEKKNRGWSHWIEGDQLHLEMFCEGQVCKQTFQRA
|
Intracellular transport of retinol.
|
Q9EPC5
|
Q8GUJ2
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PDLP5_ARATH
|
Protein HOPW1-1-INDUCED 1
|
Arabidopsis
|
MIKTKTTSLLCFLLTAVILMNPSSSSPTDNYIYAVCSPAKFSPSSGYETNLNSLLSSFVTSTAQTRYANFTVPTGKPEPTVTVYGIYQCRGDLDPTACSTCVSSAVAQVGALCSNSYSGFLQMENCLIRYDNKSFLGVQDKTLILNKCGQPMEFNDQDALTKASDVIGSLGTGDGSYRTGGNGNVQGVAQCSGDLSTSQCQDCLSDAIGRLKSDCGMAQGGYVYLSKCYARFSVGGSHARQTPGPNFGHEGEKGNKDDNGVGKTLAIIIGIVTLIILLVVFLAFVGKCCRKLQDEKWCK
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Modulates cell-to-cell trafficking. Has a positive role in innate immunity. Required for systemic acquired resistance (SAR) which is mediated by the signaling molecules azelaic acid (AzA), glycerol-3-phosphate (G3P), and salicylic acid (SA) . Negative regulator of plasmodesmata permeability triggered by SA during immune responses, through regulation of callose deposition . Delays the trafficking of Tobacco Mosaic Virus (TMV) movement protein (MP). Required for symplastic signal transport .
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Q8GUJ2
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Q8ZRZ0
|
SYI_SALTY
|
Isoleucyl-tRNA synthetase
|
Salmonella
|
MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGFDSPYVPGWDCHGLPIELKVEQEFGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGRIIKNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFRAVDQDAVKAKFGLPGVSGPVSLVIWTTTPWTLPANRAISLAPDFDYALVQIDGQAVILAKDLVESVMQRIGAAEYTILGTVKGAELELLRFTHPFMGFDVPAILGDHVTLDAGTGAVHTAPGHGPDDYVIGQKYGLETANPVGPDGTYLPGTYPTLDGVNVFKANDIVIELLKEKGALLHVEKMQHSYPCCWRHKTPIIFRATPQWFVSMDKEGLRQQSLKEIKGVQWIPDWGQARIESMVANRPDWCISRQRTWGVPMSLFVHKETQELLPIERTLAAMEEVAKRVEVDGIQAWWDLDPKEILGEDADQYEKVPDTLDVWFDSGSTSYSVVDARPEFAGHAADMYLEGSDQHRGWFMSSLMISVAMKGKAPYRQVLTHGFTVDGQGRKMSKSIGNTVSPQDVMNKLGADILRLWVASTDYTGEMAVSDEILKRAADSYRRIRNTARFLLANLNGFNPATDMVKPEEMVVLDRWAVGCAKTAQQEILKAYEAYDFHEVVQRLMRFCSVEMGSFYLDIIKDRQYTAKADSVARRSCQTALYHIAEALVRWMAPIMSFTADEIWGYLPGEREKYVFTGEWYDGLFGLEENEEFNDAFWDDVRYIKDQVNKELENQKANGIKSNLEAKVTLKYADDANGTIKKLKLLGEEVRFIFITSQFVISEQAGGIDDENIQYNAGNTTVQAVVTRAEGDKCPRCWHYTTDVGKVAEHADICGRCVSNIAGNGEQRKFA
|
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
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Q8ZRZ0
|
Q9GZP1
|
NRSN2_HUMAN
|
Neurensin-2
|
Homo
|
MMPSCNRSCSCSRGPSVEDGKWYGVRSYLHLFYEDCAGTALSDDPEGPPVLCPRRPWPSLCWKISLSSGTLLLLLGVAALTTGYAVPPKLEGIGEGEFLVLDQRAADYNQALGTCRLAGTALCVAAGVLLAICLFWAMIGWLSQDTKAEPLDPEADSHVEVFGDEPEQQLSPIFRNASGQSWFSPPASPFGQSSVQTIQPKRDS
|
May play a role in maintenance and/or transport of vesicles.
