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accession
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Full Name
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147
⌀
taxon
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46
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sequence
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2.75k
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5.51k
AlphaFoldDB
stringlengths
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10
C1FTP0
VATE_CLOBJ
V-ATPase subunit E
Clostridium
MSNLENLTSKIIEDANKEAEKLLSEAKKEENKIVNEKVKKGEKVKEQIIEKSKGEAKTKAERVISNTQLKVRNNKLEAKQEMINKVFDEAVIKLQNLPQEEYLNFIKNSILSLDIEGDEEIIVSPNDKNKIDISFILTLNNKLKAKGKKDLLKISNENRNIKGGFILYKNGIEINNSFEALVDSLRDELEQEIIEALFS
Produces ATP from ADP in the presence of a proton gradient across the membrane.
C1FTP0
O44326
HMP2_CAEEL
Protein humpback-2
Caenorhabditis
MLLHSTNSYSIFTDHEVETRTSRIRSAMFPDWIPPTSAAEATNSTTSIVEMMQMPTQQLKQSVMDLLTYEGSNDMSGLSLPDLVKLMCDHDESVVARAVHRAYMLSREDPNFFNAPGFDHRSFVEALMAASKSSNVNVRRNAIGALSHMSEQRGGPLLIFRSGGLAEIIRMLYDSLESVVHYAVTTLRNLLMHVSDSRAQARALNAVEALTPHLHKTNPKLLAQVADGLYFLLIDDAPSKITFLSLLGPQILVSILREYSDHRKLIYTVVRCIRSLSVCPSNKPALISLGCLPALYVELCTAKDERSQTAILVAMRNLSDSATNEENLTQLIIKLLEIIRVANDGMTACACGTLSNLTCNNTRNKQTVCSHGGIDALVTAIRRLPEVEEVTEPALCALRHCTARHSLAEEAQSELRFCQAFPVILDQLETLRTPVIKAALGVIRNSALLQTNLIELTQEQTANGHTAVSLTMDILRRAITAIEENPDIAVDGVPMWGVIEGAVSALHQLANHPAVAAACCDDIGQVGNPECPPFLDLLHRLLAHPRLGSMDDEVLEREILGLLYQLSKRPDGARAVESTGVSALLMESRGSQYKSVVTYANGVLSNLKRGDSAAIMNMSNSYDYEMSGSAADWQRDGLERELFAEMYPTNDGGHSESINMALNNSQMRPNHNWYDTDL
Required for cell migration during body enclosure and cell shape changes during body elongation . Plays a role in recruitment of the cadherin protein hmr-1 to adherens junctions .
O44326
Q123F6
EFTU_POLSJ
Elongation factor Tu
unclassified Polaromonas
MAKGKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLASKFGGEAKGYDQIDAAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLARQVGVPYIIVFLNKCDMVDDAELLELVEMEVRELLDKYDFPGDKTPIIHGSAKLAMEGDKGPLGEQAIMKLADALDTYIPLPERAVDGAFLMPVEDVFSISGRGTVVTGRVERGVIKVGEEIEIVGIADTQKTTCTGVEMFRKLLDQGQAGDNVGILLRGTKREDVQRGQVLCKPGSIKPHTHFTGEIYVLSKDEGGRHTPFFNNYRPQFYFRTTDVTGAIELPEGKEMVMPGDNVSITVKLINPIAMEEGLRFAIREGGKTVGAGVVAKIIA
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Q123F6
B2GBB7
RS20_LIMF3
30S ribosomal protein S20
Limosilactobacillus
MPIIKSAIERVRVNEKAAARNASQMSAMRTAIKKFDKAKLAGADNLDDLYKAAISAIDHAHSKGLIKANKAARDKSRLSARYAK
Binds directly to 16S ribosomal RNA.
B2GBB7
Q3MEJ8
PANCY_TRIV2
Cytidine monophosphate kinase
Trichormus
MRLLTTVAALRCYLNKRRWESQLTASEEQILDSMTSWYQTAIGLVPTMGSLHQGHLSLIERARHENSTVIVSIFINPLQFGPNEDYGRYPRTLEQDRQLCEQAGVDAIFAPSPEELGIPQKNIQESQVTQVIPPSVMISGLCGHSRLGHFQGVATIVTKLLNLVQPDRAYFGQKDGQQLAVIKRLVADLNLPVEIVACPTVREASGLACSSRNQYLTAPEKQQAAVLYRGLLQAEAAFKAGVRYSSRLREVVRQELAKVSSVLVEYIELVEPTTLMPLDKIQEEGMLAIAARLGSTRLIDNTILRDRQPIIAIDGPAGAGKSTVARQVATKLGLVYLDTGAMYRAVTWLVLQQGIAIDDDCAIAELANNCKIELTPSQDLQSPVRVWINDTDVTQDIRTIEVTSQVSAIAAQAAVREALVKQQQRWGKRGGLVAEGRDIGTHVFPDAEVKIFLTASVGERARRRQQDFQKQGQPEVSLEQLEKDIAERDWKDSTRKVSPLQKAADAVELQTDGLSISDVASQIVDYYQQRLSQW
Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively.
Q3MEJ8
Q5NVC7
RNF34_PONAB
RING-type E3 ubiquitin transferase RNF34
Pongo
MKAGATSMWASCCGLLNEVMGTGAVRGQQSGFAGATGPFRFTPNPEFSTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSVCSVLQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLILRNIPTDTCREKEDLVDLVLCHHGLGSEDDMDTSSLNSSRSQTSSFFTRSFFSNYTAPSATMSSFQGELMDGDQTSRSGVPAQVQSEITSANTEDDDDDDDEDDDDEEENAEDQNPGLSKERVRASLSDLSSLDDVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERLQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS
E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells. Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation.
Q5NVC7
P59226
H31_ARATH
Histone H3.1
Arabidopsis
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVAALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
P59226
A2BMD5
RL6_HYPBU
50S ribosomal protein L6
Hyperthermus
MAKAVYVAEEVRVPEGVEVSIDGLKVTVKGPKGELTRDFSHARNIVIRLDEDEEGKKVVVEAYFANRRVKALVGTIAAHIENMITGVTKGFRYKLKIVYSHFPVTVKVQGDKVVIENFLGEKAPRIAKIMPGVTVKVQKDDVIVEGIDIEAVGQTAANIEQATKVKDKDRRVFIDGIYIYEKGVAE
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
A2BMD5
B1IMF1
TGT_CLOBK
tRNA-guanine transglycosylase
Clostridium
MYKLLKKSGKARRGEFTTPHGVIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVVKKMGGLHKFMNWDRPILTDSGGFQVFSLSKIRKIQEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTIAMAFDECVENPAPREYVEKSVERTTRWLHRCKDEMNRLNSLPDTINNKQMLFGINQGGTYEDIRIEHAKTIAKMDLDGYAIGGLAVGESHEDMYRIIDAVVPHLPEDKPIYLMGVGIPSNILEAVDRGVDFFDCVLPARNGRHAHVFTKEGKINLLNAKFELDDKPIDEGCQCPACKHYTRSYIRHLFKAKEMLAMRLCVLHNLYFYNNLMEEIRDAIDGDYFKEYKERKLKEWGGRA
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
B1IMF1
O01929
NH153_CAEEL
Nuclear hormone receptor family member nhr-153
Caenorhabditis
MTPPQKSKPKRNRRKIYKILPQNQCPSVCQICRNPAIGYHYEVPSCNGCKTFFRRTIITGRKFKCFKVSNCLDGNDVIDTSKRVCRACRFEKCVQAGMNPMAIQAEAKTDEGEELKKLIAKKFENGEKLNDGTVFFNVHDRLNQILGKLIKIETKLEKVHDNGMPMGFLDQRDLSTALSSKVIYNNMEIPSMSYTPVKISKNTGLPKRRSRNFVHSSCLASIEYSKTFDFSSAIDISSKIILLKNTALSCANLTNAYTTFRKLKSDTLLYPDGSIYGPPRRKNGPLIEKQRSFLQNTLISFMTNNVDKTEYILLKAIVLCNPAIIDLPYADSKHIQREREVYAQCLFRYCLLQHGTLHGPARFSALLSIFNVLENQQKEQKDYYLYIKLIHSQKHKDPEVLKKKCISVIYDQIMD
Orphan nuclear receptor.
O01929
P25079
RBL_SOLTU
Ribulose bisphosphate carboxylase large chain
Solanum
MSPQTETKASVGFKAGVKEYKLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIERVVGEKDQYIAYVAYPLDLFEEGSVTNMLTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALFKAQAETGEIKGHYLNATAGTCEEMMKRAVFARELGTPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFIEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIVFNFAAMDVLDK
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
P25079
Q83GN3
MURE_TROWT
UDP-MurNAc-tripeptide synthetase
Tropheryma
MTLQGKPYRLSDLIKQTGVRLTDCSNQFSDRFVSGITQIAQSVERDDIFVAFQGKTRHGVEFLDQVQSCAAVLTDNKGRHIMQSDCLPTRSTPILVTDSPRSDLIVLAKRVYPIDDIRIFGITGTNGKTSTMHIAAKLLEMMGISCGISTTIGSSASESDSCLTTPELCQLYARIFTAKQARADFFALEASSHAINRGRLGDIVLEVAAFTNLTPEHMEEHKNMEAYYQAKKALFLNKRSNSAVINIDTPYGIRLFKETGCSASVISENTKYGLDHKLFWQASVRRVGLSFGFTLISPSGYRVESSISLLGKAFALNTCMAIVILCNLGIDIERIDSVLRKAGGLKMVLPGRMEVFQTGNSPRVIVDHGHTVDAVETALVAAKSITRGRLITIINADGQRDPSKRKHLGQLCGAYSDKLFITDGHSRFENPAEIRRMILDGVEGPRRQVEQIPSMTQAVLAAIDIARSDDTVLCSGFGDDPYLDVLGKKIPYSLRDEVRRGLERFAQGT
Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Q83GN3
Q93MW7
LIP_STRRM
SRL
Streptomyces
MRLSRRAATASALLLTPALALFGASAAVSAPRIQATDYVALGDSYSSGVGAGSYDSSSGSCKRSTKSYPALWAASHTGTRFNFTACSGARTGDVLAKQLTPVNSGTDLVSITIGGNDAGFADTMTTCNLQGESACLARIAKARAYIQQTLPAQLDQVYDAIDSRAPAAQVVVLGYPRFYKLGGSCAVGLSEKSRAAINAAADDINAVTAKRAADHGFAFGDVNTTFAGHELCSGAPWLHSVTLPVENSYHPTANGQSKGYLPVLNSAT
Catalyzes the hydrolysis of p-nitrophenyl esters, alpha- and beta-naphthyl esters, and triacylglycerols, with a preference for medium acyl chain length (C8-C12). Shows a much higher hydrolysis rate of glycerol esters of unsaturated C16 and C18 fatty acids than that of their saturated counterparts, and a preference for cis double bond. Is also able to hydrolyze several natural oils and Tween detergents. Also displays thioesterase and phospholipase activities, towards palmitoyl-coenzyme A and diheptanoyl glycerophosphocholine, respectively. Shows transesterification activity of racemic 1-phenyl ethanol with vinyl acetate in hexane, proceeding with partial (R)-enantioselectivity.
