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
|
|---|---|---|---|---|---|---|
A8LM72
|
RL6_DINSH
|
50S ribosomal protein L6
|
Dinoroseobacter
|
MSRIGKKPVELPTGVTASVSGQTIEVKGPKATRSFTATDDVTLKVEDNVITIEPRGKSKRARQQWGMSRTMVGNLVTGVTNGFKKELEIQGVGYRAQMQGNTLKLNLGLSHEVNYEVPAGVTVTCPKVTEIVIEGTDEQLVGQVAANIRDWRKPEPYKGKGIRYKGEFIFRKEGKKK
|
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.
|
A8LM72
|
A5FQR6
|
IF2_DEHMB
|
Translation initiation factor IF-2
|
Dehalococcoides
|
MVEKTSKPSAKTEVAPPVKIIELGAAVSVKELADSLETNPVEVIKALMRKGIMANINQVIDFDIAKGVIEAAGFEAKLKILKKSAAKKASPAKEKLSNFPLRPPVVTIMGHVDHGKTRLLDAIRSTNVMEKEVGGITQHIGAYQVEIKGHKITFLDTPGHEAFTAMRARGAQATDITILVVAADDGVMPQTLEALDHAKAAGVPIILAINKMDKPEANPDRVKQQLAEVGLVVEEWGGDTLAIPTSARENKGINELLEAVLLIAELEDLRADPNQPASGVVIEAEMDKTKGPMATVLVQSGTLKLGDTVVAGNTWGRVKAMFNDVGKRIKKAEPSTPVALLGMESVPQVGDKIIAVATEKQARDMVNENSQSTRKTNAVSLTNVYDQVSQGNIKELNIILKTDVQGSLEPIKDSLEKLSTDKIKININRSGAGNVTESDVMLAMASGGLIIGFSTGIETNAQRLADAEDIDIRHYDIIYKLIEDVDKALQGLLEPTIKEVIDGRAEVRAVFESTKKLSIAGCMVLEGKLVKNSQVRLLRGGEVIVDAPSNSLRRFKEDVKEVVAGYECGVGLKDFNEFQKSDILEFYHKEKSR
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A5FQR6
|
Q8I1A6
|
SH3G3_DROWI
|
SH3 domain-containing GRB2-like protein
|
Sophophora
|
MAFAGLKKQINKANQYMTEKMGGAEGTKLDMDFMEMERKTDVTVELVEELQLKTKEFLQPNPTARAKMAAVKGISKLSGQAKSNTYPQPEGLLAECMLTYGKKLGEDNSVFAQALVEFGEALKQMADVKYSLDDNIKQNFLEPLHHMQTKDLKEVMHHRKKLQGRRLDFDCKRRRQAKDDEIRGAEDKFGESLQLAQVGMFNLLENDTEHVSQLVTFAEALYDFHSQCADVLRGLQETLQEKRSEAESRPRNEFVPKTLLDLNLDGGGGGLNEDGTPSHISSSASPLPSPMRSPAKSMAVTPQRQQQPCCQALYDFDPENPGELGFKENDIITLLNRVDDNWYEGSVNGRTGYFPQSYVQVQVPLP
|
Required presynaptically at the neuromuscular junction. Implicated in synaptic vesicle endocytosis.
|
Q8I1A6
|
P54404
|
TBG2_EUPCR
|
Gamma-2-tubulin
|
Moneuplotes
|
MPREIITCQVGQCGNQIGMEFWKQLCMEHGISPEGILEEYALDGEDRKDVFFYQADDEHYVPRAVLIDLEPGVIKQIQNSPYSNLYNPENFFVSKTMDGAGNNWAKGYCEGAKYEEEIIEMIDREADGSDSLEGFVLTHSIAGGTGSGFGSYLLEKLNDHYPKKLVQTYSVFPNDNDIVVQPYNCILSMKRLVLNADCVVVLDNTAITSIAVDRLKLLHPTISQVNSIVSTVMAASTTTLRYPGYMNNDLVGLIASLVPTPRCHFLMTGYTPLSLNDQKVSSIRKTTVLDVMRRLLQTRNIMTSGAIKKGAYMSILNIIQGDVDPTQVHKSLQRIRERNVANFIPWGPASIQVALSKKSPYIESDNKVSGLMLANHTGIRSIFQVLYGQYRQFRKRDAFLGTYRETKIFQDNLDEFDSSEEVVKDLIDEYAAAEKMDYINRGKDDEDMDYDPRAPPNFRPIE
|
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
|
P54404
|
Q95A26
|
ATP6_PONPY
|
F-ATPase protein 6
|
Pongo
|
MNEDLFTPFTTPTVLGLPAAILVILFPPLLVPTSKHFINNRLITTQQWLIRLTLKQMMITHNTKGRTWSLMLTSLIIFIASTNLLGLFPYSFTPTTQLSMNLAMAIPLWASTVAMGLRFKAKISLAHLLPQGTPTPLIPMLIIIETISLFIQPLALAVRLTANITAGHLLMHLIGSATLTMLTINLPLTLITLTILTLLTILEIAVALIQAYVFTLLVSLYLHDNS
|
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
|
Q95A26
|
A1VRR7
|
TRPB_POLNA
|
Tryptophan synthase beta chain
|
Polaromonas
|
MYDYHQPDLAGHFGIYGGSFVSETLTHAINELKDAYARYQNDPKFLAEFNYELKHFVGRPSPIYHAARMSREQGGAQIYLKREDLNHTGAHKINNTIGQAMLARRMGKQRIIAETGAGQHGVATATICARYGLECVVYMGSEDVKRQSPNVYRMNLLGATVVPVESGSKTLKDALNEAMRDWVANVDNTFYIIGTVAGPHPYPMMVRDFQSVIGTECLSQMPEMNAGRQPDAVVACVGGGSNAMGIFHPYIAHENTRLIGVEAAGEGLDSGKHSASLQRGLPGVLHGNRTYVLQNDDGQVTETHSISAGLDYPGVGPEHAYLKDIGRAEYVGITDTEALQAFHYLCRTEGIIPALESAHAVAYAMKLAKTMRSDQSILVNLSGRGDKDIGTVADLSGADFYDRPSMRGLGVKGGVATSPESFDASGAKGAGSQS
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
A1VRR7
|
Q09FP7
|
RK23_NANDO
|
50S ribosomal protein L23, chloroplastic
|
Nandina
|
MDGIKYAVFTDKSIRLLGNNQYTSNVESGSTRTEIKHWVELFFGVKVIAMNSHRLPGKGRRMGPIMGHTMHYRRMIITLQPGYSIPPLRKKRT
|
Binds to 23S rRNA.
|
Q09FP7
|
Q1GK14
|
RL6_RUEST
|
50S ribosomal protein L6
|
unclassified Ruegeria
|
MSRIGKKPVELPSGVSASLSGQTIEVKGPKGAQTFTATDDVTLTVEDNVVKVEPRGKSKRARQQWGMSRTMVANMVQGVTQGFKKELEIQGVGYRAQMQGNTLKLNLGYSHDVDFTAPEGVTITAPKQTEIVVEGADAQAVGEVAAKIRDWRRPEPYKGKGIRYKGEFIFRKEGKKK
|
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.
|
Q1GK14
|
O33509
|
FMT_RICAK
|
Methionyl-tRNA formyltransferase
|
spotted fever group
|
YFSYNDKVIKILEAEYLNTIHHVTAGTVISDKLEIACGSGILQVKKLQQESKKALNVEEFLRGTNILKATILK
|
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.
|
O33509
|
Q3T165
|
PHB1_BOVIN
|
Prohibitin 1
|
Bos
|
MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ
|
In the plasma membrane, cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 produced through the activation of distal signaling intermediates. Upon CD40 engagement, required to activate NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation.
|
Q3T165
|
Q3E9B4
|
OFP8_ARATH
|
Ovate family protein 8
|
Arabidopsis
|
MEKRMKLRVSRIVRSSLSSCRPRDLYDVVETCAVTSKATSSERFFVTKAKTKTPSRPKSHASSCPRASPIFPPNPFYEESRSFRDLRKKVKTNRKQRSQFGSDPLFASRFKSTGSWYWSCSEEEDEGDKEESEDDDSDTLFSSRSFSSDSSKAESFAVVKKSKDPYEDFRTSMVEMIVERQIFAPAELQQLLQCFLSLNSRQHHKVIVQVFLEIYATLFSP
|
Transcriptional repressor that regulates multiple aspects of plant growth and development through the regulation of BEL1-LIKE (BLH) and KNOX TALE (KNAT) homeodomain transcription factors.
|
Q3E9B4
|
B6J8N7
|
SUCC_COXB1
|
Succinyl-CoA synthetase subunit beta
|
Coxiella
|
MNLHEYQSKHLLKKYNIPVPASEVVFNPDAAVDAAAKIGGDRWVVKAQVHAGGRGKAGGVRLVKNKEELKSAVKALLGTRLVTYQTDERGQPVNQILVEQTSDIARELYLGAVIDRASQRIVFMASTEGGVEIEKVAEKSPEKILKVTVDPAIGLQPFQCRQLFFGLGLQDLKQMRSFTDIVMGLYRLFTERDLSLLEINPLVITGSGELICLDAKINIDDSALYRQSELREMRDTTQEDEHETMAQQWELNYIKLDGNIGCMVNGAGLAMATMDLIKLSGGDPANFLDVGGSATKERVTEAFKIIASDKNVKGILVNIFGGIVRCDLIADGIISAVKEVGIDVPVVVRLEGNNAQLGAKKLADSGMNIIAAKGFADAAEQIVKQVGVIA
|
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
|
B6J8N7
|
Q8NGP8
|
OR5M1_HUMAN
|
Olfactory receptor OR11-208
|
Homo
|
MFSPNHTIVTEFILLGLTDDPVLEKILFGVFLAIYLITLAGNLCMILLIRTNSHLQTPMYFFLGHLSFVDICYSSNVTPNMLHNFLSEQKTISYAGCFTQCLLFIALVITEFYILASMALDRYVAICSPLHYSSRMSKNICVCLVTIPYMYGFLSGFSQSLLTFHLSFCGSLEINHFYCADPPLIMLACSDTRVKKMAMFVVAGFNLSSSLFIILLSYLFIFAAIFRIRSAEGRHKAFSTCASHLTIVTLFYGTLFCMYVRPPSEKSVEESKITAVFYTFLSPMLNPLIYSLRNTDVILAMQQMIRGKSFHKIAV
|
Odorant receptor.
|
Q8NGP8
|
Q8XHH1
|
LGT2_CLOPE
|
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase 2
|
Clostridium
|
MRIVLGEIFGLKIYSYGFMIGLGIICATLLFLKRGTQRGYNEDKLFNATILTVISGILGGKILYIITEWKTVMQDPSLIFRDFGNGFVIYGAIIGGALGIALCSLKNKWNVLELADLVVPGLALAQGFGRIGCLLAGCCYGAETTSSIGIIFPADSLAPAGVPLYPTQIFSSIFDFALGLFLLWYGNKNKEKGKTMSMYMIIYSIGRFFVEFLRNDPRGSVGLLSTSQFISIFILIGGILLYNINKLKGRKETGEK
|
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
|
Q8XHH1
|
Q6YW50
|
CKX7_ORYSJ
|
Cytokinin oxidase 7
|
Oryza sativa
|
MAARCSIAFMIMASCLSVVVSGGLPGDLFALSVASKLRVDRNSTARASSDFGRIVAAAPEAVLHPATPAEIAELVRFSASSPSPFPVAPRGQGHSARGQSLAPGGVVVDMRALASRRGRVNVSAGAAPYVDAGGEQLWADVLRATLEHGLAPRVWTDYLRITVAGTLSNAGIGGQAFRHGPQIANVLELDVITGTGDMVTCSRDKDSDLFFAVLGGLGQFGIITRARIGLMPAPKRVRWVRLAYSDVATFTKDQELLISKRASEAGFDYVEGQVQLNRTLTEGPKSTPFFSSSDIGRLAGLASKSVSGVIYVIEGTMYYNESTSTTMDQKLESILGQLSFEEGFVFTKDVRYVQFLDRVREEERVLRSIGMWDVPHPWLNLFVPRSRILDFDAGVFKGVFAGANPVGVILMYPMNTNMWDDCMMAVASDDDVFYAVGLLRSAAVIGDVERLEKENEAVLAFCHNEDIGCKQYLPYYTSQDGWQRHFGAKWSRVADLKAKYDPHRILSPGQRIFSSPASMVVVSM
|
Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group.