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Q9GZP1
|
A9WSE5
|
RUVA_RENSM
|
Holliday junction ATP-dependent DNA helicase RuvA
|
Renibacterium
|
MISFLRGPVAHIGLSAAVIDVGGVGMLVQATPKTLGTLRLGQESTLTTAMIVREDSMTLYGFADPDEREVFEILLTVSGIGPRLGLAVLAVLEPETIRVATSTGDGKTFTKVPGIGPKVAGRIVLELAGKLVPHGTVNGAPASPSAQWKPQVVAAMTSLGWSEKDALASVEKATADSPELISDGNVAEILRTTLRWLGQDGARTSAGRQVTARG
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
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A9WSE5
|
Q7U581
|
SYE_PARMW
|
Glutamyl-tRNA synthetase
|
Parasynechococcus marenigrum
|
MVRVRLAPSPTGTLHIGTARTAVFNWLYARRQQGSFLLRIEDTDKERSKPEYTQNILEGLRWLGIDWDEEPLIQSEQVQQHRAAIETLLQKGLAYRCYANEAELDAMREAQKASNQAPRYDNRHRNLTPEQEAAFQSEGREAVIRFRIDDNAEIRWNDMVRGAMSWRGADLGGDMVVARRAPADQIGDPLYNLVVVVDDAAMAISHVIRGEDHIANTAKQLLLYEALDLPAPTFAHAPLILNAEGRKLSKRDGVTSINDFRTMGYTAEAIANYMTLLGWSVPEGMEERFTLPEAAAVFSFDRVNKAGARFDWDKLNWLNGQVLHALPAQQLLDDLRPLWAEQGWTLPDDSSWGLELCELLGPSLTLLKEGVEQATPFFKCPDLEDDGVRQLEADGARTAVAQLLQILEAEPWDGKDTDRAKQLLADAAKGAGVKKGVVMKSLRAALLGRLQGPDLITTWCLLARIGEDLPRLQRCLA
|
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
|
Q7U581
|
C1D1L8
|
RSMH_DEIDV
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Deinococcus
|
MTLPEDTTTAESLIHTSVLSAEVLEALAPTPGKTIVDGTLGGAGHTRLLLEAGAHVYGIDQDPFALDRAREAGLPNLTVLQGNYRDMVSLLEQAGVSQVDGILLDIGVSSFQLDDAGRGFSYHTEAPLDMRMSQSGESAADVVNTYEEEDLAAIIYEYGEDRLSRRIARAIGQARQKAPIETTVQLAEIVKRAYPGFSKGIHPARRTFQALRIHVNDELGALRDGLQAAETLLRPGGRLAVISFHSLEDRIVKRFLLGSEVLQPLTKRPVVASDEEQAINPRSRSAKLRAAERVVVQEAS
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
C1D1L8
|
A8FX10
|
BIOB_SHESH
|
Biotin synthase
|
Shewanella
|
MSDIQLRHDWKHDEIEALFALPMNDLLFKAHSLHRQVFDPNEVQISRLLSIKTGACPEDCKYCPQSARYDTGLEKERLIEIEKVLTEARSAKAAGASRFCMGAAWRNPHARDMPYLKDMVSEVKAMGMETCMTLGMLSGTQAEELAEAGLDYYNHNLDTSPEYYGEIITTRTYQDRLDTLSNVRSAGMKVCSGGIVGMGEQASDRAGLLQQLANMEQHPDSVPINMLVKVAGTPFENLDDLDPLEFVRTIAVARIIMPHSRVRLSAGREKMTDEMQAMCFFAGANSIFYGCKLLTTNNPEENEDMTLFKRLGLHPEQGKYATVEDDKEVMAKASAKANAIKDKQSGAFYDAGAL
|
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
|
A8FX10
|
Q8MHW5
|
CXB2_GORGO
|
Connexin-26
|
Gorilla
|
MDWGTLQTILGGVNKHSTSIGKIWLTVLFIFRIMILVVAAKEVWGDEQADFVCNTLQPGCKNVCYDHYFPISHIRLWALQLIFVSTPALLVAMHVAYRRHEKKRKFIKGEIKSEFKDIEEIKTQKVRIEGSLWWTYTSSIFFRVIFEAAFMYVFYVMYDGFSMQRLVKCNAWPCPNTVDCFVSRPTEKTVFTVFMIAVSGICILLNVTELCYLLIRYCSGKSKKPV
|
Structural component of gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.
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Q8MHW5
|
P28541
|
SECY_METVA
|
Protein transport protein SEC61 subunit alpha homolog
|
Methanococcus
|
MKIKPILELIPEVKRPLKGVSFKEKIQWTGLVLILYFILGTIDIYMGGAEMPAMFAFWQTVTASKMGTLITLGIGPIVTAGIIMQLLVGSELISLDLSKPMNRALFQGLQKLFGIFLCFLEAVMFVGAGAFGVVNSTLALILVLQLALGAILVIYLDEIVSRYGIGSGIGLFIAAGVAQTIFVGAFGAEGYLWKFFSAMSVGSLGIAFEYILPILSTLFVFLVVVYVESIRVEIPLAHGRVKGAVGKYPIKFIYVSNLPVILAAALFANIQLWGMFLDRMGYPILGQYSNGTAVSGIAYYFSTPYGISNIISDPLHAIFYTLMMVIFCILFGLFWVETSGLDAKSMAKKLGNLDMAIKGFRKSQKSIEQRLKRYIKPITVMGSAFVGFLAAAADFTGALGGGTGVLLTVSIVYRLYEQLVQEQLSELHPAVAKFVGKR
|
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
|
P28541
|
C1DQ99
|
MURG_AZOVD
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Azotobacter
|
MGANVLIMAGGTGGHVFPALACAREFQARGYAVHWLGTPRGIENDLVPSAGLPLHRIQIGGLRGKGLATLLKAPFQLIRSLFQARRIMNELRPVCVLGMGGFVTGPGGVAAKLTGAPLVIHEQNAVAGTSNRALAPLADRICEAFPDTFKPTGKRRTTGNPVRSELFLDSSRQIPDGRRLRLLVLGGSLGAEPLNKLLPAALALIPVEQRPELFHQAGRQHHESTADRYREAGVEAEVVPFIEDMARVYAWADLVVCRAGALTVSELAAAGLPALLVPLPHAIDDHQTRNADYLAREGAAFLLPQATTTAADLAARLSEVSMHPEQLEGMAARARRLAKPDATRTVVDICLEVARG