Q93MW7
A1JPP9
ARNB_YERE8
UDP-4-amino-4-deoxy-L-arabinose aminotransferase
Yersinia
MQNFLPFSRPAIGSDEINAVVNVLGSGWITTGPQNQQLETDFCAAFGCKHAVAVCSATAGMHITLMALGIGPGDEVITPSQTWVSTINMIVLLGAEPVMVDIDRDTLMVNAADIEAAITSKTKAIIPVHYAGAPCDLDALRQIAQQYKIPLIEDAAHAVGTRYGDQWVGEKGTTIFSFHAIKNITCAEGGLIATDDDELAAKVRRLKFHGLGVDAFDRQIQGRSPQAEVVEPGYKYNLSDIHAAIAVVQLQRLPEINARRQALAARYHQALVDSPLQPLFVPDYAHQHAWHLFMVRVDKERCGIDRDSLMARLKEVGIGSGLHFRAAHTQKYYRERYPSLHLPNTEWNSARLCTLPLFPDMLDSDVDRVVDALATIIGPHRV
Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
A1JPP9
B1A926
RPOC1_CARPA
Plastid-encoded RNA polymerase subunit beta'
Carica
MIDRYKHQQLRIGLVSPQQISAWANRILPNGEIVGEVTKPYTFHYKTNKPEKDGLFCERIFGPIKSGICACGNYRVIGDEKEDPKFCEQCGVEFVDSRIRRYQMGYIKLACPVTHVWYLKRLPSYIANLLDKPLKELEGLVYCDFSFARPITKKPTFLRLRGSFEYEIQSWKYSIPLFFTTQGFDTFRNREISTGAGAIREQLADLDLQIIIDYSFLEWKELGEEGPTGNEWEDRKIGRRKDFLVRRMELAKHFIRTNIEPEWMVLCLLPVLPPELRPIIQIDGGKLMSSDINELYRRVIYRNNTLTDLLTTSRSTPGELVMCQEKLVQEAVDTLLDNGIRGQPMRDGHNKVYKSFSDVIEGKEGRFRETLLGKRVDYSGRSVIVVGPSLSLHRCGLPREIAIELFQTFVIRGLIRQHLASNMGVAKSKIREKEPIIWEILQEVMQGHPVLLNRAPTLHRLGIQAFQPILVEGRAICLHPLVRKGFNADFDGDQMAVHVPLSLEAQAEARLLMFSHMNLLSPAIGDPISVPTQDMLMGLYVLTSGTRRGICANRYNPCNRKNYQNERIDDNNYKYTKEPFFCNSYDAIGAYRQKRINLDSPLWLRWQLDQRVIASREAPIEVHYESLGTYHEIYGHYLIVRSVKKEILCIYIRTTVGHISLYREIEEAIQGFCRACSYDT
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
B1A926
A4W6S6
LPXA_ENT38
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Enterobacter
MIDKTAFIHPTAIVEEGAVIGANAHIGPFCIVGPHVVIGEGTVLKSHVVVNGHTIIGRDNEIYQFASIGEVNQDLKYAGEPTRLEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLFMVNAHIAHDCTVGSRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGAHVMIGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLMYRSGKTLEEAKPEVAALAEQHPEVKAFTEFFERSTRGLIR
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
A4W6S6
Q822R2
DNLJ_CHLCV
Polydeoxyribonucleotide synthase [NAD(+)]
Chlamydia
MESMYSREQYLSLCKELEKDDYCYYVLHNAVISDYDYDMKMQKLLAIEAQHPEWKVLWSPSMRLGDRVSGNFPVVAHSHPMLSIANAYTLEELNDFFSRVEKTLGYAPIYTLELKIDGIAVAIRYEQGILVQALSRGNGQKGEDITANIRTIRSLPLRLPKDAPEFLEVRGEVFFKRETFEQINAAQRQAEKPEFANPRNAAGGTLKLLSAKEAAQRNLELSVYGSLSDENTESHYDNLMLCKRWGFPIFGQPRQCQTIAEVVKSLDEIEGLRDQLPMEIDGVVIKVDDVEAQKALGMTAKHYRWALAYKYAPERAETILENILIQVGRTGVLTPVAKLSPVFLSGSRVSRASLYNEEEIERKDIRIGDTVYVEKGGEIIPKVVGVCLEKRPEGTQPWVMPEFCPVCHGKVTRESDKVSVRCTNPLCSAGAIEKIRFFVGRGALDIDHLGEKVITKLFDLGVIHRCCDIFKITEEDLLQVPGFKDKSVKNVLKSIEKAKQAPLDRFIAALGIPYVGVRVASALAQHFLNLEAVMGASLEELKSIEGIGDKVAESIEAYFNQQDTIEEIQKMLSLGVNVLPYHRESSSCLGKTFVITGTLKKMTRSEAEASIRNCGGKVGSSVSKSTDYLVVGEDPGSKFKKAQELEIPILNENDLLKILYPN
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.
Q822R2
Q6C423
JHD1_YARLI
[Histone-H3]-lysine-36 demethylase 1
Yarrowia
MPNRCDFCTSSSTKDKQQWTQCDGCDRWVHDVCVSITDPVSYAKYHCPTCTKTKGPSLYKRQSKRKKIDIDYAAMHSGNVDMSLRTRHVHSSRFTDVAASAQNKEPFKRVSGTELTLDWAQSSDGLNEPVIVPKEYKDTLGMYIPEDLTVRQVAEAVGMESPVEVINVVSQNGSPGWNMGKWTEYYEDIEGRDTILNVISLEISASALGKTIVRPTLVRELDLVDRVWPTNTDAARESKPRVSLYALMSVEDSFTDFHIDFAGSSVFYHVLKGRKSFMFIRPTARNLAAYSQWCLSADQNVVFLPDVLSPDSDIYTVHLSPGDTMYIPSGWIHAVHSPQDSLVVGGNFITPLNMKTQIDIAGIEVRTKVPMKFRYPLFAGVMWYYVLQLLANPERLNTMSTKERDGLNSVAEYLSGFIKTMSPTMKDVQYRRFVANFPMEIRPFPGKTLLDYCAMLDFYPKGVQETVDIDIRKKKGESKEKHKIESQLPEEKILQGSKLESKEEVQTENF
Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
Q6C423
B8D6S0
MNMG_BUCAT
Glucose-inhibited division protein A
Buchnera
MFNLRNFDVIVVGAGHAGTEAAMASSRMGCKTLLLTQKISDLGALSCNPAIGGIGKSHLVKEIDALGGMMAKAIDYSGIQFRILNSSKGPAVRSTRAQADKILYHETVKKILKKQNNLLILEAEVKDLIFKNYSVVGVLTQNEINFYSRSVVLAAGTFLGGKIHIGLKSYSAGRIGDKSAIDLSVRLRELSLRVNRLKTGTPPRIDINTVNFNNLLIQNSDTPVPVFSFMGNVSHHPKQIPCYLTHTNEKTHEIIRKNLDKSPIYTGFLKGLGPRYCPSIEDKIVRFPDRKSHQVFLEPEGLSSIKVYPNGISTSLPIEVQEQIVASIKGLEKSKIIRPGYAIEYDFFDPKDLNLTLESKLIKGLFFAGQINGTTGYEEAASQGLLAGLNAALSSKNTEGWFPRRDQAYLGVLIDDLTTQGTEEPYRMFTSRAEYRLSLREDNADLRLTEIGRKLGLVNDSRWIRYNQKVLNIQTEMNRLKKNKISPISPDADILKKLYNINLIKEISMSELLKRPQIRYQDLQSLESFRTGIVDLEAIGQIENEIKYAGYIKRQSEEIERHLKNENTFLSSICDYNKIRGLSSEVVKKLNDYKPISIGQASRISGITPAAISILLIHLKKESYKHTL
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
B8D6S0
Q74JN5
RNZ_LACJO
tRNase Z
Lactobacillus
MEIQFLGTSAGQPSKSRNVSCIALKLLDELNEVWLFDVGEATQHQILKTNIRPRKVTRIFISHTHGDHIFGLPGFLSSRSFQGDGGPLTIYGPAGIEQFVQTSLRVSKTRVSYPIKYVVLKEDGLIFENDIFAVYTARLDHRVPSFGFRVVEKPRPGELLMDKVAEYNVPNGPLLGQLKAGKIITLSDGQKLDGRDFLGEERPGRIVTIIYDTRPTKNIGELADNADVLVHESTFDGGEEKMAHRYFHSTCLDAARVARDHNVGELYLTHISARYTGRAGRQLEHDARKIFKHTHLANDLDNFEITLRG
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Q74JN5
Q7N3J4
DAPE_PHOLL
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Photorhabdus
MTCPVIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERMPFGDTNNFWAYRGIGPTLAFAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHGTVKVVEALMSRNERLDYCLIGEPSSQHRLGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWDEGNEFFPATSMQIANIHAGTGSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILAGQPFLTAKGELVNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQRVMEQLIQ
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
Q7N3J4
A9B9X0
RS15_PROM4
30S ribosomal protein S15
Prochlorococcus
MTLNTQEKQKLINTHQNHGTDTGSAEVQVAMLSERISKLSNHLQKNIHDFSSRQGLLKMIGQRKRLLNYLRDKSNKRYTDIITKLKLRG
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
A9B9X0
Q4U923
RTCB_THEAN
3'-phosphate/5'-hydroxy nucleic acid ligase
Theileria
MTKTYKYEDQLHFIQKSDDVKNLFIIKKGFVPNMNVEGHLFANDNLSKLLFDELKQFTDDPGSFLPALKQLANVAALPGIVKSSIALPDAHSGYGFSIGNVAAFDMDNCNSIVSPGGVGFDINCGVRLLRTNLLYKDIEPIKEQLVQKLFDLIPVGVGCQGKIPCDYGDLDNILEYGMDWSVCSGYSWAEDKEHCEDFGRMIQADPTVVSYRAKKRGLSQIGTLGAGNHYGEVQVSIYSNIYVVEEIYDEYSAKVMGIDRIGQVCIMTHSGSRGLGHQVASDALVDMENSLNKSKIKVNDKQLACARINSDEGKKYLKGMAAASNYAWVNRSVMTHLTRKAFEEVLKESADDLDMHVVYDVSHNIAKIEDHMVDGKLKRLLLHRKGSTRAFPPYHPLISADFQHIGQPVLVGGTMGTCSYVLTGTQLAMDLTLGSTCHGSGRTLSRNKSRRVLDYNEVLNNLKEKGISIRVASPKLVTEEAPESYKDVSEVVQTCHDSGISKKCVKLRPVAVIKG
Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs.
Q4U923
P37965
GLPQ_BACSU
Glycerophosphodiester phosphodiesterase
Bacillus
MRKNRILALFVLSLGLLSFMVTPVSAASKGNLLSPDRILTVAHRGASGYVPEHTILSYETAQKMKADFIELDLQMTKDGKLIVMHDEKLDRTTNGMGWVKDHTLADIKKLDAGSWFNEAYPEKAKPQYVGLKVPTLEEVLDRFGKHANYYIETKSPDTYPGMEEKLIASLQKHKLLGKHSKPGQVIIQSFSKESLVKVHQLQPNLPTVQLLEAKQMASMTDAALEEIKTYAVGAGPDYKALNQENVRMIRSHGLLLHPYTVNNEADMHRLLDWGVTGVFTNYPDLFHKVKKGY
Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols.
P37965
A1E9N0
RK22_HORVU
50S ribosomal protein L22, chloroplastic
Hordeum
MTSFKLVKYIPRIKKKKSGLRKLARKVPTDRLLKFERVFKAQKRIPMSVFKAQRVLDEIRWRYYEETVMILNLMPYRASYPILKLVYSAAANATHYRDFDKANLFITKAEVSRSTIMKKFRPRARGRSFPIKKSMCHITIVLNIVKKSK
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
A1E9N0
Q9KUT4
ARGR_VIBCH
Arginine repressor
Vibrio
MRNVDKQDNLVRAFKALLKEERFGSQGDIVEALKNEGFDNINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGVPTASSSLRELVLDVDYNNALVVIRTGPGAAQLIARLLDSLGKSEGILGVVAGDDTIFITPTLDVPVKELFHSVCELFEYAG
Regulates arginine biosynthesis genes.