|
Q6YW50
|
Q8I7M8
|
CDK17_CAEEL
|
PCTAIRE-motif protein kinase
|
Caenorhabditis
|
MTAYSPADSNAEARLLSGGSDPISDTENLLDLAYEVGTSSSDNTRYDRESENDEEEIGVGWEDTTSSSLNKRMCKSATFHDFCDDSEYSRRPVTTLHEEDFDEEEEDEFEDASDRRNLDEDDVEYEDEDDEDDIVVEEEEITPEDIEHSPTGVTTQTTPPSNNTSKSKKKKKRKSDEEDGLRKMKKSSTFASFLNMFVSRRRSGRDSGERLMSRSTCMLRPSISLSVVQESMILGSDGESVEVSPCTSDQTPTGVPPRYIVNVKMRQKTARKWSEEEIQKRLSLPADLRLPVAVVDKLNRTPTLDQPLTRKNRRASLSEIGFGKLETYEKLDKLGEGTYATVFRGRSILTNKFVALKEIRLEQEEGAPCTAIREVSLLRNLRHANVVTLHDIIHTDRLLTLVFEYVDRDLKQYMDSCNNAMQMNNIRLFLYQLLRGLAYCHQRRVLHRDLKPQNLLITAKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTDYSTHIDMWGVGCILFEMIAGRALFPGGTPTEQLGLIFRTLGSPRPDRHPTICEKPTFYPYANRHYNPDPLCRQIPRIDAHGFELLMKFLQYEGKDRVSAAEAVKHPFLRTIAVKCCHLRDEQSVLEADGIHIERELLASDHHHSSRRHHRGTLVKDKYRMHSSHHT
|
Sufficient for synaptic vesicle trafficking in the DA9 motor neuron.
|
Q8I7M8
|
P08481
|
IPSG_PANLE
|
Double-headed protease inhibitor, submandibular gland
|
Panthera
|
ASPPEVNCSQYNRKGSGIACSKQLKPICGIDHKTYSNECMFCLLNQNKQFQIRKLYDDKCQIECTNYSAICTMEYFPLCGSDGKVYSNKCSFCNEVVKRRGTLFLAKYGQCK
|
This inhibitor is composed of two homologous actively inhibiting halves: one which inhibits trypsin, the other which inhibits elastase.
|
P08481
|
A5WCC8
|
CRCB_PSYWF
|
Putative fluoride ion transporter CrcB
|
Psychrobacter
|
MQWIAIGMGAAFGACLRALLGRLNPLHAWIPLGTLGANVLGGLLIGMAMVVFMKAGQLWHPNVKLFVMTGFLGGLTTFSTFSSEVFALLNSGKVMAGLVLIAVHVLLTLTATAMGYYLTRLCF
|
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
|
A5WCC8
|
Q9CLG7
|
RMUC_PASMU
|
DNA recombination protein RmuC homolog
|
Pasteurella
|
MQQDLNKTIEDFNQLLSKFEAVQQAKNQLEQHVVKYQTTAEGLQVRLIERDDKLAYLQKELDEEQARHNDIAEKITALKERFGIASAQAESLAKQLEHSQANFTRKEQENQELMAKLTTLSQELTELKTTLSEKEKHFAEQQQHIEQSKQQLSTEFQNLANRILDEKSRSFSQSNQTALDSLLKPFREQIEGFQKRVNEIHSESVKGNAGLEAEIKKVLEIGLNMSQQADNLTSALKGEKKTLGNWGEVQLERALQLAGLLEGEHYSAQAHLKDGEGKHNYPDFVLNLPDNKHLIIDSKMSLVAYESAVNAEDDLKRQNKLREHIKAIKNHIDDLSRKDYSNLIGMRSPNFVLMFIAVEPAYIEAMKMDPTLFNYGYEKNVILVSHTTLMPILRTVANLWRIERGNAEAKEISARAGDIYNQICVIAERLGKLGNTLSSASSHYNSTVTALVGQQGLVGKVERFKDLSAKANKTMPNVELLHHAVESERLDVIKADTPEAQPQKDNTAQ
|
Involved in DNA recombination.
|
Q9CLG7
|
A6W0S1
|
YCIB_MARMS
|
Inner membrane-spanning protein YciB
|
Marinomonas
|
MKILFDFLPIVIFFVVYKMTGNIIIATAILIPATIIQVGFTWFKNRTIEKMHLVSLALVVLLGGATVLLGDGDFIKWKPTIVNGLFAIAFLGSQFIGDKNIIQRMMGDKLDLPFKVWRTLNLAWVGFFIVSGVTNLYVAFSYSEEIWVDFKLFGLLGMTIVFIILQGIYLSSHLQNKE
|
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
|
A6W0S1
|
A4W3W3
|
ILVD_STRS2
|
Dihydroxy-acid dehydratase
|
Streptococcus
|
MTDTNKLKDFRHRSSVYDSMVKSPNRAMLRATGMTDDSFEKPIVGVISTWAENTPCNIHLHDFGKLAKEGVKEAGAWPVQYGTITVADGIAMGTPGMRFSLTSRDIIADSIEAAMGGHNVDAFVAIGGCDKNMPGSMIAIANMDIPAVFAYGGTIAPGNLNGKDIDLVSVFEGIGKWNNGDLTAEEVRQIECNACPGPGGCGGMYTANTMATAIEVMGMSIPGSSSHPAESPEKKADIEEAGRAVVRMLELGIKPSDIMTREAFEDAITVTMALGGSTNATLHLLAIAHAANVDLTLEDFNDFQERVPHLADLKPSGKYVFQDLYNVGGVPAVMKYLLKNGFLHGDRITCTGKTVAENLKNFADLTPGQDVIMPLENPKRADGPLIILKGNLAPEGAVAKVSGVKVRNHTGPAKVFDSEEEAIEAVLTDEIVDGDVVVVRYVGPKGGPGMPEMLSLSSMIVGKGQGDKVALLTDGRFSGGTYGLVVGHIAPEAQDGGPIAYLRTGDLVTVDQDTKEITMHVSDQEIEERKKTTVIPPLYSRGVLGKYAHTVSSASKGAVTDFWRPERTGKK
|
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.
|
A4W3W3
|
Q1LSP8
|
EPMA_BAUCH
|
EF-P-lysine lysyltransferase
|
Candidatus Baumannia
|
MNKLISWKPRASIHNLFIRAKIINNIRIFFINRGLLEVETPVMSHTTVPDIYLFPFQTNLYFLEKVPEKGVPMYLITSPEYHMKRLLAAGSGPIFQICHSFRNQEYGNYHNPEFTLLEWYRPYYNMVDIMDEVNIFLQTIIHCDSAEMLSYQQVFRLHVGIDPLLAELDELNQVLVKFNLSSTISLYNDRDKLLDFLFLMLVRPHLGNNKPVFIYNFPASQSLLAELNSDDHRVAERFEVYFHGIELANGSRELTDADLQRERFMQENNKQVAMNRPPRLIDEQLLAALECGLPSCSGVALGIDRLLMLTLKAKHISEVMAFSVTDA
|
With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.
|
Q1LSP8
|
A9AAH5
|
RF1_METM6
|
Translation termination factor aRF1
|
Methanococcus
|
MSGNSSTDMYLFKKSLKELKGKKGKGTELISVYVPAGRRLSDISQYLRQELSQSSNIKSKTTMKNVQSAIEVILQRLKLLKEPLEMGVIIFAGMIPRGGPGTEKMEVYVLEPPEPVKTFVYRCDSLFYTDPLEDFIQDTEVYGVILVDRNEATIGTVKGKTITVLKKLTSGVPGKFKAGGQSARRLERLIDDAAHQFMVRIGEYATESFMPILEEKKLKGLLLGGPGNTKNEFAEKDYLHHELKKKIIDTFDLCYTEEFGIRELLDKASDLLRDLDLMKEKNLIQRFFKELIKDDGGLSAYGEAQVMKYLEMGAIDTLIVTEDIGITRVTIKCNNCDYTQEVNVKTNEMFKFEEQLKTKACPTCGGAMYIDEEKDIIEHLSDLCNVHNTDIIVVSTDTEEGSQISRAFKGMAAILRYKL
|
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
|
A9AAH5
|
B4TUM9
|
AAS_SALSV
|
Long-chain-fatty-acid--[acyl-carrier-protein] ligase
|
Salmonella
|
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKKLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE
|
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
|
B4TUM9
|
Q3U0B3
|
DHR11_MOUSE
|
Short-chain dehydrogenase/reductase family 24C member 1
|
Mus
|
MTRAGMERWRDRLALVTGASGGIGAAVARALVQQGLKVVGCARTVGNIEELAAECKSAGYPGTLIPYRCDLSNEEDILSMFSAVRSQHSGVDICINNAGMARPDTLLSGSTSGWKDMFNVNVLALSICTREAYQSMKERNIDDGHIININSMCGHRVPPQSVIHFYSATKYAVTALTEGLRQELLEAQTHIRATCISPGLVETQFAFKLHDKDPGEAAATYEHIKCLRPEDVAEAVIYVLSTPPHVQVGDIQMRPTEQVT
|
Catalyzes the conversion of the 17-keto group of estrone, 4- and 5-androstenes and 5-alpha-androstanes into their 17-beta-hydroxyl metabolites and the conversion of the 3-keto group of 3-, 3,17- and 3,20- diketosteroids into their 3-hydroxyl metabolites. Exhibits reductive 3-beta-hydroxysteroid dehydrogenase activity toward 5-beta-androstanes, 5-beta-pregnanes, 4-pregnenes and bile acids. May also reduce endogenous and exogenous alpha-dicarbonyl compounds and xenobiotic alicyclic ketones.
|
Q3U0B3
|
A9WSU7
|
RL14_RENSM
|
50S ribosomal protein L14
|
Renibacterium
|
MIQQESRLKVADNTGAKEILAIRVLGGSGRRYAGIGDVIVATVKDAIPGGNVKKGDVVKAVIVRTKKERRRADGSYIKFDENAAVILKNDGDPRGTRIFGPVGRELRDKKFMKIISLAPEVL
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
A9WSU7
|
P11053
|
FERH_NOSS1
|
Ferredoxin, heterocyst
|
Nostoc
|
MASYQVRLINKKQDIDTTIEIDEETTILDGAEENGIELPFSCHSGSCSSCVGKVVEGEVDQSDQIFLDDEQMGKGFALLCVTYPRSNCTIKTHQEPYLA
|
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Donates electrons to the nitrogenase.