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
C1DQ99
|
A6UWS1
|
MTD_META3
|
Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase
|
Methanococcus
|
MVVKIGIIKCGNIGMSPLIDLALDERADRTNIDVISIGSGAKMGPNQVVEVTTKMVEDIKPDFIIYVGPNPAAPGPAKAREILSASDIPSVIIGDAPGIKAKDKMAEEGLGYILIKCDPMIGARRQFLDPVEMAMFNADVIRVLAGTGAARVVQNAIDDIVEAIEAGNEIELPKIVVTDAKSVAAAEFSNPYAKAKAMAAFAMAEQVANIDVKGCFMTKEMEKYIPIVASAHEMIRTAAKLVDEARELEKATDSVSRKPHGADGKRLNKTKLMEKPE
|
Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
|
A6UWS1
|
Q0I0T2
|
PEPQ_SHESR
|
Proline dipeptidase
|
Shewanella
|
MDHLAHHYHAHIAELNRRVAEIVSREALSGLVIHSGQPHRMFLDDINYPFKANPHFKAWLPVLDNPNCWLVVNGRDKPQLIFYRPVDFWHKVSDVPEMFWTEHFEIKLLTKADKVAELLPSDITNWAYLGEHLDVAEVLGFTSRNPDSVMSYLHFHRTTKTEYELECMRRANQIAVQGHLAAKNAFYNGASEFEIQQQYLSAVGQGDNEVPYGNIIALNQNAAILHYTALEHQNPARRLSFLIDAGASYFGYASDITRTYAFEKNRFDELITAMNKAQLELIDMMRPGVRYPDLHLATHGKVAQMLLDFELATGDAQGLVDQGITSAFFPHGLGHMLGLQVHDVGGFSFDERGTHIPAPEAHPFLRCTRILAPNQVLTMEPGLYIIDTLLNELKQDSRGQQINWRTVDELRPFGGIRIEDNVIVHQDRNENMTRELGLA
|
Splits dipeptides with a prolyl residue in the C-terminal position.
|
Q0I0T2
|
Q8FW10
|
UGPB_BRUSU
|
sn-glycerol-3-phosphate-binding periplasmic protein UgpB
|
Brucella
|
MFTRLITTSALTGAIALTIGSQAFAQTELAWWHGMTGANNEMVNELSKEFNESQSEYKIVPVYKGNYPETLNAGIAAFRSKQPPAILQVFDAGSGVMMAAEGAIVPAAEVLEKGGYKFDKSQYLPGIVAYYSKPDGTMLSFPYNSSSPILYYNKDAFKKAGLDENKPPKTWPEVFEAAKKIKASGASPCGFTSTWLTWIQTENFAAWNNVPYGTNENGLAGTDVKLEINSPLYVEHFQAIADLAKDGTFRYGGRTSEAKQLFTSGECAMLTESSGGLGDVVKSGINYGIGQLPYYEGHGPQNTIPGGASLWVFAGLSDDQYKGIAEFFNFLSQTKIQVKLHEKSGYLPVTLAAYEETKKSDFYEKNPGRETPILQMMGKEPTENSKGVRLVNLPQVRDILNEEFEAMLGGKQDAKTALDNAVKRGNAAIAAAQ
|
Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import.
|
Q8FW10
|
Q0TME7
|
ADD_CLOP1
|
Adenosine aminohydrolase
|
Clostridium
|
MNLLNLPKIELHCHLDGSLRVETAIELAKKEGVKLDSYEYDKVKELLVIPKECNSLEDYLNRFALPVKLLQRAENLERVAFELMEDASKENVKYIEIRFAPLLHLEKGMTQKEVIESVIKGIRKAEELYDIKGNLILSCLRHHSIDSVYEVIEEGKNFIGKGVVAIDLAGGELENFVKPYEEVMKLARKAGFRVTIHAGETGYGKNVRDAIELLGAERIGHGLFIFNDEEAYNLVKEKGVTLEMCPKSNIDTKGVNKYEEHPIYKYHKDNIKVNLSTDNRTVSNINLTEEFENVHKTFNIDFEDYKKIYLNSVEASFCSEELKEKLKLSIII
|
Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
|
Q0TME7
|
Q8D268
|
SERC_WIGBR
|
Phosphohydroxythreonine aminotransferase
|
Wigglesworthia
|
MKDIFNFGSGPSMLPKIVLKKIKRDLFNWKNTNVSVMEISHRNKNFLKVIENIKNDIKFLLSVSNDYNIILLQGGARAQFSGIPMNLTNNFSDLADYINTGYWGMYAAIEAKKYCSVNIIDVIEKKDKLSILPMKNWNISKNSVYLHYCPNETINGTAIYETPKFKNKIVVADFSSTILSRPIDVNKFDIIYASSQKNIGVSGMTIMIFKKNIFLKQNKFTPSILNYEIIYKNNSLFNTPPTFNWYVSGLVLKWLIDQGGVKKINNINKIKSKLIYDIIDKSKFYKNNIYDEYRSYMNIIFYLPNKKLNNLFLKLSKINGLLFLKGHRAVGGIRASMYNSMTIKGAKKLANFMKYFEKRYG
|
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
|
Q8D268
|
Q2U0J6
|
HEPH_ASPOR
|
Heptelidic acid biosynthesis cluster protein H
|
Aspergillus subgen. Circumdati
|
MASLTGAAAVLLAFILAYSTALTIYRLFFHPLARFPGPRLAAATKWYEFYFDIIKSPGGQFFKELSRMHDVYGPIVRVNPDEIHVRDAAWFEVLYAPNPTKRNKYRPSAEMAGLTLGIHGTVDHDLHRRRRMAIAPMFNKQSILSAEHLIKQHIDELTDVFESYLGTNNPINLQTTFLAYTTDVLYHYMFDTDAGYQRDSGAAQQWRHSMDAVAQATPFLKQFPSLLSRVALIPLPMLIWVLKRIQPDVAGLLGTHQLMASIVSKYMASKPEEDQDELIATKAVKPRTLFHAIEASSLPPHEKAPTRLAQEGLTVLFAGGETGSRLLAHTVYHLLKNPEILEKVRKEILDAAGDSNQLPDMKALEALPWLTASVRESLRLRAATTSRLPLVTEKPLAYADWVIPPNTPVSMSHGDILHNEDIFPDPMKFMPSRWFNASPQQNRLFVPFGKGTRMCVGMNFAYCEIYMSLAVILARFDLELYDTRWERDVHYTRDCFLGEPDPASPGIRVKVVADHKTFTRS
|
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy sauce brewing.
