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AlphaFoldDB
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C4LB58
PLSY_TOLAT
Lysophosphatidic acid synthase
Tolumonas
MLALTFAMSGIAYLLGSVSNAVLISRLCDLPDPREYGSHNPGATNVLRSGNRLAALIVFLLDMLKGTIPVYLAWYLGIPPLYLGFIGIAACLGHMYPLYFHFRGGKGVATALGALLPLGLDMGSFMIVTWLIVLLFTGYSSLAAIGAALLAPLYTYCLKPEYTLPVAMLCCLIILRHHENISRLLQGHEPQVWSRHPLKRHRR
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
C4LB58
A6H5H4
YCF3_CYCTA
Photosystem I assembly protein Ycf3
Cycas
MPRSQRNDNFTDKTFTIVADILLRIIPTAPGEKEAFTYYRDGVMSAQSEGEYAEALQNYYEAMRPEIDPYDRSYILYNIGLIHMSNGEHTEALEYYFQALKRNPSLPQAFNNMAVICHYRGEQAIRQGDPETAEAWSDRAAEYWKQAIALAPGNYIEAQNWLKITGRLGE
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
A6H5H4
P54300
LUXP_VIBHA
Autoinducer 2-binding periplasmic protein LuxP
Vibrio
MKKALLFSLISMVGFSPASQATQVLNGYWGYQEFLDEFPEQRNLTNALSEAVRAQPVPLSKPTQRPIKISVVYPGQQVSDYWVRNIASFEKRLYKLNINYQLNQVFTRPNADIKQQSLSLMEALKSKSDYLIFTLDTTRHRKFVEHVLDSTNTKLILQNITTPVREWDKHQPFLYVGFDHAEGSRELATEFGKFFPKHTYYSVLYFSEGYISDVRGDTFIHQVNRDNNFELQSAYYTKATKQSGYDAAKASLAKHPDVDFIYACSTDVALGAVDALAELGREDIMINGWGGGSAELDAIQKGDLDITVMRMNDDTGIAMAEAIKWDLEDKPVPTVYSGDFEIVTKADSPERIEALKKRAFRYSDN
Binds to the signaling molecule autoinducer 2 (AI-2), a furanosyl borate diester, (3a-methyl-5,6-dihydrofuro-[2,3d][1,3,2]dioxaborole-2,2,6,6a-tetraol). This complex then interacts with the LuxQ sensor protein.
P54300
Q5G267
NETR_MACMU
Serine protease 12
Macaca
MTLARFVLALVLGALPEVVGFDSVLNDSFHHRHRHSPPPGPQYPYYLPTHQRPPRTRPPPPLPRFPRPPRALPAQRPHALQAGHTPRPHPWGCPAGELWVSVTDFGAPCLRWAEVPPFLERSPPANWAQLRGQRHNFCRSPDGTGRPWCFYGDARGKVDWGYCDCRHGSVRLRGGKNEFEGTVEVYASGAWGTVCSSHWDDSDASVICHQLQLGGKGIAKQTPFSGLGLIPIYWSNVRCRGDEENILLCEKDIWQGGVCPQKMAAAVTCSFSRGPAFPIIRLVGGSSVHEGRVELYHAGQWGTICDDQWDDADAEVICRQLGLSGIAKAWHQAYFGEGSGPVMLDEVRCTGNELSIEQCPKSSWGEHNCGHKEDAGVSCTPLTDGVIRLAGGKGSHEGRLEVYYRGQWGTVCDDGWTELNTYVVCRQLGFKYGKQASANHFEESTGPIWLDDVSCSGKETRFLQCSRRQWGQHDCSHHEDVSIACYPGSEGHRLSLGFPVRLMDGENKKEGRVEVFINGQWGTICDDGWTDKDAAVICRQLGYKGPARARTMAYFGEGKGPIHVDNVKCTGNERSLADCIKQDIGRHNCRHSEDAGVICDYFGKKASGNSNKESLSSVCGLRLLHRRQKRIIGGKNSLRGGWPWQVSLRLKSSHGDGRLLCGATLLSSCWVLTAAHCFKRYGNSTRNYAVRVGDYHTLVPEEFEEEIGVQQIVIHREYRPDSSDYDIALVRLQGPEEQCARFSSHVLPACLPFWRERPQKTASNCYITGWGDTGRAYSRTLQQAAIPLLPKRFCEERYKGRFTGRMLCAGNLHEHKRVDSCQGDSGGPLMCERPGESWAVYGVTSWGYGCGVKDSPGVYTKVSAFVPWIKSVTKL
Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
Q5G267
A5EXS0
AROB_DICNV
3-dehydroquinate synthase
Dichelobacter
MKRLTVHTAEKAQQYPILIAPDLIKNASLWHLYCSAPHIAIITNETVAPLYLSSLKAALTDKKVIDIILLDGECHKNLATYQHILTTLLEAHLGRDGLLIALGGGVINDITGFVAATYQRGICWITFPTTLLAQVDAAVGGKTGVNHACGKNMIGAFYPPQAVLMDTATLSTLPPREFSAGLAEVIKYALIYDISFLSWLEQHMDAVLRKEKISLENMIMNCCRYKSEIVCADEREQGMRALLNFGHTFGHALETITAYRHWLHGEAVAIGMRMAAELSEMRGLISADEKARVISLLQRAHLPTAIDIQLNCEDIYQTLFLDKKVRAGQLRFVLLSGLGQAHVVDDVTETEIFAVIAASRSENESFARF
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
A5EXS0
Q6D602
CCME_PECAS
Heme chaperone CcmE
Pectobacterium
MSAPRKTRLYAILAVVCGAVLTIALMLYALSSNIDLFYTPSEILYGKNETQEKPAIGQRLRVGGMVMPGSVRRDSQSLEVRFTVYDAKGSVDVTYNGMLPDLFREGQGVVAQGILDTDDHIAAKEVLARHDENYTPPEIKAAMEGQNGHAPAAGPEGKRL
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Q6D602
P20069
MPPA_RAT
P-55
Rattus
MATAVWAAARLLRGSAALCARPKFGSPAHRRFSSGATYPNIPLSSPLPGVPKPIFATVDGQEKFETKVTTLDNGLRVASQNKFGQFCTLGILINSGSRYEAKYLSGIAHFLEKLAFSSTARFDSKDEILLTLEKHGGICDCQTSRDTTMYAVSADSKGLDTVVGLLADVVLHPRLTDEEIEMTRMAVQFELEDLNMRPDPEPLLTEMIHEAAFRENTVGLHRFCPVENIGKIDREVLHSYLKNYYTPDRMVLAGVGVEHEHLVECARKYLLGVQPAWGAPGAVWMLTAQWHSTRGGSSRWRETCQMSALRPPRFQSSHIYGGARELLLLEEDFIPFAVLNMMMGGGGSFSAGGPGKGMFSRLYLNVLNRHHWMYNATSYHHSYEDTGLLCIHASADPRQVREMVEIITKEFILMGRTVDLVELERAKTQLMSMLMMNLESRPVIFEDVGRQVLATHSRKLPHELCTLIRNVKPEDIKRVASKMLRGKPAVAALGDLTDLPTYEHIQAALSSRDGRLPRTYRLFR
Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
P20069
Q3ATL0
SYE_CHLCH
Glutamyl-tRNA synthetase
Chlorobium
MVGQRVRTRFAPSPTGYLHVGGLRTALYNFLFAKKMKGDFIIRIEDTDQSRKVEGAQQNLIKTLEWAGIIADESPQHGGSCGPYIQSERLDIYAKHCKQLLEDHHAYYCFATPEELEENRQLQLKQGLQPKYNRKWLPEEMGGTMPESLIRQKLEAGEPYVIRMKVPDYISVWFEDIIRGPIEFDSATIDDQVLMKSDGFPTYHFASVIDDHLMEISHIIRGEEWLSSMPKHLLLYEFFGWEAPKVAHLPLLLNPDRSKLSKRQGDVAVEDYIRKGYSSEAIVNFVALLGWNEGEGCEQEVYSLQELTDKFSLERVGKAGSIFTLDKLKWLEKQYIKNRSVEKLLSVVKPLLLEELEKKPSIMAREQITSDSYLSSVIELMRERVGFEHEFVTFSTYFYFEPESYDEESVKKRWQPNTNELLADFIPQLEALSDFTAENIEAALKAFVEPKGMKNAVLIHPLRIVTSGVGFGPSLYHMLEVLGKETVLRRIRKGLECITMPA
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).
Q3ATL0
B2J1K8
SEPF_NOSP7
Cell division protein SepF
Nostoc
MNNIFSKLRDFVGLNEQVEYEYYEEEPETDNNYQNLYQQENPQPPAPQESATAQNRRWREPVPTMGDDIAAGSKPMGNVIGMPGAINGISEVLVLEPRTFEEMPQAIQALRERKSVVLNLTIMDPDQAQRAVDFVAGGTYALDGHQERIGESIFLFTPSCVQVSTQGGVLHEVPQPPARPSRPTGSPNQTWGNETNRMAQ
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
B2J1K8
Q23125
MFRN_CAEEL
Mitoferrin
Caenorhabditis
MGGGGEDEYESLPTHSVPVHLTAGALAGAVEHCVMFPFDSVKTRMQSLCPCPETKCPTPVHSLMSIVKREGWLRPLRGVNAVAAGSMPAHALYFTVYEKMKGYLTGNSAGHSNTLAYGASGVVATLIHDAIMNPAEVVKQRMQMAFSPYGSSLECARCVYNREGVAAFYRSYTTQLAMNVPFQAIHFMSYEFWQHVLNPEHKYDPKSHLIAGGLAGGLAAALTTPMDCVKTVLNTQQAAEADPANRRIFLQARYRYRGISDAVRTIYSQRGLSGFSCGLQARVIFQVPATALSWSVYELFKFMLSFEGGHSS
Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly.
Q23125
Q0CY32
SCONB_ASPTN
Sulfur metabolite repression control protein B
Aspergillus subgen. Circumdati
MDSTQVSFKSIFGGTPEPTDEVDAEPDPTQHGPHSFNNVTTTSAKLADENVAPFLAKHIPEQYAPLGSRTGKPEDLSSANSKYCYRHRPDLKCRRQADEPSMDKLQRDLETLPQSDQQGIAHIWSLFSAAPAKHRKLILQGLMAQCCFPQLSFVSATVRDLIRIDFLTALPPEISFKILCYLDTTSLCKAAQVSRRWRALADDDVVWHRMCEQHIHRKCKKCGWGLPLLERKRLRESKREIELRATTWDISGPSPTVTSTGEQQREQSAAPESSSSGKRKQDTSDEETAVVKRQCSSLAPDSENDDAFFKKRYRPWKEVYKDRFKVGTNWKYGRCSTKIFKGHTNGVMCLQFEDNILATGSYDATIKIWDTETGEELRTLYGHESGIRCLQFDDTKLISGSMDRSLKVWNWRTGECISTYTGHRGGVIGLHFDATILASASVDKTVKIWNFEDKSTCLLRGHTDWVNAVRVDTTSRTVFSASDDCTVRLWDLDTKQCIRTFHGHVGQVQQVIPLPREFEFEEHDAECENDNVSTVSDDPGSPAPQTTFGVSSIEPASQSSMFGPSFDNGRPAPPRYIVTSALDSTIRLWETTTGRCLRTFFGHLEGVWALGADTLRIVSGAEDRMVKIWDPRTGKCERTFTGHSGPVTCIGLGDSRFATGSEDCEVRMYSFQS
Component of the SCF(sconB) E3 ubiquitin ligase complex involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor.
Q0CY32
P32865
GPRK1_DROME
G protein-coupled receptor kinase 1
Sophophora
MADLEAVLADVSYLMAMEKSKCTPAARASKKLNLPDPSVRSVMYKYLEKEGELNFHKIFNEVLGYLLFKDFCENDSEEPIQQLKFFEQIKLFEKTECYDERKKMARDIYDNFIMEEMLSHTYEYSKHAVASVQKYLLKNEVPVDLFEPYLEEIFTQLKGKPFKKFLESDKFTRFCQWKNLELNIQLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGEMLALNERNMLQAVSTGIDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGIFSEDEMKFYAAEVILGLEHMHKRCIVYRDLKPANILLDENGHIRISDLGLACDFSKKKPHASVGTHGYMAPEVLSKGTSYDSCADWFSFGCMLYKLLKGHSPFRQHKTKDKLEIDKMTLTMNVELPESFSLELKNLLEMLLQRDVSKRLGCMGNGADEVKMHNFFCGIDWHQVYIQKYTPPLVPPRGEVNAADAFDIGSFDEEDTKGIKLNDADQDLYKMFSLTISERWQQEVSETVFDTVNTETDKLEQKRKLKQKQHFDADEKESDCILHGYIKKLGGSFASLWQTKYAKLYPNRLELHSESGNNKPELIFMDQVEDISSDFILHKNENCIQIRINDGTRDGRIILTNSDEIGLKEWSSSLRSAHKISQDLLGSMAKKAGKIYGSERDVNKSMYIFGGNCSTKTSNGSN
Specifically phosphorylates the activated forms of G protein-coupled receptors.
