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
|
|---|---|---|---|---|---|---|
A9WFP8
|
RL10_CHLAA
|
50S ribosomal protein L10
|
Chloroflexus
|
MPTPRKIETVSTLTEKLNRAQLVVVADYRGDGKGMSVADMTELRRKLREHGGEVVVAKNTLLKIAAHNTGHEALDPLLAGPTAVTLGYDDVSKVAKALLDYLKSGNKSFTVRGALLGNTLLPADALEQVTKLPSREQALAQVVGGIAAPVSGVVGVLNAAISNVLYVLQARIDQLQPQGETA
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
A9WFP8
|
P63154
|
CRNL1_MOUSE
|
Crooked neck homolog
|
Mus
|
MAASTAAGKQRIPKVAKVKNKAPAEVQITAEQLLREAKERELELLPPPPQQKITDEEELNDYKLRKRKTFEDNIRKNRTVISNWIKYAQWEESLKEIQRARSIYERALDVDYRNITLWLKYAEMEMKNRQVNHARNIWDRAITTLPRVNQFWYKYTYMEEMLGNVAGARQVFERWMEWQPEEQAWHSYINFELRYKEVERARTIYERFVLVHPAVKNWIKYARFEEKHAYFAHARKVYERAVEFFGDEHMDEHLYVAFAKFEENQKEFERVRVIYKYALDRISKQEAQELFKNYTIFEKKFGDRRGIEDIIVSKRRFQYEEEVKANPHNYDAWFDYLRLVESDAEADTVREVYERAIANVPPIQEKRHWKRYIYLWVNYALYEELEAKDPERTRQVYQASLELIPHKKFTFAKMWLYYAQFEIRQKNLPFARRALGTSIGKCPKNKLFKGYIELELQLREFDRCRKLYEKFLEFGPENCTSWIKFAELETILGDIERARAIYELAISQPRLDMPEVLWKSYIDFEIEQEETERTRNLYRQLLQRTQHVKVWISFAQFELSSGKEGSVAKCRQIYEEANKTMRNCEEKEERLMLLESWRSFEDEFGTVSDKERVDKLMPEKVKKRRKVQADDGSDAGWEEYYDYIFPEDAANQPNLKLLAMAKLWKKQQQEREAAEQDPDKDIDESESSSF
|
Involved in pre-mRNA splicing process.
|
P63154
|
Q55988
|
PFKA2_SYNY3
|
Phosphohexokinase 2
|
unclassified Synechocystis
|
MGTKRIGILTSGGDCPGLNAVIRAVVKASALKGWEVYGIPYGTDGFVEVAHGKYQAEDLLLTKHGYALPGMLKGLDVLQFLSGSVLGSLSKGHPEQPAIAEAILKGYAILDLEALIVIGGDGSLDIIYDLAQKGNWHIIAIPKTIDNDVPFTDLAVGFSTAVDIVTQALYDLTFTAASHERIIIVQVMGRDAGHLTLHAGIAGGADIILIPEITPCLTSEIIRNCCYQLMNLRKSGRHFALIVISEGVHDQNNKKNKHIADYLAEEISETSQHLCDIKDPAFCDLISLDIRATTLGHLQRSGTPLSFDRLLATVFGIRAVELIEQEIYDQVVIWRSGKVEHADLKPIISIIKECHQENRCPFPVDRDGFMVKTAKSLGIYLGED
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
Q55988
|
Q0I748
|
EX7L_SYNS3
|
Exodeoxyribonuclease VII large subunit
|
unclassified Synechococcus
|
MSAESLPSYSVRELNNAIGVLLERGFAPRFVIQATVSRPQVKKGHLWLTLSDGEASITAVAWASKLKQLDFVPADGDGVTVIGKLNFWSARASLAVQVLDMRPSLTTVLRRFETVKAQLLEEGVIDPSRHRKLPAYPNRLAVLTSVPSSALADMLRTAQDRWPLSELLVVPIPVQGEVAPIICGVLNRLAETHHQLGLDAIVIARGGGSREDLMVFDDAEVCRKLATFPLPVVTGLGHEDDLTVADLVADHRAATPTAAMVTLMPSRESAQQTITQRRSRLSEYKRWRLEQANSRLRDRHLLLDALRPEVTLQRRRDQWQQRQQLLRALSPQRWLNRGFAMLNTTNGQPIQSINDISLNEQLQILLKDGVIQAVAKTIQANETSNSKTSP
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
|
Q0I748
|
O75037
|
KI21B_HUMAN
|
Kinesin-like protein KIF21B
|
Homo
|
MAGQGDCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDSTRDPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVNEAVTGLPDGTPPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVVVNQDKTSQQISALRAEIARLQMELMEYKAGKRVIGEDGAEGYSDLFRENAMLQKENGALRLRVKAMQEAIDAINNRVTQLMSQEANLLLAKAGDGNEAIGALIQNYIREIEELRTKLLESEAMNESLRRSLSRASARSPYSLGASPAAPAFGGSPASSMEDASEVIRRAKQDLERLKKKEVRQRRKSPEKEAFKKRAKLQQENSEETDENEAEEEEEERDESGCEEEEGREDEDEDSGSEESLVDSDSDPEEKEVNFQADLADLTCEIEIKQKLIDELENSQRRLQTLKHQYEEKLILLQNKIRDTQLERDRVLQNLSTMECYTEEKANKIKADYEKRLREMNRDLQKLQAAQKEHARLLKNQSRYERELKKLQAEVAEMKKAKVALMKQMREEQQRRRLVETKRNREIAQLKKEQRRQEFQIRALESQKRQQEMVLRRKTQEVSALRRLAKPMSERVAGRAGLKPPMLDSGAEVSASTTSSEAESGARSVSSIVRQWNRKINHFLGDHPAPTVNGTRPARKKFQKKGASQSFSKAARLKWQSLERRIIDIVMQRMTIVNLEADMERLIKKREELFLLQEALRRKRERLQAESPEEEKGLQELAEEIEVLAANIDYINDGITDCQATIVQLEETKEELDSTDTSVVISSCSLAEARLLLDNFLKASIDKGLQVAQKEAQIRLLEGRLRQTDMAGSSQNHLLLDALREKAEAHPELQALIYNVQQENGYASTDEEISEFSEGSFSQSFTMKGSTSHDDFKFKSEPKLSAQMKAVSAECLGPPLDISTKNITKSLASLVEIKEDGVGFSVRDPYYRDRVSRTVSLPTRGSTFPRQSRATETSPLTRRKSYDRGQPIRSTDVGFTPPSSPPTRPRNDRNVFSRLTSNQSQGSALDKSDDSDSSLSEVLRGIISPVGGAKGARTAPLQCVSMAEGHTKPILCLDATDELLFTGSKDRSCKMWNLVTGQEIAALKGHPNNVVSIKYCSHSGLVFSVSTSYIKVWDIRDSAKCIRTLTSSGQVISGDACAATSTRAITSAQGEHQINQIALSPSGTMLYAASGNAVRIWELSRFQPVGKLTGHIGPVMCLTVTQTASQHDLVVTGSKDHYVKMFELGECVTGTIGPTHNFEPPHYDGIECLAIQGDILFSGSRDNGIKKWDLDQQELIQQIPNAHKDWVCALAFIPGRPMLLSACRAGVIKVWNVDNFTPIGEIKGHDSPINAICTNAKHIFTASSDCRVKLWNYVPGLTPCLPRRVLAIKGRATTLP
|
Plus-end directed microtubule-dependent motor protein which displays processive activity. Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation. Plays a role in lerning and memory. Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to cell surface.
|
O75037
|
Q6CZT4
|
PLY1_PECAS
|
Pectate lyase I
|
Pectobacterium
|
MKYLLPSAAAGLLLLAAQPTMAANTGGYATTDGGDVSGAVKKTARSLQEIVDIIEAAKKDSSGKVVKGGAFPLVITYNGNEDALIKAAEANICGQWSKDPRGVEIKEFTKGITILGTNGSSANFGIWVVNSSNVVVRNMRFGYMPGGAKDGDAIRIDNSPNVWIDHNEIFAKNFECAGTPDNDTTFESAVDIKKASTNVTVSYNFIHGVKKVGLSGSSNTDTGRNLTYHHNIYSDVNSRLPLQRGGQVHAYNNLYDGIKSSGFNVRQKGIALIESNWFENALNPVTARNDDSNFGTWELRNNNITSPSDFAKYKITWGKPSTPHINADDWKSTGKFPAVSYSYSPVSAQCVKDKLANYAGVGKNQAVLTAANCK
|
Involved in maceration and soft-rotting of plant tissue.