|
Q2U0J6
|
Q8Z3I0
|
PNP_SALTI
|
Polynucleotide phosphorylase
|
Salmonella
|
MLNPIVREFQYGQHTVTLETGMMARQATAAVMVSMDDTAVFVTVVGQKKAKPGQDFFPLTVNYQERTYAAGRIPGSFFRREGRPSEGETLIARLIDRPVRPLFPEGFVNEVQVIATVVSVNPQVNPDIVAMIGASAALSLSGIPFNGPIGAARVGYINDQYVLNPTQDELKESKLDLVVAGTEAAVLMVESEAELLSEDTMLGAVVFGHEQQQVVIQAINDLVKEAGKPRWDWQPEAVNDALNARVAALAESRLSDAYRITDKQERYAQVDVIKSETIEQLIAEDETLDANELGEILHAIEKNVVRSRVLAGEPRIDGREKDMIRGLDVRTGVLPRTHGSALFTRGETQALVTATLGTARDAQVLDELMGERTDSFLFHYNFPPYSVGETGMVGSPKRREIGHGRLAKRGVLAVMPDMDKFPYTVRVVSEITESNGSSSMASVCGASLALMDAGVPIKAAVAGIAMGLVKEGDNYVVLSDILGDEDHLGDMDFKVAGSRDGISALQMDIKIEGITKEIMQVALNQAKGARLHILGVMEQAINAPRGDISEFAPRIHTIKISTDKIKDVIGKGGSVIRALTEETGTTIEIEDDGTVKIAATDGEKAKYAIRRIEEITAEIEVGRIYNSKVTRIVDFGAFVAIGGGKEGLVHISQIADKRVEKVTDYLQMGQEVPVKVLEVDRQGRVRLSIKEATEQSQPAAAPEAPASEQAE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
Q8Z3I0
|
Q65V80
|
XERC_MANSM
|
Tyrosine recombinase XerC
|
Basfia
|
MQTYLQKYWNYLRNERQVSSYTLTNYQRQMDAVMKILQENDIQNWRQVSPSVVRFILAQSKKSGLHEKSLALRLSALRQFLAFLVLQGELKVNPAIGISAPKQGKHLPKNINAEQLNKLLDNNSKEPIDLRDKAMLELMYSSGLRLSELQGLNLTSLNFRSREIRVLGKGNKERILPFGRHASHSVQEWLKVRLLFNPKDDALFVSSLGNRMSNRSIQKRMEIWGVRQGLNSHLNPHKLRHSFATQMLEASSDLRAVQELLGHSNLSTTQIYTHLNFQHLAEVYDQAHPRAKRRK
|
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
|
Q65V80
|
F9WZD2
|
GSS1_ZYMTI
|
Geranyltranstransferase
|
Zymoseptoria
|
MDKFSQSPPLRDDLVRGSSLNWTKEKENILKGPFNYLESHPGKDIRSQLIAAFNAWLDVPEESLNVIRRVVAMLHTASLLIDDVEDNSQLRRGIPVAHNVFGTAQTINSANYVYFCALKELAILNNPAVIQIYTEELVNLHRGQGMDLFWRDTLTCPSEDDYLEMVGNKTGGLFRLAIKLMCAESPSHNAHPDPFQRNDYVPLVNTIGLLFQILDDYKNLSDTIYTQNKGLCEDLTEGKFSFPIIHAIRADPGNLVLINILKQKTTDDEVKKYAVAYMDRAGSFSYTRKVLRGLTKKALTQVDEVDAGRGRGEQMKTILEKLRVDRNHQRGVLTPAAGGASIA
|
Geranylgeranyl pyrophosphate synthase; part of the gene cluster 4 that mediates the biosynthesis of an isoprenoid secondary metabolite.