P32865
Q3J7B0
KDSB_NITOC
CMP-2-keto-3-deoxyoctulosonic acid synthase
Nitrosococcus
MSYKVIIPARYGASRLPGKPLLDLAGKPMLLHVVEKAQKSGAEEVLVATDDRRIEAIVQNHGVQVCMTSVQHDSGTNRLAEAVTQKDYPDQTIIINVQGDEPLLPPSLITQAAEDLKTHPKADIATLCVPIANREELFDPNIVKVVRDIQGYALYFSRAPIPWAREDFAAKTGNRWPTSWSYYRHVGLYAYRASFLRRYPQLPVSPLEQAECLEQLRVLYHGGRIHVAIAGTIPPPGVDTLADLERVRQLLVTQERNHN
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Q3J7B0
Q90ZF9
CENPH_CHICK
Centromere protein H
Gallus
MAGRLSESVGSGPGAEAETAADPDAKRDVLEHLCARTHLKQLVMEFDTACPPDEGCNSGAEVNFIESAKETLEEVGKVKSAFESKALVIKRIQLMDALRKRVKENDGCARLIVETMRDIIKLNWEIIQAHQQARVIRENLNDIRRKRYFLKQAEGEKALRIFTTVRKKKEVVRMKIAEKLKFIHRNVQYERKVTTLVQNILQNIIVGCQINWAKDPSLRAIILQLEKDISIQNLL
Component of the CENPA-HI complex, a centromeric complex involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. Required for the localization of CENPC but not CENPA to the centromere. It however may be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex.
Q90ZF9
Q95220
MMP14_RABIT
Membrane-type-1 matrix metalloproteinase
Oryctolagus
MSPAPRPSRRLLLPLLTLGTALASLGSAQSNSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQRFYGLRVTGKADTDTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVHYAYIRDGREKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTEKFLLPDDERRGIQQLYGSQSGSPTRCLLNPGQPSGLLFRISPGNPTYGPKICDGNFDTVAVFRGEMFVFKERWFWRVRNNQVMDGYPMPIGQLWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPAGGRPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV
Endopeptidase that degrades various components of the extracellular matrix, such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15 in association with pro-MMP2. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis.
Q95220
A8AY67
RECR_STRGC
Recombination protein RecR
Streptococcus
MLYPTPIAKLIDSFSKLPGIGIKTATRLAFYTIGMSDDDVNEFAKNLLAAKRELSYCSICGNLTDEDPCAICRDESRDQSTILIVEDSRDVSAMENIQEYHGLYHVLHGLISPMNGVGPDDINLKSLITRLMDSEVSEVIVATNATADGEATSMYISRVLKPAGIKVTRLARGLAVGSDIEYADEVTLIRAIENRTEL
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.
A8AY67
Q6K8X6
ORR23_ORYSJ
OsRRB5
Oryza sativa
MRAAEERKGVVPAARRRDQFPVGMRVLAVDDDPVCLKVLETLLLRCQYHVTTTNQAAIALKMLRENRDMFDLVISDVHMPDMDGFKLLELVGLEMDLPVIMLSVNGETKTVLKGITHGACDYLLKPVRIEELRNIWQHVIRRKFSTRDRANLDFYEECNKPPNADSDHVHGHVTCGSPDQSGRPSKKRKEYCSEEEDEGEVNTQDIDDPSAPKKPRVVWSVELHRKFVAAVNQLGIDKAVPKRILELMNVEKLTRENVASHLQKYRLYLKRLSAVASQQVSIVAALGGRDPFLHMGGFEGLQGYQAFTSSAALSSFTPHGLLNSPRNNPAALGTQGVPASKSIQTMSGSHTLSHSINDANKYHLSLPGNQKGNLGQGLATSLGQTQMQQKWIHEETDDLSTILSGNGLSNGMSGTLQSVTSSPLLPQELAECTQAKIVSQPSIRTSSVSSEHIEGAVGVSSGLLESRVSQQSTIPLSGFSANGLLIHGSFNNTCANKLGGTSSSCAPARSSNDLMVARDTKGGASSFGGAMLLPPDTEQKYLNFGGGNGLKQKFDDRTADSLFDLKFVWSSVPSSQLASNIGAHHAMSQRWNNSSSNSSNIGARMIGQATSSGSTVIPQMKTDFLVSGDMAMPKNASDLSIPKLQSELSSSSCSFDGLLNSIVKVEKDDVTFSDDLGCGDFYSLGACI
Transcriptional activator that binds specific DNA sequence. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. May directly activate some type-A response regulators in response to cytokinins.
Q6K8X6
Q9H2H8
PPIL3_HUMAN
Rotamase PPIL3
Homo
MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCIFHRNIKGFMVQTGDPTGTGRGGNSIWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTYRPLNDVHIKDITIHANPFAQ
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.
Q9H2H8
B1ZRT0
NUOD1_OPITP
NDH-1 subunit D 1
Opitutus
MATEFTVPDSAARIATAQQAGGGTPVRSGPPDEGGEFSGDRMSLSMGPSHPSTHGVLRIQMELEGEILTKADPIIGYLHRGDEKIAENMTYNQFVPYTDRLDYLAPLANNMAYVIAVEKLAGLTVPPRCQAIRVITAELARISSHLMGLGAFGLDVGAWTVLVLSLNQREFLYNLFEDLTGARFTTSYTRIGGVTRDVPPGWLENVGTFCDKFLPALEEILSLLTRNKIFLDRTVGVGVISKEDAIAYGITGPNARGSGIATDLRKDRPYSGYEQYEFDVPVGTKGDCYDRYLVRGEEMRQSVRIIRQVIKNFPGGDWYATEAKKVFLPPKGKVLSSMEELIQQFMLVTEGPQMPAGEVYFEAENPKGILGFYIVSKGGGVPYRLKIRSPSFCNLSLVPKLCQGVLISDVVAILGSLDFVMGECDR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B1ZRT0
P0DD78
RADA_STRP3
Branch migration protein RadA
Streptococcus
MAKKKATFICQECGYQSPKYLGRCPNCSAWSSFVEEVEVKEVKNARVSLAGEKSRPVKLKDVDNISYHRTQTDMSEFNRVLGGGVVPGSLILIGGDPGIGKSTLLLQVSTQLANKGTVLYASGEESAEQIKLRSERLGDIDNEFYLYAETNMQAIRTEIENIKPDFLIIDSIQTIMSPDITGVQGSVSQVREVTAELMQLAKTNNIATFIVGHVTKEGTLAGPRMLEHMVDTVLYFEGERHHTFRILRAVKNRFGSTNEIGIFEMQSGGLVEVLNPSQVFLEERLDGATGSAVVVTMEGSRPILAEVQSLVTPTVFGNARRTTTGLDFNRVSLIMAVLEKRCGLLLQNQDAYLKSAGGVKLDEPAIDLAVAVAIASSYKEKPTSPQEAFLGEIGLTGEIRRVTRIEQRINEAAKLGFTKVYAPKNALQGIDISQGIEVVGVTTVGQVLKAVFS
DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
P0DD78
Q824L3
PYRE_CHLCV
Orotate phosphoribosyltransferase
Chlamydia
MMSFEEEQLRDHAVVNLYRIGAIRFGDFILSDGKKTPIYVDMRLVISCPDVLQTIASLIWRLRPSFNSSLLCGVPYTALTLATCISLKYNISMVLRRKELKHPNQEDKIKVEGLFSPGQTCLVINDVIASGRSILDTAKALEDEGLNIRESLVFLDRQVGGADALKEAGIKLRSVFTLEELVKALLSKCQLSETDAAIARTLLETF
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Q824L3
Q143C7
MINE_PARXL
Cell division topological specificity factor
Paraburkholderia
MSILSFLLGEKKKSASVAKERLQLIIAHERAGGHAPADYLPALQRELVAVISKYVKISHEDIRVSLERQDDLEVLEVKIEIPQA
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Q143C7
A6TD85
FUCM_KLEP7
Type-2 mutarotase
Klebsiella
MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLRVSDLLQAIIPLFELDSYAPPVVMMAAVEGDALDPTVEQRYRQALSTQAPCPDIVRIDRFAFYDRAQKAFAIVITGECAKYGNILLKKGVTP
Involved in the anomeric conversion of L-fucose.
A6TD85
Q9NR28
DBLOH_HUMAN
Second mitochondria-derived activator of caspase
Homo
MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRPWHKTVTIGFGVTLCAVPIAQKSEPHSLSSEALMRRAVSLVTDSTSTFLSQTTYALIEAITEYTKAVYTLTSLYRQYTSLLGKMNSEEEDEVWQVIIGARAEMTSKHQEYLKLETTWMTAVGLSEMAAEAAYQTGADQASITARNHIQLVKLQVEEVHQLSRKAETKLAEAQIEELRQKTQEEGEERAESEQEAYLRED
Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.
Q9NR28
A5ULP6
TPIS_METS3
Triose-phosphate isomerase
Methanobrevibacter
MNTPIVILNYKTYLESSGENALELARALKSASEESGITMVAAPQAADIYRIQDQISLPIFAQHIDPITPGGHTGSNLIETLIEAGISGSLINHSENRMKLADIDEVIQLCKQNDIESCVCTNNIATSKAIATFSPDAVAVEPPELIGTGIPVSQAQPEVVEDSVKGVKSINKKIKVLCGAGISTGDDMKAAMDLGADGVLLASGIVKAKNPKEALLDLVSKL
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
A5ULP6
A7HBU9
LIPA_ANADF
Sulfur insertion protein LipA
unclassified Anaeromyxobacter
MTARKPGWLRVNVPGGARYQQVRDTVKGLALHTVCEEAHCPNVAECWGGGTATVMLMGDVCTRGCRFCNVKTDAHPPPLDPDEPRHLAEAIAELGLDYIVVTSVDRDDLPDGGAGHFADAIRRLKDIPQLLVEVLTPDFRGDAEAVRTVGRARPDVFANNLETVRRLTPVVRDLKAGYDQTLAVLARMKREFPRIVTKSSIMVGLGETEDELLEAMGDLRAAGVEILTLGQYLRPSAWHLPVVEYVKPEKFAAWREAGLGLGFRYVASGPLVRSSYRAAELFLRGELASRPPGP
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.
A7HBU9
B6I7S9
BIOB_ECOSE
Biotin synthase
Escherichia
MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVKAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVEGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
B6I7S9
Q7U5G0
HEMH_PARMW
Protoheme ferro-lyase
Parasynechococcus marenigrum
MSRVGVVLLNLGGPERIQDVGPFLYNLFADPEIIRLPSPALQKPLAWLISTLRSGKSQEAYRSIGGGSPLRRITEQQARELQSLLRQRGLDATTYVAMRYWHPFTESAVADMKADGMDEVVVLPLYPHFSISTSGSSFRELQRLRQGDAAFEQLPIRCIRSWFDHPGYIKAMAELIAEEVRNSDDPEKAHVFFSAHGVPKSYVEEAGDPYQQQIEACTDLIMKSLAEHMGHSNPHTLAYQSRVGPVEWLKPYTEEALEQLGEAKTNDLVVVPISFVSEHIETLEEIDIEYRELATEAGVVNFRRVRALDTYPPFIEGLADLVTTSLEGPEVSLDAAAELPTKVKLYPQEKWEWGWNNSSEVWNGRLAMLGFSAFLLELISGHGPLHALGLL
Catalyzes the ferrous insertion into protoporphyrin IX.
Q7U5G0
P80411
MK3_PALPR
Metalnikowin III
Palomena
VDKPDYRPRPWPRPNM
Antibacterial peptide active against Gram-negative bacteria.