|
Q6CZT4
|
Q8Z0U3
|
DEOC_SALTI
|
Phosphodeoxyriboaldolase
|
Salmonella
|
MTDLKASSLRALKLMDLTTLNDDDTNEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTLKEQGTPDIRIATVTNFPHGNDDIDIALAETRAAIAYGADEVDVVFPYRALIAGNEQVGFDLVKACKDACAAANVLLKVIIETGELKEEALIRKASEISIKAGADFIKTSTGKVPVNATPESARIMMEVIRDMGVSKTVGFKPAGGVRTAEDAQKFLAIADELFGANWADSRHYRFGASSLLASLLKALGHGDGKSASSY
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
Q8Z0U3
|
A3CLQ8
|
EX7S_STRSV
|
Exodeoxyribonuclease VII small subunit
|
Streptococcus
|
MSKEKKFEENLADLEVIVQKLENGDVALEEAIAEFQKGMKLSKELQASLDKAEKTLVKVMQADGTETEME
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
|
A3CLQ8
|
Q9TTU2
|
KAD6_RABIT
|
Dual activity adenylate kinase/ATPase
|
Oryctolagus
|
MRLPNILLTGTPGVGKTTLGKELASRSGLKYVNVGDLAREGELYDGFDEEYNCPILDEDRVIDELDTQMRDGGVIVDYHGCDFFPERWFHIVFVLRTETSVLYKRLETRGYSEKKLNDNIQCEIFQVLYEEAMESYKEEIVHQLPSNKPEELEENISQILKWIEQWIKDHNS
|
Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. May have a role in nuclear energy homeostasis. Has also ATPase activity. May be involved in regulation of Cajal body (CB) formation.
|
Q9TTU2
|
Q3MHH4
|
SYQ_BOVIN
|
Glutaminyl-tRNA synthetase
|
Bos
|
MAALDSLSLFTGLGLSEQKARETLKNTVLSAQLREAATQAQQTLGSSIDKATGTLLYGLASRLRDPRRLSFLVSYITSRKIHTETQLSAALEYVRSHPLDPINTEDFEQECGVGVVVTPEQIEEAVEAAINRHRAKLLVERYHFSMGLLMGEARAALKWADGKMIKHEVDMQVLHLLGPKTETDLEKKPKVAKARPEETDQRTAKDVVENGEVVVQTLSLMEQLRGEALKFHKPGENYKTPGYVTTPHTMDLLKQHLDITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAIYDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRDQAYVCHQRGEELKGHNPLPSPWRDRPIEESLLLFEAMRKGKFAEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDTWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVAAGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLEPLQVVITNFPATKALDIQVPNFPADETKGFHQVPFGSTVFIERMDFKEEPEPGYKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLKVTCRRADAGEKPKAFIHWVSQPLTCEIRLYERLFQHKNPEDPAEVPGGFLSDLNPASLQVVEAALVDCSVALAKPFDKFQFERLGYFSVDPDSNQGQLVFNRTVTLKEDPGKV
|
Glutamine--tRNA ligase. Plays a critical role in brain development.
|
Q3MHH4
|
A0A0G2Q9D6
|
GYRB_MYCBP
|
DNA gyrase subunit B
|
Mycobacterium tuberculosis complex
|
MGKNEARRSALAPDHGTVVCDPLRRLNRMHATPEESIRIVAAQKKKAQDEYGAASITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATTVNVVLLEDGGVEVADDGRGIPVATHASGIPTVDVVMTQLHAGGKFDSDAYAISGGLHGVGVSVVNALSTRLEVEIKRDGYEWSQVYEKSEPLGLKQGAPTKKTGSTVRFWADPAVFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTQDEVVDEVVSDVAEAPKSASERAAESTAPHKVKSRTFHYPGGLVDFVKHINRTKNAIHSSIVDFSGKGTGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDRKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQKVCNEQLTHWFEANPTDSKVVVNKAVSSAQARIAARKARELVRRKSATDIGGLPGKLADCRSTDPRKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDIGKLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIENGHVFLAQPPLYKLKWQRSDPEFAYSDRERDGLLEAGLKAGKKINKEDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV
|
A type II topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Relaxes negatively supercoiled DNA in an ATP-independent manner. A linear reaction intermediate can be trapped in the presence of the antibiotic ciprofloxacin . Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
|
A0A0G2Q9D6
|
A7HZL1
|
RL22_CAMHC
|
50S ribosomal protein L22
|
Campylobacter
|
MSKSTIKFVRLSPTKTRLIAKEIQGMNAEFALATLEFTPNRGAKYIANAILSAVANGGFEPNEVIVKSCRVDAGPVLKRFRPRARGTASRIRKPTSHIMVEVSKPSKEA
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
A7HZL1
|
A6LJT9
|
ISPE_THEM4
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Thermosipho
|
MEQSSGAVIRSYAKINLFLDVTKKRDDGYHEILSLFQNISLYDRLIITKIDRGLEIKTNVDIENNILYKTWDVFSSNFKEPEFGLRIVLEKNIPMQAGLGGGSSNAAALLFYLSDQLKIPKNKIIKIAAKIGSDVPFFLIGGTAVVKGKGEIIEPLPPLLGYYVKLITANGISTKEAYNLLNSTLFNKAPCSPYALYEAYYHRNIDEIKRCTYNIFEKVIAKQNREIAQNIKKLKKNSIVSTLTGSGSAVYGISFREGDFNFVPRGVEYEEINI
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
A6LJT9
|
Q99MS4
|
PRS29_MOUSE
|
Tryptase-like proteinase
|
Mus
|
MLIQLCLTLFFLGCSIAGTPAPGPEDVLMGIVGGHSAPQGKWPWQVSLRIYRYYWAFWVHNCGGSIIHPQWVLTAAHCIRERDADPSVFRIRVGEAYLYGGKELLSVSRVIIHPDFVHAGLGSDVALLQLAVSVQSFPNVKPVKLPSESLEVTKKDVCWVTGWGAVSTHRSLPPPYRLQQVQVKIIDNSLCEEMYHNATRHRNRGQKLILKDMLCAGNQGQDSCYGDSGGPLVCNVTGSWTLVGVVSWGYGCALRDFPGVYARVQSFLPWITQQMQRFS
|
Involved in embryo hatching and implantation.
|
Q99MS4
|
Q05526
|
PLYW_DICD3
|
Exopolygalacturonate lyase
|
Dickeya
|
MSIFTDLNTSRKWQIDQWLSAVNSHIEKIQQYGHSVVNPTPLLADGFEIKTQSPVVWQFPDGHDAPISNFASQQNWLRLLISMSVITETEKYRHLAFCQSEYFLNRFVDENSGLFYWGGHRFINLDTLASEGPESKSMVHELKHHLPYYEFLHQVNPEKTRHFIQGFWNAHVEDWSCLDLGRHGDYARQRDPDVFLHSRHDVVTPANWPELPLTKGLTFVNAGTDLIYAAFVYARHTGDAHAAAWGKHLYRQYVLARNPETGMPVYQFSSPLQRQPVPADDNQTQSWFGDRAQRQFGPEFGAIAREANVLFRDMRPLLIDNPLAMLDILRHQPDAEILTWVIAGLKNYYQYAYDVNSNSLRPMWNNGQDMTDYCFKRDGYYGKAGTVLKPFPLEGDYLLPLVRAWLLSDDDDLHTLIVTMLSRLEKQGIHQSASPFLLLAITELAHAKQSAQWAEYAWQMAEILFKRYFHHGLFVRSEHHRYVRLDDPFPAILLTLIAACRNKWSEVPAVLTQGGYIHGDYRINGESRVIYDTEFIYPEKLIH
|
Catalyzes the formation of unsaturated digalacturonates from polygalacturonate or short oligogalacturonates.
|
Q05526
|
Q8PNR2
|
RL6_XANAC
|
50S ribosomal protein L6
|
Xanthomonas
|
MSRVAKKPVSLPKGVELNVQPGLVSVKGPKGTLTLPKPAGVEIAIDGGVATLSANDPSQIALTGTVRAILANMVKGVSEGFERKLELVGVGYRAAMQGKDLSLALGFSHPLVFVAPEGITLSTPTQTEIVVQGADKQRVGEVAAKIRGFRPPEPYKGKGVKYAGEVIIRKEAKKA
|
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.
|
Q8PNR2
|
Q746Z9
|
ISPD_GEOSL
|
MEP cytidylyltransferase
|
Geobacter
|
MAVFALVPAAGMGKRMGASINKQYLILAGRPILAHTLSVFEGASFVDGIFVITPEDEIPFCRDHVVERYGFTKVRGIVAGGAERQHSVLNGLRAMEGTVADDDVILIHDGVRPFVSTDVLARATAVAREDDGALVAVPAKDTVKTVEDGIITGTPPRETLWLAQTPQAFRYAVIRAAHEIADAERFLGTDDAMLVERLGRSVRIVVGDYRNIKITTPEDMVLAEAFLKELAA
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q746Z9
|
Q5E781
|
HSCB_ALIF1
|
Co-chaperone protein HscB homolog
|
Aliivibrio
|
MNHFELFGLPNQFELDGGLLSLQFRELQKRFHPDNFATSSERDRLLSIQKAAQINDAYQTLKNPVSRAEYILSEQGHDIRGEQTTMQDPMFLMQQMELREELESLPSSSDPESALFDFAENVTAMRKSQLVQLQELLKNEAWIEAAQSVRKLKFIEKLNQEVEQLEEKLLG
|
Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.
|
Q5E781
|
Q13822
|
ENPP2_HUMAN
|
Extracellular lysophospholipase D
|
Homo
|
MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCKGRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQHFKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYGRPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFRKTSRSYPEILTLKTYLHTYESEI
|
Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids . Major substrate is lysophosphatidylcholine . Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility . Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP . Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation . Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein . May have a role in induction of parturition . Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor . Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids . Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) .