|
F9WZD2
|
Q91WR5
|
AK1CL_MOUSE
|
Dihydrodiol dehydrogenase type 3
|
Mus
|
MNSKCHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAIDAGFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYTSKVWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMALKPGEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKSIGVSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKLLDFCKSKDIVLVAYGVLGTQRYGGWVDQNSPVLLDEPVLGSMAKKYNRTPALIALRYQLQRGIVVLNTSLKEERIKENMQVFEFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDEY
|
NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione into androsterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad substrate specificity and acts on various 17-alpha-hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-ketosteroids. Reduction of keto groups is strictly stereoselective. Reduction of 17-ketosteroids yields only 17-alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids yields only 3-alpha-hydroxysteroids.
|
Q91WR5
|
B0KIS4
|
DNAJ_PSEPG
|
Chaperone protein DnaJ
|
Pseudomonas
|
MSKRDYYEVLGVERGASEADLKKAYRRLAMKYHPDRNPGDKESEDKFKEANEAYEVLSDASKRAAFDQYGHAGVDPSMGGGGAGFGGANFSDIFGDVFSDFFGGGRGGGRGGAQRGSDLRYTLELNLEEAVRGTTVSIRVPTLVNCQPCDGSGAKKGSTPSTCPTCGGIGQVRMQQGFFSVQQTCPRCHGQGKIITDPCTSCHGEGRVEEYKTLSVKVPAGVDTGDRIRLSGEGEAGTHGGPTGDLYVVISVREHEIFQRDGKHLYCEVPISYTDAALGGELEVPTLDGRVKLKIPEGTQTGKQFRLRGKGVAPVRGGGAGDLLCRVAVETPVNLSRRQRELLEELRDSLEGDSSHSPKASGWFDGVKRFFGDL
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
B0KIS4
|
C3PLF4
|
UBIE_RICAE
|
Demethylmenaquinone methyltransferase
|
spotted fever group
|
MNQTNFGFKKVDYTKKQGLVNNVFSNVADKYDLMNDLMSLGLHRLWKDEFIRQIPNLNSHILDVASGSGDIALKLAKKARDRVNNISLTLSDINEEMLKQAKKKAIDLNLFQNLKFTVASAEELPFPDDSFDYYTIAFGIRNVPDINKALKEACRVLKPMGKFICLEFSKVKEGYIKDFYKFYSFNIIPSIGQMIAGNKEAYEYLVESIDLFPSQDEFRIMIKDAGFEEVGYKNLSGGIVAIHSAYTQ
|
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
|
C3PLF4
|
Q5D7J2
|
TRIM5_PAPAN
|
TRIM5alpha
|
Papio
|
MASGILLNVKEEVTCPICLELLTEPLSLPCGHSFCQACITANHRKSMLYKEGERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGLKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISDLEHRLQGSMMELLQGVDGIIKRIENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRELTDVRRYWVDVTLAPNNISHAVIAEDKRQVSSRNPQITYQAPGTLFSFPSLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDAMYNIEQNENYQPKYGYWVIGLQEGVKYSVFQDGSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS
|
Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2.
|
Q5D7J2
|
C5BDA3
|
CLSA_EDWI9
|
Cardiolipin synthase A
|
Edwardsiella
|
MSTFYTVISWLAIFGYWLLIASVTLRILMKRRAVPSAMAWLLIIYILPLVGIIAYLSFGELHLGKRRAERARTMWPSTARWLADLRSCRSIFATHNSEVAAPLFQLCERRQGIAGVKGNQLQLLTSTDDTLNALIRDIELAHTSIEMMFYIWQPGGLADRVAEAMMAAARRGIRCRLMLDSAGSVAFFRSPYPAMMREAGIEVVEALQVNLLRVFLRRMDLRQHRKVVLIDNFIAYTGSMNLVDPRYFKQDAGVGQWIDVMARMEGPVATTMGIYYAFDWEMETGKRILPPEPICNILPFEKESGHTIQVIASGPGFPEELIHQSLLTAVYSARQQLVMTTPYFVPSDDLLHAICTAAQRGVDVSIIVPKKNDSMMVGWASRAFFTEMLAAGVKIYQFEGGLLHTKSVLVDGQLSLVGTVNLDMRSLWLNFEITLVIDDDGFGSDLACVQEDYIARSSLLDPLEWLKRPLWQRVVERLFYFFSPLL
|
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
|
C5BDA3
|
Q2JZQ0
|
OIAX_RHIEC
|
3-oxo-isoapionate-4-phosphate decarboxylase
|
Rhizobium
|
MITLTYRIETPGSVETMADKIASDQSTGTFVPVPGETEELKSRVAARVLAIRPLENARHPTWPESAPDTLLHRADVDIAFPLEAIGTDLSALMTIAIGGVYSIKGMTGIRIVDMKLPEAFRSAHPGPQFGIAGSRRLTGVEGRPIIGTIVKPALGLRPHETAELVGELIGSGVDFIKDDEKLMSPAYSPLKERVAAIMPRILDHEQKTGKKVMYAFGISHADPDEMMRNHDIVAAAGGNCAVVNINSIGFGGMSFLRKRSSLVLHAHRNGWDVLTRDPGAGMDFKVYQQFWRLLGVDQFQINGIRIKYWEPDESFVSSFKAVSTPLFDAADCPLPVAGSGQWGGQAPETYERTGRTIDLLYLCGGGIVSHPGGPAAGVRAVQQAWQAAVAGIPLEVYAKDHPELAASIAKFSDGKGA
|
Involved in catabolism of D-apiose. Catalyzes the decarboxylation of 3-oxo-isoapionate 4-phosphate to L-erythrulose 1-phosphate.