|
P11053
|
Q2K6G8
|
TYSY_RHIEC
|
Thymidylate synthase
|
Rhizobium
|
MQQYLDLLAHVMEKGSDRGDRTGTGTRSVFGYQMRFDLGEGFPVLTTKKLHLRSIVHELLWFLKGETNIRYLKENGVSIWDEWADENGDLGPVYGAQWRSWPAPDGGHIDQIANLVKGIVNNPNSRRHIVSAWNPAEVDQMALPPCHCLFQFYVADGKLSCQLYQRSADVFLGVPFNIASYALLTMMVAQVTGLKGGDFVHTLGDAHLYHNHFDQAKLQLTRRPKPLPFMRINPEVKDIFGFTFDDFELIGYEADASIKAPIAV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
Q2K6G8
|
O04351
|
OFP2_ARATH
|
Ovate family protein 2
|
Arabidopsis
|
MGNYKFRISEMLPNAWFHKLKDVTKHSKPKNKASSSSSNTCSKKKPSSDSLPQHSYFSNSLVANNPPHHNSPRNSLHTKKMSKRKTLYKPSLKPLTPPPLLVSASFNKSKINDQDSSYSLFPAIETSPESFVYSFYEEDDDDEFVEFSNFKINTKNKAFTKQKVKVIDSVEKACTASKPIKKPQKSHLSVKISRDEDDNEYKAEKKYQRQVSSGRKPSAGINLKRVNSPRIQLSGTRRSTSRRSESKQDVLESFAVMKRSVDPKKDFRESMIEMIEENNIRASKDLEDLLACYLTLNPKEYHDLIIHVFEQIWLQLTKTK
|
Transcriptional repressor that regulates multiple aspects of plant growth and development through the regulation of BEL1-LIKE (BLH) and KNOX TALE (KNAT) homeodomain transcription factors.
|
O04351
|
A7NLW9
|
PYRD_ROSCS
|
Dihydroorotate oxidase
|
Roseiflexus
|
MLYHLIRPLLFRLDAERAHDVVTAMFRATSRMPLLPRLISALYAWDDPALMVEWAGLRFASPLGVAAGFDKRADLVDALALLGFSHVEVGTVTPRPQPGNPGPRLFRLPEDMALINRLGFNSHGMVAVAKALRARRSRRVIVGVNIGKNRDTPLERAVEDYAATFVALAPLADYVAVNISSPNTPGLRRLHERAALEELLRELMRLNHGLLYPRPIALKISPDETLDQIEEVVRAGCEAGVAAFIATNTTLAREGLRSRLANETGGLSGRPLAPRARQVIRAIYRLTRGTPPVIGVGGVLTADDAYAHIRAGARLVQLYTGMVYAGPAIAREIKRGLAQLLRRDGFVSVTQATGVDAEWEGAIRQRG
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
A7NLW9
|
Q7W006
|
PURT_BORPE
|
Phosphoribosylglycinamide formyltransferase 2
|
Bordetella
|
MSTFPAPVLGTPLSPTATRVMLLGAGELGKEVVIALQRLGVEVIAVDRYADAPGHQVAHRAHVVSMTDPQALRQVIEQERPHVVVPEIEAIATDLLVALEDEGAVHVTPTARAAHLTMNREGIRRLAAETLGLPTSPYRFVDTEQALREAIDGGIGYPCVIKPVMSSSGKGQSIIRSADDIAAAWRYAQEGGRVGAGRVIVEGFIEFDYEITLLTVRARGADGQIVTQFCEPIGHRQVDGDYVESWQPHPMSPVALQRSREIALAVTGDLGGLGIFGVELFVAGDQVWFSEVSPRPHDTGMVTLISQVQNEFELHARALLGLPVDTRLRQPGASSVIYGGVDARGVAFEGVAQALAEPGTDIRLFGKPESYAKRRMGVGLAVADDVDQARAKAARVSQAVRVRA
|
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
|
Q7W006
|
A4J2F8
|
GCSPA_DESRM
|
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
|
Desulforamulus
|
MKFIPHTDEERRQMLKHLAVENTDQLFKDIPSELRLNRDLAVEGGLSEMELQSHMNSLAGLNTGVDQTICFLGAGAYDHYIPSAVKHILSRSEFYTAYTPYQPEISQGVLQSIFEYQSMICLLTGMDAANASMYDGASALAEAALMACAVTRRDKVLVASTLHPEYREVVKTYLHGPGIEISEIAYQEGLSQLADIDQKLDKKTAAVLVQYPNFFGCIEDLGKIAEQAHAKGALLVVCVDPIALGILKSPGQCGADIVVGEGQSLGIPLSYGGPYLGFMACKDKYLRKMPGRIVGQTVDVEGRRGYVLTLQAREQHIRRDKATSNICSNQALCALAATVYLSLVGRQGFKQVAELCLQKTAYAKELLAALPGYQLPWQTPVFKEFVLKTKEAPEVINRELLKENILGGLDLGGYYPELAGHMLFCVTEKRSRREIELLAARLGAIS
|
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
|
A4J2F8
|
Q18919
|
RCORB_CAEEL
|
Suppressor of presenilin 1
|
Caenorhabditis
|
MDLYDDDGESAQSEKVDVPSEESTIAGPETDIPAETIEENVPEVEENTLLEEDSLVDVDSPRPSQQRSKPSKSKRKRKRSSSGESSAAEPEIDAGAKVKGPLSNTNKEINVGTEFQAKIADLNLNDKACNEDRDDQDELIWNTPETIDDEKLEAFIRESSDRYLIPIDRALYILTINNFNFDSAIAEVARRNELKDVWTDQEITLFENCYQIFGKNFSQIRSALCHRSLQSIVQFYYESKKRVKYLNFVNSKCDDSSSSEETETPSPYPEAIFESMCDNCGEKAENMQINNAMNRPECRACLIYFNQTGVPRPTSLRLVLAERIRNQVSCPDNMKEYMKDFDKLSAQATGSTFQKRIIVKDQCVEYIIDVDKIPSSSCTENGNVGETSSPSAQKTEIQSESDGSGPLIWRHKKTVCMEEIEVLADDSRRKMFEACQHGSKVDIKLVASWKNDMTNLRKRVEQTYYDPDLNPTYLFSHDRVHYSQDWTQLERSQVIRCFNMYGAHFEHIADVIGTKTPDQVYQFYLENQKAIDAADEEFLADMKNPERLADMEEEEDSI
|
Probable corepressor protein, which probably participates in the transcriptional repression of the presenilin protein hop-1 . Probably acts via the formation of a multiprotein complex that deacetylates and demethylates specific sites on histones . Acts redundantly with the transcriptional repressor lin-35 to play a role in vulval morphogenesis and promote germline proliferation .
|
Q18919
|
B5XW51
|
RF1_KLEP3
|
Peptide chain release factor 1
|
Klebsiella
|
MKSSIVAKLEALYERHEEVQALLGDAATIADQDKFRALSREYAQLSDVARCYTDWRQVQEDIETAQMMLDDPEMREMAQEELRDAKEKGDQLEQQLQVLLLPKDPDDERNAFVEVRAGTGGDEAALFAGDLFRMYSRYAESRRWQVEILSANEGEHGGFKEVIAKFSGDGVYGRLKFESGGHRVQRVPATESQGRIHTSACTVAVMPELPEAEMPDINPADLRIDTFRSSGAGGQHVNTTDSAIRITHLPTGIVVECQDERSQHKNKAKALSVLGARIRAAEVAKRQQAEASTRRNLLGSGDRSDRNRTYNFPQGRVTDHRINLTLYRLDETMEGKLDMLIEPIVQEYQADQLAALSEQE
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
B5XW51
|
Q8XJ55
|
DAPB_CLOPE
|
4-hydroxy-tetrahydrodipicolinate reductase
|
Clostridium
|
MVKVILNGCSGKMGSVISNLAETKFPNVEIVAGIDNNTNAQRSYPIFAKPEDCNISYDVLLDFSRADALKSLVQFSKKTKKPLILCSTGYTAEDLKFIEESSKEIPLFRSANMSIGINLVNNLLKKVAPVLYENFDIELVERHHNQKVDAPSGTALLLAHTIQDSLNEETKLLYGREGIAKREKNEICVNTVRGGGIIGDHEVIFAGDGEVIEINHKAISRDVFAIGALKACEYMADKTKAGKYSMDDVLQLNF
|
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
|
Q8XJ55
|
P74977
|
HSTB_YEREN
|
Y-STB
|
Yersinia
|
MKKIILALVLMLFSFCTLGQETASMHLDDTLSAPIAAEINRKACDTQTPSPSEENDDWCCEVCCNPACAGC
|
Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells. Could play an important role in pathogenesis.
|
P74977
|
B0TJ76
|
RIMM_SHEHH
|
Ribosome maturation factor RimM
|
Shewanella
|
MSSKQEPVILGKLGSSFGIKGWLKITTYTDSVEGIFDYSPWLIKEQGEWREVKVAQWRFQGKAVVACLEGVTTRDEAQALTNCEIAVPAEQMQDLPEDEFYWRDLIGCEVINTKGYNMGTVQEIVETGSNDVLLVKANAKDGFGKAERMIPFVTDQFIQKVDLAAKQILVDWDPDF
|
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
|
B0TJ76
|
P39982
|
HHY1_YEAST
|
Hypersensitivity to hygromycin-B protein 1
|
Saccharomyces
|
MSLSFLLFSPFLPPCFSSISICLSVLSTVSFFFAFTIPHYVLRCGSVDEWHIHSSAEDFRTQRCVCAVKLSASLLGCLLACASWSLLLEVSRIKWHVGTAYS
|
Involved in vacuolar trafficking.
|
P39982
|
Q9BY66
|
KDM5D_HUMAN
|
[histone H3]-trimethyl-L-lysine(4) demethylase 5D
|
Homo
|
MEPGCDEFLPPPECPVFEPSWAEFQDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRVQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERKILDLYSLSKIVIEEGGYEAICKDRRWARVAQRLHYPPGKNIGSLLRSHYERIIYPYEMFQSGANHVQCNTHPFDNEVKDKEYKPHSIPLRQSVQPSKFSSYSRRAKRLQPDPEPTEEDIEKHPELKKLQIYGPGPKMMGLGLMAKDKDKTVHKKVTCPPTVTVKDEQSGGGNVSSTLLKQHLSLEPCTKTTMQLRKNHSSAQFIDSYICQVCSRGDEDDKLLFCDGCDDNYHIFCLLPPLPEIPRGIWRCPKCILAECKQPPEAFGFEQATQEYSLQSFGEMADSFKSDYFNMPVHMVPTELVEKEFWRLVSSIEEDVTVEYGADIHSKEFGSGFPVSNSKQNLSPEEKEYATSGWNLNVMPVLDQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMKMLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAAFPETLDLNLAVAVHKEMFIMVQEERRLRKALLEKGVTEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVCLSHINDLCKCSSSRQYLRYRYTLDELPTMLHKLKIRAESFDTWANKVRVALEVEDGRKRSFEELRALESEARERRFPNSELLQRLKNCLSEVEACIAQVLGLVSGQVARMDTPQLTLTELRVLLEQMGSLPCAMHQIGDVKDVLEQVEAYQAEAREALATLPSSPGLLRSLLERGQQLGVEVPEAHQLQQQVEQAQWLDEVKQALAPSAHRGSLVIMQGLLVMGAKIASSPSVDKARAELQELLTIAERWEEKAHFCLEARQKHPPATLEAIIRETENIPVHLPNIQALKEALTKAQAWIADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKNSCYTLLEVLCPCADAGSDSTKRSRWMEKALGLYQCDTELLGLSAQDLRDPGSVIVAFKEGEQKEKEGILQLRRTNSAKPSPLAPSLMASSPTSICVCGQVPAGVGVLQCDLCQDWFHGQCVSVPHLLTSPKPSLTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLPEGEALQCLTERAIGWQDRARKALASEDVTALLRQLAELRQQLQAKPRPEEASVYTSATACDPIREGSGNNISKVQGLLENGDSVTSPENMAPGKGSDLELLSSLLPQLTGPVLELPEAIRAPLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLDRIRTLLELEKFEHQGSRTRSRALERRRRRQKVDQGRNVENLVQQELQSKRARSSGIMSQVGREEEHYQEKADRENMFLTPSTDHSPFLKGNQNSLQHKDSGSSAACPSLMPLLQLSYSDEQQL
|
Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May play a role in spermatogenesis. Involved in transcriptional repression of diverse metastasis-associated genes; in this function seems to cooperate with ZMYND8. Suppresses prostate cancer cell invasion. Regulates androgen receptor (AR) transcriptional activity by demethylating H3K4me3 active transcription marks.