Q9KUT4
P0A368
CR1AA_BACTE
Insecticidal delta-endotoxin CryIA(a)
Bacillus cereus group
MDNNPNINECIPYNCLSNPEVEVLGGERIETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFPVQIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEADPTNPALREEMRIQFNDMNSALTTAIPLLAVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDAATINSRYNDLTRLIGNYTDYAVRWYNTGLERVWGPDSRDWVRYNQFRRELTLTVLDIVALFSNYDSRRYPIRTVSQLTREIYTNPVLENFDGSFRGMAQRIEQNIRQPHLMDILNSITIYTDVHRGFNYWSGHQITASPVGFSGPEFAFPLFGNAGNAAPPVLVSLTGLGIFRTLSSPLYRRIILGSGPNNQELFVLDGTEFSFASLTTNLPSTIYRQRGTVDSLDVIPPQDNSVPPRAGFSHRLSHVTMLSQAAGAVYTLRAPTFSWQHRSAEFNNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQISTLRVNITAPLSQRYRVRIRYASTTNLQFHTSIDGRPINQGNFSATMSSGSNLQSGSFRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVPAEVTFEAEYDLERAQKAVNELFTSSNQIGLKTDVTDYHIDQVSNLVECLSDEFCLDEKQELSEKVKHAKRLSDERNLLQDPNFRGINRQLDRGWRGSTDITIQGGDDVFKENYVTLLGTFDECYPTYLYQKIDESKLKAYTRYQLRGYIEDSQDLEIYLIRYNAKHETVNVPGTGSLWPLSAQSPIGKCGEPNRCAPHLEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHARLGNLEFLEEKPLVGEALARVKRAEKKWRDKREKLEWETNIVYKEAKESVDALFVNSQYDQLQADTNIAMIHAADKRVHSIREAYLPELSVIPGVNAAIFEELEGRIFTAFSLYDARNVIKNGDFNNGLSCWNVKGHVDVEEQNNQRSVLVVPEWEAEVSQEVRVCPGRGYILRVTAYKEGYGEGCVTIHEIENNTDELKFSNCVEEEIYPNNTVTCNDYTVNQEEYGGAYTSRNRGYNEAPSVPADYASVYEEKSYTDGRRENPCEFNRGYRDYTPLPVGYVTKELEYFPETDKVWIEIGETEGTFIVDSVELLLMEE
Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae.
P0A368
B0RDF9
NADD_CLAMS
Nicotinate mononucleotide adenylyltransferase
Clavibacter
MTTAATPRLRIGVMGGTFDPIHNGHLVAASEVQQHLQLDEVIFVPTGQPWQKQTVTDGEHRYLMTVIATAANPRFTVSRVDIDRAGTTYTIDTLRDIRRTHPDAELFFITGADAIQQILGWKDVAELWDLAHFVAVTRPGHDLTESGLPHADVRLLEVPALAISSTDCRARVGRGFPVWYLVPDGVVQYISKHHLYRSPL
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
B0RDF9
Q8FWP6
LIVB7_BRUSU
Leu/Ile/Val-binding protein homolog 7
Brucella
MEKHLIALSVAALLAGAAPASADIKMGSLYPFSGPLALLGDESARGLEIAVEEINAKGGVQGEKIVLVRGDAVDNNQAIGEARRLISVENVAGIFGTFSSGRAVAASQVSELAGVPYFELGAVADEITDRGLENVYRANPYARDFAQMIVEMLQKKIAPKLGKDSKDLKIAVIYEDSSYGTSVAKHEETFLKEAGLNMVLSQSYPGNTVDMSSLVLDLKSAGADVVLQTSYQSDSVLFLQQANEGGYKPSAIVGAGGGYSLQPTADAVGHDVIEAAYDVDFTQFAVNTSFTPGLEEFVEAYKKKYGETPRSGHSLTNYVGAKVILEALNKVKGFDAAAVKQALSAVDIEAGKTAMGYGFKFDQNNQNERASMMGMQWQDGKLVTVYPDAAAISEIRLPQ
Component of an amino-acid transport system.
Q8FWP6
A8AKS6
DCUP_CITK8
Uroporphyrinogen decarboxylase
Citrobacter
MTELKNDRYLRALLRQPVDVTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNAELACEVTLQPLRRYPLDAAILFSDILTIPDAMGLGLYFEAGEGPRFTSPVACKADVDKLPIPDPEDELGYVMNAVRTIRRELKGDVPLIGFSGSPWTLATYMVEGGSSKAFTVIKKMMYADPQALHALLDKLAKSVTLYLNAQIKAGAQSVMIFDTWGGVLTGRDYQQFSLYYMHKIVDGLLRENDGRRVPVTLFTKGGGQWLEAMAETGCDALGLDWTTDIADARRRVGHKVALQGNMDPSMLYAPPARIEEEVATILAGFGQGEGHVFNLGHGIHQDVPPEHAGAFVDAVHRLSEQYHR
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
A8AKS6
P20255
PA2BF_PSEAU
Phosphatidylcholine 2-acylhydrolase
Pseudechis
NLIQFGNMIQCANKGSRPSLNYADYGCYCGWGGSGTPVDELDRCCQVHDNCYEQAGKKGCFPKLTLYSWKCTGNVPTCNSKTGCKSFVCACDAAAAKCFAKAPYKKENYNIDTKKRCK
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
P20255
P50041
PYG4_THEVB
Phycobilisome rod-core linker polypeptide CpcG4
Thermosynechococcus
MDLPLLAYKPTTQNHRVASFGIADQNEDTPYIYRLEDAASYSEIREVIWACYRQVFSEHATLAFNRQITLESQLVNRVITVRDFIRGLAKSERFYNTVVAVNDNYRLVDVCLRRFLGRSAYNEEEKIAWSIKIGTLGFYGFVDALLDSEEYTNAFGDFTVPYQRKRMEGRPFNLVTPRYGFEYRDKVGTTKTDWRFTLEKFYDRKFQERRLPEGDPRKYRDLAAAIAPKTRYAQQLRAADIDYLAKVPRRR
Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.
P50041
B4T5A5
TUS_SALNS
DNA replication terminus site-binding protein
Salmonella
MSRYDLVERLNGTFRQIEQHLAALTDNLQQHSLLIARVFSLPQVTKEAEHAPLDTIEVTQHLGKEAEALALRHYRHLFIQQQSENRSSKAAVRLPGVLCYQVDNATQLDLENQIQRINQLKTTFEQMVTVESGLPSAARFEWVHRHLPGLITLNAYRTLTLINNPATIRFGWANKHIIKNLSRDEVLSQLKKSLASPRSVPPWTREQWQFKLEREYQDIAALPQQARLKIKRPVKVQPISRIWYKGQQKQVQHACPTPIIALINTDNGAGVPDIGGLENYDADNIQHRFKPQAQPLRLIIPRLHLYVAD
Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.
B4T5A5
Q96I51
RCC1L_HUMAN
Williams-Beuren syndrome chromosomal region 16 protein
Homo
MALVALVAGARLGRRLSGPGLGRGHWTAAGRSRSRREAAEAEAEVPVVQYVGERAARADRVFVWGFSFSGALGVPSFVVPSSGPGPRAGARPRRRIQPVPYRLELDQKISSAACGYGFTLLSSKTADVTKVWGMGLNKDSQLGFHRSRKDKTRGYEYVLEPSPVSLPLDRPQETRVLQVSCGRAHSLVLTDREGVFSMGNNSYGQCGRKVVENEIYSESHRVHRMQDFDGQVVQVACGQDHSLFLTDKGEVYSCGWGADGQTGLGHYNITSSPTKLGGDLAGVNVIQVATYGDCCLAVSADGGLFGWGNSEYLQLASVTDSTQVNVPRCLHFSGVGKVRQAACGGTGCAVLNGEGHVFVWGYGILGKGPNLVESAVPEMIPPTLFGLTEFNPEIQVSRIRCGLSHFAALTNKGELFVWGKNIRGCLGIGRLEDQYFPWRVTMPGEPVDVACGVDHMVTLAKSFI
Guanine nucleotide exchange factor (GEF) for mitochondrial dynamin-related GTPase OPA1. Activates OPA1, by exchanging bound GDP for free GTP, and drives OPA1 and MFN1-dependent mitochondrial fusion . Plays an essential role in mitochondrial ribosome biogenesis. As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation of core subunits of the oxidative phosphorylation system .
Q96I51
P17152
TMM11_HUMAN
Protein PMI
Homo
MAAWGRRRLGPGSSGGSARERVSLSATDCYIVHEIYNGENAQDQFEYELEQALEAQYKYIVIEPTRIGDETARWITVGNCLHKTAVLAGTACLFTPLALPLDYSHYISLPAGVLSLACCTLYGISWQFDPCCKYQVEYDAYKLSRLPLHTLTSSTPVVLVRKDDLHRKRLHNTIALAALVYCVKKIYELYAV
Plays a role in mitochondrial morphogenesis.
P17152
Q57PR2
SUFS_SALCH
Selenocysteine reductase
Salmonella
MTFPVEKVRADFPILQREVNGLPLAYLDSAASAQKPNQVIDAESAFYRHGYAAVHRGIHTLSAQATESMENVRKQASRFINARSAEELVFVRGTTEGINLVANSWGTENIRAGDNIIISEMEHHANIVPWQMLCERKGAELRVIPLHPDGTLRLETLAALFDDRTRLLAITHVSNVLGTENPLPDMIALARQHGAKVLVDGAQAVMHHVVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPPWEGGGSMISTVSLTQGTTWAKAPWRFEAGTPNTGGIIGLGAAIDYVTSLGLDKIGDYEQMLMRYALEQLAQVPDITLYGPAQRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAWYGVPAMCRASLAMYNTHEEVDRLVAGLTRIHRLLG
Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
Q57PR2
Q87Y33
RUVC_PSESM
Holliday junction resolvase RuvC
Pseudomonas
MTLILGIDPGSRITGYGVVRDTGRGCVYVASGCIRTGTGSGELHERLQIVYRGVREVIKTYGPVTMGIEKVFMARNADSALKLGQARGAAIVAGAEEALEIAEYTATQVKQAVAGTGGANKEQVMMMVMHLLKLTQKPQIDASDALAIALCHAHTRSSLIPHGLGTARSRGGRLRL
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
Q87Y33
C1FNE4
PRSA_CLOBJ
Foldase protein PrsA
Clostridium
MKSAKKLLSVLCLGIFILTFTACDMVEKTPEAKAKSTIAKVNGEKIQRKDLDESPSMQQVLSQIKTQYGEEFEKTEQGKEVIKEQKKQILENLITEKVLLQKGKELKVIPKDEELNKEADKKVNEIKAVYNNDEKKFEETLKSTGFTKETLKEYLKDQIVIEKVINEVTKDVKVEDKDAQKYYNENQSMFTEKPNTMNVSHILVKTEDEAKKVKKRLDAKEDFAKVAKEVSQDTGSKDKGGLLGDISYSDSNFDPTFMKAAIALKSGAISNPVHTQFGYHIIKINSKKEYPVKKFDSVKEDIKKQLKQEKQQEAYTKKIEEWKKASKIKTYEKNLL
Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
C1FNE4
Q9F284
CGIA_ZOBGA
Iota-carrageenase
Zobellia
MKLQFKPVYLASIAIMAIGCTKEVTENDTSEISEVPTELRAAASSFYTPPGQNVRANKKNLVTDYGVNHNDQNDDSSKLNLAIKDLSDTGGILTLPKGKYYLTKIRMRSNVHLEIEKGTVIYPTKGLTPAKNHRIFDFASKTEEKIENASIVGKGGKFIVDLRGNSSKNQIVADVGNVTNFKISNFTIKDEKTIFASILVSFTDKAGNAWPHKGIIENIDQANAHTGYGLIQAYAADNILFNNLSCTGGVTLRLETDNLAMKTAKKGGVRDIFATKIKNTNGLTPVMFSPHFMENGKVTIDDVTAIGCAYAVRVEHGFIEIFDKGNRASADAFKNYIEGILGAGSVEVVYKRNNGRTWAARIANDFNEAAYNHSNPAVSGIKPGKFATSKVTNVKATYKGTGAKLKQAFLSYLPCSERSKVCRPGPDGFEYNGPSLGVTIDNTKRDNSLGNYNVNVSTSSVQGFPNNYVLNVKYNTPKVCNQNLGSITSCN
Hydrolyzes iota-carrageenans, sulfated 1,3-alpha-1,4-beta galactans from red algal cell walls, with an inversion of anomeric configuration. Also active against hybrid iota-/nu-carrageenan, not active against kappa- or lambda-carrageenans.