|
Q2JZQ0
|
Q0I662
|
UREG_SYNS3
|
Urease accessory protein UreG
|
unclassified Synechococcus
|
MSSKLRLGVAGPVGSGKTALVQALCRRLRDRLQLAVVTNDIYTQEDAQFLTRSGALEPERIRGVETGGCPHTAIREDCSINRAAVSELEHQFPGLDLVMVESGGDNLAASFSPELVDLCIYVIDVAAGDKIPRKGGPGITRSDLLVINKIDLASFVGADLGVMEQDTLRMRRNRPWCFTNLRTEEGLDRVEEFVLQQIPN
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
Q0I662
|
Q5YW78
|
ECTA_NOCFA
|
L-2,4-diaminobutyric acid acetyltransferase
|
Nocardia
|
MSLQTLSTPTAEPVEEPRPVEAPWQVSDRIGTALLRAPQLGDAAEIWRIAKDSRVLDTNSSYAYLLWCRDFPGTTVVAEVDGRAVGFVIGYLRPESPDTVFVWQVAVSPTERGRGTGTALIQKLLDRVAPHGVTALETTISPDNPASIAMFAAVARRRGAQLTKQPLFDAGVFPDEHAPEDLYRIAPIAQEIR
|
Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
|
Q5YW78
|
A4J5Q8
|
MIAB_DESRM
|
tRNA-i(6)A37 methylthiotransferase
|
Desulforamulus
|
MAEKHQDKMTNAMNNSKLYLIQSFGCQMNERDAESLAGMLEDLGYCPTSAQEEADIILLNTCCVRETAESKVFGLLGRLRKLKVAKPDLILGVCGCMSQQEDAAKRIRRSFPFVDLIFGTHNIHELPRMIHQVQENHEAVLEVWATEKGITESIPVKRKDKLKAWVTIMYGCNNFCTYCIVPYVRGRERSRQPEDIIDEIKELVQEGYKEVTLLGQNVNSYGKDFKNNYRFADLLMAIDDITGLERVRFMTSHPRDFDQRLIEVVASAKKVCEHYHLPAQAGSNRVLKMMNRGYTREHYLELIRKIKERVPNASITADLMVGFPGETEEDFQETLDLVKQVRYDSAFTFVYNIRSGTPAAKLEQVSEEVKSERIQRLIELQNLISLENNQREEGRVLEVLVEGETKTNPDLLAGRTRTNKLVVFQGSGHLPGQLVQIRITKGRPNLLEGEVVPNGT
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
A4J5Q8
|
B3PGV8
|
GPMI_CELJU
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
|
Cellvibrio
|
MSAKKPVVLLILDGYGYSERTKYNAVYAAQTPVYDNLWKTCPNTLIDTSGMAVGLPAGQMGNSEVGHTTIGAGRVVYQSFTRINKSISDGDFFTNPEYVKAIDSAIANDRAVHILGLLSEGGVHSHQDHLYAMINMAVERGAKQVYLHAFLDGRDTPPRSAEASLQKAQDVFAKLGTGRVASIVGRYFALDRDNRWDRVKTAYDVMVTGEAEFDALTAVDGLKAAYERGENDEFVKATVICGEDEEVATINDGDSVIFMNFRPDRAREITRALIDENFTGFDRGETHPAIAHFVQTTEYASDIKAPIAFPPEDLSNSFGEYIAGLGKTQLRIAETEKYAHVTFFFNGGNEVVYPGEDRILVPSPKVATYDLQPEMSAPEVTDKLVEAIESGKYDAIICNYANCDMVGHSGLFDAAVKAVEAVDVALGRVLAAVKKVDGEALITADHGNVEEMFDEETGQPHTQHSTLPVPFIFVSSRKGKLASGGSLADVAPTILALMDLPQPKEMTGRNLITLEG
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
B3PGV8
|
Q1D749
|
RS4A_MYXXD
|
30S ribosomal protein S4 A
|
Myxococcus
|
MARYTASACRICRRENLKMYLKGDRCYTDKCAIERRPYPPGQHGQGRVKFSGYGVQLREKQKVKRMYGLLENQFRGYYHRASAAKGKTGDNLLQQLELRLDNVVFRMGFADTRNEARQLVRHGHFQVNGRKVNIPSFAVKPGTAVEVVEKSRKVLRISEALETVDRRGIPQWISLDKKAFKGTVTTVPNREDLTMPISEQLIVELYSK
|
With S5 and S12 plays an important role in translational accuracy.