|
Q9BY66
|
Q9LFP0
|
APT5_ARATH
|
Adenine phosphoribosyltransferase 5
|
Arabidopsis
|
MFAAENGLKGDPRLEAISAAIRVVPNFPKKGIMFQDITTLLLDHKAFKHTIDIFVDRYKDMQISVVAGVEARGFLFGPSIALAIGAKFIPLRKPGKLPGKVISESYELEYGHDRLEMHVGAVEPRERVIIIDDLVATGGTLSAAMSLLESQGAEVVECACVIGLPEVKGQHKLKGKPLYVLVEPSGLDEFC
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. May contribute to the recycling of adenine into adenylate nucleotides and the inactivation of cytokinins by phosphoribosylation. Possesses low activity toward adenine, but can efficiently convert cytokinins from free bases (active form) to the corresponding nucleotides (inactive form).
|
Q9LFP0
|
Q941T1
|
P5CS2_ORYSJ
|
Glutamyl-gamma-semialdehyde dehydrogenase
|
Oryza sativa
|
MGRGGIGGAGLVAAVAKADVENTDSTRGFVKDVKRIIIKVGTAVVTGPNGRLAMGRLGALCEQVKQLNFEGYEVILVTSGAVGVGRQRLKYRKLVNSSFADLQNPQMDMDGKACAAVGQSVLMAIYDTLFSQLDVTSSQLLVTDRDFMDPSFGNQLRETVNSLLDLKVIPVFNENDAISTRRQPYEDSSGIFWDNDSLARLLAQELKADLLIMLSDVEGLYSGPPSDPQSKIIHTYVHEQHGKLISFGEKSRVGRGGMQAKVAAAFTASSKGIPVVIASGFAIDSIIKVMRGEKIGTLFHREANQWGCSKEATAREMAVAARDCSRHLQKLSSEERKKILLDIADALEANEDLITSENQADLDLAQDIGYDKSLVARMTIKPGKIKSLAGSIREIADMEDPISHTLKRTEVAKDLVFEKTYCPLGVLLIIFESRPDALVQIASLAIRSGNGLLLKGGKEAMRSNTILHKVITGAIPDVVGKKLIGLVKNKDEIADLLKLDDVIDLVIPRGSNKLVSQIKAATKIPVLGHADGICHVYIDKSADMDMAKRIVLDAKVDYPAACNAMETLLVHKDLNRTEGLDDLLVELEKEGVVIYGGPVAHDTLKLPKVDSFHHEYNSMACTLEFVDDVQSAIDHINRYGSAHTDCIITTDGKAAETFLQQVDSAAVFHNASTRFCDGARFGLGAEVGISTGRIHARGPVGVDGLLTTRCILRGSGQVVNGDKGVVYTHRELPLQ
|
P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants. Involved in abiotic stress tolerance.
|
Q941T1
|
B2TKE1
|
DEOB_CLOBB
|
Phosphodeoxyribomutase
|
Clostridium
|
MKKYNRIFTIVIDSLGIGGMPDSMEYGDKGVDTLGHIAESVEKFNIPNLEKLGISNLHPIKHVKAAEKPLAHYMKMKEASVGKDTMTGHWEMMGLHITKPFQTFTDTGFPQELLDELTKRTGHNIVGNKSASGTEILDELGEHQMKTGDMIVYTSADSVLQICGHEETFGLDELYRCCEIARELTLKDEWKVGRVIARPYLGSKKGEFKRTSNRHDYALKPYGSTALNTLKDNGFDVISVGKISDIFDGEGITESNKSKSSVHGMEQTLEIMDKDFKGLCFVNLVDFDALWGHRRNPVGYAEEIEKFDIKLGKVLEKLKEDDLLIITADHGNDPTYVGSDHTREFVPFIAYSPSMKENGLMDTVDSFATIGATIADNFELKMPENTIGKSVLEKLV
|
Phosphotransfer between the C1 and C5 carbon atoms of pentose.
|
B2TKE1
|
D9RZP4
|
ECFT_THEOJ
|
Energy-coupling factor transporter transmembrane protein EcfT
|
Thermosediminibacter
|
MREITIGQYIPGNSVIHRLDPRTKILITTAFMVLLFVIDDFTGYAFPAVFIIAVSILSGISLKYMMRGLRPLVIIIVLTFVLNLFMIKGRVIYEIGPLDITYEGLYQGTFMVLRLIMLIVGTSLLTLTTSPIALTDGIESLLKPFRRVGVPAHELAMMMTIALRFIPTLMEETDKIMKAQMARGADFASGNVVQRARSLVPLLVPLFINAFRRADDLAMAMESRCYRGGENRTRMKQLRMTSADLAAFIATGLLAVGSIMSRFIW
|
Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
|
D9RZP4
|
Q1LT56
|
DEF_BAUCH
|
Polypeptide deformylase
|
Candidatus Baumannia
|
MSLLPILYYPDHRLRQISKPVNKINNSIYRIVYDMFDTMYHKNGIGLAAPQVNINLNIIVIDVSENKEQRLVLINPELLAKSGETGIHEGCLSIPEQHGFVPRAKNIKVRALDLNGNSFNLETNDLQAICIQHEMDHLVGKLFIDYLSPLKRQRLLKKMKQLIRNLD
|
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
|
Q1LT56
|
B0JPS9
|
QUEF_MICAN
|
PreQ(0) reductase
|
Microcystis
|
MVQSSEKIEVKYGEREIAEGTLITFPNPRPGRNYDIQITLPEYTCKCPFSGYPDFATIYLSYVPDQKVMELKAIKLYINSYRDRYISHEEAINQILDDLVAACEPLQMKVKGDFHPRGNVHTVVEVMYKKE
|
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
|
B0JPS9
|
A0A0E3D8N4
|
PEND_PENCR
|
Penitrem biosynthesis cluster protein D
|
Penicillium
|
MTNSLLNNGDMVQGVELPDADQQFWWDSLAPILSRMLQCSKYSVQSQANILSFFKDFIVPSYGPRPSIDGEFFWKSYVTYNHTPGQVSFNFHKNKCTVRLSNVPTAPLAGTASDPFNQKGVVQTIKHIQKALPGMDMTIFDYFSEAFLVADEDTVGLDARKPVPQYNQLVVASMLGYDFEPVPRVKVYFNPRWKALQMNIENHDLIWTAINNLGSPIKSYKRTLDLLQECGNPRQPGGWIFQPEFISFDMGENMSNTARLKLYGFTTKTCWSHIESIYTLDRRLDDAETQRGLAVLKRLWHLALSIPEDHDENQDLPPCPHLTAGVIYNYELRENSAKPEAKIYIPVRFYGSGDGKVIEGLVDFFKSEGWDELATSYQRDFVSVFSTPDGKMVGEHHDISFSYKNDHPYVTAYYRPELIRPMERHIV
|
Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads to a epoxidized-GGI that is substrate of the terpene cyclase penB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase penQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase PC-15 which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase penD (Probable). A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase PC-16 and the P.simplicissimum ptmI-ortholog not yet identified in P.crustosum, leads to the production of the prenylated form of penijanthine (Probable). The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase PC-22 (Probable). A series of oxidation steps involving 4 cytochrome P450 monooxygenases (PC-21, PC-05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14) are required for the transformation of PC-M4 to penitrems A and E. Synthesis of these final products is proposed to proceed via penitrems D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC-14, PC-23) (Probable).
|
A0A0E3D8N4
|
Q9I9M5
|
FZD1_XENLA
|
Frizzled-1
|
Xenopus
|
MKHSHLLQRCSAQLCTRGSSLILSLLLSVCLSVEGQYNGEKGISIPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSIYAPVCTVLEQALPPCRSLCDRARQGCEALMNKFGFQWPESLRCEKFPINGAGELCVGQNTTESGTPTPAVPETWTSNSRTYYRDKFMCPRALKVPAYVNYHFLGEKDCGAPCEVGKVHGLMYFAPEELNFARIWIGIWSVLCCASTLFTVLTYLVDMKRFSYPERPIIFLSGCYTMVAIAYIAGFLLEDKVVCNERFAEDGYKTVAQGTKKEGCTFLFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAIKTITILAVGQVDGDTLSGVCFVGINNVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGIFSVLYTVPATIVIACYFYEQAFREQWEKSWISQSCKTYAIPCPSTGHPPMSPDFTVFMIKYLMTLIVGITSGFWIWSGKTLNSWRKFYTRLTNSKQGETTV
|
Receptor for Wnt proteins. Functions in the canonical Wnt/beta-catenin signaling pathway . The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes . A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable).
|
Q9I9M5
|
Q7NYR7
|
SYM_CHRVO
|
Methionyl-tRNA synthetase
|
Chromobacterium
|
MIRMTKRKILVTSALPYANAGLHLGHMLEQIQTDIWVRFQKMRGHECYYVCADDTHGAPIMLAAEKRGITPEQLVNEVRELHVADSQGFLIGHDNYYSTNSPENKALAEQVYLALKADDKIACRTIEQLFDPEKQMFLPDRFVKGECPKCSAKDQYGDNCEVCGATYAPTELKNPYSAVSGAKPVLKTSEHFFFRLGECADFLKAWTSGASRRADGAVQPHLQPESLNKMNEWIGGGLQDWDISRDAPYFGFEIPGAPGKYFYVWLDAPIGYMASFKNLCERLNLNFDEWFAKDSQTEMYHFIGKDILYFHALFWPAMLNYSGLRAPTGVFAHGFLTVDGQKMSKSRGTFIQAKSYLDCGLNPEWMRYYIAAKLNGRIEDIDLNLNDFVARVNSDLVGKFVNIASRSAGFIAKRFDGMLAAQVSDGEILAKLQAAAEELAAAYEAREYAKALRDVMALADIVNGYVDANKPWELAKQEGQDARLQDVCTVLVNAFRLLAIYLKPVLPKLAEGVEAFLDVAPLSWHDAETLLLGKKINAYQHLMQRIDPALIDKLIEANKQNMQAIQDAPAAAAHEPLAETIKIDDFAKVDLRVGKVLECNFVEGSDKLLQFKVDLGFETRNIFSGIRKAYQEPEKLVGRHVIVVANLAERKMRFGVSQGMIVCASGVDDSEGLFLLDVDAGVKPGMRVG
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
Q7NYR7
|
D0ZCI3
|
PAGP_EDWTE
|
Lipid A acylation protein
|
Edwardsiella
|
MKTHNDILAALAALPLFLTGAAFAAEPGMLDTLRNNIVQTWEQPQHYDLYLPAITWHARFAYSQEKIDSYNERPWGAGFGQSRWDEKGNWHGLYLMAFKDSFNKWEPIGGYGWEATWRPLEGSDFHWGAGYTVGVTMRDNWRYIPIPVILPMASVGYGPLTLQMTYIPGTYDNGNVYFAWLRLQF
|
Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors.
|
D0ZCI3
|
Q5M8N0
|
CNRP1_MOUSE
|
CB1 cannabinoid receptor-interacting protein 1
|
Mus
|
MGDLPGLVRLSIALRIQPNDGPVFFKVDGQRFGQNRTIKLLTGSSYKVEVKIKPTTLQVENISIGGVLVPLELKGKEPDGERVVYTGIYDTEGVAPTKSGERQPIQITMPFTDIGTFETVWQVKFYNYHKRDHCQWGSPFSVIEYECKPNETRSLMWVNKESFL
|
Suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels.