P80411
H3K2Y6
MED12_ARATH
Protein CRYPTIC PRECOCIOUS
Arabidopsis
MQRYHAANCTSAVNNSAIGGASARDSGRADSSSIGNYSLNSRRPPPLTPYKLKCEKDGLNSRLGPPDFHPPTSNSPEENLTKEYVQFGYKETVDGLKESEEIILSQVHTFSKPVVHKCKEAVRKCLRAINESRALKRKAGQVYGVPLSGSLLCKPGFPEQRSCGEETKKRWIESLSQQHKRLRSLADNIPGYRRKTLFEVLIRNNVPLLRATWFIKVTYLNQVRPSPAAISSGTPDKTQASRCEQWTKDVIEYLQYLLDELLSRNSSFPAQQTRDRSPQMLYTGSMQKNSPASTSLYGEETSLHFKWWYMVRLLQWHHAEGLLFPNLIVDWVLKLLQEKEIFEILQLLLPIVYGVLESIVLSQTYVQSLVAIAVRFIQEPAPGGSDLVDNSRRAYTLSALIEMVRYLVLAAPDTFVASDFFPLPPSVAACGPNDVSYTSKAYENLEKLRSNSAEISAQFQGRGVLSRFEFLSFDYTISTIQRSADDLAKIASAGYPQHNVAKAVQALDKALSDGDIRAAYSYLFEDLCNGAVDEAWITDVSPCLRSSLRWIGAISTSFVCSVFFLIEWATCDFRDFRAGVPKDIKFSGRKDCSQVYLVIQLLKQKILGGEFTARKGKNCRNNFLGVSKPSGSMDAFESPGPLHDIIVCWIDQHEVHKGGAKRLQLLVFELIRSGIFNPIAYVRQLIVSGMIDVIQPAVDPERRMRHHRILKQLPGCFVHETLEEAQLFGGDKLSEAVRTYSNERRLLLRELLVEKGKYWNNLVLSDQKSKKISTSLSSVIFPRACNAKSNSKGPRKHTKSSVDIRELKERISALLQFPGMSCGVETPVRDEFQNSVKRSSGSVYSKMDQPEATPGCEDCRRAKRPKMNDEKSSCYQGNSPIASDEEDNWWIKKGSKTVESSLKVDPQIEITKQVPRGRQKMARKTQSLAQLQAARIEGSQGASTSHVCDNKVSCPHHGPGVEGENQKVVDVFRTSTPVDMVSVGNSLKQLQFVDKRSIAVWLTTAVRQLVEEPQKSSVRVGQFNRGAPVEEKNTIRWKLGADELYSILFLLDISLDLVSAVKFLLWLLPKANSTPSFAVQGGRNLVTVPRNVENNMCEIGEAILVSSLRRYENILLSADLVPEAMTALMNRAASLMSSNGKISGSAALVYTRYILKRYGSLPSVVEWHNNFKATSEKKLLSELDHTRSGNGEYGNPLGVPAGVDNPDDYLRKKISIGGARPSRVGLSMRDVLQRHVEEATHYLKKLIGTGTMKASLAEKNDDGYQVAQQIVVGLMDCIRQTGGAAQEGDPSLVSSAVSAIINSVGLSVARITDFSLGNIYQNHPSGVDSSNIARYILRIHITCLCLLKEALGERQSRVFEIALATESSTALTGVFAPVKGSRGQHQLSPESYDSNANNSTIDMSNGTGKMALSRATKITAAVSALVIGSITHGVITLERIVGLLRLKDYLDFVQFVRRTKSSSNGSARSMGASKVESPIEVYVHWFRLLVGNCKTVSEGLVLELVGESSVVAISRMQRMLPLKLVFPPAYSIIAFVLWRPFVSNSNSNSSVHEDTHRLYQSLTMAFHDVIKHLPFRDVCFRDTQGLYELIVADSTDAEFASVFESHGLDMHLKSVAFAPLRARLFLNSLIDCKVPSSGYSHEGVSEAKNRHQGNGTKLVDKLVSVLDCLQPAKFHWQWVELRLLLNEQALAEKLENHDMPLTDAIRSSCPTSEKPDASENEKNFIQILLTRLLVRPDAVPLFSEVVHLFGRSVEDSMLKQAEWFLAGQDVLFGRKTIRQKLIIVGESKGLPTKPQFWKPWGWCNSSSSDHITANKAGKKRKFEITSIEEGEVIEEGSGSRKVLLPRVLDENSPSVGYGITTERAFVQLVLPCIDQSSDESRSTFVNELVRQFSNIEQQLSSVTNRSTTSNKQMGTASSGSEISSNKGSTRKGLRGGSPSLARRSSANTTDTSPPPSPAALRASMSLRLQFLLRLLPVICGEPSFKNTRHALASTIVRLLGSRVVYEDYAVCSPRSELSKAETESTIDPSSMADLSSEVLFDRLLFVLHGLLSNHQPKWLKPRPSSNESSKDFTLFDRDAAESLQNELSRMQLPDTIRWRIQAAMPILLPSLRCSLSCQPHSVPPTALTLVQPSGSTAAAGTNQRNSPAISKSGTAAAQGKLKPTMLAPHQQQEADNTDVVDPWTLLEDGTSSGLSSSNASNSSDMANLRATCWLKGAVRVRRTDLTYVGSVDDDS
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Flowering regulator which suppresses FLC expression, promotes FT and TSF expression and up-regulates SOC1 and FUL mainly in an FT-dependent manner under long-day conditions. Involved in diverse developmental aspects through gene regulation and modulation of the auxin response. Acts closely together with MAB13. Involved in the regulation of embryo patterning and cotyledon organogenesis by transiently repressing a transcriptional program that interferes with this process.
H3K2Y6
C4K3X0
RNPH_HAMD5
tRNA nucleotidyltransferase
Candidatus Hamiltonella
MRPSGRTAQQLRPLTFTRHYTKYAEGAVLVEFGETRVLCTATVEEGVPRFLKGQNKGWITAEYSMLPRSTHQRHARESVKGKQGGRTLEIQRLIARALRAAVDLTKLGEFTIKLDCDVLQADGGTRTAAITGACVALQDALQKMRVEGKLKSNPMKGLVAAVSVGVVGGESICDLEYIEDAIAETDMNVVMIEEGAGRKIIEIQGTAEGAPFSHQQLLELLALADDGIKTIFQAQKKVLEK
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
C4K3X0
A4TET2
FOLD_MYCGI
Methenyltetrahydrofolate cyclohydrolase
Mycolicibacterium
MMRVGAITLDGKATRDEIFVDLRERVARLAAAGRTPGLATVLVGDDPGSHAYVRGKHADCAKVGINSIRRDLPADISQAVLDETIDELNANPECTGYIVQLPLPKHLNENAALERIDPSKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRFEVEIAGAHVAVLGRGVTVGRPLGLLLTRRSENATVTLCHTATRHLPEITREADIIVAAAGVPHMVTADMVRPGAAVVDVGVSRDDAGKLVGDVHPGVWDVAGHVSPNPGGVGPLTRAFLLTNVVERAEANL
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
A4TET2
B1J2V4
METE_PSEPW
Methionine synthase, vitamin-B12 independent isozyme
Pseudomonas
MALAHNLGFPRIGRDRELKKAQEAFWKGELDEAGLRKVGRDLRAAHWQAQKDAGIELLPVGDFAWYDQVLTHSLTFGVIPERFRGHDGAKPTLQTLFAMARGVATGRSANCCGGAHAQEMTKWFDTNYHYLVPEFTVDQQFALSWEQLFEEVDEAKALGHAAKPVVIGPLTYLWLGKAKGGDFDKLELLDRLLPVYDEILNRLAGQGVEWVQIDEPILVLDLPQEWKNAYERVYNILQRAPLKKLVATYFGGLEENLGLAANLPVDGLHIDLVRAPEQYPTILDRLPAYKILSLGLVNGRNVWACDLEKAVDVLRHAAERLGDRLWVAPSCSLLHSPVDLGREDQLDTELKSWLAFAVQKCQEVAVLAKAVNQPDAAEVAAALARSRAIQAGRASSPRIHKPAVQARVHAIKPGDSQRQSAFGQRIAKQRAGLNLPAYPTTTIGSFPQTPAIRLARQAFKQGKLTEADYVEAMHSEIRHAVQIQENLGLDVLVHGEAERNDMVEYFAEQLDGYVFTRFGWVQSYGSRCVKPAVIYGDLSRPEAMTVAWIRYAQGLTRKVMKGMLTGPVTMLMWSFPREDVSRETQARQLALAIRDEVLDLEAADIKIVQIDEAAFREGLPLRRSAWPAYLEWATEAFRLCASGVRDETQIHTHMCYSEFNDVIESIAAMDADVITIETSRSDMELLEAFEKFDYPNEIGPGVYDIHSPRVPSREEMVKLLRKAALRIPAERLWVNPDCGLKTRAWPETEAALVNMVAAARELRATA
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
B1J2V4
C9J202
AG1L2_HUMAN
Putative glycosyltransferase ALG1L2
Homo
MGATAGWAVTVYDKPASFFKEAPLDLQHRLFMKLGSTHSPFRARSEPEDPDTERSAFTERDSGSGLVTRLHERPALLVSSTSWTEFEQLTLDGQNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCIPWLEGRGLPPLLGSVDLDVCLDTSSSGLDLPMKVVDMFRCCLPACAVNFKCLHELVKHEENRLVFEDSEELAAQLQYFADAFLKLS
Putative glycosyltransferase.
C9J202
P26492
FLAV_DESDE
Flavodoxin
Desulfovibrio
MSKVLIVFGSSTGNTESIAQKLEELIAAGGHEVTLLNAADASAENLADGYDAVLFGCSAWGMEDLEMQDDFLSLFEEFNRIGLAGRKVAAFASGDQEYEHFCGAVPAIEERAKELGATIIAEGLKMEGDASNDPEAVASFAEDVLKQL
Low-potential electron donor to a number of redox enzymes.
P26492
B2S0V7
TIG_BORHD
PPIase
Borrelia
MILNDDVKLIPGSKVEAVIKISKEFVKGKYNEILQDYSSRLKIKGFRIGKVPFSIIEGKYSDNIRALTIEKLIHKSLEEFFKSATYKPLGYAVPKILDEKLEIDFNKDFEFTVVYEAYPEFEIPDISNVEVEIPEVTVSDSDVEDELKLLQLENAMVVDDSGDVKVGSIVRVDFVELDDSLSEILTTKRQDFVFTVGESNNYYGFDNDIIGMKKDEEKIIEKNYSADYKFSELANSFKRLKIIIKDIKKRDIPELDDDFAKDIKDSFNTLEELKAHIRENMLRLVKEKRESLKLSKLLSDVSEKLNIEIPSAMFEAELKNVVNEFSTQNKIDLKKLNDSSMGLEGVSDVFKENVLKKLKSKLVFQKIVDNDLTEITDADLEDELVKQAEDTKMRLSEIKKFYQEKNLLGILKDEIKRQKVKDKILKNVKEIKLKEIAFRDFINYKTGE
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
B2S0V7
Q9X1I8
KAD_THEMA
Adenylate monophosphate kinase
Thermotoga
MMAYLVFLGPPGAGKGTYAKRLQEITGIPHISTGDIFRDIVKKENDELGKKIKEIMERGELVPDELVNEVVKRRLSEKDCERGFILDGYPRTVAQAEFLDGFLKTQNKELTAAVLFEVPEEVVVQRLTARRICPKCGRIYNLISLPPKEDELCDDCKVKLVQREDDKEETVRHRYKVYLEKTQPVIDYYDKKGILKRVDGTIGIDNVIAEVLKIIGWSDK
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.
Q9X1I8
A2BU00
SPEA_PROM5
Biosynthetic arginine decarboxylase
Prochlorococcus
MTNFDSKKLNKHWTIEDSISTYGIDKWGDQYFSINSLGNISITPNRNSKKTIDLFKLVNEIKSREINTPLILRFNDILKDRITELNNAFSQAIETYNYKNIFQGVFPIKCNQQKNVLEKIIEYGDYWDFGLEVGSKSELLIGLSLLENKKSLLICNGYKDKKYIEIAILARKLGKQPIIVIEQIDEVQRIIEAVKNLRSTPILGIRSKLSSKSSGRWGKSVGDNSKFGLSIPEIMLTIKELKEASLINEMKLLHFHIGSQISDISVIKDALQEASQIFVELSKLGAPMKYIDVGGGLGIDFDGTKTSSNTSTNYSLQNYANDVVATIKDSCEVNNIQHPIIISESGRAIVSHCSVLIFDVLGTSHVSSQIKVSHQKKTSLIIKNLIDTHNQLKNLRNKKEDLSEIIELWNDAKKFKKDCLVAFRLGFISLGERAYAEELTWACAKEISSHLDNEKIIHPDLSEITETLSSTYYANLSVFKSIPDTWAINQIFPIIPIHRHLEEPICKGNFADLTCDSDGKLNNFIDNGKIKSLLNLHRPEENNDYLIGIFMAGAYQEALGNFHNLFGNTNVIHIDINEDNTYKIKNIIKENSKSEILELLDYSSDNLVESIRINTEFAINNKTLSIEEARKLIDQIETSLRKSSYLSE
Catalyzes the biosynthesis of agmatine from arginine.