|
Q13822
|
Q2PC20
|
PPM1K_BOVIN
|
Protein phosphatase 2C isoform kappa
|
Bos
|
MSTAALLTLVRSGGNQVRRRVLLRARGLQDDRWVMPTCHSSTSEPKWSRFDPDGSGRPATWDNFGIWDNRLEEPILLPPSIKYGKPIPKVSLQNVGSASQIGKRKENEDRFGFAQLTNEVLYFAVYDGHGGPAAADFCHTHMEKCILDLLPKEENLETVLTLAFLEIDKTFARHAHLSADATLLTSGTTATVALLRDGIELVIASVGDSRAILCRKGKPMKLTIDHTPERKDEKERIKKCGGFVAWNSLGQPHVNGRLAMTRSLGDLDLKTSGVIAEPETKRIKLHHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPNEAAHAVTEQAIQYGTEDNTTAVVVPFGAWGKYKNSEITFSFSRSFASSGRWA
|
Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.
|
Q2PC20
|
Q6DDU7
|
YKT6A_XENLA
|
Xsnare1
|
Xenopus
|
MKLYSLSVLYKGENKVHLLKSAYDVSSFSFFQRSSIQEFMAFTSQLIVERSDKGSRSSVKEQEYLCHVYVRNDSLAGVVIADNEYPPRVCFTLLEKVLEEFSTQVDRIDWPSGSPATIQYNALDSYLSKYQNPRDADPMSKVQAELDETKIILHNTMESLLQRGEKLDDLVSKSEVLGTQSKAFYKTARKQNSCCDIM
|
Vesicular soluble NSF attachment protein receptor (v-SNARE) mediating vesicle docking and fusion to a specific acceptor cellular compartment. Functions in endoplasmic reticulum to Golgi transport; as part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in early/recycling endosome to TGN transport; as part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase activity.
|
Q6DDU7
|
B9LTX1
|
GUAAB_HALLT
|
GMP synthetase
|
Halorubrum
|
MVETEEFIAEAKAEIREAIGDANAVIALSGGVDSSVAATLAYEAVGDQLTPVYVDTGLMRKGETEEIRETFSFMESLRVIEAQERFFDRLAGVTDPEEKRHVIGEGFIDEFETVANDVGADYLVQGTIYPDRIESEGNIKSHHNVGGLPDIVDFEGIVEPVRDLYKDEVREVARALGLEEVISERMPFPGPGLAVRIVGEVTPEKAAVAREATHVVEEELEEYDPWQAFAAVLGKATGVKGDNRVHGWVVAVRSVESRDGMTARAQELDWSTLQRIQSRITGENENVARVVYDVTHKPPATIEYE
|
Catalyzes the synthesis of GMP from XMP.
|
B9LTX1
|
C9YID6
|
CBIM_CLODR
|
Energy-coupling factor transporter probable substrate-capture protein CbiM
|
Clostridioides
|
MKQNIKLGVIAALMLIVLTPVTSNAMHIMEGYLPVKWSIAWGVIFIPFFLVGLKSIGKIVKQDPKKKVLLALCGAFVFVLSALKIPSVTGSCSHPTGVGLGAIMFGPSVMFVLGTIVLIFQALLLAHGGITTLGANAFSMAIIGPIISFLIFKALKKKDGNNAMPVFLAAAIGDLATYTVTSIQLALAFPDPSGGVMASAIKFLGIFFMTQIPIAIAEGILTVIVYNLITENGEKSILENNDKGVKANEC
|
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
|
C9YID6
|
Q74L76
|
RS8_LACJO
|
30S ribosomal protein S8
|
Lactobacillus
|
MVMTDPIADYLTRIRNANMAKHTSVEIPASSMKKSLSEILKNEGFIRDYQVEDDNKQGMIKIFLKYGPNNERVISGLKRISKPGLRNYVSAENLPKVLNGLGIAIISTSAGVITDKEAREKNVGGEVIAYVW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
|
Q74L76
|
Q2NA97
|
TRPD_ERYLH
|
Anthranilate phosphoribosyltransferase
|
Erythrobacter
|
MKTLPLAVPHMSQDEAEEVFGWILDGEASEEEIARFLLAMTERSETADEIAGAARALRDRLIPVEAPEGAVDCCGTGGDGHHTLNVSTAVSLVVAAAGVPVAKHGNRAASSKSGAADTLEALGLDMEAVGRTAEKTLAEIGICFLFAKNHHPAMGRIQPIRQRLGKRTIFNLMGPLSNPAGVKRQLIGIARPGYVPIYAEAKAKLGTERTYIVSGDEGLDELSLAGGNELADVCGNEFEMRRVYAEMIGLPHAPVEAIRGGDAAHNAMALKALLEGTPGPYRDAVVFNAAATLMAAGAVEDWEVGAAMAVESLDSGKANELLGKWIEMAV
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q2NA97
|
Q9VNH6
|
EXOC4_DROME
|
Exocyst complex component Sec8
|
Sophophora
|
MDAPPPTKPPRGVKYGKDESAGCGFLVNVIKSLGFSETTEERQKEKQKIEAEFKRSDLRLNELVSRHDQQLTQVLPLFSQVSSEVTASRERIHAVKENLGVCKRLLQCRRDELRKMWMDAVQHKYVLEMLEQIQELRKVPQRVVGYTAKRQYLHASKALTDALTTLNGPLQAVEGLSDLRTDLQTRRQQLYQRLHEELVTQVYTNSANEALSSFQRTNSSRLNSSFTRGIGARRSTDRIEANARVRKALAEMAQSFDLDKAEVIEDADLIYPELSMSYFVAIIVESFGMLHKVPDSLETLRVQIQTELLNVVRHTTHQLSVSGATADTNPLLSLLEVIFKQFKAIAKTHSLLLKNYLSVGQKYSVVGPQPYDLTDFWAQAQSVLQLLLTDYLDIQNAAADESAQTGFSEPTSNINSYFLRRKVPSTKRSMFKFDKSSHVGTSNNSDAFKEHRRNASDASVDDNLAGQLGGSGKGSTSGLFPHEKKQREKILICTPDQSIITKVYLPLMGYIKEIENFMKCKPGQPCSLHDFLDNYIKDTFLTKGHNRNLQLTIESLSKNQDAWRTIISPEEIKALNLSRPLLQSTVMVERRLMETKNLIQDLPCYSEDLLKMVCALLKAYREICQAAYRGIVQPDSEDKRIYSVAWLKDEDISRFLKTLPNWTDLKTYSQKSRHNRKLHRGSFEPSEEESPLQVQQRNIREAEMLTSNLGEGGITQQEILVEISVLKELAILQESMEWFSCRVSEFANDLRRPLVNGLNAVPAECGADIAVKDGTIKVMTNLALEFDELANTCLLVLHLEVRVQCFHYLRSKSSVRTNSYVGSKDDILEPDRQVQVLTKRLSEMDEAFSATLHPRKTRYIFEGLAHLASRILIQASNYLEHIDQITVQRMCRNAIALQQTLSNITASREVALDQARHFYELLCMEPDEILNALLERGTQFSEMQLLNALQLSCKSFGITDANLLASYQQKLSDILGAKPSKGVVV
|
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Involved in regulation of synaptic microtubule formation, and also regulation of synaptic growth and glutamate receptor trafficking. Does not appear to be required for basal neurotransmission.
|
Q9VNH6
|
Q2RQE9
|
FLGI_RHORT
|
Basal body P-ring protein
|
Rhodospirillum
|
MTAPAGFLPRVGRLIAVALTAVFLLAPTGAEAASRIKDLADFEGVRDNILVGYGLVVGLKGTGDKLDDVTFTKESLIGMLERLGVNTREGKLDPDNVAAVMVTGTLPPFARQGSRIDVTISALGTAKSLAGGTLMVTPLIGADGEVYAVAQGQAQIGGYAVQGQSASVQKGVPTSGRIPNGALVEAEVPFNLSAMESVKISLRNPDFTTARRIAQAINAFLGTELARPLDPGTVLVAVTAGYEGNAVALLTDIEQLLVEPDTVARVVIDEATGTIVIGEKVRINTVAIAQGNLTIRVTETPQVSQPAPFSQGGQTAVVPRTNIQVDEGKDNKLTVVNGGVNLQDLVNSLNALGVGPRDMISILQAIKSAGAMQAEIQVM
|
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
|
Q2RQE9
|
B8F789
|
SYD_GLAP5
|
Aspartyl-tRNA synthetase
|
Glaesserella
|
MMRSHYCGVLNRTHVGEQVTLSGWVHRVRNLGRFIFMQIRDREGIVQVFFDEKDEALFKQASALRAEACVQIKGEVIARDTSQINKEMATGEIEVLVKELVVYNNSEVLPLDFNQNNTEEQRLKYRYLDLRRPEMAERLKTRAKITSFVRRYMDDNGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIAKCFRDEDLRADRQPEFTQIDVETTFMTAPEVRAMMEKMIRGLWLDRLNVDLGEFPQMTFAEAMRRYGSDKPDLRNPLELVDVADILKDVEFKVFSGPANDPEGRVAVIRVPNGAEITRKQIDEYTQFVGNYGAKGLAWAKVNDVNAGLEGLQSPIAKFLTDDVVKALLARVNAQNGDIIFFGADSEKVVTDAMGALRLKVGRDLGLTDLTAWKPLWVVDFPMFEKDDEGNWSAMHHPFTAPKDLSPEELVQNPKGAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFGILGINEEEQKEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTTAAACLMTDAPSFGNPKALAELAIQTTVEKES
|
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
|
B8F789
|
B2U350
|
GLO2_SHIB3
|
Glyoxalase II
|
Shigella
|
MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLNKLSALPDDTLVCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEERFAWLRSKKDRF
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
B2U350
|
A1EA65
|
NDHH_AGRST
|
NADH-plastoquinone oxidoreductase subunit H
|
Agrostis
|
MSLPLTRKDLMIVNMGPQHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNAPEFLENIQIPQRASYIRVIMLELSRIASHLLWLGPFMADLGAQTPFFYIFRERELIYDLFEAATGMRMMHNYFRIGGVAADLPYGWIDKCLDFCDYFLRGVVEYQQLITQNPIFLERVEGVGFISGEEAVNWGLSGPMLRASGIQWDLRKVDPYECYNQFDWKVQWQKEGDSLARYLVRVSEMRESIKIIQQAVEKIPGGPYENLEVRRFKKAKNSEWNDFEYRFLGKKPSPNFELSKQELYVRVEAPKGELGIYLVGDDSLFPWRWKIRPPGFINLQILPQLVKKMKLADIMTILGSIDIIMGEVDR
|
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.