|
Q5M8N0
|
B5BB76
|
SYE_SALPK
|
Glutamyl-tRNA synthetase
|
Salmonella
|
MKIKTRFAPSPTGYLHVGGARTALYSWLFARHHGGEFVLRIEDTDLERSTPEAIEAIMDGMNWLNLEWDEGPYFQTKRFDRYNAVIDEMLEAGTAYKCYCSKERLEQLREDQMAKGEKPRYDGRCRHSHEHHADDEPCVVRFANPQDGSVIFDDQIRGPIEFSNQELDDLIIRRTDGSPTYNFCVVVDDWDMEITHVIRGEDHINNTPRQINILKALNAPVPMYAHVSMINGDDGKKLSKRHGAVSVMQYRDDGYLPEALLNYLVRLGWSSGDQEIFTREEMIKLFSLGAVSKSASAFNTDKLLWLNHHYINTLAPEYVATHLQWHIEQENIDTRNGPQLAELVKLLGERCKTLKEMSQSCRYFYEDFSEFDADAAKKHLRPVARQPLEVVRDKLSAITDWSAENVHHAIQATADELEVGMGKVGMPLRVAVTGAGQSPALDVTVHAIGKTRSIERINKALGFIAERESQQ
|
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).
|
B5BB76
|
A7NEI8
|
IF2_FRATF
|
Translation initiation factor IF-2
|
Francisella
|
MAEITVGQLAQQTNKEVDALLKQLKSFGIEKSSEKDTLTPTEMKTLLEKINSAKNTATRKKVTSVKLDGKHKINVSVKRKRRVAKKMEQQESTTLEQPQELETMVQEVSQQVDIVKEQDNIEQIVENKEAVKVQEQRQAEIAKPVIKDSGFKITAMPEIKIEEIVAEDDEGLAASDKQAKKKAAKKVFSEAVNTNTKYKCEEEEKKSKAKKAGGKGFKKANPRQLSQLAGDLESFDEFGAKKGKLKAPKVKKQEFTKPVENTVRTVEIHEGITVSELAQKMAVKGAEIVKVLFNMGVMATINQSLDQDTAILIVEEMGHKYTLHNENALEEAVTIVDRSSYKKISRAPVVTIMGHVDHGKTSLLDYIRQTRVVAGEAGGITQHIGAYSVKTDKGSITFLDTPGHEAFTSMRARGAKSTDIVILVVAADDGVMPQTEEAIQHAKAARVPIVVAVNKIDKPEADSDKVISELAQRNVIPESWGGDVMFVNVSAKTGEGVADLLEAVLLQSEVLELEAFAEGLAEGVVIESRLEKGRGPVATVLVQNGNLKQGDNILCGTEYGRVRAMHNDLGKKIKAAGPATPVEILGLSGVPAAGDEMVVIENEKKAKELAAQRSQKQKEAKIAQEQSLKLSNMFNNMGKEGEQQVLKIILKGDVQGSVEAIRESLLKLSTDEVKVDIIASGIGAITSSDVTLAVASTAVVIGFNVRADSAAKKLAETDGVEFRYYNIIYDLIDDVKKAMSGLLSPEMKEQIIGIAEVREVYRSSKFGSIAGCMVIEGVVKRTNPIRVLRNNVVIYEGTLESLKRFKDDASEVKKGLECGIGVKNYNDVREGDQIEVFEVIEVAKEL
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A7NEI8
|
P83216
|
HSP4_OCTVU
|
Sperm protamine P4
|
Octopus
|
RRRRRRRGHRGRRGRGGRRSRGRRRRAA
|
Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
|
P83216
|
Q5HLI0
|
GPMA_STAEQ
|
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
|
Staphylococcus
|
MPKLILCRHGQSEWNAKNLFTGWADVKLSKQGIEEAQSAGKKIYGNQIEIDIAFTSLLTRALETTQYILAGSDQQWIPVYKSWRLNERHYGGLQGLNKDDARKKWGEDQVHQWRRSYDVRPPRESEEQREAYLKNRRYQHIDHRMMPYCESLKDTLERVVPFWTDHISQHLLDDKTVLVSAHGNSIRALIKYLEGLSEEDIVGYEIKTGAPLVYELTDDLVVKDKYYL
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
Q5HLI0
|
P01094
|
IPA3_YEAST
|
Saccharopepsin inhibitor
|
Saccharomyces
|
MNTDQQKVSEIFQSSKEKLQGDAKVVSDAFKKMASQDKDGKTTDADESEKHNYQEQYNKLKGAGHKKE
|
Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity.
|
P01094
|
Q749Y6
|
AROA_GEOSL
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Geobacter
|
MVSLSSHPARALRGEIAVPGDKSISHRSIMLGSIARGVTTVSGFLRGEDNIATLDAFRAMGVQVHDDGETLRIEGKGLHGLTEAEDVIDCGNSGTSIRLLTGLMAAQRFYTVLTGDRYLRRRPMRRVVEPLSRMGACIHGRDNGEKAPLAIVGRPLTGIAYDSPVASAQVKSALMLAGLYADGATRVTEPHLSRDHSERMFRHFGARLETDAAGVTVYGGHELDGRDIVVPGDISSAAFFLVAALIVPGSELLIRGVGVNPTRTGILDILAAMGGSVELLDQREVSGEPVADLLVRSSALKGIEIGGDVVPRAIDEFPVICVAAALAEGTTVIRDARELRVKETDRIAAMAANLRAAGATITETADGMIIEGTGRLNGVTVESFGDHRIAMSMLVAGLAASGAITVSDTECIATSFPTFTALLDKVAVR
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
Q749Y6
|
Q8Z9L4
|
CAIC_SALTI
|
Crotonobetaine/carnitine--CoA ligase
|
Salmonella
|
MDIVGGQNLRQMWDDLAGMYGDKTALIFESCEGIVRQFSYASLNEEINRTANLFYYLGIRKGDRVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLGEESAWILQNSQVSLLVTSAQFYPMYREIRQDNSTPLNHICLIGEQLPADDGVSHFSQLQARQSATLCYTPALSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQIALRDDDVYMTVMPAFHIDCQCTAAMPAFSAGSTFVLLEKYSARAFWDQVRKYQATVTECIPMMIRTLMVQPATPTDRQHHLREVMFYLNLSAQEKDAFTERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRVGFSYEAEIRDDQNRPLPAGEIGEICIKGIPGKTIFKEYYMQPEATARALEPEGWLHTGDSGYQDEDGYFYFVDRRCNMIKRGGENVSCVELENIISAHPKIQDIVVVGIKDAIRDEAIKAFIVLNEGETLSEAEFFSFCENNMAKFKVPSFMEIRTDLPRNCSGKIIKKNLK
|
Catalyzes the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle. Also has activity toward crotonobetaine and gamma-butyrobetaine.
|
Q8Z9L4
|
Q5X703
|
LIPA_LEGPA
|
Sulfur insertion protein LipA
|
Legionella
|
MGKLIDIPIVVESGQKYKTSQGVTAIKDGIKSSGQDHERLPKPKWLRIVNHTTPAYSQVKEQVQKHRLATVCEEAKCPNISECWSHGTATIMLMGAVCTRACRFCSVDTGNPHGWLDAEEPENTAETVALMNLDYVVLTSVNRDDLPDGGANHYAKTIRAIKKRSPRTKVEALTPDFQGSERDVAVLLDSGVDVFAQNVETVERLTHPVRDNRAGYQQTLNVLAFAKKYRPDVLTKTSLMLGLGETDEEIIQTMDDLRTHHVDILTLGQYLQPTKNHLPIARYVTPETFSELRQIGLKKGFFEVASGPLVRSSYRADRVFKRDNLGLDV
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
|
Q5X703
|
Q6D0F3
|
THIQ_PECAS
|
Thiamine import ATP-binding protein ThiQ
|
Pectobacterium
|
MIALEKLTYFYQHLPMRFDFHVKPGERIAILGPSGAGKSTLLNLVAGFLMADSGELRLNGESHRETSPAKRPVSILFQENNLFPHLTIGQNIALGLHPGLRLNAAQRATLQQIADRVGLTDLLDRLPSQVSGGQRQRAALARCLVRHQPILLLDEPFSALDPALRQEMLDLVESVCEERKFTLLMVSHNLDDAMRIAKRTVLIVDGQIYYDGPTQALQDGSADAAAILGISRSSSD
|
Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.
|
Q6D0F3
|
P42698
|
DR111_ARATH
|
REQUIRED FOR SNC4-1D protein 2
|
Arabidopsis
|
MLGGLYGDLPPPTDDEKPSGNSSSVWSSSTKMAPPTLRKPPAFAPPQTILRPLNKPKPIVSAPYKPPPPSNSSQSVLIPANESAPSHQPALVGVTSSVIEEYDPARPNDYEEYKREKKRKATEAEMKREMDKRRQEDEERDKREREEREKERERDNSDPSRLNISGEEAWKRRAAMSGGGSGGKGRSSSPPGNVDGFSIGKSETSGLGVGAGGQMTAAQRMMAKMGWKQGQGLGKSEQGITTPLMAKKTDRRAGVIVNASENKSSSAEKKVVKSVNINGEPTRVLLLRNMVGPGQVDDELEDEVGGECGKYGTVTRVLIFEITEPNFPVHEAVRIFVQFSRPEETTKALVDLDGRYFGGRTVRATFYDEEKFSKNELAPVPGEIPGY
|
Seems to be involved in the resistance to UV light and chemical DNA-damaging agents . Regulates the splicing of the receptor-like kinase SNC4/LRKL-2.6 .
|
P42698
|
O27784
|
MER_METTH
|
Methylene-H(4)MPT reductase
|
Methanothermobacter
|
MKFGIEFVPNEPIEKIVKLVKLAEDVGFEYAWITDHYNNKNVYETLALIAEGTETIKLGPGVTNPYVRSPAITASAIATLDELSNGRATLGIGPGDKATFDALGIEWVKPVSTIRDAIAMMRTLLAGEKTESGAQLMGVKAVQEKIPIYMGAQGPMMLKTAGEISDGALINASNPKDFEAAVPLIKEGAESAGKSLSDIDVAAYTCCSIDEDSAAAANAAKIVVAFIAAGSPPPVFERHGLPADTGAKFGELLGKGDFGGAIGAVDDALMEAFSVVGTPDEFIPKIEALGEMGVTQYVAGSPIGPDKEKSIKLLGEVIASF
|
Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT.
|
O27784
|
Q8DVS3
|
Y394_STRMU
|
Nucleoid-associated protein SMU_394c
|
Streptococcus
|
MMNMQNMMKQAQKLQKQMEKKQSELASMTFVGKSAQDLVVATFTGNKKLVSIDFKEAVVDPDDRETLQDMTVQAINDALGQIEDATQKTMGAFAGKLPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q8DVS3
|
P43318
|
PA2_RHONO
|
Phosphatidylcholine 2-acylhydrolase
|
Rhopilema
|
GLIKPGTLWCGMGNNAETYDQLGPFADVDSCK
|
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
P43318
|
P42072
|
CTLA4_RABIT
|
Cytotoxic T-lymphocyte-associated antigen 4
|
Oryctolagus
|
MARLGFQRQGTQLDLASRTWSCAALFSLLFLPVFSKALHVSQPAVVLASSRGVASFVCEYASSHKATEVRVTVLRQANSQMTEVCAMTYTVENELTFIDDSTCTGISHGNKVNLTIQGLSAMDTGLYICKVELMYPPPYYVGMGNGTQIYVIEPEPCPDSDFLLWILAAISSGLFFYSFLITAVSLSKMLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN
|
Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28.