|
Q1D749
|
Q8RC98
|
TSAD_CALS4
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Caldanaerobacter
|
MAKDIVILGIETSCDETAAGVVKNGKEVLSNVIYSQINVHKKYGGVVPEIASRKHIEAISFVVEEALNEAKLSLDEVDAIAATYGPGLVGPLLVGLSYGKALAYAKGKPFIGVNHIDGHIAANYIGGNLTPPFVCLVASGGHSHIVYVKDYGEYEVMGKTLDDAAGEAFDKVARALGLGYPGGPAIEKAAKLGNMEAIEFPKSFMEEGNFDFSFSGVKTAVLNYLNRQKQKGEEVNIYDVAASFQRNIVEVLVKKLVEAARFKNVSKVSIAGGVASNGFLRQKLEEDAKKFGLSVYYPEKIYCTDNGAMIAAAAYYDFVKGKFSGMDLNAIPYLKIGESDC
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q8RC98
|
P21809
|
PGS1_BOVIN
|
PG-S1
|
Bos
|
MWPLWPLAALLALSQALPFEQKAFWDFTLDDGLPMLNDEEASGAETTSGIPDLDSLPPTYSAMCPFGCHCHLRVVQCSDLGLKAVPKEISPDTTLLDLQNNDISELRKDDFKGLQHLYALVLVNNKISKIHEKAFSPLRKLQKLYISKNHLVEIPPNLPSSLVELRIHDNRIRKVPKGVFSGLRNMNCIEMGGNPLENSGFEPGAFDGLKLNYLRISEAKLTGIPKDLPETLNELHLDHNKIQAIELEDLLRYSKLYRLGLGHNQIRMIENGSLSFLPTLRELHLDNNKLSRVPAGLPDLKLLQVVYLHTNNITKVGVNDFCPVGFGVKRAYYNGISLFNNPVPYWEVQPATFRCVTDRLAIQFGNYKK
|
May be involved in collagen fiber assembly.
|
P21809
|
B0TPZ1
|
PSRP_SHEHH
|
Pyruvate, water dikinase regulatory protein
|
Shewanella
|
MLRKVFYISDGTAITAEVFGHAVLSQFPLEFDALTIPFVETEAKAEAVKAQINDCFITTGERPLVFHSIVKPEIRDVIYSSEGLDYDFLNTFVAPLEKQLGIAATPAMHRTHGKANEGYEARIDAINYAMENDDGQTMKHMDKADLILLGVSRCGKTPSSLYLSMQFGIKAANYPFTEDDMDNLKLPDALKRNKGKLFGLTIDPERLHEIRHSRMSNSRYSSLRQCRMEVKEVEMMYQKERIPFVNTTNHSVEEIATKILEITGLKRHMF
|
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
|
B0TPZ1
|
Q977Y1
|
MOAC_THEVO
|
Molybdenum cofactor biosynthesis protein C
|
Thermoplasma
|
MIDFDGNMINISRKDVVARKATAVGRIYLRKETITAIKNNQVKKGNVIEISRAVGTMYAKNTFLQIPYCHNIPIEGVDVDFSLGENYVEVTCSTTTSYKTGIEMEAINCVNGALLNIWDMVKYLEKDETGNYPETRIEGVHVIKKTKSQE
|
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
|
Q977Y1
|
Q1ACE1
|
CHLN_CHAVU
|
Light-independent protochlorophyllide reductase subunit N
|
Chara
|
MLEKISDTLTFECETGNYHTFCPISCVAWLYQKIEDSFFLVVGTKTCGYFLQNALGVMIFAEPRYAMAELEEGDISAQLNDYEELKRLCIQIKKDRNPSVIVWIGTCTTEIIKMDLEGMAPKLEAEIGIPIVVARANGLDYAFTQGEDTVLAAIVHRCPDYKLQNKTDLTDNDIQEDATRFSFLKLRKNNIRSISATNSHPPLVLFGSLPTTVSSQLNLELKRNQIEVSGWLPTQRYTDLPSLGEGVYVCGVNPFLSRTATTLMRRKKCKLISAPFPIGPDGTRAWIEKICNVFNIQPTGLEERENKIWDGLEDYLDLVRGKSVFFMGDNLLEISLARFLIRCGMIVYEIGIPYMDKRYQAAELMLLQKTCEMMNVPLPRIVEKPDNYNQIQRIRELKPDLAITGMAHANPLEARGISTKWSVEFTFAQIHGFTNARDILELVTRPLRRNQSLHELGWNNLVKVNSQ
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
|
Q1ACE1
|
Q97EI5
|
RL16_CLOAB
|
50S ribosomal protein L16
|
Clostridium
|
MLMPKRVKHRKVQRGRMKGKATRGNFIAYGDFAIQATECAWITSNQIEAARIAINRYVKRGGKLWIKIFPDKPVTQKPAETRMGSGKGSPEYWVAVVKPGRVLFEMSDVTEEQAREAFRLASHKLPIKTKFVTRKDFEEMGGEANEG
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q97EI5
|
Q0JQ12
|
CKX1_ORYSJ
|
Cytokinin oxidase 1
|
Oryza sativa
|
MAAIYLLIAALIASSHALAAHGAGGGVPLAAAAPLPFPGDLAASGKLRTDPNATVPASMDFGNITAALPAAVLFPGSPGDVAELLRAAYAAPGRPFTVSFRGRGHSTMGQALAAGGVVVHMQSMGGGGAPRINVSADGAYVDAGGEQLWVDVLRAALARGVAPRSWTDYLHLTVGGTLSNAGVSGQTYRHGPQISNVLELDVITGHGETVTCSKAVNSDLFDAVLGGLGQFGVITRARVAVEPAPARARWVRLVYADFAAFSADQERLVAARPDGSHGPWSYVEGAVYLAGRGLAVALKSSGGFFSDADAARVVALAAARNATAVYSIEATLNYAANATPSSVDAAVAAALGDLHFEEGFSFSRDVTYEEFLDRVYGEEEALEKAGLWRVPHPWLNLFVPGSRIADFDRGVFKGILQTATDIAGPLIIYPVNKSKWDAAMSAVTPEGEEEVFYVVSLLFSAVANDVAALEAQNRRILRFCDLAGIGYKAYLAHYDSRGDWVRHFGAKWDRFVQRKDKYDPKKLLSPGQDIFN
|
Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group.