|
A1EA65
|
Q6D2N7
|
TRUA_PECAS
|
tRNA-uridine isomerase I
|
Pectobacterium
|
MSETTQAAAIQAAAVAENERAPLKIALGIEYDGSQYYGWQRQIDVASVQACLEKALSKVADEPIEVLCAGRTDAGVHGTGQVVHFTTQAIRKDAAWTMGVNANLPPDIAVRWVKAVHEDFHARFSATARRYRYIIYNHRYRPAVLSHGMTHFYHPLDVERMERAGQCLLGENDFTSFRAVQCQSRTPWRNVNHLKVTRHGNYIVVDIKANAFVHHMVRNIVGSLMDVGCGNRPESWIAELLAAKDRTLAGATARAEGLYLVAVDYPARFALPQPTMGPLFLAD
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q6D2N7
|
A0KR27
|
RSMG_SHESA
|
16S rRNA 7-methylguanosine methyltransferase
|
Shewanella
|
MLSAQLEAYLAEINLPATAEQKKQLLDFVGMLNKWNKAYNLTSVRDPEAMLVRHIMDSLVVSPHLQGERFIDVGTGPGLPGIPLAIMNPDKTFVLLDSLGKRIRFQKQVAFELGIHNISSIESRVEAYQPEQKFDGVLSRAFASIHDMLTWCHHLPAEHGQFYALKGLLSDEEMQQIPAGFVVTETIELQVPRLDEQRHLLKIIKE
|
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
|
A0KR27
|
B1YC43
|
EF1B_PYRNV
|
aEF-1beta
|
Pyrobaculum
|
MSAEVALVYRVLPESVEVDIEKLKTSVINKLSPKYKVDRVEVEEIGFGIKALRFFIRMPESDEYSSDEVEELLRSVEGVGGYELEYFSRLSF
|
Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA.
|
B1YC43
|
A5A6S6
|
TM38A_RABIT
|
Transmembrane protein 38A
|
Oryctolagus
|
MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRRHPVASWLCAMLHCFGSYILADLLLGEPLIDYFSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFIMIATGWVKGSGVALLSNVEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTMFMVSCKVFLTATHSHSSPFDVLEAYVCPVLFGTGSGGDHPQDNHGAWPGGPPSGALATKSKEELSEGSRKKKTKKAD
|
Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.
|
A5A6S6
|
B7N815
|
SFSA_ECOLU
|
Sugar fermentation stimulation protein A
|
Escherichia
|
MEFSPPLQRATLIQRYKRFLADVITPDGRELTLHCPNTGAMTGCATPGDTVWYSTSDNTKRKYPHTWELTQSQSGAIICVNTLWANRLTKEAILNESISELSGYSSLKSEVKYGAERSRIDFMLQADSRPDCYIEVKSVTLAENEQGYFPDAVTERGQKHLRELMSVAAEGQRAVIFFAVLHSAITRFSPARHIDEKYAQLLSEAQQRGVEILAYKAELSAEGMALKKSLPVTL
|
Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism.
|
B7N815
|
A4YKS8
|
GLO2_BRASO
|
Glyoxalase II
|
unclassified Bradyrhizobium
|
MAADIRVFTCLSDNFGYLIHDPATGATASVDAPEAGPIVRQLEANGWTLTDILITHHHYDHVGGVAELKQRYGCRVIGPHDRKAAIADVDLRVAHGDVVKVGELLARVLETPGHTLDHVSYVFDADKAVFAADTLFSIGCGRVFEGTYPMMWDSLLKLRTLPDDFRLYCGHEYTASNVKFALTVDPDNEALKARAAEVTRLRAANQPTIPVLLGEEKQANVFLRADDPAIAVRLRMKGASAEEVFGELRERKNKS
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
A4YKS8
|
Q5XIP6
|
FEN1_RAT
|
Flap structure-specific endonuclease 1
|
Rattus
|
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYIFDGKPPQLKSGELAKRSERRAEAEKQLQQAQEAGAEEEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALAKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRVLQELGLNQEQFVDLCILLGSDYCESVRGIGPKRAVDLIQKHKSIEEIVRRLDPSKYPVPENWLHKEARQLFLEPEVLDPESVELKWSEPNEEELVKFMCGEKQFSEERIRSGVKRLNKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGPAKKKAKTGGAGKFRRGK
|
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
|
Q5XIP6
|
A6WHQ9
|
MURI_SHEB8
|
Glutamate racemase
|
Shewanella
|
MSRPILVFDSGIGGLSVLAEIRKSLPHSDYCYLFDNARLPYGELEEQVLIAGCVALVCDLVARTNAMIVVVACNTASTVVLPALRANLSIPVVGVVPAIKPAAQMSKSKRIGLLATPGTVKRHYTHELISQFADDCHVELFGCSELVMMAEQKIATGEMDMHRLADLLAPVVAAQLDVLVLGCTHFPMIQAELQQVLGAGVTLMDSGAAIAKRVVTLLTQQNLIVEQRRVTNEREAVGQSAMQAFYTKAEISEGLTTTLIDCGFSTIERITTTN
|
Provides the (R)-glutamate required for cell wall biosynthesis.
|
A6WHQ9
|
C0MDW7
|
UVRC_STRS7
|
Excinuclease ABC subunit C
|
Streptococcus
|
MNELIKHKLELLPDSPGCYLHKDKAGTIIYVGKAKNLRNRVRSYFRGSHDTKTELLVSEIADFEFIVTGSNTEALLLEINLIQENMPKYNIKLKDDKSYPFIKITNEPFPRLLITRQIKKNDGLYFGPYPDAYTATEVKKLLDRIFPFKKCKNPVNKVCFYYHLGQCQAHTICHTDKAYWDSLVADVKQFLNGKDDKIIDDLRSKMLEASHNQEFERAAEYRDLISGIATMRTKQRVMSKDLQDRDIFGYFVDKGWMCVQVFFVRQGKLIQRDVNMFPYYNEAEEDFLTYVGQFYSDQRHLIPKEVFIPETIDETLVAAIVPARIVKPQRGEKKQLVALATKNARVSLQQKFDLLEKDLRKTSGAIEHLGQLLGIEKPVRIEAFDNSNIQGTSPVAAMVVFVDGKPSKKDYRKFKIKTVIGPDDYASMREVIYRRYSRVKHEGLQAPDLIIVDGGQGQVKAARDVIEHQLGLSIPVAGLQKNDKHQTHELLFGNPLAVVELPRNSEEFFLLHRIQDEVHRFAITFHRQVRSKNAFSSKLDHIAGLGPKRKQLLLKRFKSMAALEQASLEEIQQLGIPKTVAEALIDHLTSKSDT
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
C0MDW7
|
A1TYL3
|
RL18_MARN8
|
50S ribosomal protein L18
|
Marinobacter
|
MSANNERLRRARKVRMKIRELGTDRLCVHRTPRHMYAQVTTADGSKVLATASTLDKELRQGATGNVDAAKKVGQLIAERAKAAGIEKVAFDRSGYRYHGRVQALADAAREAGLQF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
A1TYL3
|
Q69AA9
|
CPS12_ACTPL
|
Stealth protein cps12A
|
Actinobacillus
|
MNKMNRKFSKLLKNPHIFFRDFLNKKYPIKNTELPFSESEEANLIEANQKLDKIIQKNTLQQANIDVVFTWVDGSDPSWQAKYSQYAPNYQAKSALYATDIARFEDHNELYYSVHAVLKYMPWVRHIFIITDNQKPKWLDETRQEKITLIDHQDIIDKEYLPTFNSHVIEAFLHKIPNLSENFIYFNDDVFIARELQAEHFFQANGIASIFVSEKSLSKMRDKGIITPTLSASEYSIRLLNKYYDTNIDSPLVHTYIPLKKSMYELAWLRYEKAILGFLPNKLRTNNDLNFANFLIPWLMYFEGKAMPKIDICYYFNIRSPNAISLYKKLLLKQQMGEEPNSFCANDFNSNYSIENYRNNLISTLNNYYKF
|
Part of a capsular polysaccharide synthesis locus.