|
P42072
|
P42481
|
EFTU_THIDL
|
Elongation factor Tu
|
Thiomonas
|
MAKSKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLSSKFGGEAKAYDQIDAAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIIVFLNKCDMVDDAELLELVEMEVRELLSKYDFPGDDTPIIKGSAKLALEGDKGELGEGAILKLAEALDTYIPTPERAVDGAFLMPVEDVFSISGRGTVVTGRVERGIIKVGEEIEIVGLKPTLKTTCTGVEMFRKLLDQGQAGDNVGILLRGTKREEVERGQVLCKPGSIKPHTHFTAEVYVLSKDEGGRHTPFFNNYRPQFYFRTTDVTGAIELPKDKEMVMPGDNVSITVKLIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
P42481
|
Q8UE71
|
COBT_AGRFC
|
N(1)-alpha-phosphoribosyltransferase
|
Agrobacterium tumefaciens complex
|
MSMSGLPFDDFRALLRELPGPDTHALVAAKERNAQLTKPAGSLGRLEEIAMWLAAWSGRSPAVTRPLVAIFAGNHGVTRHGVTPYPTSVTQQMVENFAAGGAAINQICVANDLGLKIFDLALDYPTGDITCEPALSERDCAATMAFGMEAIAGGTDLLCVGEMGIGNTTIAAAINLALYGGTAEEWTGPGTGSEGEVMARKIAAVKAAVEFHKDHLSDPLEIMRRLGGREIAAIAGAILAARVQRIPVLIDGYVATAAAALLKAANSSALDHCLIGHVSGEPGHLAAVEKLGKTPLLALGMRLGEGTGAALAAGIVKAAAACHSGMATFEAAGVDTRISPRTEH
|
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
|
Q8UE71
|
Q0H8X2
|
BI1_USTMA
|
Intron-encoded endonuclease bI1
|
Ustilago
|
MRLLKTHPILGLANSYLIDSPQPSNISYMWNFGSLLGVCLIIQILTGVFLAMHYTPSVDLAFISVEHIMRDVNYGWLIRYLHANTASFFFIFVYLHIGRGLYYGSYKSPRTLLWSIGVIILVLMMAIAFLGFNGQKYMCFYNIDITIIQYLSIPTLITPSTRLKPILDKHNIKPVLLFENLTNSETKKIAYQALKPFSGIYMIVNLITEKYYVGSAVTGNLYMRFHKHLFSFTGNKRVANAVNKYGLSEFAFLVLEIVPQKDKIDSTLLLNREDYYLETLKPEYNIAPLASNSLGWKHSEESLAKMRENYSEERRQQVANINKGKTLSEETRELIRKSALLRKSMSSETRMKCAVNVQPVTIINLDGTNIMNFVSIKEASIAISCNEKTIRRALNGNGIVKKNYIVKVIK
|
Mitochondrial DNA endonuclease involved in intron homing.
|
Q0H8X2
|
A3MKP1
|
ALLA_BURM7
|
Ureidoglycolatase
|
pseudomallei group
|
MKTLSIEPLTRAAFAPFGDVIETQGAKQIPINLGTTMRFHDLAKIDVADEGGRPLVNLFRGQPRTLPFEVTMLERHPLGSQAFVPLTDRPYIVVVAPAGDLDASKIRAFVTSGWQGVNYAKGVWHHPLIALGEVSDFIVVDRGGDGRNLNEQNLPESLWLTDDALLAVGA
|
Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
|
A3MKP1
|
B7KGG1
|
GPMI_GLOC7
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
|
Gloeothece citriformis
|
MADAPIAPVVLVILDGWGYRQTTDYNAIAVANTPVMDSLWEAYPKTLIRTSGKDVGLPEGQMGNSEVGHLNIGAGRIVPQELVRITDAIEDGSIFQSPVLINLCDEVKGRGGKLHLIGLSSAGGVHSHLCHLLGLLDLAKLHSVSDVCVHAITDGRDTNPTEGVNVIEAIQAHIDKIGVGRISTVCGRYYAMDRDRRWDRVKKAYDLLTEDGEGDGRSASQILKDFYAQDITDEFILPTRVAPGAIEPGDGIIFYNFRPDRARQLCYAFTMPDFDGFERDLIQPLSFVTFTQYDPKLPVKVVFEPQSLTNILGEVIAKKGLRQFRTAETEKYPHVTYFFNGGLEQPFEGEDRELIQSPMVATYDKAPVMSAEAVTDTACAAIKKGIYSLVVMNYANPDMVGHTGNMEAAVQAIEAVDRCLGRLLGCINKMGGTVLITADHGNAEYMRDEEGNPWTAHTTNPVPFILVEGEKRKIPGHGANVVLRNDGRLADIAPTILDILQLPQPNNMTGKSLIEPAGFDVKTNRTPVRISL
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
B7KGG1
|
A5WG99
|
TTCA_PSYWF
|
tRNA 2-thiocytidine biosynthesis protein TtcA
|
Psychrobacter
|
MQTNFSQPQTFNPADITRNVIDNNQDDMVDSLDSDEEDLDLDLDLELSDEQEIAHKGVKSARFKKLQKKLRKQVSHAIRDFNMIEDGDVVMVCVSGGKDSYTLLDILLFLKRIAPINFDVVAVNLDQKQPGYPEEVLPNYLQQQGIPHYILEKDTYSVVKSVVPEGKTYCSACSRLRRGSLYGFAKQIGATKIALGHHRDDILATFFLNLFHGGSLKAMPPKLLSDDKQNVLIRPLAYVEEKDIIKYARYKEFPIIPCNLCGSQENLQRAMINDMLRQWDDAHPQRLASIFKAMQNVAPSQLADRELFDFESLTLQRDDSKRDFEGHNIQVGVANELAEIGLPTQPDIKPFESATAAKKIPTINPIID
|
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
|
A5WG99
|
Q06GK9
|
NDHI_PIPCE
|
NADH-plastoquinone oxidoreductase subunit I
|
Piper
|
MFPMITGFMNYGQQTVRAARYIGQSFAITLSHTNRLPVTIQYPYEKSITSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWKLETDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRLPISVIEDYTIQTNNYELNSYKKMTDKPLDSEKITN
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
Q06GK9
|
B5XK69
|
OLHYD_STRPZ
|
Myosin cross-reactive antigen
|
Streptococcus
|
MYYTSGNYEAFATPRKPEGVDQKSAYIVGTGLAGLAAAVFLIRDGHMAGERIHLFEELPLAGGSLDGIEKPHLGFVTRGGREMENHFECMWDMYRSIPSLEIPGASYLDEFYWLDKDDPNSSNCRLIHKRGNRVDDDGQYTLGKQSKELIHLIMKTEESLGDQTIEEFFSEDFFKSNFWVYWATMFAFEKWHSAVEMRRYAMRFIHHIDGLPDFTSLKFNKYNQYDSMVKPIIAYLESHDVDIQFDTKVTDIQVEQTAGKKVAKTIHMTVSGEAKAIELTPDDLVFVTNGSITESSTYGSHHEVAKPTKALGGSWNLWENLAAQSDDFGHPKVFYQDLPAESWFVSATATIKHPAIEPYIERLTHRDLHDGKVNTGGIITITDSNWMMSFAIHRQPHFKEQKENETTVWIYGLYSNSEGNYVHKKIEECTGQEITEEWLYHLGVPVDKIKDLASQEYINTVPVYMPYITSYFMPRVKGDRPKVIPDGSVNLAFIGNFAESPSRDTVFTTEYSIRTAMEAVYSFLNGERGIPQGFNSAYDIRELLKAFYYLNDKKAIKDMDLPIPALIEKIGHKKIKDTFIEELLKDANLM
|
Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate, and of linoleate at its cis-9- and cis-12-double bond to yield 10-hydroxy-12-octadecenoate and 10,13-dihydroxyoctadecanoate. Is not active on trans-double bonds and esterified fatty acids as substrate; is only active on cis-9- and/or cis-12-double bond of C16 and C18 fatty acids without any trans-configurations, producing 10-hydroxy and 10,13-dihydroxy derivatives. Appears to play a role in oleic acid detoxification and bacterial virulence.
|
B5XK69
|
Q4FMP0
|
THIG_PELUB
|
Thiazole synthase
|
Candidatus Pelagibacter
|
MVNDKLIIDKKKFNSRLIVGTGKYKSMAECAKAIKLSGAEIVTVAVRRVNISDKKKPLLMDYIDPKKITYLPNTAGCFNSEEALRTLRLAREIGGWKLVKLEVLGDKKNLFPDMIETLKSTEVLTREGFRVMVYCNDDPLMAKRLENVGACAIMPLAAPIGSGLGIQNTTNIKIIRSQTKLPLIIDAGLGQASDAAIAMELGCDGVLANTAIAKAKKPFQMALAFKNGVIAGRQSYLAGRIEKSIYGSASSPKTGII
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
Q4FMP0
|
Q15363
|
TMED2_HUMAN
|
p24 family protein beta-1
|
Homo
|
MVTLAELLVLLAALLATVSGYFVSIDAHAEECFFERVTSGTKMGLIFEVAEGGFLDIDVEITGPDNKGIYKGDRESSGKYTFAAHMDGTYKFCFSNRMSTMTPKIVMFTIDIGEAPKGQDMETEAHQNKLEEMINELAVAMTAVKHEQEYMEVRERIHRAINDNTNSRVVLWSFFEALVLVAMTLGQIYYLKRFFEVRRVV
|
Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing.
|
Q15363
|
Q163V9
|
PURL_ROSDO
|
Phosphoribosylformylglycinamidine synthase subunit II
|
Roseobacter
|
MQEPAITPDLIASHGLSPDEYDRILNIVGRTPTFTELGIFSAMWNEHCSYKSSKKWLRTLPTTGPQVICGPGENAGVVDIGDGQAVVFKMESHNHPSYIEPYQGAATGVGGILRDVFTMGARPIAAMNSLSFGEISHPKTRQLVNGVVAGVGGYGNCFGVPTVGGEVRFDPAYNGNCLVNAFAAGLADADKIFYSAASGVGMPVVYLGAKTGRDGVGGATMASAEFDDTIEEKRPTVQVGDPFTEKRLMEATLELMQTGAVISIQDMGAAGLTCSAVEMGDKGNLGVRLDLEKVPVREEAMTAYEMMLSESQERMLMVLRPELEQEAKAVFDKWDLDFAIVGETIAEDRFLIVHNGEVKADLPLKTLAGTAPEYDRPWVATPAADPLGDVPDVDPIDGLRALISSPNYASKDWVFTQYDTMVMADTVRIPGIGAGIVRVHGTDKALAFTSDVTPRYVQANPVEGGKQAVAEAYRNLSAVGATPLATTDNMNFGNPEKPEIMGQFVGAIKGISAAVAALDMPIVSGNVSLYNETDGTAILPTPTIGAVGLIAHLDDVIGCDVRDGHVALVLGETHGHLGQSAILSEVYNRAEGDAPPVDLDQEKAHGDFIRANRAYIKACTDLSDGGLALAAFEMAENAGVGVCLDASDTATLFGEDQGRYLIACNFDQAEALMIAASQAGLTLTSVGKFTGQAVRFGASSAPLAELSDVYRQSFGAALA
|
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
|
Q163V9
|
Q2SYN3
|
HBOH_BURTA
|
D-(-)-3-hydroxybutyrate oligomer hydrolase
|
pseudomallei group
|
MTTIRGGSRRASLPALALLGVLLGACHSDDNAQVNTLPGFVSGNVRKTAYDGASDDLLTAGLGKTGLGSDTRPGFANPAQPTAAELRRLAIYSNYRALVDITPNGGYGRFWGPNVDLAGNDTLGEGKIAGTEYLAYSDDGSGRKNVTLLVQVPASFDPANPCIVTATSSGSRGVYGAIAAAGEWGLKRGCAVAYNDKGGGNGAHEIGTGVVTLIDGTLASASSAGSASLFTASESSSALAAFNSAFPNRYAYKHAHSQQNPEQDWGRVTLQAVEFAYWALNEQFGPAIDGARHGVRYRPGDITTIAASVSNGGAAALAAAEQDTRGWITAVVVGEPQINVRMTPGVTVEQGGVPAPSFGRPLADYATLANLLQPCAAAAVAAVGAPYLSALPVGLTQSIRVQRCATLAAAGLVSGADTASQANDALAQLHAAGYLADSDLLQAPMWDSQAIPAIAVTYANAYTRSRVTDNLCNFSFATTNSVTGAVAPPATSPMTSLFGAGNGVPPTNGINLVFNGASGGVDHRLATPDASFAGAFCLRQLWTANQLGIGANVDAVRVAANLQRKPAIIVQGRSDALVPVNHASRAYVAQNSATEGRASQLSFYEVTNGQHFDAFLSVPGFDTRFVPVHYYDEQALNLMWNHLKSGAPLPPSQVIRTVPRGGVPGAAPALSTANLPPIVQSPGSNAITVNAGVIDVPL
|
Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.