|
Q0JQ12
|
B1JUA5
|
HIS6_BURCC
|
ImGP synthase subunit HisF
|
Burkholderia cepacia complex
|
MALAKRIIPCLDVTAGRVVKGVNFVELRDAGDPVEIARRYDDQGADELTFLDITATSDQRDLILPIIEAVASQVFIPLTVGGGVRAVEDVRRLLNAGADKVSMNSSAVANPQLVRDAADKYGSQCIVVAIDAKRVSADGETPRWEVFTHGGRKNTGLDAIEWARKMAELGAGEILLTSMDRDGTKSGFDLALTRGVSDAVPVPVIASGGVGSLQHLADGIKDGRADAVLAASIFHYGEHTVGEAKRFMSDQGIPVRL
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
B1JUA5
|
Q12L26
|
DXS_SHEDO
|
1-deoxyxylulose-5-phosphate synthase
|
Shewanella
|
MSFDISKFPVLAKANTPEDLRKLPQNMLSQVSTELRQFLLQSVGNSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKIMTGRRDEMHTIRQKNGLHPFPWREESEYDTFSVGHSGTSVSAALGMAIAADKEAAGRKVVAVIGDGAMTGGMVFEAMNHAGDLHKDMLVVLNDNEMSISENVGALNNHLAQLMSGRLYTTIREGSKKVLQGMPVIKEMAKRTEEHLKGMVVPGTLFEELGFNYIGPIDGHDVDALVETMRNMRSLKGPQILHIMTKKGRGYEPAEKDPIGWHAVPKFDPDQFKKPATKPGLPTFSQVFGKWLCDVAAQDDKLLAITPAMREGSGMVEFSQRFPEQYFDAAIAEQHAVTLAAGFACEGFKSVVAIYSTFLQRGYDQLIHDVALQRLPVLFAIDRGGIVGADGATHQGAFDLSFMRCIPNLVIMAPADENECRQMLYTGYRYQDGPTAVRYPRGFATGAEQIEQMTALPIGKGRVCRQGKKIAILNFGTTLASALEVAEQLDASVADMRFIKPLDVDLLHTLALEHDVIVTIEENAIMGGAGSGVIEALHKLKICKPVLQIGLPDEFIKHGAPDEIIAELRLDSKGILAQIQEYLSE
|
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
|
Q12L26
|
A8GPA1
|
SYI_RICAH
|
Isoleucyl-tRNA synthetase
|
spotted fever group
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MANTKYYPEVSSNANFAAIEREILKFWQDNNIFQKSIDGRNGESEFIFYDGPPFANGLPHYGHLLTGFIKDVYARYQTVKGKKVERRFGWDCHGLPAEMQSEKELGISGRLAITNFGIEKFNAHCRASVMEYASDWEEYVTRQARWVDFKNSYKTMDKNFMESVLWAFKELYNKGLLCESMRVVPYSWACETPLSNFETRLDNSYRERSDKAVTVSFVLRDKLHEIPAFAGMISRESEMTVGGDYQEYRILTWTTTPWTLPSNLAIAVGSDIDYALVPQENICYIIAASSVSKYAKELGLSGEENFEIIKGSQLQGLRYKPLFDYFEHHPNSFKIFDVDFVVEGDGTGVVHMAPGFGEDDQILCESKGISLVCPVDNSGKFTKEIPDLEGVQVFDANDKIIIKLKEQGNWLKTEQYIHNYPHCWRTDTPLIYKAVPSWYVKVTQFKDRMVELNQQINWIPHHVKDNLFGKWLENARDWSISRNRFWGTPLPVWKSDDPKYPRIDVYGSIEELEKDFGVKVTDLHRPFIDKLTRPNPNDPTGKSTMRRIEDVFDCWFESGSMPYGQAHYPFENKEWFEDHFPADFIVEYSAQTRGWFYTLMVLSTALFDRPPFLNCICHGVILDATGQKLSKRLNNYADPLELFDQYGSDALRVTMLSSNIVKGQELLIDKDGKMVFDTLRLFIKPIWSSYHFFTMYANADSLKGEISFASENVLDVYILSKLKIAVSKIEESLDNFDTQTAYHAVLEFFEVLNNWYIRRSRARFWKSEKDTDKQNAYNTLYSCLKTMAIAMSALVPMISEAIYKGLCHCEETSTLSSRDLIAGSSKSINNLNPVVKPRDYTPSVHHNDQISVHLCNYPTLSDFEINHELVATMDNVLDICSNSLFIRSTKNIRVRQPLASITIISKHNNDLKAFENLIKDEINVKSVIYCDDLENYASKKLSINFPMLGKRLPAKMKEIIAASKKGDWKAIAGGLTICGETLNNEEYKLILEPYSHIKGAASFENNSSLLILDLELTAELIEEGYARDIVRFIQQARKDAGFSITDRILIEIISEFDLSEIIYNYGDFITEQTLGEFSKNFTPDYVSKVELEDHPIQLKIKKS
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Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
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A8GPA1
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