Q9F284
Q8VDP6
CDIPT_MOUSE
Phosphatidylinositol synthase
Mus
MPEENIFLFVPNLIGYARIVFAIISFYFMPCCPFTASSFYLLSGLLDAFDGHAARALNQGTRFGAMLDMLTDRCATMCLLVNLALLYPRATLLFQLSMSLDVASHWLHLHSSVVRGSESHKMIDLSGNPVLRIYYTSRPALFTLCAGNELFYCLLYLFNFSEGPLVGSVGLFRMGLWVTAPIALLKSVISVIHLITAARNMAALDAADRAKKK
Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme.
Q8VDP6
B4S195
PURA_ALTMD
IMP--aspartate ligase
Alteromonas
MAKNVVVLGTQWGDEGKGKVVDLLTDRAKYVVRYQGGHNAGHTLVIDGEKTVLHLIPSGILRDNVTCIIGNGVVLSPDALMKEMTMLEERGVPVRERLKISEACPLILPYHIALDVAREKARGAKAIGTTGRGIGPAYEDKVARRGLRVGDLFNAEDFAAKLKEVLDVHNFTLTQYYGEEAVDFEETLNGAMEVADILKAMVVDVTDELDKAHKAGLPIMFEGAQGTLLDIDHGTYPYVTSSNTTVGGVATGAGFGPLKLDYVLGIVKAYTTRVGSGPFPTELDCEVGQHLGVKGHEFGATTGRKRRTGWFDAVAMKRAVQINSITGFCLTKLDVLDGLESLQICVGYKDADGNVKDVPPMAADGYDKVTPVYEEMPGWTDNTFGVTEFEGLPQAAKNYIKRLEELTGVPVDIVSTGPDRNETIVLRSPYDA
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.
B4S195
Q0AXL4
FMT_SYNWW
Methionyl-tRNA formyltransferase
Syntrophomonas
MRIVFMGTSHFAIPSLKALIASEHEIAGVVSQPDKQRGRGRKVTPTPVKEIAEQYKLELLQTANIKTPESIKRIKQWKPELIIVVSYGQIIPLSILEYPRHGCINVHASLLPRYRGAAPVQRALMDGIKSSGITIMFMDEGLDTGDIIMQEAIAVDDNINHGELEKILADMGADLLLQVVDRLVQGEKLPRVVQDDSQASYAARISKEDEIINWSEPAYAIHNRIRALNPQPGAYSYINGTKVKIFASKVRSEAGSGVIAEVIEVDKNTFQVQTGEGILEVLEIQKAGKKRMPTSEFLKGFTLHPGVLLGSKEG
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Q0AXL4
P40039
FCY21_YEAST
Fluorocytosine resistance protein 21
Saccharomyces
MPQTHEMSLNGTQYLKYELKDLESRAHDAKTPSTNEFYDDVESHGTEELVEAKLSFLNRIAAGLSAETKGIEPITEDEKTDDSILNAASMWFSANMVLPAYAIGALGPMVFDLNFGQSVFVIIFFNLLGLVSVAFFSVFGAELGLRQMILSRYLVGNIAARIFSFINFIACIGWGIVNTVASSQVLNMVNPGHQCPLWAGCIVIIGATVIVTFFGYGVIHAYEKWAWVPNFAVFLVIIARLARSKKFVLGEWTSGPTTAGNVLSFGSTVYGFAAGWTTYAADYTVYMPRKTNKYKIFFSLVVGLATPLYFTMILGAAVAMAAIGDPAWKTYYDENSIGGLTFAVLVPNSVHGFGQFCCVLLSLSTIANNVPNMYTIALSVQATWEPLAKVPRVIWTLLGNAAALGIAIPACYYFSTFMNYFMDSIGYYLAIYIAIACSEHFIYRRSFSAYNVDDWDSWERLPIGIAGTAALIVGAFGVALGMCQTYWVGEISRLIGDYGGDIGFELGLSWAFIVYNIARPFELKYFGR
Probable purine-cytosine permease.
P40039
Q1XDN9
EFTS_NEOYE
Elongation factor Ts, chloroplastic
Neopyropia
MTLQISAQVVKALRDKTGAGMMDCKKALQANNGNEEKALESLRQKGLASANKKSNRTAIEGLLESYIHTGGRIGVLVEVNCETDFVARRPEFQKLAKDIAMQIAASPNVEYVSTQDIPSEIINLEQRVEAGKDDLKNKPVDRIETIIEGRMKKRLKELSLLDQMFIRNQDISIEDLINQNIAVLGENIKIRRFVRFLLGGGEENLKVNFADEVADILNKK
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Q1XDN9
Q9CZB0
C560_MOUSE
QPs-1
Mus
MAAFLLRHVSRHCLRAHLNAQLCIRNAAPLGTTAKEEMERFWKKNTSSNRPLSPHLTIYKWSLPMALSVCHRGSGIALSGGVSLFGLSALLLPGNFESYLMFVKSLCLGPTLIYSAKFVLVFPLMYHSLNGIRHLLWDLGKGLAIPQVWLSGVAVVVLAVLSSGGLAAL
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Q9CZB0
B1IDB7
TPIS_CLOBK
Triose-phosphate isomerase
Clostridium
MRTAIIAGNWKMNKTVKEAVELVKELKPLVKDAKCDVVVCPTYVCLPAVLEEVKGSNIKVGAQNMHFEESGAYTGEIAPKMLEELGVHYVIIGHSERRQYFNETDETVNKKVKKAFEHNLIPIVCCGESLEEREGNITEKVLEGQIKVGLKELSKEQVEKLVIAYEPIWAIGTGKTATDEQANETIGYIRTVVKDMYGESVADKVRIQYGGSVKPGTIKAQMAKEEIDGALVGGASLKAKDFAAIVNY
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
B1IDB7
P35318
ADML_HUMAN
ProAM N-terminal 20 peptide
Homo
MKLVSVALMYLGSLAFLGADTARLDVASEFRKKWNKWALSRGKRELRMSSSYPTGLADVKAGPAQTLIRPQDMKGASRSPEDSSPDAARIRVKRYRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGYGRRRRRSLPEAGPGRTLVSSKPQAHGAPAPPSGSAPHFL
AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels.
P35318
C3PG33
RISB_CORA7
6,7-dimethyl-8-ribityllumazine synthase
Corynebacterium
MSKEGLPTPKDVSGKGLRVAVVTATWNAEICDQLHRRALETAEAAGAIVTPLRVVGALELPVVVQAAARTHDAVVALGCVVRGGTPHFDYVCDSVTQGLTRIALDESTPVANGVLTVNDYEQAVDRAGFADSAEDKGAEAMQAALETVHTLRTLDESNLK
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
C3PG33
P0CV26
RLR80_PLAVT
Secreted RxLR effector protein 80
Plasmopara
MKKRALPIVIFVISLQQSSQSFAVLDLLDQLFHKILNLSSRSISCSNCLKHRLQIPYFCSLHKGLNTVHKFRSLRTFQQCHELSKSNQKCHLSVMTRQVLRSRIMRALPLIKESLLLAQFLQ
Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins.
P0CV26
Q8UEQ7
MOBA_AGRFC
Molybdopterin-guanine dinucleotide synthase
Agrobacterium tumefaciens complex
MIAPPRKIPGLVPPGLILAGGLSRRMGSNKAMVTLGDAPLLSHVIRRVTPQVSDVTINAAITDKGSWAEGFGLPLLPDTLNGHAGPLAGVLAGMRHFRDRETAGSHFLTAPADSPFFPNDLVVRLCEHLSDDAIVIAASSGQLHPVFALWPVALADDLEDWLKNDANRRIRAFLARHVTIGVAFPPLETARGSLDPFFNINTPDELALARSQLETMET
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Q8UEQ7
G5EFF1
ASD2_CAEEL
Alternative splicing defective protein 2
Caenorhabditis
MDCDNGVVSEISDDKELLNLETVIPPPPNDSGHEFIGPSSGPPQVTITPSGVQSGSANGVSTSQQQQYSAEYLSQLLKDKKQLAAFPNVFHHLERLADEEINKVRVVLFQCEFSKESAPLPDAEGDSTVHTEKVFVPAKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGRGSMRDKKKEELNRGKPNWEHLSEELHVLIQCEDTENRAKVKLMRAVEEVRKLLVPAPEGEDDLKRKQLMELAIINGTYRSGTDQSALAAAQLAAVKHQQQPFAAALQAAALQRGVLPMMANGLSRSPTMAVCGAPIVMSPSGRASSAGATATSQAALIMQQQSQLHAANAGNAALQQQAALLQQQQAAEYQQLLLSQAGLYDFSAMQQQYAAVGQNAAVAAAQAQAQAQYGALAAAAAANSAGNQQYADYAGVDLTSQQSAHGGYYVRRWA
RNA-binding protein that binds to the 5'-NACUAAY-N(1,20)-UAAY-3' consensus sequence in pre-mRNA introns to promote alternative splicing . Required for mutually exclusive alternative splicing where it modulates the switch between mutually exclusive exons during pre-mRNA maturation . Involved in muscle-specific gene expression regulating the alternative splicing of genes such as let-2 and unc-60 to ensure that their respective isoforms are expressed in muscle . Promotes the removal of intron 10 from let-2 pre-mRNA to allow for the exclusive expression of the muscle-specific let-2 isoform (as opposed to the non-muscle-specific isoform expressed in embryos) in body wall muscles during late larval and adult stages of development . Binds cooperatively with RNA-binding protein sup-12 to intron 1A of the unc-60 pre-mRNA to promote alternative splicing and expression of the muscle specific isoform of unc-60 .