|
Q2SYN3
|
C5FMY5
|
SUB3_ARTOC
|
Subtilisin-like protease 3
|
Microsporum
|
MGCIKVISVFLAAVAAVDARAFFHNRGGNDVIPNSYIVVMKDGVTAEDFDSHISSVATTHSINKAKRGSETVGHKDSFNINGWRAYNGHFDEATIESILNDDKVDYVEHDRVVKLAALTTQPNAPTWGLGRVSHKAPGNKDFVYDSSAGQGVTIYGVDTGIDINHPEFRGRIRWGTNTVDNDNTDGNGHGTHTAGTFAGTTYGVAKKANIVAVKVLSAGGSGSTAGVIKGIDWCVTDAKAKGALGKAALNLSLGGAFSQANNDAVTRAQNAGIFVAVAAGNDNKDAKNSSPASAPAVCTAASSTIDDQKSSFSNWGTIVDIYAPGSNILSAAPGGGTRTLSGTSMASPHVCGVGAAMLAQGVSVAQACDRIKQIANAVIKNPGTGTTNKLLYNGSGR
|
Secreted subtilisin-like serine protease with keratinolytic activity that contributes to pathogenicity.
|
C5FMY5
|
Q3J1W3
|
CHEB2_CERS4
|
Protein-glutamate methylesterase/protein-glutamine glutaminase 2
|
Cereibacter
|
MKVGNTLMAARAREGRTRVLIVDDSAMVRQALALGLSTDPRLEVVGTASGAEAARAQMAALKPDVVTLDLEMPQMDGLTFLRSYMESAPVPTVVISSLTRTSGETAMRAMEAGAVDIISKPSLGAGQGLPAIMRDVCARVWAAARARLAPPDGAAPAPVATGASEDWIHALGASTGGVQALSRILPFFPAQSPGLLVVQHMPEGFTAAFARRLDALCRMRVREAADGDLVLPGLVLIAPGGLRHMEIERAGGVCRVRLVAGAPVSYSRPSVDRMFLSLAAAAGPRVSAALLTGMGRDGAAGLLAIRRAGGRTFAQDEGSSAVFGMPLAARDLRAAEEILTLDDIPARMMLAAAADTRAPSLASND
|
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
|
Q3J1W3
|
P07188
|
LCP3_DROME
|
Larval cuticle protein III
|
Sophophora
|
MFKILLVCSLAALVAANANVEVKELVNDVQPDGFVSKLVLDDGSASSATGDIHGNIDGVFEWISPEGVHVRVSYKADENGYQPQSDLLPTPPPIPAAILKAIAYIEANPSKN
|
Component of the larval cuticle.
|
P07188
|
Q96303
|
PHT14_ARATH
|
H(+)/Pi cotransporter
|
Arabidopsis
|
MAREQLQVLNALDVAKTQWYHFTAIIIAGMGFFTDAYDLFCISLVTKLLGRIYYHVEGAQKPGTLPPNVAAAVNGVAFCGTLAGQLFFGWLGDKLGRKKVYGMTLMVMVLCSIASGLSFGHEPKAVMATLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFVSAVFAMQGFGIMAGGIFAIIISSAFEAKFPSPAYADDALGSTIPQADLVWRIILMAGAIPAAMTYYSRSKMPETARYTALVAKDAKQAASDMSKVLQVEIEPEQQKLEEISKEKSKAFGLFSKEFMSRHGLHLLGTTSTWFLLDIAFYSQNLFQKDIFSAIGWIPPAQSMNAIQEVFKIARAQTLIALCSTVPGYWFTVAFIDVIGRFAIQMMGFFFMTVFMFALAIPYNHWTHKENRIGFVIMYSLTFFFANFGPNATTFVVPAEIFPARFRSTCHGISAASGKLGAMVGAFGFLYLAQNPDKDKTDAGYPPGIGVRNSLIVLGVVNFLGILFTFLVPESKGKSLEEMSGENEDNENSNNDSRTVPIV
|
High-affinity transporter for external inorganic phosphate. Acts as a H(+):phosphate symporter in both low- and high-Pi conditions. Confers sensitivity to arsenate.
|
Q96303
|
Q21WX8
|
LPXA_ALBFT
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
Rhodoferax
|
MTTIHATAIVDSQAQLDSSVTVGPYSLIGPNVKVGAGTTIGPHCVIEGHTTIGRDNRIFQFSSLGAIPQDKKYAGEPCELVIGDRNTIREFCTFNIGSPGDLGVTRVGDDNWLMAYVHLAHDCVVGNKTIFANNSQLAGHVHVGDWAILGGFTVVHQFVKIGAHSMTALCTVLLADLPPFVMCQGQPAQARSMNYEGLRRRGFSPERIAVVKAMHKALYRESLTLQLARERIADLVKNSPESLPDVEMMLLFLEQTSPQRGIVR
|
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q21WX8
|
A1XIM6
|
MEP4_TRIVO
|
Fungalysin MEP4
|
Trichophyton
|
VHSVVDYVSAAEYQVYPWGINDPTEGNRTTLHLPWLKTLSTDWHIDGKGWYSTTRGNNAIAQENPTGGPEYENNYRPKSPLFIFKYPYSKAMTPPSSYRDASITQLFYTTNVYHDVLYILGFNEKAGNFQINNWNKGGVGGDYAILNSQDGSGVNNANFATPPDGQPGRMRMYTWNASIPERDGCFEAGIVIHEYTHGVSNRLTGGPENSRCLAALESGGMGEGWSDFFATAIRLKPGDTRATDYTMGEWASNRPNGIRKYRYSTSLTTNPHMYVDADGLTSVHAIGNIWASMLYELLWNLIDKHGKGDVTKIRPVLKNGVPTDGRHLAMKIVLDGMALQPCLPNFVQARDAILDADKNLTQGSNKCEIWKAFAKRGLGVGAVFNLSKRTGS
|
Secreted metalloproteinase probably acting as a virulence factor.
|
A1XIM6
|
Q2T281
|
ARGB_BURTA
|
NAG kinase
|
pseudomallei group
|
MSEPIDLSQISPSLKAEILAEALPYIRRYHGKTVVIKYGGNAMTEERLKQGFARDVILLKLVGINPVIVHGGGPQIDQALKKIGKQGTFIQGMRVTDEETMEVVEWVLGGEVQQDIVTLINHFGGHAVGLTGKDGGLIHARKLMMPDRDNPGEYVDIGQVGEVEAINPAVVRALQDDAFIPVISPIGFGEDGLSYNINADLVAGKLATVLNAEKLVMMTNIPGVMDKEGNLLTDLSAREIDALFEDGTISGGMLPKISSALDAAKSGVKSVHIVDGRIEHSVLLEILTEQPFGTMIRSH
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
Q2T281
|
Q1IX87
|
RL6_DEIGD
|
50S ribosomal protein L6
|
Deinococcus
|
MSRIGRQPIAVPNGVTVNAQNGVFTAKGPKGELSVPYNTALNITQENGQLLVTRPSDRQEHRALHGLTRTLVANAVKGVSDGYTINLELRGVGYRARLVGKNLELTIGYSHPVVIEPPAGVTFAVPEPTRIDVMGIDKQLVGQVAANVRKVRKPDAYHGKGVRFVGEQIALKAGKAGATGGKGKK
|
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.
|
Q1IX87
|
Q89LF9
|
PCS_BRADU
|
CDP-diglyceride-choline O-phosphatidyltransferase
|
Bradyrhizobium
|
MILWRIVRPGAAMAYVQTGLVLIAEAMDTQQDSLKPRPAMRAAAFSVHVFTAFGAAIALLAMLEAVREHWAAMFQWLGVALIIDAIDGPIARRLDVKNVQPNWSGDVLDLVVDFVTYVFVPAYAIVASGLLLPVAAPLLGVAIIVTSALYFADLRMKADDNHFRGFPALWNAAAFYLFLLHWPPLWSTLLVAALVVLTFVPFHVLHPVRVVRLRWLTMSLIGIWAVLSLYTLDMDFRVGPGVTLALCAIALWISFSDALIRFARSFA
|
Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP.
|
Q89LF9
|
Q0TPW8
|
VATB_CLOP1
|
V-ATPase subunit B
|
Clostridium
|
MLKEYRTVTEVVGPLMAVEGVEGVKYDELVEIEMQTGELRRGKVLEVNGDKAMVQLFEGSAGINLKNTKVRFLGRPLEIGVSEDMLGRVFDGMGRPKDNGPNIIPEKRLDINGEAINPVARNYPSEFIQTGISAIDGLNTLVRGQKLPVFSGSGLPHKELAAQIARQAKVLNSDSKFAVVFAAIGITFEEAEFFVDEFTKTGAIDRSVLFMNLASDPAIERIATPRMALTTAEYLAYEKGMHVLVIMTDITNYCEALREVSAARKEVPGRRGYPGYLYTDLSTLYERAGRLVGKEGSITQIPILTMPEDDKTHPIPDLTGYITEGQIILSRELYKKGIMPPIDVLPSLSRLKDKGIGKGKTREDHADTMNQLFSAYAQGKQAKELAAILGESALSDVDKAYAKFAEAFENEYVSQGFTTNRTIEETLNLGWKLLKILPRTELKRIRDEYLEKYMPVGEDE
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
|
Q0TPW8
|
A5CCA2
|
RECR_ORITB
|
Recombination protein RecR
|
Orientia
|
MHKDSNIIEELIFSFAQLPGLGNRSARRIVLYLMQDKEVRIKNLNNQLTSVLNNIMECDYCGNLDVVSICNICRHSERDSSIIAIVESVADLWALERSKVFKGWYHVLGKTLSAVSGNDAINSLKLPKLLNRIREYKVQEIILATNSTIDGQMTAFFVIDYLKDENLKISKLASGIPLGGELDYLDEGTLLAAFKARQSHDLL
|
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
|
A5CCA2
|
Q466A3
|
COFH1_METBF
|
FO synthase subunit 2 1
|
Methanosarcina
|
MNNRIPEDLIERAYQGKSTKEDGLLLLEVPPFELFRFADELRSLTAGDTVTYVVNRNINFTSRCVGTCGFCAFRTNDGKVLSIEEIMEKVREAEKAKATEVCIQGGLLPDVGLDFYQEIAESIKAEFPEMHIHAFSPMEVYHASHISGIKVSEALSKLKRSGLDTMPGTAAEILSDRVRKIICPSKLRTAEWIEVVTQAHAAGIPTTATMMYGHVETPEERIEHILTIREIQKETGGITEFVPLPFMPYNNPVGEKIIREGRYATPGLDDLKIYAISRILLHGHVDNIQASWVKLGKKLSQFALQCGANDLGGTLMEESISRLAGAPNGESISVEELEWMIYGAGRVPKERTTLYKGVRELASRNPGRITGCGASE
|
Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
|
Q466A3
|
Q1C5H3
|
HSCB_YERPA
|
Hsc20
|
Yersinia
|
MDYFTLFGLPARYLIDGNQLTTRYQELQRQFHPDRFATQPERERLASMQQAATINDAYQTLKHPLKRAEYMLSLQGFDLGNEQHTMRDTAFLMEQLELREELDAIERKPDAETLLAEFSRRVAQMTTTRTQQMVEQLDAQLWVQAADTVRKLRFLDKLQQQVEQLEERLFDDFA
|
Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.