|
Q69AA9
|
Q5ZKN5
|
FA53A_CHICK
|
Dorsal neural-tube nuclear protein
|
Gallus
|
MVTLITEKLQNQSLDDLTCKTYNINLYSSEKLNKSGSLFSFEINEDSPWKALNGGCPIQTDARNSAYPFPVCPFSTGPASNGALQWQQEPSSTSMVSGWISELNLNENSGQPLAPPTKRHCRSLSEPDELARCRSPWKPGNSKVWTPVSKRRCNSGGSATLQRCNSHGSATLQRSTSISLPQNILSLNNVFTVTSFNTSPVPRPSSASSGFVDSSEGSTSSSTRWNSGGPCDFNPRRRLSLSQEHITETGNLLPSANSTPTSTPELSRRQGLLRCRSQPCVLNEKKSRLKRRREEDVRWNRPSLDFFKMTRTLKNSKSLCSLDYEDDDDDTQMKTIVSSPCDSNDLMNIITPGSSPMKEQLDEVRHHGSCQGSFKTRDYKKAAAVCESDEDTSDCESTEEGIFPLDCGDLDLEQIENN
|
May play an important role in neural development; the dorsomedial roof of the third ventricle.
|
Q5ZKN5
|
A1SW90
|
NAGZ_PSYIN
|
N-acetyl-beta-glucosaminidase
|
Psychromonas
|
MRPVILDVEGYELDSEEKEILAHPLVAGIILFTRNYYDIEQLKALVKDIRRYAGNELLIAVDHEGGRVQRFRDDFTRLPSAGSLIEKNDMKTACELAFSSAWVMASELIACDIDFSFAPVLDLNGISNVIQNRAFSSSITETVTLAEAYINGMKSAGMVSTGKHFPGHGSVEADSHTALPVDSRSELEIFTKDIKPFENLIKKGALDAVMPSHVVYSQCDLQPAGFSSYWLDDVLRTRLGFKGVVISDDLSMHGASFVGNHLSRAESAIQAGCDLILACNDRSGAVSILDNLKVKPTAQYHAVNQLRSTKNKFILPLNKNPIWIKNKQMLMQLSEQF
|
Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
|
A1SW90
|
A9BDG5
|
RL10_PROM4
|
50S ribosomal protein L10
|
Prochlorococcus
|
MGRTLESKKQIVEELKALLDQAEMALVIDYQGLTIKEMSDLRTRLGPSSGICKVTKNTLMRKAIDGDTSWSSLESLLNGTNAFVLVKGDVGGALKAVQAFQKETKKSKTKGGLFEGKLLSQDEIKAIANLPTKEVLMAQIAGALNSIATKMAVGINEVPSGLARSLKQHADSGEN
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
A9BDG5
|
P00115
|
CYC6_SYNP3
|
Soluble cytochrome f
|
unclassified Synechococcus
|
MKTLLTILALTLVTLTTWLSTPAFAADIADGAKVFSANCAACHMGGGNVVMANKTLKKEALEQFGMNSADAIMYQVQNGKNAMPAFGGRLSEAQIENVAAYVLDQSSKNWAG
|
Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
|
P00115
|
O26377
|
GGR1_METTH
|
Geranylgeranyl reductase 1
|
Methanothermobacter
|
MIIMVTEVDVLVIGAGPAGSTAAKHAALGGADVLLIDKKSEIGAPKRCAEGVSIGGLESLGIEPNPRWITKKLDGVRMVSPNGTDVWLTSDKVELPEAGYILERKVFDKFMAMDAARAGSRIMVKTIATGMERTDDGYLVSAECMGEKFEIKARIVIAADGPESRVARWAGLNTATRPKDMESAAQFEMVGVEMEDNNCIEFYFGSVAPGGYALDIPEGDDIANVGLGVLSTETDKSAYEHLLEFVESCPATRNAQPVELNIGGDPVGGMPKKLVADSLMVVGDAAGQVNPLTGGGIISGMKGGMLAGQVAAAAVSEGDVTARRLGEYERLCREEIGDEISKYLKVKEYLLTLSDSELDSIAEAFQDVEFEKVSTTELVKKLIKVSPKALLKLGKLF
|
Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains.
|
O26377
|
Q4L459
|
TAGH_STAHJ
|
Teichoic acids export ATP-binding protein TagH
|
Staphylococcus
|
MSVSVNINNVTKEYRIYRNNKERIKDALIPKNKNNTFFALDDVSITAHEGDVIGLVGINGSGKSTLSNMIGGSISPTSGNIERNGEVSVIAINAGLNGRLTGVENIEFKMLCMGFKRKEIKQLMPQVIEFSELGEFIHQPVKNYSSGMRAKLGFSINVTINPDILVIDEALSVGDQTFTQKCLDKIYEFKEANKTIFFVSHNIRQVREFCTKIAWIEGGKLKEYGDLEEVLPKYEQFLKDFKKKSKADQKAFRKGLDEKRFIVK
|
Part of the ABC transporter complex TagGH involved in teichoic acids export. Responsible for energy coupling to the transport system.
|
Q4L459
|
P15410
|
BXC1_BOMMO
|
Bombyxin C-1 A chain
|
Bombyx
|
MKLVMLLVVVSAMLVLGGAQTASQFYCGDFLARTMSSLCWSDMQKRSGSQYAGYGWPWLPPFSSSRGKRGIVDECCYRPCTIDVLMSYCDN
|
Brain peptide responsible for activation of prothoracic glands to produce ecdysone in insects.
|
P15410
|
O88758
|
KCNS1_RAT
|
Voltage-gated potassium channel subunit Kv9.1
|
Rattus
|
MVSEFPGPGSRVPWRPRDEALRVNVGGVRRLLSARALARFPGTRLGRLQAAVSEEQARRLCDDYDAAAREFYFDRHPGFFLGLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALATCCRARYLERRVTRPRAWDEDSDAPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSAEDVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGAALGDRRGASGEELGDLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEEKNVGFDTIPACWWWGTVSMTTVGYGDVVPETVAGKLAASGCILGGILVVALPITIIFNKFSHFYRRQKALEAAVRSSGQREFEDLLSSVDGVSDVSLETSRETSQEGRSTDLETQAPSEPAKSHSY
|
Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2.
|
O88758
|
A4IZB0
|
RSMH_FRATW
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Francisella
|
MQESINDLNINPQGIYIDATFGRGGHSKAILNRLTTGRLIAFDKDLDAISYARENFQFSNFEIVHASFASIYDYCLQHSLLGKIDGIIMDLGVSSPQLDNAARGFSFTHNGPLDMRMDVSKGITASQALEELSVDDLSYIFKVYGEERFAKKIALRIKDYIQQNGSIRTTLELAELIRATIGKKEKKNPATRCFQALRIYVNNELKDLEALLENILAVIKSGGRIAVISFHSLEDRIVKQKFSALINPKQELNRITKMLPQDSSQIKLKWITKKSKANEDELNQNVRSRSAILRVVEKL
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A4IZB0
|
Q5F938
|
SYP_NEIG1
|
Prolyl-tRNA synthetase
|
Neisseria
|
MKASQFFISTLKEAPAEAAFASHKLMIRAGLIKANASGLYTWMPMGLRVLRKVENVVREEMARAGSVELLMPVVQPAELWQESGRWEFYGKELLRLKDRHERDFCMGPTCEEVIADIVRKEINSYKQLPKNFYHIQTKFRDEVRPRFGVMRAREFVMKDAYSFHADYASLQATYDAMYDAHCRIFTRLGLAFRPVAADTGSIGGTGSHEFQVLAESGEDVIAYSDTSDYAANIELAPTLPLKGERAAAQAVLTKVHTPNVKTIESLVEFLNIPVEQTLKSIVVEGENEGELVLLLLRGDHEFNDIKAEKLAGVKSPLTMASPAAIVEQFGANGGSLGPVGFTGKVYADFATEKGADWVIGANEDDYHYTGFNFGRDAAEPEFVDLRNVVEGDESPDGQGRLKLARGIEVGHVFQLRGKYTQAMNVSFLDNNGKSQIMEMGCYGIGITRVVAAAIEQNNDEKGIIWTKAMAPFEVVIVPMNYKKSDTVREAADRIYAELLAAGADVLLDDRDERAGVLLNDSELLGIPHRIVIGDRALKEGNVEYAERRGNEAQAVAIGEIVARVTASLNA
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
|
Q5F938
|
P51038
|
CISY2_RHITR
|
Citrate synthase, plasmid
|
Rhizobium
|
MDNNNACVLVDGHSAELKLRSSTIGPNVLGIGSLYEQTKMFTYDPGFTSTASCESSITFIDGDEGVLLHRGYPIEQLAEHGDFLEVCYLLLYGELPTAAQKKDFDYRVVHHTMVHEQMSRFFTGFRRDAHPMAVMCGCVGALSAFYHDSTDITDPHQRMVASLRMIAKMPTLAAMAYKYHIGQPFVYPKNDLDYASNFLRMCFAVPCEEYVVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPFACIAAGIACLWGPAHGGANERALNMLTEIGTVDRIPEYIARAKDKNDPFRLMGFGHRVYKNYDPRAKIMQKTAHEVLGELGIKDDPLLDIAIELERIALTDDYFIEKKLYPNVDFYSGITLKALGFPTTMFTVLFALARTVGWIAQWNEMIEDPDQRIGRPRQLYTGAPLREYVPLSKR
|
The exact function of the plasmid-encoded citrate synthase is not clear, it could help nodulation by allowing the bacteria to use citrate as a chelator of iron and calcium.