A2BU00
A1WXX0
GLMM_HALHL
Phosphoglucosamine mutase
Halorhodospira
MAEERSYFGTDGIRGRVGEAPITPDFVLRLGWAAGRVLAGEGQRKVVIGKDTRLSGYMFESALEAGFAAAGVHSLMLGPMPTPAIAYLTRTLHARAGVVISASHNPHHDNGIKFFGPDGYKLDDATEEAIERLLQDGPPQMVRCEELGRATRINDAVGRYIEFCKGSVQRQIDLRGLRVVVDCAHGATYQAAPAVLAELGADVVVIGNEPDGLNINVDHGSQHPERLCQRVVEASADVGVAFDGDGDRVIMVDRYGRVIDGDGLLYIIATARVARGQVRGAVVGTQMTNLGLEVALQELGLVLERTRVGDRYVLERLLQVGGTLGGESSGHIICLDRTTTGDGLISALQVLEAMVTTGRPLDELVAGMHYYPQRLVNVPVSRGPDVIRLPAVTEAVEEAEHQLGDHGRVLLRPSGTEPLLRVMVEGADEGQVNRLADWLAVTVETAARGAATDPI
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
A1WXX0
A5G7R0
RL9_GEOUR
50S ribosomal protein L9
Geotalea
MKVILKENIENLGHIGDIVKVAPGYARNYLLPKGFALEATTKNAKALDHAKKHLEYKKNKVLEQARVLAAKIEGLALNLSHQAGEEGKLFGAVTNMELAEQMKAQGIEIDRKKIILAEPIKHLGEFTATVKIHPEVNATLKVTVSKA
Binds to the 23S rRNA.
A5G7R0
B3QTP2
YBEY_CHLT3
Endoribonuclease YbeY
Chloroherpeton
MSIIISKTVKQELPEEKIRKAIELVLQGEKCEAEEISAVYCGDRLIRKINIEHLAHDYPTDTISFRLNSGNAIEGEFYISCDTVRRNAQEYESSFENELLRVTIHSVLHLIGFEDQSAAQKAEMTQKENRYLAALFHHDEK
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
B3QTP2
A7MEM7
ACCA_CROS8
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Cronobacter
MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSVIPEPLGGAHRNPEAMAQSLKTQLLADLADLDVLSKDDLLNRRYQRLMSYGYA
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
A7MEM7
Q80ZN5
CST13_MOUSE
Cystatin-T
Mus
MARFLQTLLFLVIMVEFVSRRVEAWGSPQIVRPFEDIPKSYVYVQHALWYAMKEYNKASNDLYNFRVVDILKSQEQITDSLEYYLEVNIARTMCKKIAGDNENCLFQQDPKMKKMVFCIFIVSSKPWKFELKMLKKQCKDI
May perform a specialized role during sperm development and maturation.
Q80ZN5
Q2NEV4
TFE_METST
Transcription initiation factor TFIIE
Methanosphaera
MAKKKVKYTFDYDSKFLNEHNVKKLAYELTHDSDTSNKILDCLFTAEVTDEQIAEATGIKLNFVRKILYKFYDVGMANYTRKKDPETQWFTYYWRFDSRKAAQILEKQYNHHNQEIKESIEYEENNMFFVCPNGCRYPFDEATEFQFICPRCNEKLEFKDNSDLIHDLKKLESAYKINE
Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation complexes. Seems to translocate with the RNA polymerase following initiation and acts by binding to the non template strand of the transcription bubble in elongation complexes.
Q2NEV4
Q5FTN3
HIS6_GLUOX
ImGP synthase subunit HisF
Gluconobacter
MLKLRVIPCLDVKDGRVVKGVNFVSLRDAGDPVEQAKLYDAAGADELTFLDITASVENRDTILDVVRRTAEAICLPLTVGGGVRTCEDMRRLLLAGADKCAVNSAAIKNPDLIREASERFGSQCIVVAIDARSNGKGGWEVYAKGGREPTGLDVVEWARKMQDLGAGEILLTSMDRDGTRAGFDLDLLRAVCGAVTVPIVASGGVGELQHFVEGAEVGASGLLAASVFHFGQFRIDEVKNALNKAGLPVRLGE
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Q5FTN3
B7UNN5
FIEF_ECO27
Cation-efflux pump FieF
Escherichia
MNQSYGRLVSRAAIAATAMASLLLLIKIFAWWYTGSVSILAALVDSLVDIGASLTNLLVVRYSLQPADDNHSFGHGKAESLAALAQSMFISGSALFLFLTGIQHLVSPTPMTDPGVGVIVTIVALICTIILVSFQRWVVRRTQSQAVRADMLHYQSDVMMNGAILLALGLSWYGWHRADALFALGIGIYILYSALRMGYEAVQSLLDRALPDEERQEIIDIVASWPGVSGAHDLRTRQSGPTRFIQIHLEMEDSLPLVQAHMVADQVEQAILRRFPGSDVIIHQDPCSVVPREGKRSMLS
Divalent metal cation transporter which exports Zn(2+), Cd(2+) and possibly Fe(2+). May be involved in zinc and iron detoxification by efflux.
B7UNN5
Q87KQ4
RPOB_VIBPA
Transcriptase subunit beta
Vibrio
MVYSYTEKKRIRKDFGTRPQVLDIPYLLSIQLDSFDKFIEQDPEGQYGLEAAFRSVFPIQSYNGNSELQYVSYRLGEPVFDVKECQIRGVTYSKPLRVKLRLVIFDKDAPAGTVKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARVIPYRGSWLDFEFDPKDNLYVRIDRRRKLPASIILRALGKSTEEILDIFFEKVNFEVKDQTLLMELVPDRLRGETASFDIESNGKVYVEQGRRVTARHIRQLEKDGVDHIEVPVEYIVGKVASKDYINEATGEIIVNANQEISLEALANLSQAGHKALEVLFTNDLDHGPFMSETLRIDSTVDRISALVEIYRMMRPGEPPTKEAAEALFESLFFSEERYDLSTVGRMKFNSSIGREDAQEQGTLDETDIIEVMKKLIAIRNGKGEVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDAVMPQDLINAKPISAAVKEFFGSSQLSQFMDQNNPLSEVTHKRRISALGPGGLTRERAGFEVRDVHVTHYGRLCPIETPEGPNIGLINSLSAFARCNEYGFLETPYRRVVDGVVTDEVDYLSAIEEGQFVIAQANAKLNEDGTFADELITARQKGESGLHPREHAQYMDVATNQVVSIAASLIPFLEHDDANRALMGANMQRQAVPTLKADKPLVGTGIERNVAVDSGVTAVAKRGGVIQSVDASRIVVKVNEEELVPGEAGIDIYNLTKYTRSNQNTCINQRPCVMPGEPVARGDVLADGPSTDLGELALGQNMRIAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELTCVARDTKLGSEEITADIPNVGESALSKLDESGIVYIGAEVKGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDTSLRVPNSVSGTIIDVQVFTRDGVEKDKRALEIEQMQLKEAKKDLTEEFQILEGGLLNRVKAVLIEGGYSEAKLDATDRKKWLELTLEDDALQTQLEQLAEQWDELKADFDKKFETKRRKITQGDDLAPGVLKIVKVYLAVKRRIQPGDKMAGRHGNKGVISKINPVEDMPYDEKGQPVDIVLNPLGVPSRMNIGQILEVHLGLAAKGIGDKINQMVKEQQELAKFREFLQKVYDLGDTRQKVDIASLSDDEVRTLIKNLRGGLPIATPVFDGAPEASIKALLELADLPTSGQLTLFDGRTGDAFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGNHSMEPGMPESFNVLLKEIRSLGINIELEDEE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q87KQ4
A5CD16
RPPH_ORITB
(Di)nucleoside polyphosphate hydrolase
Orientia
MDDKIKNYNNLPYRIGVGMVIINQKKEIFTGQRIDSARQYWQMPQGGIILGETYSKAVLREMKEEIGCNKAIIMAESRNWYSYHIPKFLVHKLWNSNFKGQKQKWFLIKFLGKDEDININTIYPEFSQWKWMNSNQLINNALPFKRKLYKAVINEFHIFLL
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
A5CD16
S0DL59
APF5_GIBF5
Apicidin F synthesis protein 5
Fusarium fujikuroi species complex
MHPDVEQELAYTLLIELMAHQFAYPVRWIETQDHILGEVNAERIIEIGPSPILTNMMKRTIASRFSNSDQALNINRHLMSPDNGNPDIYYKYEPTEEPDLPELGSQSNTVKVSGSPAWEVQRPVTASHIPSGPVDEIEDTKVPVSAILISLLAPKLKKDPRAIPMTGTISNLVGGRSTLSNEIVGDLLAEFPNRVPDKPEEMPLSSLSETLSTSHDGQLGKATSALVMKMVSSRLPGGYSLSNARLYLREKWGLPPRRQDAVFLLALQRQPTSRLLSSTDVDSFLDANAAAYFGQENLSIPSRGSVQSAAPAVDAKALLLAKQQNDALLRDIMGVIQGHTAAKNESQDATLQASDSEAAATKKLDMWISEHGDDYAKGMAPIFDAKKQRIYDSYWNWNAQDTILLFQRKLQGQMSSVKELEQLSTSIVNRACGRTLEQLDYIIAQAERDPTVDSGLLKPMQLLRQTCVETQERQPVFINLSPDMAPLTTISSDGRLIFSEIPRALPCSKILSTNEASSIAFPVSRADGVAVSYSPQLTEILCHDLKDSRRSGFSFSGKNVLLTGAGEGSIGNHILRHLLAGGARVTVTTSSFSEKVTAMFQSIYARHGSKGSVLRVVPFNQGSHGDVQNLVKYIYADASWDLDFILPFAAISENGRDIEDLDSKSEIAHRAMLTNLVRLVGAVASQKRQRDTITRPATVVLPLSPNHGLLGNDGLYSESKRSLETLIPKWSSETWGSYIALAGVIIGWTRGTGLMDSNDVIAQAVESLGVRTFSAVEMAANIVSVMGGRFNAECQETPIIVDMGGGLGSVKNFKAKLTSARQELNAYAELKRLTAQESSRDKAYVATDAHAKTSKRLRGRANILLPLPKNLNYEVDIAPFAASLDGMVDLSRVVVITGFAELGPLGNSRTRWEMEESGTLSLEGCVEMAWLMGLITYHNGIDKKGDHYSGWVDTKTSDAICDDEIPGKYLEFMAKHSGIREVEPEISDNGYDPSKKESLIEVALQRDLAPFETSIETAETLKRQHGDKAIVTQDASSGNCQVQLKAGAVVMVPRASRFNRTVAGQIPLGWTAKRYGISDDIIEQVDPVTLFSLVCTVEALLCSGIIDPYEFYQHIHVSQFANCLGSSMGGLTSLRKMHRDRYLDRSVKSDLVQETFINTTGAWINMLLSSSSGPIRTPVGACASSLESLDTACDLIMLKKAKVCLVGGFEDFVEDLSYEFGCMKATCDTDAEYAAGRVPKEMSRPTASSRSGFVESQGCGVQVLTSAELALEMGLPIFGIVAYTSMAADKAGRSVPAPGKGVLTNAREKSTIPNPMLSLGYRKRLLELRRTQIYQNISDHLDILNSEIALFQESETASPGDLKAFRENRELRIRQDAQAQDAEVTFSLGNQFWKSQDAGDISPIRGSLAVWGLGIDDISVASLHGTSTVQNDLNETMVIQEQMKHLGRRQGNLLPCVCQKWLTGHSKGAAGAWMVNGCLQMMNTGLVPGNRNADNVDEKLREHRHLAFPNTNLQMDDIKACSVTSFGFGQKGGQALLVHPRYLFATIGRERYDGYISKRDKRWRKACFRLSEAMVQGNMVSKCIKTEAPYTSADGVAALLDPTARF
Fatty acid synthase; part of the gene cluster that mediates the biosynthesis of the cyclic tetrapeptide apicidin F (APF) . The non-ribosomal peptide synthetase apf1 incorporates four different amino acids to produce apicidin F: L-phenylalanine, D-pipecolic acid (D-pip), N-methoxy-L-tryptophan and L-2-aminooctanedioic acid . L-Phenylalanine is the only proteinogenic amino acid directly used by apf1 . The 3 other apf1 substrates are non-proteinogenic and have to be modified by other enzymes of the cluster . Lysine is converted to delta-1-pyrroline-5-carboxylate (P5C) which is reduced to L-pipecolic acid (L-pip) by apf3 . L-pip is epimerized to D-pip, probably by apf1 activity, prior to incorporation . L-Tryptophan is N-oxidyzed by one of the cytochrome P450 monooxygenases (apf7 or apf8), and further methylated at the hydroxy group by the O-methyltransferase apf6 to yield N-methoxy-L-tryptophan . The synthesis of the fourth apf1 substrate is more complex . The fatty acid synthase apf5 is involved in the synthesis of the octanoic acid backbone of L-2-aminooctanedioic acid by fixing one acetyl-CoA unit and three malonyl-CoA units . Then one of the cytochrome P450 monooxygenases (apf7 or apf8) may oxidize this backbone to 2-oxooctanoic acid . The aminotransferase apf4 is predicted to catalyze the exchange of the keto group with an amino group . The next step would be the oxidation of 2-aminooctanoic acid by one of the cytochrome P450 monooxygenases (apf7 or apf8). The last step is the oxidation of 2-amino-8-hydroxyoctanoic acid to 2-aminooctanedioic acid is catalyzed by the FAD-dependent monooxygenase apf9 .