|
Q1C5H3
|
Q6GPB6
|
KCMF1_XENLA
|
RING-type E3 ubiquitin transferase KCMF1
|
Xenopus
|
MSRHEGVSCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQCILTRVDFDLYYGGEAFSVEQPQSFTCPYCGKMGYTETSLQEHVTSEHAETSTEVICPICAALPGGDPNHVTDDFAAHLTLEHRAPRDLDESSGVRHVRRMFHPGRGLGGPRARRTNMHFTSSSTGGLSSSQSSYSPSNREAMDPIAELLSQLSGVRRSTGGQLNSSGPSASQLQQLQMQLQLERQQAQAARQQLETARNATRRNNASNVTTTITQSTAATNTSSTENNQQSIQNSQFLLTRLNDPKMTEAERQSIESERADRSLFVQELLLSTLMQEESSSSDEDERGEIADFGAMGCVDIMPLDVALENLNLKESNKGNEPPPPPL
|
Has intrinsic E3 ubiquitin ligase activity and promotes ubiquitination.
|
Q6GPB6
|
Q5I2J3
|
TBA_GIBZE
|
Alpha-tubulin
|
Fusarium
|
MREVISINVGQAGCQIANSCWELYCLEHGIQPDGYLTEERKAQDPDQGFSTFFSETGNGKHVPRAIYCDLEPNVVDEVRTGAYRNLFHPEMMITGKEDASNNYARGHYTVGKELIDGVLDKIRRVADNCAGLQGFLVFHSFGGGTGSGFGALLMERLSVDYGKKSKLEFCVYPAPQTATSVVEPYNSILTTHTTLEHSDCSFMVDNEAIYDICRRNLGLERPNYENLNRLIAQVVSSITASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVAYSPVISAAKAAHEANSVQEMTMSCFEPNNQMVKCDPRHGKYMATCLLYRGDVVPNDAHAAVATLKTKRTIQFVDWCPTGFKLGICYQAPENVPNGDLAKVSRAVCMLSNTTAIAEAWSSLSLKFDLMHSKRAFVHWYVGEGMEEGEFSEAREDLAALERDYEEVATDSMGDEELEAEY
|
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.
|
Q5I2J3
|
Q9ZAU2
|
DNRV_STRPE
|
Anthracycline biosynthesis protein DnrV
|
Streptomyces
|
MTRFAPGAPAWFDLGSPDVAASADFYTGLFGWTATVVSDPGAGGYTTFSSDGKLVAAVARHQIDTPYHRPYGPGNDQHGMPAIWTVYFATDDADALTKRVETAGGEVIMTPMDVLGLGRMAVFADPAGAAFAVWRKGVMEGAEVTGVPGSVGWVELVTDGIGAARDFYPATLGLAPADTGLKGVTDPVWHIGDTPVAGTQELGVTGAVRPHWAVLFAVHDCDATVRRAVELGGSVENEPADTPRGRRADLLDPHGAGFSVVELREGYPAAAGGAS
|
Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, it acts jointly with DoxA in the conversion of 13-deoxycarminomycin and 13-deoxydaunorubicin to yield carminomycin and daunorubicin, respectively. In vitro, it also acts jointly with DoxA in the C-14 hydroxylation of daunorubicin to form doxorubicin, although this strain is not a doxorubicin producer.
|
Q9ZAU2
|
A7ZIX5
|
ENTS_ECO24
|
Enterobactin exporter EntS
|
Escherichia
|
MNKQSWLLNLSLLKTHPAFRAVFLARFISIVSLGLLGVAVPVQIQMMTHSTWQVGLSVTLTGGAMFVGLMVGGVLADRYERKKVILLARGTCGIGFIGLCLNALLPEPSLLAIYLLGLWDGFFASLGVTALLAATPALVGRENLMQAGAITMLTVRLGSVISPMIGGLLLATGGVAWNYGLAAAGTFITLLPLLSLPALPPPPQPREHPLKSLLAGFRFLLASPLVGGIALLGGLLTMASAVRVLYPALADNWQMSAAQIGFLYAAIPLGAAIGALTSGKLAHSARPGLLMLLSTLGSFLAIGLFGLMPMWILGVVCLALFGWLSAVSSLLQYTMLQTQTPEAMLGRINGLWTAQNVTGDAIGAALLGGLGAMMTPVASASASGFGLLIIGVLLLLVLVELRRFRQTPPQVTASDS
|
Component of an export pathway for enterobactin.
|
A7ZIX5
|
O35082
|
KLOT_MOUSE
|
Klotho peptide
|
Mus
|
MLARAPPRRPPRLVLLRLLLLHLLLLALRARCLSAEPGQGAQTWARFARAPAPEAAGLLHDTFPDGFLWAVGSAAYQTEGGWRQHGKGASIWDTFTHHSGAAPSDSPIVVAPSGAPSPPLSSTGDVASDSYNNVYRDTEGLRELGVTHYRFSISWARVLPNGTAGTPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDTYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGVRGSSRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGRVSIALSSHWINPRRMTDYNIRECQKSLDFVLGWFAKPIFIDGDYPESMKNNLSSLLPDFTESEKRLIRGTADFFALSFGPTLSFQLLDPNMKFRQLESPNLRQLLSWIDLEYNHPPIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIRLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQDKELLPKSSALFYQKLIEDNGFPPLPENQPLEGTFPCDFAWGVVDNYVQVDTTLSQFTDPNVYLWDVHHSKRLIKVDGVVAKKRKPYCVDFSAIRPQITLLREMRVTHFRFSLDWALILPLGNQTQVNHTVLHFYRCMISELVHANITPVVALWQPAAPHQGLPHALAKHGAWENPHTALAFADYANLCFKELGHWVNLWITMNEPNTRNMTYRAGHHLLRAHALAWHLYDDKFRAAQKGKISIALQADWIEPACPFSQNDKEVAERVLEFDIGWLAEPIFGSGDYPRVMRDWLNQKNNFLLPYFTEDEKKLVRGSFDFLAVSHYTTILVDWEKEDPMKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLRFKYGDLPMYVTANGIDDDPHAEQDSLRIYYIKNYVNEALKAYVLDDINLCGYFAYSLSDRSAPKSGFYRYAANQFEPKPSMKHYRKIIDSNGFLGSGTLGRFCPEEYTVCTECGFFQTRKSLLVFISFLVFTFIISLALIFHYSKKGQRSYK
|
The Klotho peptide generated by cleavage of the membrane-bound isoform may be an anti-aging circulating hormone which would extend life span by inhibiting insulin/IGF1 signaling.
|
O35082
|
B1W0A2
|
ATPE_STRGG
|
F-ATPase epsilon subunit
|
Streptomyces
|
MAAELHVELVAADRSVWSGEATLVVARTTSGDIGVMPGHQPLLGVLESGPVTIRTSEGGTVIAAVHGGFISFADDKLSLLAEIAELADEIDVERAERALELAKSDADAAAQRRADVRLRAVAVR
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
B1W0A2
|
Q58655
|
HJA3_METJA
|
Probable archaeal histone 3
|
Methanocaldococcus
|
MAELPVAPCVRILKKAGAQRVSEAAGKYFAEALEEIALEIARKSVDLAKHAKRKTVKVEDVKAALRG
|
Binds and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. Increases the resistance of DNA to thermal denaturation (in vitro).
|
Q58655
|
Q57RT4
|
RLMH_SALCH
|
rRNA (pseudouridine-N3-)-methyltransferase RlmH
|
Salmonella
|
MKLQLVAVGTKMPDWVQTGYTEYLRRFPKDMPFELIEIPAGKRGKNADIKRILDKEGEQMLAAAGKNRIVTLNIPGKPWDTPQLANELERWKQDGRDVSLLIGGPEGLSPACKAAAEQSWSLSALTLPHPLVRVLVAESLYRAWSITTNHPYHRE
|
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
|
Q57RT4
|
Q3M3H8
|
SYE_TRIV2
|
Glutamyl-tRNA synthetase
|
Trichormus
|
MTVRVRIAPSPTGNLHIGTARTAVFNWLFARHHGGTFILRIEDTDLERSRPEYTENIMTGLRWLGLNWDEGPFFQSQRLDLYQKAVKQLLDQGLAYRCYTTSEELEALREAQKAKGEAPRYDNRHRHLTPEQEAEFKAQGRSFVIRFKIDDEREIVWNDLVRGKMSWRGSDLGGDMVIARASENDTGQPLYNFVVVIDDIDMQISHVIRGEDHIANTAKQILLYEAFGAKIPEFAHTPLILNMEGRKLSKRDGVTSISDFQQMGFTSEGLVNYMTLLGWSPPDSTQEIFTLEAAAKEFTFERVNKAGAKFDWAKLDWLNSQYIHNTPVDQLTDLLIPYWEAAGYSFAGGRDRPWLEQLVGLLSASLTRLTDAVDMSKLFFSETVELSEEGSKQLQQEGSKAVLEAIIAALEAQTQLTENAAQDIIKQVVKAQNVKKGLVMRSLRVALTGDVHGPDLIQSWLLLNQIGLDKPRLSQAIAASL
|
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).
|
Q3M3H8
|
Q32KN0
|
ZN572_BOVIN
|
Zinc finger protein 572
|
Bos
|
MEQEQKLLVSDSNGLTKKESLKNTITGDESKNNLKTVQFSNSKADKERASKWSRSDGPENYKDEDTKEILLTGSQGGKTERDDSYENDSNLGSQRNCTEKEEEQPNHWGWSPGDHTGPAGQQNPSFGDKPYKCSECWKSFSNSSHLRIHQRTHSGEKPYRCSECGKCFSNSSHLIQHLRTHTGEKPYQCGECGKSFSNTSHLIIHERTHTGEKPYKCPECAKSLSSSSHLIQHHRSHTGEKPYECPLCGKCFSHSYVLVEHQRTHTGEKPYKCPDCGKSFSQSSSLIRHQRTHTGEKPYKCPECGKGFGCNSTLIKHQRIHTGEKPYQCIECGKNFSRSSNLVTHQKMHTDDKTYQSSEYEESLSQNYSLIEECRIQPGEKPYKCCECGKSFGLSSHLIRHQRTHTGEKPYRCSECWKTFSQSSTLVIHQRTHTGEKPYKCPDCGECFSQSFNLIRHRRTHMGEKPYKCTDCEKCFSRSAYLSQHRKIHVGKSFESPEVEDFPHEWTWKNYSGEIALIPSFSVPSSSPS
|
May be involved in transcriptional regulation.
|
Q32KN0
|
C0QA34
|
CSRA_DESAH
|
Translational regulator CsrA
|
Desulforapulum
|
MLVLTRKVGESIRISDDIVVKVIDIGKNRIRIGIDAPSTVSVLRNEVYEEIHQENILSSRGSVTDLAKAATLWARKSKKEE
|
A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW.
|
C0QA34
|
Subsets and Splits
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