G5EFF1
Q02WN1
SYT_LACLS
Threonyl-tRNA synthetase
Lactococcus cremoris subsp. cremoris
MIKITFPDGNIKEFESGVTTFEIAKSISPSLAKKTLAGKVNGKLIDATRAINEDSDFEIVTPDHEDALGILRHSAAHLFAQAAKRHFPNIHLGVGPAIQDGFYYDTDNEAGQISNDDLATIEAEMKKIVKENFKSERKEVSKEEAKEIFANDPYKLELIEEHNEDEGGLTIYTQGEYTDLCRGPHVSSTGVIKFFHLLNVAGAYWRGNSDNKMMQRIYGTAWFSKEELEANLKLREEAKERDHRKLGRELDLFFNDAELGAGTAYWLPAGATIRRIIERFVVDQEVKNGYQHVITPVMMNLNTYKQSGHWQHYHEDMYPPMDMGDGEEMELRPMNCPSHIAIYKHHVHSYRELPIRIAEFGMMHRYEKSGALSGLQRVREMTLNDGHTFVMLEQVQEEFSKILQLIMDMYRDFGINDYSFRLSYRDPKDTVKYFPDDEMWEKSQAMLKATMDDMKLDYVEAEGEAAFYGPKLDIQVKTALGNEETLSTIQLDFLNPENFDISYVGADGEKHRPVMIHRGVISTLERFIAYLIEVYKGAFPTWLAPTQATIIPVNNEIHADYAWKIQRELQDKGFRVVVDEANEKMGWKIRQSQTHKIPYQIVIGDQEQANGTVNIRRYGSKETEVIPFEDFIEKISADVANFSRVD
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Q02WN1
Q1RLX4
TPC11_DANRE
Protein foie gras
Danio
MSPARWDLPPELCCRPMAFVALTGLDVVYNAIHRAIWDAFCANRRADRVPISFKVLPGDHEYPKCRTKRTSYEWYIPKGILKTGWMNKHLNLVPALVVLFYELDWDDPQWKEKQSECATKVEIVRTSLQGRNTKVAVVLIQKKTPLPPGEDLVASERASALCGACDLSGKSLFVLPHTDHLVGYIIRLENAFYEHAQTYYYNEIRRVKSHKEFLNKTTHQLLFVRHQFKMGFFSELKQDTQNALKYYRTAYSLVHELRAHETNVLEIKTMAGFINYKICRLCFQHNTPLDAIAQFRKHIDLCKKKIGSAELAFEHTAWMSKQFQSFGDLFDEAIKLGLTAIQTQNPGFYYQQAAYYAQERKQQAGQLCSHEPGVGYPAPDPLETTSGALDFYGQRPWRQGHQSIDPPDSEKEKQGILALQVKERDVLHSELIIALLSNAVAQFKKYKCPRMKSHLMVQMGEEYYHAKDYTKALKLLDYVMCDYRTERWWSLLTSIVCTALKCSYLMGQVKDYITYSMELVGRASILSEEQKSRIEKNLIKVLMNEVPEPEPDCDPVSVKAAQSLWSDRVSLAGNNEFTIDVQDYVPFVQCKAKFLSPSFHIDEPVQLHVYVRADCPHPVRFSKLCVSLSNQEYNQYCLLEDAYKGKDILEPSSQENMCLVPGKTRKYCFNFVAKTEDVGKKIEITSVGLMLGRETGRYVYLNWRGGWGDAASSHESLQASRSFKRRTRLPEQHVDWDAVSVQSSTMIISRVPKISVQLTHEPPALTNEMFCMTVTIKSEEDTVGKDIKLTAGLKPGQDANLTQSTQITLNGSEVCDDSHPALLPDIPLGDLQPGQKIVKPLYIRCVSTGSRIFLFHVAYSVSATVEGKDITCKCHKDETVTVETVVPFEVAMKFVSSKFEHLERVYVDIPFLLMMDILSASPWPIELVESEVQLASSMTAIDQPQSQVEGVTLQTSECASECFLLKCPPVQNGTSTVASGHYIISWKRKSTFTETSVVRTVITLPHVMVENIPLYVHAEVPSFGRVRESLPVRYHLENRTGLVQDVEISVEPSDAFMFSGLKQVRMRILPGAEQEMLYNFYPLMAGYQVLPQLNINLLRFPNISSQLLRRFLPSRIFVKPQGRNGDASIEAA
Involved in endoplasmic reticulum to Golgi apparatus trafficking at a very early stage.
Q1RLX4
A6L1Z2
G1095_PHOV8
Glycosyl hydrolase family 109 protein 5
Phocaeicola
MRTFKSLMISLCMGTTLCMCLPQTTTAQTVSSGDSWTWDKGTIVIDTPERPTGQKSVLGLTTPKMEVVRVGFVGLGMRGPGAVERFTYIPGTQIVALCDYEASRAEKCQDILKKASMPKAAIYSGEKGYEELCKRTDIDLVYIAADWLHHFPVAKCALENGKNVAIEVPSAMNLQECWDLINLSEKTRKHCMILENCCYDWFEMNTLNMAQQGVFGEVIRAQGAYIHNLSPFWDHYWKNGKEDKLGWRLDYNMKHRGDVYATHGLGPVAQALDIHRGDRITTLVAMDTKSVVGKDLVEKRTGEECKEFRNGDHTTTLLRTANGKVIEIQHNVMTPQPYNRLYQLTGSKGFANKYPVEGYALDAAQLTASGVQPKVDDLNSHGFLPQAEMEALVEKYQHPILKKYGEMAKEVGGHGGMDFIMDSRLVYCLQNGLPLDMDVYDLAEWCCLAELGAISMDNGCAAVAFPDFTRGEWNVTKGYKHAYASPEDENANMEKAKAFTAKLKEQGAKEWAKEAKKKKK
Glycosidase.
A6L1Z2
Q6CLQ8
GEP3_KLULA
Found in mitochondrial proteome protein 38
Kluyveromyces
MKSRLQAFKQFTRFVSCKSCGVELQSKNPSVTGYYKPPRAVRKDAGTIEDLKYLMFTQELQLKKHEIGLLDPDTDPDYKEPIPKRLVCKRCVDAISHNRYNSSDFPIHSFNDIKGALPHAANVYHVVSLSDFPLSLDKTILAEKNNRNYLLLSKADQITYKSSMLPHKGSAFFAEFCRRHIGVHVKKVVLFSNPRNWNIPSVINALAKRCYLLGNPNVGKTSLINSLLHEKSTSFQAQLDKRGNVIGPPKGHEQIQSTRRRAIFNEGGVSHIPNFTRTMQTYLIEDKVVNDLPGYTMDPTKVSDLANYIEKETLDNIRKTSKFKIDKLIKQNYTSLTGSKTGKCLSFGGIFHLVPPNSTINQVVNYIPLPEHEFSNVEKAVSLSLEVLQSENHSLRQFFALKKPFTDIKMFDRHVIPPFNGAIEIVLKDIGYFQVKPTGKYGFNGLYELWVPKGIRVCIREPLSKLISKSYEKYIESGDIADVCPTDRPLISDTYIMNHTEEDTFARMREMYINRTSKDILSRRLLQKDPNDIVGTLQSPPSNLYWYYKW
May be involved in the mitochondrial lipid metabolism.
Q6CLQ8
A0RPN4
HSLV_CAMFF
ATP-dependent protease subunit HslV
Campylobacter
MFHATTILAYKGNKGSIIGGDGQVSFGNTVLKGNAVKIRKLLGGKILAGFAGSTADAFNLFDMFERILESTKGDLLKAVIEFSKEWRKDKVLRKLEAMMLVLDREHIFLLSGTGDVVEPEDGKIAAIGSGGNYALAAARALDKFADINEEELVKESLKIAGEICIYTNTNIKTYALWDEK
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
A0RPN4
Q40073
RCAA_HORVU
Ribulose bisphosphate carboxylase/oxygenase activase A, chloroplastic
Hordeum
MAAAFSSTVGAPASTPTNFLGKKLKKQVTSAVNYHGKSSKANRFTVMAAENIDEKRNTDKWKGLAYDISDDQQDITRGKGIVDSLFQAPTGHGTHEAVLSSYEYVSQGLRKYDFDNTMGGFYIAPAFMDKLVVHLSKNFMTLPNIKIPLILGIWGGKGQGKSFQCELVFAKMGINPIMMSAGELESGNAGEPAKLIRQRYREAADMIKKGKMCCLFINDLDAGAGRMGGTTQYTVNNQMVNATLMNIADAPTNVQLPGMYNKRENPRVPIVVTGNDFSTLYAPLIRDGRMEKFYWAPTRDDRIGVCKGIFQTDNVSDESVVKIVDTFPGQSIDFFGALRARVYDDEVRKWVGSTGIENIGKRLVNSRDGPVTFEQPKMTVEKLLEYGHMLVQEQDNVKRVQLADTYMSQAALGDANQDAMKTGSFYGKGAQQGTLPVPEGCTDQNAKNYDPTARSDDGSCLYTF
Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.
Q40073
C5CEC0
GCH4_KOSOT
GTP cyclohydrolase FolE2
Kosmotoga
MRDVQSEKDHRNIPINMVGIKGLKYPIIVMDRTNKRQHTIGTFNLFVDLPKDFRGTHMSRFVEVLDRHNMKVTPKNMESILDDMREALKATVAHVTVDFPYFIRKNAPISGIGSYSSYNCGFISTKNKEFDFILKVEVPVLTVCPCSKEISDRGAHNQRAMVNVQVRMNSLVWIEEIIEMVEDAASAPIFTLLKREDEKFITEVSYDNPRFVEDVSREVVLRFMNDPRISWYRVEVSSQESIHNHEAYACIEKGKSL
Converts GTP to 7,8-dihydroneopterin triphosphate.
C5CEC0
Q9SE26
ACEA_DENCR
Isocitratsysase
Dendrobium
MASSSVPPMITEEEARFEAEVSAVESWWRTDRFRLTRRPYSARDVVSLRGTLHHSYASDQMAKKLWRTLKSHQSAGTASRTFGALDPVQVTMMAKHLDTIYVSGWQCSSTHTATNEPGPDLADYPYNTVPNKVEHLFFAQLYHDRKQHEARVSMTREQRAKTPYVDYLRPIIADGDTGFGGATATVKLCKLFVERGAAGVHIEDQSSVTKKCGHMAGKVLVAVSEHINRLVAARLQFDVMGVETVLVARTDAVAATLIQSNVDLRDHQFILGATNPDFKRRSLAAVLSAAMAAGKTGAVLQAIEDDWLSRAGLMTFSDAVINGINRQNLPEYEKQRRLNEWAAATEYSKCVSNEQGREIAERLGAGEIFWDWDIARTREGFYRFRGSVEAAVVRGRAFAPHADLIWMETSSPDLVECGKFAQGMKASHPEIMLAYNLSPSFNWDAAGMTDEEMRDFIPRIAKMGFCWQFITLGGFHADALVTDTFAREFAKQGMLAYVERIQREERNNGVDTLAHQKWSGANYYDRYLKTVQGGISSTAAMGKGVTEEQFKEESRTGTRGLDRGGITVNAKSRL
Involved in storage lipid mobilization during the growth of higher plant seedling.