S0DL59
Q8ZND6
PTA_SALTY
Phosphotransacetylase
Salmonella
MSRIIMLIPTGTSVGLTSVSLGVIRAMERKGVRLSVFKPIAQPRAGGDAPDQTTTIVRANSTLPAAEPLKMSHVESLLSSNQKDVLMEEIIANYHANTKDAEVVLVEGLVPTRKHQFAQSLNYEIAKTLNAEIVFVMSQGTDTPEQLNERIELTRSSFGGAKNTNITGVIINKLNAPVDEQGRTRPDLSEIFDDSSKAQVIKIDPAKLQESSPLPVLGAVPWSFDLIATRAIDMARHLNATIINEGDIKTRRVKSVTFCARSIPHMLEHFRAGSLLVTSADRPDVLVAACLAAMNGVEIGALLLTGGYEMDARISKLCERAFATGLPVFMVNTNTWQTSLSLQSFNLEVPVDDHERIEKVQEYVANYVNAEWIESLTATSERSRRLSPPAFRYQLTELARKAGKRVVLPEGDEPRTVKAAAICAERGIATCVLLGNPDEINRVAASQGVELGAGIEIVDPEVVRESYVARLVELRKSKGMTEPVAREQLEDNVVLGTLMLEQDEVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPEQVYVYGDCAINPDPTAEQLAEIAIQSADSAIAFGIEPRVAMLSYSTGTSGAGSDVEKVREATRLAQEKRPDLMIDGPLQYDAAVMADVAKSKAPNSPVAGRATVFIFPDLNTGNTTYKAVQRSADLISIGPMLQGMRKPVNDLSRGALVDDIVYTIALTAIQASQQQQ
Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. Required for acetate recapture but not for acetate excretion when this organism is grown on ethanolamine (EA); is unable to complement an eutD deletion during growth on EA . Works with proprionate kinase PduW to capture exogenous propionate and regenerate propionyl-CoA during degradation of propionate and 1,2-propanediol (1,2-PD) .
Q8ZND6
P0A4I2
CUTR_STRLI
Defective melC1 suppressor protein
Streptomyces
MRVLVVEDEQLLADAVATGLRREAMAVDVVYDGAAALERIGVNDYDVVVLDRDLPLVHGDDVCRKIVELGMPTRVLMLTASGDVSDRVEGLEIGADDYLPKPFAFSELIARVRALGRRTSVPLPPVLERAGIKLDPNRREVFRDGKEVQLAPKEFAVLEVLMRSEGAVVSAEQLLEKAWDENTDPFTNVVRVTVMTLRRKLGEPPVIVTVPGSGYRI
Member of the two-component regulatory system CutS/CutR, involved in the regulation of copper metabolism. CutR suppresses a defective melC1 gene, encoding a putative copper-transfer gene, probably by altering copper metabolism.
P0A4I2
Q1LRD4
PYRC_CUPMC
Dihydroorotase
Cupriavidus
MTQKLTITRPDDWHLHLRDGAALAAVLPDTARQFARAIIMPNLKPPVTTVDQASAYRARILAALPAGMAFEPLMTLYLTDNTPPEEIVAARASGFVHGVKLYPAGATTNSDAGVTDIRRCAATLEAMQREGVPLLVHGEVTDGDIDIFDREAVFIDRVMKPLRRDFPELKVVFEHITTRDAAQYVAEAEGPVGATITAHHLLYNRNAIFTGGIRPHYYCLPVLKREIHREALVKAATSGSPRFFLGTDSAPHARGLKEHACGCAGCYTALHAMELYAEAFDAAGALDKLEAFSSFNGPAFYGLPRNSGTLTLTREDWELPAELPYGDTTLVPLRAGETLRWKAS
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Q1LRD4
A1TRM7
MNMC_ACIAC
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
Acidovorax
MSEPIDWLPDGTPFNPRFGDRYHSHTGLAQAREVFLRGCGLPGAWAGQAMWRVLETGFGCGLNFLATWAAWRADPARPRLLHFVSCEAFPVSADDLLRSMQGHGELEPLARALHAQYWGLLPGVHRLAFEGGQVLLTLYIGDAQAMLRQQQPVADAVYLDGFSPQVNPELWDVHTLKAVARCCRRGTRLATWSVAGAVREGLAQCGFRVQKVPGLPPKRSNLQAEFDPAWEPRPVQPELPDVRVAGGPSSVLVIGGGLSGAAVAASLARRGWQVRVLDQGAEPAAGASGLPAGVFAPHVSPDDSLLSRLSRCGVRATLQALEASGLSEGEDWSACGVLEHEVDGKHRLPPAWAGDAAVGAEWSRPADAAALEAAGLPGATVAYWHARGGWLRPARLVRALLAHPGIHWQGRSAVARLEPVAAPGGATHWQAYGSDGTVLAEAPHVVVAAGYGSRPWLPARYPIHPLRGQVSWGTRADSPAAAWPPFPVNGHGNLVPHAGTAGGGIWVMGSTFERGQTELPPAPQEQAQAHAANAAKLEQLLPALAQGLAPAIAGPGAAPGHWAAVRCTAPDRLPFVGPVDAARQAGLWVCAAMGARGLTLSQLCGELLAARMMGEPLPVEVRLARALSTERLPAD
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
A1TRM7
O07002
ASPP_BACSU
L-aspartate transporter
Bacillus
MSKQGNFQKSMSLFDLILIGMGAIFGSAWLFAVSNVASKAGPSGAFSWILGGAIILLIGLVYAELGAALPRTGGIIRYPVYSHGHLVGYLISFVTIVAYTSLISIEVTAVRQYVAYWFPGLTIKGSDSPTISGWILQFALLCLFFLLNYWSVKTFAKANFIISIFKYIVPITIIIVLIFHFQPENLSVQGFAPFGFTGIQAAISTGGVMFAYLGLHPIVSVAGEVQNPKRNIPIALIICIIVSTIIYTVLQVTFIGAIPTETLKHGWPAIGREFSLPFKDIAVMLGLGWLATLVILDAILSPGGNGNIFMNTTSRLVYAWARNGTLFGIFSKVNKDTGTPRASLWLSFALSIFWTLPFPSWNALVNVCSVALILSYAIAPISSAALRVNAKDLNRPFYLKGMSIIGPLSFIFTAFIVYWSGWKTVSWLLGSQLVMFLIYLCFSKYTPKEDVSLAQQLKSAWWLIGFYIMMLIFSYIGSFGHGLGIISNPVDLILVAIGSLAIYYWAKYTGLPKAAIDYDK
Uptake of L-aspartate with the concomitant import of a proton. Can also transport aspartate hydroxamate and L-glutamate with lower affinity and efficiency.
O07002
P08635
SAST_RAT
null
Rattus
METAVNAKSPRNEKVLNCLYQNPDAVFKLICFPWAGGGSIHFAKWGQKINDSLEVHAVRLAGRETRLGEPFANDIYQIADEIVTALLPIIQDKAFAFFGHSFGSYIALITALLLKEKYKMEPLHIFVSGASAPHSTSRPQVPDLNELTEEQVRHHLLDFGGTPKHLIEDQDVLRMFIPLLKADAGVVKKFIFDKPSKALLSLDITGFLGSEDTIKDIEGWQDLTSGKFDVHMLPGDHFYLMKPDNENFIKNYIAKCLELSSLT
Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16).
P08635
O74546
OMH3_SCHPO
O-glycoside alpha-1,2-mannosyltransferase homolog 3
Schizosaccharomyces
MGIPKSSIYFCILLFCIISFYLQSSKDGPKELKVKYVFLKKATAKQRGESSLTDSDYFPKQPNMNATLFMLCRNRDIKDALVSIQSVEDRFNHRYHYPWTFMNDAPFTKEFITATSKMVSGDATYVQLNNEEWGIPINIDLNRMLKSIRDMTDDKVIYGFSLSYRIMCRFNSGFFYRNKALSHYDYYWRVEPGVEYSCDIPYDPFRKLSDENKAYGFVISMTDYYETLPSLWNVTRDFIHQNPQYLAQNNSLDFIVNDHQGLSGDYNLCHFWSNFEIANLNFFRSPAYTDYFAHLDKNYGFFYERWGDAPVHSLAASLFLNKSQIHYFEDFGYYHLPWYHCPTDVQSHATARCLCDPTGTIDYLPFSCAIKWLENINS
Probable mannosyltransferase involved in O-glycosylation of cell wall and secreted proteins.
O74546
Q8VYU6
GOGC4_ARATH
Golgin candidate 4
Arabidopsis
MWSSVANLKENLNKIAHDVHDDDEDDDEDLTIYGSTNGGTDRRNSNGFRYSRSPMANGFESPVNPEIERYKAEINKLQKSESEIKALSVNYAALLKEKEDQISRLNQENGSLKQNLTSTNAALKESRLDLSRASNNNAIKGNGDHSPNRSQRSPTNWKNRNQMNNGIASKPNGTENDSESHKKEKEFAEMLEERTRSMASAQARELEKEREKSANLQILLQEERKQNETFKEELQSLRLDKEKTLMESNKVRRELDAKLAEIRQLQMKLNGGEQHAFGISRENLKEVNKALEKENNELKLKRSELEAALEASQKSTSRKLFPKSTEDLSRHLSSLDEEKAGTFPGKEDMEKSLQRLEKELEEARREKDKARQELKRLKQHLLEKETEESEKMDEDSRLIDELRQTNEYQRSQILGLEKALRQTMANQEEIKSSSDLEIRKSKGIIEDLNQKLANCLRTIDSKNVELLNLQTALGQYYAEIEAKEHFERELAVAKEDAMKLSARLKDVDEQLESSKKEKEEITSKVLHAENIAAEWKNRVSKVEDDNAKVRRVLEQSMTRLNRMSMDSDFLVDRRIVIKLLVTYFQRNHSREVLDLMVRMLGFSEEEKQRIGLAQQGAAGKGVVRGVLGFPGRLVGGILGGGGGSPDSHPNMASDNQSFADMWVEFLLKDAEERERREAEDAANKEQEKATVSSTQRPKYEQSDSEFSTVPLTSSNSNHRLSRLLT
Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus.
Q8VYU6
Q864K2
MSHR_CHLAE
Melanocortin receptor 1
Chlorocebus
MPVQGSQRRLLGSLNSTPTATPHLGLAANQTGARCLEVSIPDGLFLSLGLVSLVENVLVVTAIAKNRNLHSPMYCFICCLALSDLLVSGSNMLETAVILLLEAGALAARAAVVQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVLFSMLFIAYYDHAAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQCPAHQGFGLKGAATLTILLGIFFLCWGPFFLHLTLIVLCPQHPTCSCIFKNFNLFLALIICNAIIDPLIYAFRSQELRRTLKEVLLCSW
Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes.
Q864K2
Q9PIY9
RIMP_CAMJE
Ribosome maturation factor RimP
Campylobacter
MNLEALCKEAGLSFYDDELVSENGRKIYRIYVQKEGGVNLDDCARLSEILSPIFDVESPVNGEYFLEVSSPGLERKLSKIEHFAKSIGELVKITTNEKEKFEAKIIAVDDENITLENLENKEKTTINFNDIKKARTFVEW
Required for maturation of 30S ribosomal subunits.