|
P51038
|
P95334
|
DNAK_MYXXD
|
Heat shock protein 70
|
Myxococcus
|
MGKVIGIDLGTTNSCVAVMEGGEPVVIPNSEGSRTTPSMVGFTDSGERLVGQIAKRQAITNPENTVFAAKRLIGRKFDSPEGKKAIGVSPFKVASSPNGDAWVEIRGKGYSPPEVSAIVLMKMKQTAEDYLGEQVSEAVITVPAYFNDSQRQATKDAGRIAGLSVLRIINEPTAAALAYGLDKVQDGGTERIAVYDLGGGTFDISILELNAGVFEVKSTNGDTFLGGEDFDQRLIDYLAKRFAESNNGLDLRKDRMALQRLKEAAERAKHELSSAPETEVNLPFITADASGPKHLTETVDRATFEALVTDLIDRTIEPCRIALKDAGIPAQQINQVLLVGGMTRMPRVQQKVKEFFGREPHKGINPDEVVAVGAAIQGGVLKGEVKDVLLLDVTPLSLGVETAGGVFTKIIDKNTTIPCKKSQVFSTAVDNQPLVSVHVLQGEREMAADNKTLARFELVGIPPAPRGVPQIEVSFDIDANGIVHVSAKDLGTGKVQQVRVVSNSGLSEAEIQAMISDAQSHASDDKKKKELAELRNNADGLIYTTEKSLEEYASLLSEKDREEIKADLERLKEVLNTSDAAVLKESFQRLEGSAYRIADAIYTGQAS
|
Potential chaperone for other proteins involved in social motility.
|
P95334
|
P69845
|
GRAA_GRASX
|
Grammistin Gs A
|
Grammistes
|
WWRELLKKLAFTAAGHLGSVLAAKQSGW
|
Thanks to its amphiphilic alpha-helice(s), it may integrate into membrane phospholipids, leading to lysis of the membrane. Has no substantial hemolytic activity. Has antibacterial activity with a broad spectrum against various species of bacteria including both Gram-positive and Gram-negative groups.
|
P69845
|
Q9YFA8
|
DCD_AERPE
|
Deoxycytidine triphosphate deaminase
|
Aeropyrum
|
MILSDRDIRALLAIGDLVVEPLSGDTVRENGLDLRLGRGFCRFKRSDRVLDPRAPGSPGEFYECGEGDEIIVGPGEHMLLHTQEYIRLPGYVAGLVNLRSTWARTGIYIPATVVDAGFEGQLTIEVVGSGFPVKLYPGDRFLHLVLVKLQSPAMNPYRGRYQGQRGVRLPKLFAKNTG
|
Catalyzes the deamination of dCTP to dUTP.
|
Q9YFA8
|
Q9BQ24
|
ZFY21_HUMAN
|
Zinc finger FYVE domain-containing protein 21
|
Homo
|
MSSEVSARRDAKKLVRSPSGLRMVPEHRAFGSPFGLEEPQWVPDKECRRCMQCDAKFDFLTRKHHCRRCGKCFCDRCCSQKVPLRRMCFVDPVRQCAECALVSLKEAEFYDKQLKVLLSGATFLVTFGNSEKPETMTCRLSNNQRYLFLDGDSHYEIEIVHISTVQILTEGFPPGGGNARATGMFLQYTVPGTEGVTQLKLTVVEDVTVGRRQAVAWLVAMHKAAKLLYESRDQ
|
Plays a role in cell adhesion, and thereby in cell motility which requires repeated formation and disassembly of focal adhesions. Regulates microtubule-induced PTK2/FAK1 dephosphorylation, an event important for focal adhesion disassembly, as well as integrin beta-1/ITGB1 cell surface expression.
|
Q9BQ24
|
Q5LW55
|
RL16_RUEPO
|
50S ribosomal protein L16
|
Ruegeria
|
MLQPKRTKFRKMFKGRIHGLAKGGSDLNFGTYGLKALEPERVTARQIEAARRAMTRHMKRQGRVWIRIFPDTPVTSKPTEVRMGKGKGSVDYWACKVKPGRVMFEIDGVNDEIAREALRLAAMKLPIKTRVVVREDW
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q5LW55
|
Q8Z538
|
ARNT_SALTI
|
Undecaprenyl phosphate-alpha-L-Ara4N transferase
|
Salmonella
|
MKSIRYYLAFAAFIALYYVIPVNSRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWINSLGQWLFGATNFGVRAGAILTTLLAAALVAWLTFRLWRDKRTALLASVIFLSLFAVYSIGTYAVLDPMIALWLTAGMCCFWQGMQATTRTGKIGMFLLLGATCGLGVLTKGFLALAVPVVSVLPWVIVQKRWKDFLLYGWLAVLSCFVVVLPWAIAIARREADFWHYFFWVEHIQRFAMSDAQHKAPFWYYLPVLLAGSLPWLGLLPGALKLGWRERNGAFYLLGWTIMPLLFFSIAKGKLPTYVLSCFAPIAILMARFVLHNVKEGVAALRVNGGINLVFGIIGIVAAFVVSSWGPLKSPVWTHIETYKVFCVWGVFTVWAFVGWYSLCHSPKYLLPAFCPLGLALLFGFSVPDRVMESKQPQFFVEMTQAPLASSRYILADSVGVAAGLAWSLKRDDIMLYGHAGELRYGLSYPDVQNKFVKADDFNAWLNQHRQEGIITLVLSIDKDEDISALSLPPADNVDYQGRLVLIQYRPK
|
Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
|
Q8Z538
|
Q8EN13
|
PXPA_OCEIH
|
5-oxoprolinase (ATP-hydrolyzing) subunit A
|
Oceanobacillus
|
MQYQVDLNSDIGESYGAYTIGQDDEVMEFITSANIACGYHAGDHNIIHRTIDLAIKNNVAIGAHPGLQDLIGFGRRPMQISPEEVYQLTVYQIGAVQAFAQVKGHNLYHVKPHGALYNMAAKDTAIAKAIAQAVYDYNPNLILFGLANSELIRMGKEVGLNVANEVFADRTYQPDGSLTPRTSPNAMIHDTDEAVERVIRMVKENKIEAVDGTDISIIADTICIHGDGPKSLEFSRRLSHELKNQGISIQKREMHHG
|
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
|
Q8EN13
|
Q00728
|
H2A4_RAT
|
Histone H2A, testis
|
Rattus
|
MSGRAKQGGKARAKAKSRSFRAGLQFPVGRVHRLLRQGNYAERIGAGTPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKSQTK
|
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Q00728
|
A6GW04
|
SYY_FLAPJ
|
Tyrosyl-tRNA synthetase
|
Flavobacterium
|
MKNLVEELKWRGLFHDMMPGTEEQLTKESTTAYIGFDPTADSLHIGSMVQIILLVHLKNFGHKPIALIGGATGMIGDPSGKSDERNLLDEATLNKNVAGIKAVLSSFLDFNTTNANAPILVNNYDWMKDFSFIDFARDIGKRITVNYMMSKDSVKKRLGAEGEGMSFTEFTYQLIQGYDFQYLYKNHNCLLQMGGSDQWGNITTGTELVRRMGGEGAKAYALTTPLITKADGSKFGKSEGGNVWLTADKTSVYKFYQFWLNTSDDDAEKYIKIFTFLDKNTIDGLIEEHKTAPHLRVLQRKLTEEITILVHGKEELEKAIKASNILFGNSTSNDLKGLDAATFLEIFDGVPQAEISKTDIEAGINIVEVLNEKSGFLKSNGEARRALSANSIAVNKEKVTEEFTLTTKDMINNQFVLLQSGKKNYFVLNVK
|
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
|
A6GW04
|
Q30QQ0
|
ATPG_SULDN
|
F-ATPase gamma subunit
|
Sulfurimonas
|
MANLKDIQRQIKSVSNTQKTTRAMKLVSTAKLRRAEELAKRSRLYAAKMNQVIAEIAGRIRCNKVGGIDNRCFSKIEDPKTVDIIFVTADKGLCGGFNIQTIKAVKKLLSEYKAKNVKVRLRGIGKKGVEFFKYNEVELFDSVSNLSSKPDKEKSDEFILSSIEDFKDGKIDALYLVYNGYKNMITQELHVSKIFPVDATLYECDEPEKSMLEVEAQDEEKMLDSLVNRYAQYAMYYSLIDSVAAEHSARMQAMDTATNNAKEMVKSLNVQFNKARQAAITTELIEIISGVESMK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
Q30QQ0
|
Q48AT8
|
TUSA_COLP3
|
Sulfur carrier protein TusA
|
Colwellia
|
MTTTIFQQTNHTLDAIGLRCPEPVMMVRMNIRKIASGETLLIKCDDPSTARDIPSFCRFMEHELLAKQTDTLPFLYVIKKN
|
Sulfur carrier protein which probably makes part of a sulfur-relay system.