Q9SE26
Q9JXM2
DCDA_NEIMB
Diaminopimelate decarboxylase
Neisseria
MTLFCEQVPYPRLAEAFGTPLYVYSQSALTEAFEHYQTAFAALNPLVCYAVKANGNLSIIKHFASLGSGFDIVSGGELARVLAAGGDAAKTIFSGVGKSEAEIEFALNAGVKCFNMESIPEIDRIQKVAARLGKTAPVSLRINPDVDAKTHPYISTGLKANKFGIAYADALEAYHYAAQQPNLKIIGIDCHIGSQLTDLSPLVEACERILILVDALAAEGIVLEHLDLGGGVGIVYQDENVPDLGAYAQAVQKLIGTRRLKLILEPGRSLVGNAGSLLTRVEFVKYGEEKNFVMVDAAMNDLMRPALYDAYHHIEAVETKDIATLTANIVGPICETGDFLGKDRTIACEEGDLLLIRSAGAYGASMASNYNARNRAAEVLVDGNEYRLIRRRETLEQQMANELACLQAEHQNAV
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Q9JXM2
B7V4H6
APAH_PSEA8
Diadenosine tetraphosphatase
Pseudomonas
MAVYAVGDLQGCLDPLKCLLERVAFDPAKDRLWLVGDLVNRGPQSLETLRFLYAMRESVVSVLGNHDLHLLAVAHKSERLKKSDTLREILEAPDREPLLDWLRRLPLLHYDEQRKVALVHAGIPPQWSLEKARLRAAEVEQALRDDQRLPLFLDGMYGNEPAKWDKKLHGIDRLRVITNYFTRMRFCTEDGKLDLKSKEGLDTAPPGYAPWFSFPSRKTRGEKIIFGHWAALEGHCDEPGLFALDTGCVWGARMTLLNVDSGERLSCDCAEQRAPARPAATPA
Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
B7V4H6
B2FNY8
ACCD_STRMK
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Stenotrophomonas maltophilia group
MSWLSKLMPSGIRTDNTPSKKRSVPEGLWEKCSNCGSALYRPELEENLEVCPKCGHHMAIRARARLAALFDADSTTEIGARLGPTDLLKFKDQKKYSERIKIAQKNTGEYDALIAMRGLLKGRALVASSFDFAFMGGSMGSVVGERFALAAETAVEIGAPYVCFSQSGGARMQEGLFSLMQMAKTSAALGKLRETGLPYISVLTHPTTGGVSASFAMLGDINIAEPQALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDQICDRREMRDRLSDLLAMLGRQPAPEVA
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
B2FNY8
Q2YUF6
ILVD_STAAB
Dihydroxy-acid dehydratase
Staphylococcus
MRSDMIKKGDHQAPARSLLHATGALKSPTDMNKPFVAICNSYIDIVPGHVHLRELADIAKEAIREAGAIPFEFNTIGVDDGIAMGHIGMRYSLPSREIIADAAETVINAHWFDGVFYIPNCDKITPGMILAAMRTNVPAIFCSGGPMKAGLSAHGKALTLSSMFEAVGAFKKGSISKEEFLDMEQNACPTCGSCAGMFTANSMNCLMEVLGLALPYNGTALAVSDQRREMIRQAAFKLVENIKNDLKPRDIVTREAIDDAFALDMAMGGSTNTVLHTLAIANEAGIDYDLERINAIAKRTPYLSKIAPSSSYSMHDVHEAGGVPAIINELMKKDGTLHPDRITVTGKTLRENNEGKEIKNFDVIHPLDAPYDAQGGLSILFGNIAPKGAVIKVGGVDPSIKTFTGKAICFNSHDEAVEAIDNRTVRAGHVVVIRYEGPKGGPGMPEMLAPTSSIVGRGLGKDVALITDGRFSGATRGIAVGHISPEAASGGPIALIEDGDEITIDLTNRTLNVNQPEDVLARRRESLTPFKAKVKTGYLARYTALVTSANTGGVMQVPENLI
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Q2YUF6
A1UAF0
Y592_MYCSK
Putative S-adenosyl-L-methionine-dependent methyltransferase Mkms_0592
unclassified Mycobacterium
MTTPDGIVSALAVALARQSESHADCPLFNDPYAQVFIDAALSRGCQLPSDETSERINGIANYASSRTKWFDEYFIAAGAHGLEQMVIVAAGLDARAWRLPWVAGTTLFEIDHPGVLKFKNEALHEHGESPSVSRYVPVPADLSDGWSERLRDAGFDVSEPTAWAVEGLLPYVADGPHLLFDRIHEISPAGSRLAVEAVGTGVADWLSTQGWQVTMIGAQELMTRYGRCGDHSDTDAGMDTVFVNATRTR
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
A1UAF0
P54807
GLNB3_METBA
ORF-105
Methanosarcina
MKMVRAILRPEWTEEVTDGLAEAGYYSLTKINVFGRGKQKGITVGDVHYDELAKTMIMMAVEDEAVDKVIKIISGKAYTGNMGDGKIFVNTIEAAYTISSGEKGL
Could be involved in the regulation of nitrogen fixation.
P54807
B7KHY7
RL3_GLOC7
50S ribosomal protein L3
Gloeothece citriformis
MSVGILGTKLGMTQIFDKETGIAIPVTVIHAGPCPITQVKTPATDGYNSIQIGYGEVKEKALNKPKLGHLKKSASTPVRHLKEYRLENAADYQLGDGIKVDLFKPGDLVDVAGKTIGRGFAGYQKRHNFKRGSMTHGSKNHRLPGSTGAGTTPGRVYPGKRMAGRYGGTQVTIRKLTVVQIDTERNLILIKGAVPGKPGNLLSITPAKTVGK
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
B7KHY7
Q8VZ59
YUC6_ARATH
Protein HYPERTALL1
Arabidopsis
MDFCWKREMEGKLAHDHRGMTSPRRICVVTGPVIVGAGPSGLATAACLKERGITSVLLERSNCIASLWQLKTYDRLHLHLPKQFCELPIIPFPGDFPTYPTKQQFIEYLEDYARRFDIKPEFNQTVESAAFDENLGMWRVTSVGEEGTTEYVCRWLVAATGENAEPVVPRFEGMDKFAAAGVVKHTCHYKTGGDFAGKRVLVVGCGNSGMEVCLDLCNFGAQPSLVVRDAVHVLPREMLGTSTFGLSMFLLKWLPIRLVDRFLLVVSRFILGDTTLLGLNRPRLGPLELKNISGKTPVLDVGTLAKIKTGDIKVCSGIRRLKRHEVEFDNGKTERFDAIILATGYKSNVPSWLKENKMFSKKDGFPIQEFPEGWRGECGLYAVGFTKRGISGASMDAKRIAEDIHKCWKQDEQVKKI
Involved in auxin biosynthesis via the indole-3-pyruvic acid (IPA) pathway. Also able to convert in vitro phenyl pyruvate (PPA) to phenyl acetic acid (PAA). Required for the formation of floral organs and vascular tissues. Belongs to the set of redundant YUCCA genes probably responsible for auxin biosynthesis in shoots.
Q8VZ59
Q87IL9
PCP_VIBPA
Pyroglutamyl-peptidase I
Vibrio
MKKVLITGFEPFGGDAINPALEAVKRLEETSLDGGIIVTCQVPVTRFESISAVIDAIEAYQPDCVITVGQAAGRAAITPERVAINVDDFRIPDNGGNQPIDEPIIEQGPDAYFSSLPIKRIAQTLHESGIPCQVSNSAGTFVCNHLFYGVQHYLRDKSIRHGFVHIPLLPEQATDGNHPSMSLDMIVAGLKLVAQVVIDHESDVVVSGGQIC
Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Q87IL9
Q48FB2
DPO4_PSE14
DNA polymerase IV
Pseudomonas
MTQRKIIHIDCDCFYAAIEMRDEPELAGKPLAVGGSAERRGVIATCNYEARAYGVRSAMSSRHALKLCPDLTIVKPRMEAYKEASREIHTIFRDYTDLIEPLSLDEAFLDVSDAGHFSGSATRIAQDIRRRVSNQLHITVSAGVAPNKFLAKIASDWKKPNGLFVITPDQVEDFVASLPVTKLHGVGKVTADKLGRLGIVDCADLRGRSKLALVREFGSFGERLWSLAHGIDDRPVQNDSRRQSVSVENTYDTDLPDLAACLEKLPALLETLGNRMARMEGQYRPGKPFVKVKFHDFTQTTLEQSGAGRDLGSYEQLLAQAFARGAKPVRLLGIGVRLHDLRAAHEQLELFSQ
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.
Q48FB2
P9WNZ4
DESA2_MYCTO
Putative acyl-[acyl-carrier-protein] desaturase DesA2
Mycobacterium tuberculosis complex
MAQKPVADALTLELEPVVEANMTRHLDTEDIWFAHDYVPFDQGENFAFLGGRDWDPSQSTLPRTITDACEILLILKDNLAGHHRELVEHFILEDWWGRWLGRWTAEEHLHAIALREYLVVTREVDPVANEDVRVQHVMKGYRAEKYTQVETLVYMAFYERCGAVFCRNLAAQIEEPILAGLIDRIARDEVRHEEFFANLVTHCLDYTRDETIAAIAARAADLDVLGADIEAYRDKLQNVADAGIFGKPQLRQLISDRITAWGLAGEPSLKQFVTG
May be a desaturase involved in mycobacterial fatty acid biosynthesis.
P9WNZ4
A8IAQ0
RS8_AZOC5
30S ribosomal protein S8
Azorhizobium
MSINDPIGDLITRIRNAQMRRKDKTSTPGSRLRASLLDVLRDEGYIRGYTTTDHGNGRTEFEIELKYFDGQPVIREITRVSKPGRRVYASVKALPRVANGLGIAVLSTPQGVMADHDARDKNVGGEVLCTVF
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
A8IAQ0
B1XHZ3
ATP61_SYNP2
F-ATPase subunit 6 1
unclassified Synechococcus
MLNSLTTFSLFPLAELEVGKHFYWELGGLKVHGQVLMTSWFVIAVLVLASILATRNVQRVPGGFQNFMEYALEFIRDLAKNQLGEKEYRPWVPFIGTLFLFIFIANWSGALVPWKIIGLPEGELAAPTNDINTTVALALLTSLAYFYAGFKKRGIGYLKKYLEPTPILLPINILEDFTKPLSLSFRLFGNILADELVVGVLVFLVPLIIPLPLMALGLFASAIQALIFATLAAAYIAEAMEGHH
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
B1XHZ3
B4F233
CYSH_PROMH
PAdoPS reductase
Proteus
MSRLSLSQLVLLSIEEQRLALDEINQQLEQKTAIERVIWALEHLPNQFVLSSSFGIQAAVCLHLLTRQYPDIPVILTDTGYLFPETYQFIDELTSSLQLNLKVYRAEISSSWQEARYGKLWLQGIEGIERYNQINKVAPMEKALKELQAKTWFAGLRRQQSKSREHLPVLSIAKGIFKLLPIVDWDNKQIYQYLKQHNLPYHPLWEQGYLSVGDTHTTRKWQEGMSEEETRFFGLKRECGLHE
Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
B4F233
O25788
GLUP_HELPY
Putative glucose/galactose transporter
Helicobacter
MQKTSNTLALGSLTALFFLMGFITVLNDILIPHLKPIFDLTYFEASLIQFCFFGAYFIMGGVFGNVISKIGYPFGVVLGFVITATGCALFYPAAHFGSYGFFLGALFILASGIVCLQTAGNPFVTLLSKGKEARNLVLVQAFNSLGTTLGPIFGSLLIFSTTKMGDNASLIDKLADAKSVQMPYLGLAVFSLLLALIMYLLKLPDVEKEMPKETTQKSLFSHKHFVFGALGIFFYVGGEVAIGSFLVLSFEKLLNLDSQSSAHYLVYYWGGAMVGRFLGSVLMNKIAPNKYLAFNALSSIVLIALAIIIGGKIALFALTFVGFFNSIMFPTIFSLATLNLGHLTSKASGVISMAIVGGALIPPIQGAVTDMLTATESNLLYAYGVPLLCYFYILFFALKGYKQEENS
Intake of glucose and galactose.