Q9PIY9
O18963
CP2E1_BOVIN
CYPIIE1
Bos
MAALGITVALLVWMATLLFISIWKHIYSSWKLPPGPFPLPIIGNLLQLDIKNIPKSFTRLAERYGPVFTLYLGSQRAVVVHGYKPVKEVLLDYKNEFSGRGENPGFQMHKNNGIIFNNGSTWRDTRRFSLTTLRDLGMGKQGNEQRIQREAHFLLEVLRKTQGQPFDPTFVVGFAPYNVISDILFHKRFDYKDQTSLRLMSLFNENFYLLSSPWIQLYNNFPDYLQYLPGSHRKLLKNVSEVKSYALERVKDHQKSLEPSCPRGFLDTMLIEMAKERHSVDPMYTLENIAVTVADLLFAGTETTSTTLRYGLLILMKYPEVEEKLHEEIDRVIGPSRIPAVKDRLDMPYLDAVVHEIQRFIDLLPSNLLHEATQDTVFRGYVIPKGTVVIPTLDSVLHDRQEFPEPEKFKPEHFLNENGKFKYSDHFKAFSAGKRVCVGEGLARMELFLLLAAILQHFNLKSLVDPKDIDLSPIAIGFGKIPPRYKLCLIPRSKV
A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. 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 (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics.
O18963
O86224
KDKA_HAEIN
3-deoxy-D-manno-octulosonic acid kinase
Haemophilus
MHQFQQDNQYFIFNFDRTFEQATEFFQAEFWQKQERVIGSAKGRGITYFLQTEDWFGVNCALRHYYRGGLWGKLNKDRYRFSALETTRSFAEFHLLQRLYEAGLPVPKPIAARIQKGKLGICYQADILTEKIENAQDLTALLQTQTLPKETWMQIGRLIRKLHDLQICHTDLNAHNILLQQTEQGQKCWLLDFDKCGEKSADFWKVQNLNRLKRSFEKEVGRMNIQFTEQNWADLTSAYHQ
Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position. To a lesser extent, can use GTP instead of ATP as substrate.
O86224
P54261
GCST_SYNY3
Glycine cleavage system T protein
unclassified Synechocystis
MANLFPALRTPLYNLITEQTTKLTTFGGWEMPVQFAGLKQEHQAVREKVGMFDISHMGKFVLTGQKVLAALQSLVPSDLDRLTPGKAQYTVLLNAQGGIIDDIIVYDQGKNPEGQERVTLIVNAATTVKDKQWLLEHLPEEIDFQDLSREKVLIALQGPEALTILQPLVDQNLGELPAFGHLEAEFLREKAFIARTGYTGEDGFEIMVSPEVGKQLWQTFGSKGVTPCGLGARDTLRLEAGMGLYGQDMNDETTPLEAGLGWLVHLDSKGDFIGRAVLTEQKANGVEKRLVGLEMLAKQIARHDYPILHNGEIMGIVTSGTLSPTLQKAIALGYVPTELAKVGQELEVEVRGKTYGIKVVKKLFYRSEQKPR
The glycine cleavage system catalyzes the degradation of glycine.
P54261
Q6MSC1
SSRP_MYCMS
Small protein B
Mycoplasma
MSEHLIVKNKKAYFNYEIIQTYQAGIVLNGPEIKSIRNHDVSINEAFVLIRKKEIYILNMNVKKYQFANYIKGLEETRTRKLLLHKKEIIKILNKIKQENLTIIPVKLYFKNDYVKLEIALAKGKKLHDKRQTIKKRDTERKELKNYK
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Q6MSC1
Q9V107
TRUD_PYRAB
tRNA-uridine isomerase D
Pyrococcus
MLEELKYLSETPGIGGRIKVKPEDFIVREIIPKSIFKGNCQIYLMKKRNWETIAAIKEIAKRIGIHYSEIGFAGTKDRHAVTYQYISVCRDVRKEVEKLKIRDVELKFVGYGRPLKLGFLLGNFFLIRVRDVKRPELIPKIIEELKIKGGFPNYFGIQRFGEKRSVNHIVGKLLLEGKYEEAAEVFLGYPGNGMEGDEARKRFLETKDVDLALEEFPKFLRYERAMLYRYRETRSWKKAFLVLPRPILRIFIHAFQAYLFNLYLSRRIEEGLPLNEAIPGDIVVQVKRGIPLRTRTYRVTETNVDFVNEKIKRGEAMVSGPIFGYSYRKAHGIPGRLEEEILDENEVNVEMFKKLPKPMREPGGRRELLIKPRKFAYKRKEEEVLFKFFLPKGVYATSVLREITKH
Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Q9V107
A7N204
GUAC_VIBC1
Guanosine 5'-monophosphate oxidoreductase
Vibrio
MRIEQELKLGFKDVLFRPKRSTLKSRSQVNLTRDFTFKHSGRQWSGVPVIAANMDSVGSFAMAKALAEHGVMTAVHKHYTVEDWAEFANTADKATLNNVMVSTGTSEADFQKTKDIMAISDEFIFICIDIANGYSEHLVEYVQRVRAAFPDKVISAGNVVTGDMCEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECGDAAHGLGGMIIGDGGCSCAGDVAKAFGGGADFVMLGGMLAGHEESGGEVIEQDGKQFMKFYGMSSKSAMDKHSGGVAGYRAAEGKTVLLPFRGSVHGTIQDILGGVRSTCTYVGAAKLKELTKRTTFIRVQEQENNVFGKE
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
A7N204
Q6FRU9
SEC62_CANGA
Translocation protein SEC62
Nakaseomyces/Candida clade
MDQSAVLAIASFVRNRSELKARKGLFQDKPTDFFRYKRFVRCLKSDAYKKKSLKQPDLYPPLPEDEEKFAELARGIFVEFIKNQLVVPGQKLHSYECKEHGLKPSKDYPHLIMSTKATLDDNEYYLWHYNPKTLTDYLIVFGVIGVILAFVCYPLWPASMRRGTYYLSLAAFGFLGVFFGVAIIRLIVFLISMLFIREKGGFWLFPNLFEDCGFFDSFKPLYGFGDKETYTYIKKMKKQKKRQAKKEKLKKLKEKAN
Required for preprotein translocation.
Q6FRU9
O26148
RPO6_METTH
DNA-directed RNA polymerase subunit K
Methanothermobacter
MHMASKKLTRFERARLIGARALQISMGARPLVEIKESLDPVDIARKELEKKVMPLDVRRDK
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
O26148
A8FKP3
MIAB_CAMJ8
tRNA-i(6)A37 methylthiotransferase
Campylobacter
MSAKKLFIQTLGCAMNVRDSEHMIAELTQKENYALTEDIKEADLILINTCSVREKPVHKLFSEVGGFEKVKKEGAKIGVCGCTASHLGNEIFKRAPYVDFVLGARNISKITQAIKTPKFMGVDIDYDESEFAFADFRNSIYKSYINISIGCDKHCTYCIVPHTRGDEISIPFNIIYKEAQKAVEKGAKEIFLLGQNVNNYGKRFRNEHKKMDFSDLLEELSTIEGLERIRFTSPHPLHMDDKFLEVFANNPKVCKSMHMPLQSGSSEILKAMKRGYTKEWYLNRALKLRELCPNVSISTDIIVAFPGESEKDFEETMDVLEKVRFEQIFSFKYSKRPLTKAATMPNQIDEETASRRLSTLQNRHSEILDEIVKKQENKTFKVLFEELRAGNSIAGRTDNNFLVQVEGSEELLGQFKEVKITNAKRMVLYGEIV
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
A8FKP3
B8FT56
MURG_DESHD
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
Desulfitobacterium
MRVIVTGGGTGGHIYPALAIAKGILVHQPDAEILYIGTREGMEARLVPEAGLEFAGVSGQGLPRKLSLETLKVGGKSFKALWETKQILKKFKPDLVVGTGGYVAGPVVLTAALFGIPTLLHEQNALPGITNKILTRFVRKVMVTFPESIAHFGVRRKLVLTGLPVRPEIGNISRERGAACLGLRSDCLTLLVTGGSRGARSINQAMPTVLKHLAGRKDIQVIWATGKATYQETLESLKTQGIQWQRENWRVLEYLKDMPEAMACADLFVGRAGATTLAEIMVAGKPGILIPYPLAAENHQEFNARALEKDGAACVILDKDLTGENLWALVQGLIEKPEKLRKMAQAARSLGQPDALNKIVKVCLDTAWK
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
B8FT56
Q0KEG8
SYDND_CUPNH
Non-discriminating aspartyl-tRNA synthetase
Cupriavidus
MSSMRTHYCGLVTEQFSGQEVALTGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRPEMFKAAEEIRNEFCIRVTGKVRPRPAGTENANLTSGKIEVLCHELTVLNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQYNLRLRYKVAMEVRKFLDAQGFIDIETPMLGKSTPEGARDYLVPSRVNPGHFFALPQSPQIFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLTEQEIRDLFEDMMRTVFKNAIDVDLDARFPVMEFREAMARFGSDKPDLRVKLEFTELTEVMKDVDFKVFSSPANSDNGRVVGLRVPGGGAISRGEIDAYTQFVGIYGAKGLAWIKVNEVAKGRDGLQSPIVKNLHDAAIAEILKRTGAQDGDIIFFGADKAKVVNDSIGALRLKIGHSDFGKANGLFEDTWKPLWVVDFPMFEYDEEDARWVAMHHPFTSPKDEHLEYLETDPGKCLAKAYDMVLNGWEMGGGSVRIFRSDIQSKVFRALNINDDEARAKFGYLLDALQYGAPPHGGLAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSSVDEKQLRELHIRLRATEPKPTA
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Q0KEG8
A6TFR0
ZAPB_KLEP7
Cell division protein ZapB
Klebsiella
MTMSLEVFEKLESKVQQAIDTITLLQMEIEELKEKNNTLVQEVQSAQHGREELERENSQLKEQQQGWQERLQALLGRMEEV
Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA.
A6TFR0
Q1RII8
ISPT_RICBR
Isoprenyl transferase
belli group
MTNIKHLAIIMDGNARWAATHNLPKSEGHRAGADKVHELLPEFINLKIPYITLYTFSSENWQRSNTEISFLMRLLNIYLKKELDNLHKNGIKIKVIGRLNLLSDSLQKQINNAIELTKDNNKLTLCIAFSYGSRQEITDACTKIIASGKTEILESDIQNALYDPEMPDVDLLIRPGGVFRISNFLLWQAAYAELYFSQKYWPDFNKEDIINAIDDYSKRKRTFGKR
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Q1RII8
A1A040
CH10_BIFAA
Chaperonin-10
Bifidobacterium
MSISLTPLEDKIIVKQAEAETQTASGLFIPDNAKEKPQQGEVLAVGPGRRNDAGERIPVDVKVGDKVLYSKYGGTEVHYQGEDYLIVSARDILAILG
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
A1A040
Q8IYI0
SHLD1_HUMAN
Shield complex subunit 1
Homo
MAARDATSGSLSEESSALDLPSACDIRDYVLQGPSQEANSEAFSSLEFHSFPYSSDVDPDTSNLNIEQNNSWTAENFWLDPAVKGQSEKEEDDGLRKSLDRFYEMFGHPQPGSANSLSASVCKCLSQKITQLRGQESQKYALRSFQMARVIFNRDGCSVLQRHSRDTHFYPLEEGSTSLDDEKPNPGLSKDITHFLLQQNVMKDL
Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres.
Q8IYI0
A3CPR2
MURI_STRSV
Glutamate racemase
Streptococcus
MDNRPIGFLDSGVGGLTVVRELMRQLPHEEVIYIGDSARAPYGPRPAEQIRAYTWQLVNFLLTKDVKMIVIACNTATAVVWEEVKEKLDIPVLGVILPGASAAIKSTASGRIGVIGTPMTVSSDIYRQKIEALSPEMQVESLACPKFVPLVESNELHSSLTKKVVYETLQPLAGRVDTLVLGCTHYPLLRPIIQNRMGPDVKLIDSGAECVRDISVLLNYFEINRSREKQELNHQFYTTANAKSFSEIAESWLRLKVNVEHVSL
Provides the (R)-glutamate required for cell wall biosynthesis.