|
Q48AT8
|
Q94CE5
|
GATP_ARATH
|
Protein POLLEN-PISTIL INCOMPATIBILITY 2
|
Arabidopsis
|
MVVINSLRRLARTTQVHLHSKYATCMSGNSTSRRIFTTEAAPEKKNTVGSKGHDMLAPFTAGWQSADLDPLVIAKSEGSYVYDDTGKKYLDSLAGLWCTALGGNEPRLVSAAVEQLNTLPFYHSFWNRTTKPSLDLAKVLLEMFTANKMAKAFFTSGGSDANDTQVKLVWYYNNALGRPEKKKFIARKKSYHGSTLISASLSGLPPLHQNFDLPAPFVLHTDCPHYWRFHLPGETEEEFSTRLAKNLEDLIIKEGPETIGAFIAEPVMGAGGVIPPPATYFEKVQAVVKKYDILFIADEVICAFGRLGTMFGCDKYNIKPDLVTLAKALSSAYMPIGAILMSQEVADVINSHSSKLGVFSHGFTYSGHPVSCAVAIEALKIYKERNIPEYVAKVAPRFQDGVKAFASGSPIIGETRGTGLILGTEFVDNKSPNEPFPPEWGVGAFFGAECQKHGMLVRVAGDGILMSPPLIISPEEIDELISIYGKALKATEEKVKELKAQHKK
|
Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate or glyoxylate as amino-group acceptor, but not 2-oxoglutarate. The pyruvate-dependent activity is reversible while the glyoxylate-dependent activity is irreversible. Cannot use beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors. Modulates steady-state GABA levels in diploid pistil cells and the haploid pollen tube. Involved in the formation of a gradient of GABA along the pollen tube path. Involved in the maintenance of the shoot apical meristem (SAM) structure and subsequent adaxial-abaxial axis-dependent development of cotyledons and leaves .
|
Q94CE5
|
A8FYZ3
|
ISPE_SHESH
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Shewanella
|
MSNKLSQGWPAPAKLNLFLHINGRRADGYHELQTLFQFIDYCDYLDFKVTDTSSLKLHSNMGAAVADSDNLILRAAKLLQQVSGCAKGAEIWLDKRLPMGGGIGGGSSDAATTLVALNHLWNTQLSKDKLMAIGLQLGADVPVFINGLAAFAEGVGEELQAVFPTEYWYLVLIPNVHVSTAEIFQDPELPRDTPKLDIASLMNGSWQNDCQSLVAKRHPQVAKTLLWLLEYAPSRMTGTGACVFGEFEQQQQALDVLAKLPSDMTGLVAKGANTSSLELRLAQL
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
A8FYZ3
|
Q4JB92
|
MTNA_SULAC
|
S-methyl-5-thioribose-1-phosphate isomerase
|
Sulfolobus
|
MHFPLIPMVKLEEIKQIFKPKLLPIIWNKTKLTLLDQSRLPFEKIYVDVTKVEEVSDAIRTMKVRGAPAIGITAGYGMVLAIQDSISLEKAISDLTKAKKILDESRPTAVNLMWATSRMLNKAKDLVEQGNAKSVKELKELLEIEANKIFEEEYEAELKIGLYGIEKVNDGDTILTQCNAGGLATGTGLGTALAPAKLANALGIKVSVIAPETRPWLQGSRLTVYELMEENIPVTLIADTAVGLVMFKKMVNSVMVGADRILSDGHVFNKIGTFKEAVIAHELGIPFYALAPSSTFDMISTVDQVKIEERSPDEVRSIKGVYISPKEVKVYNPVFDVTPPKYVSAIITEYGIIYPPFDKNMRRMLGK
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
Q4JB92
|
Q9FVU0
|
P24D4_ARATH
|
p24 family protein delta4
|
Arabidopsis
|
MKKKMIPTTILLSALIFSLSPICEAVWLTVPHTGSKCVSEEIQSNVIVLADYLVISEEHSIFPTVSVKVTAPYGTVLHHRENTTNGQFAFTTQESGTYLACFEADAKSHGNKDFSINIDWKTGIAAKDWDSIARKEKIEGVELEFKKLEGAVEAIHENLIYLRNREAEMRIVSEKTNSRVAWYSIMSLGICIVVSGLQILYLKQYFEKKKLI
|
Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Required for trafficking GLL23, a component of the PYK10 complex. May act as a receptor facilitating its packing into COPII carriers and export from the endoplasmic reticulum.
|
Q9FVU0
|
Q2JXH1
|
PSAJ_SYNJA
|
Photosystem I reaction center subunit IX
|
unclassified Synechococcus
|
MSDFTKFLTTAPVAFILFSSFVFALFIEINRFFPDILTF
|
May help in the organization of the PsaE and PsaF subunits.
|
Q2JXH1
|
Q9CHW5
|
SERC_LACLA
|
Phosphohydroxythreonine aminotransferase
|
Lactococcus
|
MIYNFGAGPSVLPKEVLKKVQEELLDFEKSGMSVMEISHRSKAFQKVIDEAENDLRDLMSIPQNYKILFLQGGASSQFSMVPMNLAIGKKAYYNISGAFGEKAYDEAVKLSHFLDLMAISLGSTKKDNYNHLLKIDKSKIDEKNGAYLHLTTNNTIEGTSIFPENLPEFASLPLVADMSSNILAVDYDVSKFGLIYAGAQKNLGIAGLTIVIIREDLLNEAESLSSMMDYQILVENGSMYNTPPTFAIYVAGLVFKWVKAQGGVKKLEEMNQRKAQLLYDLIDQSDFYQNPIKNKDERSICNVVFTSPSQELDELFTQKAEEKGFKSLKGHRSVGGMRASIYNAFPLEGVVELVKFMKEFEEGYK
|
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
|
Q9CHW5
|
B2VBV2
|
GAL1_ERWT9
|
Galactose kinase
|
Erwinia
|
MSLQTTTQQIFSCAFGYAPTHTVQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVIACAKRSDRQVRTIAVDYDNQQDIFSLDEPIERHPQQLWSDYVRGVVKYLQQRAADLGGVDMVISGNVPQGAGLSSSASLEVAVGSVFRQLYQLPLSSADIALNGQQAENQFVGCHCGIMDQMISALGEKNSAMLLDCRTLDTRAVPMPSDIAVVIINTNFKRNLVGSEYNTRRQQCEAGARFFGQSSLRDVELAEFAEREHELDPLVAKRVRHVLTENARTLEAANVLARGDLARLAVLMAESHASMRDDFEITVPAVDMLVDIVKTSLGERGGVRMTGGGFGGCVVALMPRERVASVKAAVEQHYQAESGLKETFYVCTASAGAGLC
|
Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
|
B2VBV2
|
Q68RJ9
|
CART_BOVIN
|
CART(42-89)
|
Bos
|
MESPRLRLLPLLGAALLLLLPLLGALAQEDAELQPRALDIYSAVEDASHEKELIEALQEVLKKLKSKRIPIYEKKYGQVPMCDAGEQCAVRKGARIGKLCDCPRGTSCNSFLLKCL
|
Satiety factor closely associated with the actions of leptin and neuropeptide y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus.
|
Q68RJ9
|
Q4FU58
|
NUOH_PSYA2
|
NDH-1 subunit H
|
Psychrobacter
|
MQVTRIIPDVPSFLASMMTFDTWSILFMVVQSLVIFLVVVIVAAMMIIYERRMLALWQDRYGPNRVGPFGSLQLVADMLKIFFKEDWTPNFTDKFMFTLAPAVAMFTALASFAIIPISPTLGVADWDIGILFFFAMAGIAVYAVLFGGWASANKFSLLGGLRSAAQTISYEVFLGLSLMGVVALTGSFNLRAIVEAQADGWYIIPQFFGFLTFVVAGVAVTHRHPFDQPEAEQELAEGYHVEYSGMKFGMFFIGEYVNVVLISALMTCLFFGGWLAPFNLDIPFIPPAFWFMIKTLFFMTMFILARGSLMRPRYDQVMNFGWKVCLPVTLINLLVTAAVILIFSPTL
|
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. This subunit may bind ubiquinone.
|
Q4FU58
|
Q4JU23
|
RSMA_CORJK
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Corynebacterium
|
MVNERKIRLLGPNEIRQLAEELDLNPTKKLGQNFVHDPNTVRKIVKAADVTADDNVVEIGPGLGSLTLALLEAGASVTAVEIDPRLAAKLPATLEEQGAAEADVAVILKDAMEVAVQDFADAGRPLPTALVANLPYNVSVPVLLHMLEEFPSIDRVLVMVQLEVADRLAAAPGSKIYGVPSVKAGFYGSVARAATIGKNVFWPAPKIDSGLVRIDRYAEGAEPWAGGQSGAEQFDADQGIEQLDAQKLRREVFDLADAAFLQRRKTLRAALSGHFGSGQAAEEALRSAGIDPTLRGEKLSTEQFVQLAATSLRSVR
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
Q4JU23
|
O43745
|
CHP2_HUMAN
|
Hepatocellular carcinoma-associated antigen 520
|
Homo
|
MGSRSSHAAVIPDGDSIRRETGFSQASLLRLHHRFRALDRNKKGYLSRMDLQQIGALAVNPLGDRIIESFFPDGSQRVDFPGFVRVLAHFRPVEDEDTETQDPKKPEPLNSRRNKLHYAFQLYDLDRDGKISRHEMLQVLRLMVGVQVTEEQLENIADRTVQEADEDGDGAVSFVEFTKSLEKMDVEQKMSIRILK
|
Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Binds to and activates SLC9A1/NHE1 in a serum-independent manner, thus increasing pH and protecting cells from serum deprivation-induced death. Also plays a role in the regulation of cell proliferation and tumor growth by increasing the phosphatase activity of PPP3CA in a calcium-dependent manner. Activator of the calcineurin/NFAT signaling pathway. Involved in the cytoplasmic translocation of the transcription factor NFATC3 to the nucleus.