O25788
C1B2L3
GATB_RHOOB
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Rhodococcus
MTAVDTPDLLDYDEVLAKYEPVLGMEVHVELGTNTKMFCPCPTEFGAEPNTQVCPVCLGLPGSLPVVNEAAVESAIRIGLALNCSITPWGRFARKNYFYPDQPKNYQISQYDEPIATDGYLDVVLDDGTTWRVEIERAHMEEDTGKSLHVGGATGRIHGASHSLLDYNRAGVPLVEIVTKTISGAGARAPEVARAYVTALRDLLKSLNVSDVRMDQGSMRCDANASLMPIGATELGTRTETKNVNSLKSVEVAVRYEMRRQAAVLEAGGEVIQETRHFQEADGTTSPGRRKETAEDYRYFPEPDLEPVAPSAEWVEELRGTLPELPWVRRARIQADWGVSDEVMRDLVNANALDLVIATVEAGASPEAARSWWVSYLAQQANTRGVELGELPITPAQVAQVVALIDSGKLNNKVARQVVDHVLAGEGDPEQVVADHPELVVERDDTKLKAAVDEALAANPDIAEKIRGGKVAAAGKIVGDVMKATRGQADPARVKELVIEACGG
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
C1B2L3
P57309
FTSA_BUCAI
Cell division protein FtsA
Buchnera
MIISKDRKLVVGLEIGTTKVVTLVGEVLIDDNIKIIGFGTCLSKGIDKGKINNLDLIVSCIQESINKAEIMADCQITSVYLSLSNKYINCQNEIGIIPISDDEVTKEDIEHVIHIAQSVQILNEHHILHVIPQEYSIDQQYGIKNPIGLSGVRMQVKVHLITCHQNMARNIIKAVEKCDVKVDQVIFSGLASSKAVLTEDECNLGVCMIDIGGGTIDFTIYIDGSIKYSQVIPYAGNIVTSDISYAFSTSRDNAENIKIKYGSVKKPPLGSSKNIDFSDINCNFQQNLQQDALIDVIESRYVELLSLVQDQIVHLQKKLHKKGEKYELLSGIVLTGGGSNISCLTDCAEKVFQKKVRVAKPFNISGLIEKITEPCYSTVIGLLHYGKESYINIDKKKKEHSFFEIIFKRINNWFKKEF
Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
P57309
Q9KPU4
RISB_VIBCH
6,7-dimethyl-8-ribityllumazine synthase
Vibrio
MKVIEGGFPAPNAKIAIVISRFNSFINESLLSGAIDTLKRHGQISDDNITVVRCPGAVELPLVAQRVAKTGDYDAIVSLGCVIRGGTPHFDYVCSEMNKGLAQVSLEFSIPVAFGVLTVDTIDQAIERAGTKAGNKGAEAALSALEMINVLSEIDS
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Q9KPU4
Q2QL82
CTTB2_MICMU
Cortactin-binding protein 2
Microcebus
MATDGASCEPDASRAPEEAAGATAEAARKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCRKMQERMATQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEEAMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMKKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGPLTRSVACQTDLAIEGTDHVKKSPLTVPGKPSPGSAKGSVCANAAHVRPGMDRQASHGDLTGSSAPSLPPASANRIEENGPSTGSTADLPSSTAPAPGSAAQSPVAAALGPAHSAQSPCTPAPAQPGLNPRVQAARFRFQGNANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPAVGAAPRPGAPPTGDAGAYPPVGRTSLKTPGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIMDSSRASNAGAKVDNKTVASPPSSLPQGNRVISEENLPKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAETPGLNQPACSDSSLVIPTTTAFRSSINPVSASSCRPGASDSLLVTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHFECVELLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPVHAAVDTGNVDSLKLLMYHRAPAHGNSLNEEEPESDVSDLDDGEESSEGESKPVVPADLINHADREGWTAAHIAASKGFKNCLEILCRHRGLEPERRDKCNRTVHDVATDDCKHLLENLNALKIPLRISVGEIQSGNYGSSDFECENTICVLHIRKQTSWDDFSKAVSQALTNHFQAISSDGWWSLEDTAFNNTADSDIGLSLDSVRAIMLGSVPWSAGQSFTQSPWDFMRKNKAEQVTVLLSGPQEGCLSSVAYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIVHQLALCLKHRQMAAGFSCEIVRAEVDAGFSKEQLVDLFISSACLIPVKQSPVKKKIIIILENLEKSSLSELLGDFLAPLEIRSPESPCTFQKGNGTSECYYFHENCFLMGTIAKACLQGADLLVQQHFRWVQLRWDGEPMHGLLQRFLRRKLVNKFRGQAPSPCDPVCKTIDWALSVWRQLNSCLARLGTPEALLGPKYFLSCPVVPGHAQATVKWMSKLWNAVIAPRVQEAILSRASVKRQPGFGQTTTKKHPSQGQQAVVKAALSILLNKAVLHGCPLPRAELDQHTADFKGGSFPLSLVSNYNSCSKKKENGAWRKVNTSPRRKSGRFSSPTWNKPDLSNEGIKNKTISQLNCNKNASLSKQKSLENDLSLMLNLDPRLSLGSDDEADLVKELQSMCSSKSESDISKIADSRDDLRTFDSSGNNPAFSATVNNPRMPVSQKEVSPLSSHQTTECSNNKSKTEPGVSRVKSFLPVPRSKVTQCSQNTKRSSSSSNTRQIEINNNSKEENWNLHKNEQTHRKT
Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, thus controls dendritic spinogenesis and dendritic spine maintenance.
Q2QL82
Q7USA9
NUSB_RHOBA
Antitermination factor NusB
Rhodopirellula
MIARMSTRRRAREIVLQLLYEADLNDWRDAATSRKFIRSRLQGRKVLTDFAAELLDGTMARRDDIDAKLTKLSTNWALHRMPVTDRNVLRLGAYEILYSGTPGQVAISEALTLAKRYGGENSPRFINGVLDRLFKYHSNPESVSS
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
Q7USA9
B9DS40
XPT_STRU0
Xanthine phosphoribosyltransferase
Streptococcus
MKLLEERIIKDGNVLGENILKVDSFLTHQVDYHLMRDIGKVFAESYADAGITKVVTIEASGIAPAVYVAEALKVPMIFAKKHKNITMTEGILTAEVYSFTKQVTSTVSIASKFLSKDDKVLIIDDFLANGQAAKGLIEIIQQAGASVEGVGIVIEKSFQDGRQLLENMGVKVTSLARIKNFENGRLNFMEADA
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
B9DS40
O74849
GHT6_SCHPO
Meiotic expression up-regulated protein 12
Schizosaccharomyces
MAKILTIVMLVFVSMAGWMFGADTGSIGGITNMRDFQSRYADRYDPVTDTYSYSSARQGLLVGMVNTGTTVGCLLSSPLGDRFGKRKCIMGWTLVYITGVIVQLTTIPSWVQMMVAKIWTGLGIGALSVIAPGYQSESSPPHIRGAIVTTYQLFITLGIFIAACINMGTHKYTTHPEAQWRVPIGINLLWGILMFFGMLFLPESPRYLAVKGRNEECMKILTRNAGLPADHPIMQKEYNAIQADVEAELAGGPCSWPQIFSNEIRYRTLLGMGVMAFQQLTGNNYFFYYGTQVFRGTGLNSPFLAALILDAVNFGCTFGAIFVLEYFGRRGPLIVGGVWQSICFFIYASVGDRALTRPNGTSNHRAGAVMIVFSCLFIFSFAQTWAPAAYVIVGESYPIRYRSKCAAVATASNWFWNFMISFFTPFISNSIGFKYGYVFAACNLCAAIIIFLFAKETKGLTLEEINQLYLSNIKPWNTGAYQRDREDIKQSDSEKERGPTSKLHEYVEHAPNSYASTHSTESENYPQQVTNPVGL
High-affinity fructose transporter.
O74849
Q8Y015
NPD_RALSO
Regulatory protein SIR2 homolog
Ralstonia
MPTAVSDAAAPAQARAWIEAAERVMVLTGAGVSAESGVPTFRDALTGLWARFNPEDLATEAAYREHPRMVWDWYQERRARVSQVQPNPAHLAIAALATRKTVALVTQNVDGLHQRAGSVGVIELHGNLFANKWLDGCGKCDVATAEPGRPPRCAACGAMLRPGVVWFGERLPVVANYRAEEAANTCDVCLVVGTSGMVYPAAGLPGLAKDHGARVIVVNPEPSVLDETADLVIHQPAGVCLPAMLA
NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
Q8Y015
B7GVX4
RIBA_ACIB3
GTP cyclohydrolase II
Acinetobacter calcoaceticus/baumannii complex
MPIEFIATSKLPTAFGEFNISVFQDPVTGEEHVALSKGLENPPTGPVLVRVHSECLTGDAFASLKCDCGPQLQATQKLINEAGQGVILYLRQEGRGIGLTNKIRAYALQDQGHDTVDANLLLNLPADARRYDMCSIMLDHLKVKEVKLITNNPLKIQALKDQGINVVDRVPLTVGRNPFNEQYLKTKRERMDHLYQKDDF
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
B7GVX4
B2AAJ5
3HAO_PODAN
Biosynthesis of nicotinic acid protein 1
Podospora anserina
MLTQPINLPKWLEENSHLLKPPINNYCVYNEGFTVMIVGGPNARTDYHINQTPEWFYQHRGAMLLKIVDPTDNNTFKDIIIRQGDMFLLPPNTPHNPVRFADTVGIVLEQERPEGSIDRMRWYCQSCKEIVHEASFHCTDLGTQIKAAVEAFKEDEEKRTCKKCGEVAAWKPAEGSLKDPNLEEA
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
B2AAJ5
Q6HC29
MENE_BACHK
o-succinylbenzoyl-CoA synthetase
Bacillus cereus group
MMETMPNWLKQRAFLTPDRTAIEIEEEKVTFMQLHEKVVSVCEHLTHVGVKRGQKVAVLMKNGMEMITVIHALSYVGAVAVLLNTRLSREELLWQMDDAEVICLVTDQDFEAKDIPVYSFAEVMNGPKEEASIQEEFSLREAMTIIYTSGTTGKPKGVILTYGNHWASAVGSSLNLGLRDDDCWLACMPMFHVGGLSLLMKNIMYGMRILLVPKYDADFIHKALQTRGVTIISVVSKMLTDLLERLGEGTYPSSLRCMLLGGGPAPKPLLETCVDKGIPVYQTYGMTETSSQICTLSADYMLTKVGSAGKPLFQCQLRIEKDGVVVPPFAEGEIVVKGPNVTGGYFNREDATRETIQNGWLHTGDLGYLDEEGFLYVLDRRSDLIISGGENIYPAQIEEVLLSHPMVAEAGVVGMTDDKWGQVPAAFVVKSGEVTEEEILHFCEEKLAKYKVPKKACFLEELPRNASKKLLRRELRQLVEEM
Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
Q6HC29
Q4QM23
DSBD_HAEI8
Protein-disulfide reductase
Haemophilus
MKKLFLFFTLIFTAFAANSGLFDKKQTFLKVDDAFAFSATLSTDKSQLQAHWDIADGYYLYQDKISAELVGKSNPLSLHTQQAAELHQDPYFGEVKVFTHSIDGIFRGTFNNADDKVEITYQGCTEGFCYPPETKVLRIGDLAVSQEQIVEKTVEKNTALLSEQDRLADGLFHSKWTIFGFFLLGLGLAFTPCVLPMLPLLSAIVIGQQQRPNMMRAFSLAFLYVQGMALTYTLLGLAVAAIGLPFQIALQHPYVMIGLSILFVALALSMFGLFTIQLPNSLQNKLNTWSQKQTSGAFGGAFAMGMIAGLVASPCTSAPLSGALLYVAQSGDLFTGAATLYLLALGMGVPLMLITLFGNKILPKSGEWMNTVKQTFGFVMLALPVFLLSRILPEVWEPRLWAGLATVFFIWFALQMSKNGFGYAIKIISFALAMVTVQPLQNWIWQTQTTTQSAVENMPVSQVKFKQIKNTEELDRTLAENPHSIAMLDLYADWCVACKEFEKLTFSDPQVQQQFQNILLLQVNMTKNSPENKALMERFNVMGLPTILFFDQQNNEIQGSRVTGFMDADAFSNWLKALH
Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps.