A3CPR2
A4YT77
RS6_BRASO
30S ribosomal protein S6
unclassified Bradyrhizobium
MPLYEHVFLARQDASTQQVEELTTQMTGIVEGLGGKVTKTENWGVRSLTYRMNKNRKAHFVLLNIDAPSAAIAEIERQERISEDVIRYLSVRVEELEEGPSAMMRKADRDRERDDRGGGFRGERDGGGFRGDRGDRGDRGPRRPRDEETADEE
Binds together with S18 to 16S ribosomal RNA.
A4YT77
Q43210
PALY_WHEAT
Phenylalanine ammonia-lyase
Triticum
MACAWRSRSRADPLNWGKAAEELSGSHLEAVKRMVEEYRKPVVTMEGATTIAMVAAVAAGSDTRVELDESARGRVKESSDWVMNSMMNGTDSYGVTTGFGATSHRRTKEGGALQRELIRFLNAGAFGTGTDGHVLPAAATRAAMLVRVNTLLQGYSGIRFEILETIATLLNANVTPCLPLRGTITASGDLVPLSYIAGLVTGRPNSMATAPDGSKVNAAEAFKIAGIQHGFFELQPKEGLAMVNGTAVGSGLASMVLFEANVLSLLAEVLSGVFCEVMNGKPEFTDHLTHKLKHHPGQIEAAAIMEHILEGSSYMMLAKKLGELDPLMKPKQDRYALRTSPQWLGPQIEVIRAATKSIEREINSVNDNPLIDVSRGKAIHGGNFQGTPIGVSMDNTRLAIAAIGKLMFAQFSELVNDFYNNGLPSNLSGGRNPSLDYGFKGAEIAMASYCSELQFLGNPVTNHVQSAEQHNQDVNSLGLISSRKTAEAIDILKLMSSTFLVALCQAIDLRHLEENVKNAVKSCVKTVARKTLSTDNNGHLHNARFCEKDLLLTIDREAVFAYADDPCSANYPLMQKMRAVLVEHALANGEAEAHVETSVFAKLAMFEQELRAVLPKEVEAARSAVENGTAAQQNRIAECRSYPLYRFVRKELGTEYLTGEKTRSPGEEVDKVFVAMNQGKHIDALLECLKEWNGEPLPLC
This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
Q43210
Q8XL95
CITD_CLOPE
Citrate lyase gamma chain
Clostridium
MEIKKPALAGTLESSDCIVSVEPSMDNTIEINLTSTVKKQFGNEIIKVAKETLKNLGVNSVVMEINDKGALNCVIEARIEAAVCRASEINEFDWGNYKCQD
Covalent carrier of the coenzyme of citrate lyase.
Q8XL95
P77212
RCLA_ECOLI
Reactive chlorine resistance protein A
Escherichia
MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQRKNEVVNFLRNKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEIHGEKIFINTGAQTVVPPIPGITTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKRLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRMLGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSLVK
Probably involved in reactive chlorine species (RCS) stress resistance.
P77212
Q5HMC7
TENA_STAEQ
Thiaminase II
Staphylococcus
MTFSKELREASRPIIDDIYNDGFIQDLLAGKLSNQAVRQYLRADASYLKEFTNIYAMLIPKMSSMEDVKFLVEQIEFMLEGEVEAHEVLADFINEPYEEIVKEKVWPPSGDHYIKHMYFNAFARENAAFTIAAMAPCPYVYAVIGKRAMEDPKLNKESVTSKWFQFYSTEMDELVDVFDQLMDRLTKHCSETEKKEIKENFLQSTIHERHFFNMAYINEKWEYGGNNNE
Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP). Is also able to catalyze the hydrolytic cleavage of thiamine; however, this thiaminase activity may not be physiologically relevant. Therefore, is probably involved in the regeneration of the thiamine pyrimidine from thiamine degraded products present in the environment, rather than in thiamine degradation.
Q5HMC7
A1US38
RECO_BARBK
Recombination protein O
Bartonella
MKWKEQAIILGARQYGETSVILEVVTRQHGRYMGVVKGGRSRRMAALLQPGNFVEAEWWARLDEHLGLFKLEALDLCASRLMFLPEALYGLQLMASHFRLLPERDPHPILYDILHLFMQNFDEQFVNAELLVRFEMRLLEELGFGLDLSHCAVTGRQEKLYYVSPKSGRAVCEEVGLPWKNKLLLLPKFLIERTNRPVDFDDIRNGFTLTDFFLTRHVWEPRGIKQPSVRAILIQLFERRFHTKA
Involved in DNA repair and RecF pathway recombination.
A1US38
Q85X67
ATPA_PINKO
F-ATPase subunit alpha
Pinus subgen. Strobus
MGNLQIDEISSIIRKQIKQYNDAVGVGNLGTVLQVGDGIARIHGLYEVMAGELVEFGDGTVGIALNLGSDNVGVVLMGDGLMIQEGSSVRATGKIAQIPVSDAYLGRVVNALAQPIDGKGQISASEFRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKSQNVICVYVAIGQRASSVAQVVNTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYKKQHTSIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSLTALPIVETQAGDVSAYIPTNAISITDGQIFLSADLFNAGIRPAINVGLSVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKATQDQLARGQRLRELLKQSQSAPLKVEEQIATIYTGTNGYLDILEIAQVRNFLVRLREYLIKNKPQFGEIICSTGTFTEEAKALLEEAL
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Q85X67
P21647
MRKC_KLEPN
Outer membrane usher protein MrkC
Klebsiella
MKQRSICPGRLSTAIAVALCCFPPFSSGQESPGTIYQFNDGFIVGSREKVDPSRFSTSAISEGVYSLDVYTNGEWKGRYDLKITAGKDGKMGVCYTKAMLMQYGISPEKLNPQLSEKEGFCGRLQEWRHEDNVKDTLIQSSLRLDIAVPQIYEDQRLKNFVSPQFWDKGVAALNLGWMANAWNSHISSANGSDNSSAYLGVNAGLSWDGWLLKHIGNLNWQQQQGKAHWNSNQTYLQRPIPQINSIVSGGQIFTNGEFFDTIGLRGVNLATDDNMFPDGMRSYAPEIRDVAQSNALATVRQGSNIIYQTTVPPGPFTLQDVYPSGYGSDLEVSVKEGDGSVEVFSVPYASVAQLLRPGMTRYALSAGKVDDSSLRNKPMLYQGTWQHGLNNLFTGYTGVTGFDDYQAFLLGTGMNTGIGALSFDVTHTRLKSDTLDEHGQSYRATFNRMFTETQTSIVLAAYRYSTKGYYNLNDALYAVDQEKNYNSNYTVWRQKNGMTFTVNQNLPDGWGGFYLCGRVADYWNRSGTEKQYQFSYNNMYGRLSWSVDAQRVYTPDSSGHRRDDRVSLNFSYPLWFGENRTANLTSNTAFNNSRFASSQIGVNGSLDSENNLNYGVSTTTATGRQHDVALNGSYRTPWTTLNGSYSQGEGYRQSGVGASGTLIAHQHGVVFSPETGPTMALIEAKDAAGVMLPGSPGTRIDSNGYAILPYLRPYRINSVEIDPKGSNDDVAFGSTVAQVVPWEGSVVKVSFDTTLQNNITLRARQANGLPLPFAATIFGPSGKEIGVVGQGSMMFISDASAPKATVKWSGGQCSVELSQEKTKETLCR
Involved in the export and assembly of the type 3 fimbrial subunit (MrkA).
P21647
B2FNJ0
SMF1_STRMK
S. maltophilia fimbriae 1
Stenotrophomonas maltophilia group
MLAAAPLAANAADGTITFNGKVTDKTCTISTPGGKDFAVNLPTVSKNTLATAGAVAGRTPFAINLTKCSAGNVATYFEPGSTVDFNTGRLLNQASANAATNVQLQLLGSNNQVLPIKAAGAGLAQTNSQWVTVGTDGSADLNYYAEYYATAAATPGDVTSSVKYTIIYN
Involved in adherence to eukaryotic epithelial cells and abiotic surfaces. Mediates agglutination of animal red blood cells.
B2FNJ0
Q2LK95
COL10_CHICK
Collectin-1
Gallus
MSRKKEQQLRKYGTLVVLFIFQVQIFGFDVDNRPTTDVCSTHTILPGPKGDDGEKGDRGEVGKQGKVGPKGPKGNKGTVGDVGDQGMLGKIGPIGGKGDKGAKGISGVSGKKGKAGTVCDCGRYRRVVGQLNINVARLNTSIKFVKNVIAGIRETDEKFYYIVKEEKNYREALMHCRDRGGTLAMPKDEVTNALLADYISSSGLFRAFIGLNDMEKEGQFVYADSSPLQNYSNWKDGEPHDSTGHEDCVEMLSTGEWNDSECQVTIYFICEFLKKRK
Lectin that binds to various sugars: galactose > mannose = fucose > N-acetylglucosamine > N-acetylgalactosamine. Acts as a chemoattractant, probably involved in the regulation of cell migration.
Q2LK95
Q09FQ1
RR7_NANDO
30S ribosomal protein S7, chloroplastic
Nandina
MSRRGTAEEKTAKSDPIYRNRLVNMLVNRILKHGKKSLAYQIIYRALKKIQQKTETNPLCVLRQAIRGVTPDIAVKARRVGGSTHQVPIEIGSTQGKALAIRWLLGASRKRPGRNMAFKLSSELVDAAKGSGDAIRKKEETHRMAEANRAFAHFR
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
Q09FQ1
A0A5F8MPU3
CTSRT_MOUSE
C2 calcium-dependent domain-containing 6
Mus
MELPPPGNRRVSINNPQETSGRVPTTSAGFPTQSSKISLKRSTYAYRPSMMSNRSSGGQSLLPSSILQKTSLNPPGSLQSKPSNLSSVHYADEEGKPLTDKNKDKDKGRGKGKGTGTRLLTMLRKTLQGSQSDEMAIANQTPNLIPFGDVVGCLAIHIKSCRQFSQRFLGQQRFNLFMRVSINNIVKCTKIRHLKAVNNEKNLVLRFGEMKYFSVQVPRRQDDERNFIYLELMHDGGDPESPPIPLGGAESHLYEVIQKGCFTEVMHLMHKNSSICRVEVEFMFSYGNFGYGFSHQLKPLQKAIEPSMFMNIAPPPERTDPVTNVITPQRVEYPAFLSPEFNVSIGVPEASHATVVQLEKLREKPRERLERMKEEYKNMSTWIEKADYLRNLINPKMTKRDNKGSSIPSESNSSALEELERTTYDIHHRKYEAISNEYGDKEGRVIPVLKVLDQNYSEVFLPKSSDSTPLEDVLLPPIHSLQIVEENEMPHLPKTSEPEDRPHEERKSIVFSSDEELMPKHPSILKISSSQQENRRKMEKSPHFSDVLIIPDKPFEDLNTNKKGRPPIELRKSWERHPTDVACSLRKVAFAQKDYTIPVCKAETTEFKPKHQFQKLSKSGLDPFLRNINSKMSFRKKKDHDDGYRNLSTSSAEILEHEDQDPPYPGHSGSAGSDATWAENPSPVTVQMVNRDSLPPDLITATIVISDRKNKLSLDSVFNSANSLNTKSIFASDNPVVSLTKLSDSDNKLITDSSFNTTKPSNRRLSKDSNFNTTKPSDRKLSSDPSSNTTKPSDTKLFSDPSSNKLSQGPSSNASQLSGSNRLSHNPSINGNKSSYTSDLNKVSRDPSIVSTISSDPNKLSRDPSFVLAKSSDPNKLSHYPSIISAKSSDPNKLSHDPSFVSARSSDPNKLSHDPSIISARSSDPIKLSRDPSFVSARSSDPNKLSHDPSIISARSSDPNKLSRDPSINSTKLSDPSKLSRDPSIFSTKSSDPNKLYRVPSIISGMSSNPKLSRDPSIISGMSSDPKLSRDPSIISAKSSDPNKLSHDPSIISGMSSNPNKLSHDPSIISMKLSDMSKLSRESSINASKSSDTNQLSYDPNIISAKSLDSNNSSASSSPTVNSDTTTNAAEPSGTKNMLDPVVSTIDSSDKQSKLEWLPNVQGASSVTENINTHRSSNSVNFTSDIDILKQSIVLKSILSKNLQDLSDELFSKSELYTNDEGYSPPPSVHSRPSDSTDDRVLGKVQDLNSWRSSKDLLNSQVLLSPVVKNSPQDLLPEGEPGKSSDIEDYVSEKLLEAAGRNFPMNRKSSFKKKHLVSEESSSEHVLSGSIYEYVIKQIFTAPIFSQLGIGIKSSSEARMDSQNQLLTPWERSVTSHIINYEEKDSDVNLSQSKSIISQIIQSFPVNTLLESGVIKVIELDKEHQNSLLDSQTTSSTEQYSDSRSQIKLLSRQNTSSINPLDSSVSGAEYTEDCQSISTQESKYPVRDTKSDSPNDTEEMELDSNLESSSSSLDKVKDTDTAKLKNILKNIFSIFFKYNQSERRQQPEKDSESLIKHSSSSGSEHLEKTQENFNKADKKVDRKPILNPKLRMFLEKLSETEVKNLKSELSKHIQHYLVERLTESGHITKEDLPTIYHKLYLMNEKVELKEQTPFQEKYSETVKEIMSFVNNFNHHFIDKHLETKLRGFLSEILQNYFLKNLSVSNLFNETDAMALHASMSPVRSKSELGQDIADGNFGSSLKINMQYPVTKSLQHYLQDLSENELLSLKTDLSKYLQVLFIEKLYKSGLVSERQLKGISQEIISLHSPSIPLKHIKTNLPFRNESYFMREDSEEQMKYLKNGQNAALHVLLKDKCGETELSRKKERESSFSQILKENLPAIWEQKNIYTREEETLNLIQMQSFLNKNNQANPLTRSPERPSDISLKKQKKDHGFMQFTQVEGSVYKTEIQDPYSWDSRSKTIQSKPCLEKTLKMKLLDKRENNNFYKLTAQEKLDTEFSSYLKLPNCKIPKEKEPISRLSFPTWKTNTFIHVKPEIGEQSKLDHYYQRLKGNNNNNKKHLVTFAQFKNEMETLYRNPYEACNEKRAKISESQSFKYKEKEKSSRPFFFPEVLKRENTKSKRKERDHATKPKKSFHKIVRLLPATLPTTRPHLRKSAPRNLLHWTARRTIHDCLDRFDDLHAPTVKCPKKSKSGARLLGKSPEDSHNQAKHCARPYTAPEPNKRRESAAWKFASPRMVSAGLLHLYVTPAYGIRKVRSKRKLKEDIEKRPLISEIIQMLDNAE
Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CatSper complex targeting and trafficking into the quadrilinear nanodomains. Targets the preassembled CatSper complexes to elongating flagella, where it links the channel-carrying vesicles and motor proteins.
A0A5F8MPU3
Q3IH67
UREE_PSET1
Urease accessory protein UreE
Pseudoalteromonas
MFELTKRIDSNTQDAVFDTLTLPYELRIRGRLKAVTDNGHDVGLFLDRGPVLRNGDLLRASSGEVFSISAADEPVTTAYIENGLPLARLCYHLGNRHVSLAIGVDADGRHWIRFPPDHVLEELAILLGAQLTHHQAPFDPESGAYAHAGREQSHAHSHEHSHADGHTHAH
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
Q3IH67
Q20057
ERH2_CAEEL
Enhancer of rudimentary homolog 2
Caenorhabditis
MSTSSHTVLLIQTSPRLDSRTWGDYESVTDALDALCKMFEDFLSKKSAAPVTYDVSQVYEFLDKLSDVSMMIFNRETGQYIGRTRAWIKQQVYEMMRGRCQHPEGGEKVIVGY
Required for chromosome segregation and cell division in early embryos . Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively . Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing . Promotes the biogenesis of 21U-RNAs .
Q20057
Q8EX18
EFTU_MALP2
Elongation factor Tu
Malacoplasma
MAKQKFDRSKAHVNIGTIGHIDHGKTTLTAAICTYLAKKGGAKAMKYDEIDKAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAASDGPMPQTREHILLARQVGVPKMVVFLNKCDMVSDAEMQDLVEMEVRELLSSYGFDGDNTPVIRGSALKALEGDATWEAKIDELMASVDSYIPTPTRDTDKPFLLAVEDVMTITGRGTVVTGRVERGTLKLNDEVEIVGIHDTRKAVVTGMEMLRKTLDEVKAGDNAGILLRGIDRKDVERGQVLAKPGSIKPHKQFEAEIYALKKEEGGRHTPVLNGYRPQFYFRTTDVTGQITLDKGVEMINPGDNTKITVELISPIAVEEGSKFSIREGGRTVGAGTVTKVIK
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Q8EX18
Q9ZCL0
LPXK_RICPR
Lipid A 4'-kinase
typhus group
MIKLLYPQFWQERNIIAYLLLPISLIYQFLSYLRASLAYPVILPAQVICVGNCSVGGTGKTQIVIYLAKLLKAKNVPFVIITKAYGSHIKSTTIIQKGHTALEVGDEGIMLARYGTVIAAKYVKDILPLINELKPDVIIVDDFLQNPYLHKDFTIVSVDSQRLFGNRFLIPAGPLRQNPKQVLDAADLIFLVSSNQDQIPNELTPYIDKLINAQIVPSNNIDKNKNYFAFSGIGNPQRFFLTLENYRLNIVGYKIFPDHYNYLQADLENLYSLAKEHNAILITTRKDYVKFNYLNDEIICLDVELSINNPDLLNEKIFKKAKILN
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Q9ZCL0
P29489
TCPH_VIBCH
TCP pilus biosynthesis protein TcpH
Vibrio
MHKKLKAWGGATGLFVVALGVTIIALPMRQKNSHGTMIIDGTVTQIFSTYQGNLSNVWLTQTDPQGNVVKSWTTRYQTLPDPSSQKLNLIPDYSQSNASRDYNVLSIYQLGKGCFLAFPYKLLTAEKMLVFLSKRFLGSYHEPPR
Involved in TCP pilus biogenesis.
P29489
Q830Q7
RL10_ENTFA
50S ribosomal protein L10
Enterococcus
MSEAAIAKKETLVQAAAEKFESAASVVIVDYRGLTVEEVTNLRKQLRDAGVEMKVIKNSILSRAAKKVGLDGLDEVFTGPTAVAFSNDDVVAPAKIIDEFAKDAKALEIKGGVIEGKVSSVEQITALAKLPNREGLLSMLLSVLQAPVRNVAYAVKAVAEKNEEVA
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Q830Q7
Q4FNT5
HIS5_PELUB
ImGP synthase subunit HisH
Candidatus Pelagibacter
MNVTIVDYNSGNISSVINSFKEVAKDKVNIEVTSDLNKIRSSDKVVLPGQGSFKSCVDALNAINGLVETLNEFTVTNKKPLLGICVGLQMFADLGYEETETKGLGWISGKVSKIDNQNNKFKLPHIGWNEINIVKESKIFEGIKNKSHMYFVHSYEFIPDDKSVISATTDYSSNIVCSVEKENIFGTQFHPEKSDKLGLKIIENFLNL
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Q4FNT5
C4K2A3
DAPF_RICPU
PLP-independent amino acid racemase
spotted fever group
MISKINFVKMHGLGNDFVIVNKRDLSSSYDLSQLAKNMAERHTGIGCDQFIIYEEHNDFYEMIIYNIDGSSAKLCGNATRCLAKLIYLDTGKQDITVMVGNKKLLCNVNDENNISVNVGSVSFNEAWMPSRDKVWEFAERYMIDLKETICVDIGNPHVVIFSKLEPQDQKIVGERLQAKELFADGVNVNFAEVKDNKIYLSVWERGAGLTLACGSGACGSFAAGLKRGFIHSPSTIVFKHGNLTMKEENGNIIMQGAATLVARGEYYCEQ
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
C4K2A3
A9BIS5
EFTS_PETMO
Elongation factor Ts
Petrotoga
MDVSIEKIKNLRASTGAGMLDCKNALEEADGDIDKAVEILRKKGAIKAAKKAGRVTNEGIVYSYIHHNEKIGVLLLLGCETDFVARTEDFHDLAKKISLQIASMNPKWISREDVPQEIIDKEKEIYLEELKNSNKPENIKEQIVENKLGKFYSENCLLEQEYVFGEGESIKDIIDSMIAKVGENITVDKFARFAIGE
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.
A9BIS5
P12405
ATPA_NOSS1
F-ATPase subunit alpha
Nostoc
MSISIRPDEISSIIQQQIEQYDQEVKVANVGTVLQVGDGIARIYGLEKAMAGELLEFEDGTVGIAQNLEEDNVGAVLMGEGREIQEGSTVTATGRIAQIGVGEALIGRVVDALGRAIDGKGDIKASESRLIESPAPGIIARRSVHEPMQTGITAIDSMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGEDVVCVYVAIGQKASTVANVVQTLQEKGAMDYTVVVAAGASEPATLQFLAPYTGATIAEYFMYKGKATLVIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYIHSRLLERAAKLSDELGKGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSSDLFNAGIRPAVNPGISVSRVGSAAQTKAMKKVAGKIKLELAQFDDLQAFAQFASDLDKATQDQLARGQRLRELLKQSQNQPLSVAEQVAILYAGINGYLDDIPVDKVTTFTKGLRDYLKSGVNPYFQDVQSKKALGDDEEKALKAALEDYKKTFKATA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
P12405
Q8YBP0
Y3859_BRUME
Putative ABC transporter peptide-binding protein BMEII0859
Brucella
MRLRNFYSALALSAAVFAGPLYAAAPAMAAGTISGGFDVGPGGFQGNFNPLAATGGFTWLVTYFEPLVIYDDKLENIVGDLAKSFEISPDQLTYTFKLAHAKWHDGEPFTSKDAKFTFDLARNGKTGSVFAARLASIASVETPDEKTVVIKLKEPSPSMLDTLTKVMMLPEHALASIPPEQLAKNAWWSSTPIGTGPFKFNKYVADQYVELTANPDYRGGRPQVDKLINRYFADPAAAIAALRSGEIQFTYVDSNDVSTFSSDSAFRVIEGDSFVVNYVGFNQEVPLWKDLKVRQAFMHAINRDAIIQSLYGGAAKPANCVYVADRLVPKAIDAYAYDPQKARQLLDEAGWDKINGSKPITILTYYNSPLVANVLAAMQAMLAQVGINIVPRTVDTPTYNSIVYKQGGTADEFPLIFAGLQNGPDPSSINIGLNEKQIPPAGSNIMRIRMPAVTKALDAALAETNPAKRDARYQDVCKATNANLPWGTMWVANRYGVASSKLENFIWTPAPAGGPYQAHPEKWSILE
Probably part of an ABC transporter complex that could be involved in peptide import.
Q8YBP0
Q93ZG3
ACSA1_ARATH
Cockayne syndrome WD repeat protein CSA homolog
Arabidopsis
MWEAIKDRETGRIRSNSFANRFKSRRILSLQLSNRKDFVSPHRGSVNSLQVDLTEGRYLLSGAADGSAAVFDVQRATDYEASGLIAKHKCIFTVDKQHENGHKYAISSAIWYPIDTGLFITGSFDHYLKVWDTNTAQAVVDFKMPGKVYRTAMSSMAMSHTLIAAGTEDVQVRLCDIASGAFSHTLSGHRDGVMSVEWSTSSEWVLYTGGCDGAIRFWDIRRAGCFRVLDQSQTQLGFRPPILKRTAVGSKLSSVAKSSLGGQNRLKTLQSKQTGSQSVKGSSSAKASVEKSRQKRIHPGMLSTLDRATAHYGAVTGLKATNDGMYLLSAGSDSRIRLWDIESGRNTLVNFETGRIQTNKGIQLDTSDDPALVFVPCMKTVKAFGMWSGRTTLMLRGHYESVNTCCFNSNDQELYTSGSDRQILVWSPGGTVEDEMVQDEVAEDKDNWSD
Involved in UV-B tolerance and genome integrity. In association with DDB2, is necessary for repair of UV-B-induced DNA lesions.
Q93ZG3
Q1ASA8
MURB_RUBXD
UDP-N-acetylmuramate dehydrogenase
Rubrobacter
MHDGTLQRLFPAAKFDEPLRRYTAWKIGGPADALLEPSSIQELLSAVELAGEHGVPVTVLGGGTNVLVRDGGIRGLTIRLAKSLRGVKLSGETLVAEAGALYPVLANMTASRGLAGLEFATGIPGTVGGAVFMNAGAYGSETARVLLWADILRDGRVVRMGPEELGLSYRRSILHDHPGWVVLRAAYRLHPGDPEDLRERIREFRTLRMNGSPNRPSCGSTFKRPPGDFPGRVIEAAGLKGLRVGQIEVSTVHANYFVNLGGGTASDALRLMELVRERVRERLGVELEPEVRVVGEP
Cell wall formation.
Q1ASA8