Q4QM23
Q57J97
NTPPA_SALCH
Nucleotide pyrophosphatase
null
MTTLYLASGSPRRQELLTQLGFSFEQVVPGIEEQRRAQESAQQYVVRLAREKAQAGVALVPRDLPVLGADTIVVLNGEVLEKPRDAAHAAEMLRLLSGNTHQVMTAVALADSQQTLDCLVVTEVTFRTLSAQDITGYVASGEPLDKAGAYGIQGRGGCFVRKINGSYHAVVGLPLVETYELLSHFNALRDKRDKHDG
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Q57J97
A2C4Y0
KAD_PROM1
Adenylate monophosphate kinase
Prochlorococcus
MKKKLLFLGPPGAGKGTQANLFCKKYGLIHLSTGDLLRDEVSSGSVLGIKAAEIMNKGELVSDELVLSIVEGRLLNINEGWLLDGFPRNVNQANSLKDLLEKINQPLEGVILIKVADDYLIKRLVERGRQDDNEQVITNRLKIYREKTSPLIDLYKKQGILEEIEGNADIDVVFSCIEKSLG
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.
A2C4Y0
A3QFI1
4HYPE_SHELP
4-hydroxyproline 2-epimerase
Shewanella
MLKGTFFCVDAHTCGNPVRLVTSGHPDLKGRTMSEKRQDFLAQYDWIRKALMFEPRGHDMMSGAFLYPPCSDNADAAILFIETSGCLPMCGHGTIGTITAALESGLLTPKMPGQLTIDVPAGQIKVQYQQTGAKVDWVKIFNVPAYLAHKDVVLDIPGLGPLKIDVSYGGNYYAIVDPQANFPGLRHWSAGDILRWSPIVREVAHRELNCVHPDDPTVNGVSHVLWTGDTISEGSNGANAVFYGDKAIDRSPCGTGTSARLAQLYSRGELKVGDEYTHESIIGSQFVGRIEAATKVGAFDAIMPSIKGWARITGHNAITVDDNDPYAFGFQVV
Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Displays no proline racemase activity.
A3QFI1
Q4HXT5
GPI11_GIBZE
Glycosylphosphatidylinositol anchor biosynthesis protein 11
Fusarium
MSTTLIKSGPAQQQPAPKAAVPAIPLVNSPLALPASIAHSVLLAGLFYWRFDALVADPVTSLQTGLPVVAAIQAVYLMLSLPPAGSSLSSKKPRPGEKKSSDGREAKSFPLTSLAQTAVISLLLALILTPALHILLVLFGAPFLTHVPHTFLCCAHIALLAIYPVFYVRGSDPVPLQAVVGVSAPFDQTFGGFLGTVVGAWLGSVPIPLDWDREWQKWPVTIVVGAYLGYIVGSQLLGTVFYGRRWEVTPEMKEE
Acts in the GPI biosynthetic pathway between GlcNAc-PI synthesis and GPI transfer to protein.
Q4HXT5
A3PGL7
RS3_CERS1
30S ribosomal protein S3
Cereibacter
MGQKVNPIGMRLQVNRTWDSRWFAESKDYGNLLLEDLKMREFIHDYAKQAGVSKVIIERPHRKCRVTIHTARPGVIIGKKGADIETLRKKLSAFTKSELHLNIVEIRKPELDAQLVAESIAQQMERRVSFRRAMKRGVQNAMRIGALGIRVNVSGRLGGAEIARTEWYREGRVPLHTLRADIDYATSEATTPYGIIGVKVWIFKGEILEHDPQAHDRRHSEAQEGAAPRPPRRDRERA
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
A3PGL7
Q29497
CP17A_SHEEP
Steroid 17-alpha-monooxygenase
Ovis
MWVLLAVFLLTLAYLFWPKTKHSGAKYPRSLPSLPLVGSLPFLPRRGQQHENFFKLQEKYGPIYSFRLGSKTTVMIGHHQLAREVLLKKGKEFSGRPKVATLDILSDNQKGIAFADHGAHWQLHRKLVLNAFALFKDGNLKLEKIINQEANVLCDFLATQHGQSIDLSEPLSLAVTNIISFICFNFSFKNEDPALKAIQNVNDGILEVLGKEVLLDIFPALKIFPSKAMEKMKGCVETRNELLSEILEKCQENFTSDSITNLLHILMQAKVNADNNNTGPEQDSKLLSNRHMLATIADIFGAGVETTTSVIKWIVAYLLHHPSLKKRIQDSIDQNIGFNRTPTISDRNRLVLLEATIREVLRIRPVAPMLIPHKAIIDSSIGDLTIDKGTDVVVNLWALHHNEKEWQQPDLFMPERFLDPTGTQLISPSLSYLPFGAGPRSCVGEMLARQELFLFMSRLLQRFNLEIPDDGKLPSLEGNPSLVLQIKPFKVKIEVRQAWKEAQAEGSTS
A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol. Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione. Has 16-alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates androgens, relevant for estriol synthesis. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Q29497
Q1GHL1
MURI_RUEST
Glutamate racemase
unclassified Ruegeria
MAVGIFDSGLGGLTVLDAAQKRLPDVDFLYYGDNSHAPYGVRDAEDIYELTHKAVHDMWDRGCNLVILACNTASAAALRRMQEAGVPEGKRVLGVFVPLIEALTERQWGDNSPPREVAVKHVALFATPATVASRAFQRELAFRAIGVDVEAQACGGVVDAIEEGDMILAEALVKSHVDALLRKMPRPEAAILGCTHYPLMEDVFQKALGPDVQVFSQGRLVADSLAHYLERRPEMIGGGNAGYVTTGNANRVSSRATQFLRREITFEAA
Provides the (R)-glutamate required for cell wall biosynthesis.
Q1GHL1
Q5U2R4
TM10C_RAT
tRNA (guanine(9)-N(1))-methyltransferase
Rattus
MNVTVRFLRPFARYLVPYTFHRTRSNSYSRVLQRYVSSKVPSLPCHNKDSTSPPEQLELDGWKTTMKSSIQENGVSVVSDKDEDSLAATRELIEMWRLLGKEVPEHITEEELKTLMECASKSAKKKYLRYLYGKEMMKKAKQMKKEMKAAAREEAKRARSLEPSTGEEQRDFMFLRLWDRQTNIALGWKGVQAMQFGQPLVFDMAYDNYMKPSELQNTVSQLLESEGWNRRNVDPFHIYFCNLEVDGAYHRELVKRYGEKWDKLLLTATEKSPVDLFPKDSIIYLTADSPNVMTTFKHDKIYIIGSFVDKNTQTGTSLAKAKRQNLATECLPLDKYLQWDVGNKNLTLDQMIRILLCLKNTGNWEEALKFVPRRKHTGYLEVPEHSQAAFRKLKKTKTLNSFRKGSLNVHMWKR
Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends. Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. In addition to tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
Q5U2R4
P08070
TBA2_CHICK
Testis-specific
Gallus
MRECISVHIGQAGVQIGNACWELFCLEHSIQPDGTFSDPPSSDDSFATFFRETSMSKYVPRAIMVDLEPTVVDEVRTGTYRHLFHPEQLITGKEDAANNYARGHYTVGKDKVDMVSDRIRKLADSCSGLQGFLIFHSFGGGTGSGFTSLLMERLSVEYGKKSKLEFAIYPAPQASSAVVEPYNSVLTTHTTLEHSDCVFMVDNEAIYDICHRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPFPRIHFPLVTYAPIISSDRAYHEQLSVAEITSSCFEPNNQMVKCDPQQGKYMACCMLYRGDVVPKDVNVAIAAIKTNRSLQFVDWCPTGFKVGINYQPPIPTPGGDLAQVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVSEGMEEGEFAEAREDLAALEKDYDEVATDLFEDENEAGDS
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
P08070
P0DG19
TRMB_STRPQ
tRNA(m7G46)-methyltransferase
Streptococcus
MRVRKRKGAEEHLANNPHYVILNPEDAKGRWHDVFGNDRPIHIEVGSGKGGFITGMALKNPDINYIGIDIQLSVLSYALDKVLASEVPNVKLLRVDGSSLTNYFEDGEVDMMYLNFSDPWPKTKHEKRRLTYKDFLDTYKRILPEHGEIHFKTDNRGLFEYSLASFSQYGMTLRQIWLDLHASNYEGNVMTEYEEKFSNKGQVIYRVEANF
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
P0DG19
Q9SVC2
SY122_ARATH
Synt4
Arabidopsis
MNDLLSGSFKTSVADGSSPPHSHNIEMSKAKVSGGSCHGGNNLDTFFLDVEVVNEDLKELDRLCHNLRSSNEQSKTLHNANAVKELKKKMDADVTAALKTARRLKGNLEALDRANEVNRSLPESGPGSSSDRQRTSVVNGLRKKLKDEMEKFSRVRETITNEYKETVGRMCFTVTGEYPDEATLERLISTGESETFLQKAIQEQGRGRILDTINEIQERHDAVKDIEKSLNELHQVFLDMAVLVEHQGAQLDDIEGNVKRANSLVRSGADRLVKARFYQKNTRKWTCFAILLLLIIVVLIVVFTVKPWESNGGGGGGAPRQATPVQAQPPPPPAVNRRLLR
Vesicle trafficking protein that functions in the secretory pathway.
Q9SVC2
P87362
BLMH_CHICK
Aminopeptidase H
Gallus
MNAHGLSTEKAAAFTRRLRAEPQFLLAQNVATCSDPLEVCLQRQVVQDTIQVFQHAVPAEGKPVTNQKNSGRCWIFSCLNAMRLPFMKKYNIEEFEFSQSYLFFWDKVERCYYFLNAFVETAQKKEPIDGRLVQFLLTNPTNDGGQWDMLVNIVEKYGVVPKKYFPESHTTEATRRMNEILNHKMREYCLRLRNMVATGTNKEELCAAMDTMIEEVFRIVSTCLGNPPETFCWEFRDKEKNYHKFGPMTPVQFYNEHVKPYFNMEDKVCLVNDPRPQNPYCQLYTVEYLGNMAGGRKTLYNNQPIEVLKKLAATSIKDGEAVWFGCDVAKHFYSKLGINDLNIFNHELVFGVSVKNMNKAERLIFGDSLMTHAMVLTAVSEKDGQEDCYEKWRVENSWGEDRGNKGYLIMTDDWFSEYVYEVVVDKKYVPEDVLAVMEQEPIVLPAWDPMGALAK
The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity.
P87362
Q55028
NIFH_RIPO1
Nitrogenase reductase
Rippkaea orientalis
MRQIAFYGKGGIGKSTTSQNTLAGMAQAGNRIMIVGCDPKADSTRLILNCKAQVTVLHLAAERGAVEDLELSDVLLTGFENIKCVESGGPEPGVGCAGRGIITSINFLEEEGAYEDLDFVSYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMAMYAANNIARGILKYAHTGGVRLGGLICNSRNVNKEIELIEELAERLNTQMIHFVPRSKQVQEAELRRQTVIQYSPEHPQAQEYRDLGDKIVNNTKLTIPTPIDNDELEELLINYGLLGSEEEYKKVMEADMAAQALTRGAK
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
Q55028
B1I677
MNMA_DESAP
tRNA-specific 2-thiouridylase MnmA
Candidatus Desulforudis
MATVAVALSGGVDSSTTALLMKEAGHRVFTLTMATNDRVAAEAARVSAFLGLPHHVLDISGLFEQRVIGPFCAAYLEGRTPNPCIACNRDLKYGTLFRQAVEWGADYFATGHYARVRFEPEPGRYVLLRARDPRKDQSYVLFYLDQERLARLLLPLGDLTKETVREKARAAGIPFTAAESQEICFVAGDDYRTFIRRRCGQAVAEGPFVDRQGNVLGRHRGIPFYTIGQRRGLGLALGRPVFVLGFNRERNAVIVGPEEELWHTAFLAVDVHYILPQPAGGTLIEAQIRYRAKAAPARLYPQPPDAARVVFEKPQRAITPGQAAVFYQGERVVGGGIISCAVR
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
B1I677