|
O43745
|
B0TFC9
|
FOLD_HELMI
|
Methenyltetrahydrofolate cyclohydrolase
|
Heliomicrobium
|
MTAQYIDGKAIAAQLRAEIKAEVASLREQGIVPKLAVILVGDDPASVVYARSKEKAAANLGIAFELFTLPGDTTEAALLALIERLNADAAVHGIMVELPLPKQISKEKVLEAIHPLKDVDGVHPLNRGYLMAGQPGLVPATPMSCMELLARSGVELAGKRVVIIGRGETVGKPLFFLLLRRNATVTVCHTRTKDLAAEVRRAEIVIAAAGKAGLVTGEMIAPDAVVIDAGINEGEDGNIVGDVKTAEAAERASLISPVPGGVGACTTALLFRNVLFGLKLQGGMAHE
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
B0TFC9
|
Q2J725
|
RIMP_FRACC
|
Ribosome maturation factor RimP
|
Frankia
|
MGSADDQASRMREGTVEVVGAGEAGRARDRSPSGSARGRGGVRTALRARLAAGLADAGFDLEDVTVTRAGSRSVVRVVVDRDGGVDLDAVADASRLASELLDAAETDGQGLVAGPYVLEVTSPGVERPLTEPRHWRRAIGRLVTVRDRDGIVLAGRVLSADESGADLAVATDPARPGRPPRRRLARVTFAQVARATVEVEFSAEAYDDLSIESVETPSLSAVLVEPGETADLGYGEPDDDLPAAPGRESNDDGREAGPRGAAGKEMTR
|
Required for maturation of 30S ribosomal subunits.
|
Q2J725
|
B1LAW8
|
MURB_THESQ
|
UDP-N-acetylmuramate dehydrogenase
|
unclassified Thermotoga
|
MDKIFESLYKAGCDVRMFEKLSCHTSIKIGGRVKYLVLPNDVFSLERAITVLKDFPFQIMGLGTNLLVQDEDLDIAVLKTERLNQIEIKGEKVLVESGTPLKRLCLFLMEAELGGLEFAYGIPGSVGGAIFMNAGAYGGEIGEFIEAVEVLKDGRKIWLSKNEIFFGYRDSTFKREKLIITRAMMSFKKEKKETIKAKMEDYMRRRLEKQPLDLPSAGSVFKRPREDFYVGKAIESLGLKGYRIGGAQISEKHAGFIVNTGSATFDDVMKLIEFVRKKVKEKYGVELETEVEIWWNGRQW
|
Cell wall formation.
|
B1LAW8
|
O33600
|
RAD50_SULAC
|
DNA double-strand break repair Rad50 ATPase
|
Sulfolobus
|
MIIREIRLQNFLSHEDTTVKFEGSINVIIGNNGAGKSSIIDGILFGLFKRTNRDIGKNEELIKKGKKSGQVSIKFEINGDTYLIDRNVGETSRDTISLLKEGKIITLARQSTTVNNKIKEILGFDHKILMSTTIIGQGSVESVFSDFPEVMKELLKINKLEMLRESNGPIHSLIKVLTDRIRSLQSIKDILKREEAEIDRLKKEIEEIKVKLENIEREAKEKEDELNQYNTEFNRIKEIKVQYDILSGELSVVNKKIEEIALRLKDFEEKEKRYNKIETEVKELDENREKINTISSFKSILVQIDSLKSQINVVENDLKRKKEKLKRKKELEEKEKQYEEIEKRKKELEEKEKQYEEIEKRLTYVLKNIERQKNEIEKLNYVDTQDLENKIKDVSDRINQIDNELKGLLDRRGDLNGRKEQTLKIYNNLNSIEDDRCPICGRPLDSEHKAKIREEIKVQLLELNKQITALQARINSLIKEREELEATRNKLQLELQKRSKEKGIYEAKLKELQRLEEEKNKLQNEILSLLSYHQEFENIAEKEKELIDYHEEYLKNSDILEEDIQEQEQRLNELNSKLSELEKSYNDYKAKYQFLPADLKSLVSLEERIRRRISELEKLKIEYERLKEEITRMKGLKEEYEKLKEEEDALLNRISELGYSEKRYKQLEEIIDKLSKILSGIEADKGKIKGSLEEKIKNIEEKERNIEELRNKMNEESKLNLGISKLQKLREVLDNKHLQSHIMNIVRNQIENNVNEVIAKFDLSFSAVEIDFVGKSELYVYTASGQKIHINALSGGERISIALALRLAIAKALMNQFSTLILDEPTVNLDEYRRKELIDVIRSAIEIVPQIILVTHDQELIQAGDYIIRVEKKGDTSKVEVSSYDR
|
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex.
|
O33600
|
Q9ZQB9
|
CSLCC_ARATH
|
Cellulose synthase-like protein C12
|
Arabidopsis
|
MAPKFEWWAKGNNNNTRKGTPVVVKMENPNNWSMVELESPSHDDFLVRTHEKSRNKNARQLTWVLLLKAHRAAGCLTSLGSALFALGTAVRRRIAAGRTDIEISSSGVGSLQKQNHTKKSKLFYSCLKVFLWLSLILLGFEIAAYFKGWSFGTSKLQLQFIFNKGFFDWVYTRWVLLRVEYLAPPLQFLANGCIVLFLVQSLDRLILCLGCFWIRFKKIKPVPKPDSISDLESGDNGAFLPMVLVQIPMCNEKEVYQQSIAAVCNLDWPKGKILIQILDDSDDPITQSLIKEEVHKWQKLGARIVYRHRVNREGYKAGNLKSAMNCSYVKDYEFVAIFDADFQPLPDFLKKTIPHFKDNEEIGLVQARWSFVNKEENLLTRLQNINLAFHFEVEQQVNSVFLNFFGFNGTAGVWRIKALEDSGGWLERTTVEDMDIAVRAHLHGWKFVFLNDVECQCELPESYEAYRKQQHRWHSGPMQLFRLCLPAVIKSKISIGKKFNLIFLFFLLRKLILPFYSFTLFCIILPMTMFVPEAELPAWVVCYIPATMSFLNILPAPKSFPFIVPYLLFENTMSVTKFNAMVSGLFQLGSAYEWVVTKKSGRSSEGDLAALVEKDEKTTKHQRGVSAPETEAEKKAEKTKRKKKKHNRIYMKELSLAFLLLTAATRSLLSAQGIHFYFLLFQGISFLLVGLDLIGEQVE
|
Probable beta-1,4-glucan synthase rather involved in the synthesis of the xyloglucan backbone than cellulose. Seems to work simultaneously with xyloglucan 6-xylosyltransferase. Xyloglucan is a noncellulosic polysaccharides of plant cell wall and consists of a glucan backbone substituted by xylose, galactose and fucose.
|
Q9ZQB9
|
P45097
|
QUEE_HAEIN
|
Queuosine biosynthesis protein QueE
|
Haemophilus
|
MLMEKYHDFEPNFNIVEIFESLQGEGFNTGMPSVFVRFGKCNLDCPWCDTPYNNFKRWSVSQILEKVRSFSSKNIIITGGEPTIVPKIEYLLEQFKSDGYFLAIETNGLKAIPAQIDYIATSPKSLYAHKYEKRCIPFANEVRIVMDSNMPSFCELIEQKIKAKNYYLSPCEIDGKMNLLETITLLGQLNQRSNKPKWQLSLQTHKLIGIE
|
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
|
P45097
|
P50218
|
IDHC_TOBAC
|
Oxalosuccinate decarboxylase
|
Nicotiana
|
MTFDKIKVENPIVEMDGDEMTRVIWKSIKDKLICPFLELDIKYFDLGLPHRDATDDKVTVESAEATQKYNVAIKCATITPDEARVKEFNLKSMWRSPNGTIRNILNGTVFREPIMCKNIPRLVPGWTKPICIGRHAFGDQYRATDTVIQGAGKLKLVFVPEGTDEKTEFEVYNFTGAGGVALSMYNTDESVRSFAEASMNMAYQKKWPLYLSTKNTILKKYDGRFKDIFQEVYEANWKSKYEEAGIWYEHRLIDDMAAYALKSEGGYVWACKNYDGDVQSDFLAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYRVHQKGGETSTNSIASIFAWTRGLAHRATLDNNERLLDFTEKLEAACIGAVESGKMTKDLALIIHGSKLSRDHYLNTEEFIDAVADELKARLLKAKA
|
May supply 2-oxoglutarate for amino acid biosynthesis and ammonia assimilation via the glutamine synthetase/glutamate synthase (GS/GOGAT) pathway.
|
P50218
|
P0CS52
|
TRM82_CRYNJ
|
Transfer RNA methyltransferase 82
|
Cryptococcus neoformans species complex
|
MALHCPPTALATSSTSLFIAAGPALHVFNPSTSTFASCAADGTGGLIRLLAVREDGEVAATLGEDKQLAVWDIQHDRPQFRHTRTVVKKGSCLSFAKDGSIILTDKVGDVYSYPLDPVPIDPSAERPPMYTLVADPSQNPDATYLLGHVSMLNAHVMTPDGRRIITADRDEHIRVSRYPKAYVIDKYLFGHDGFVSALHIPPSNPSLLLSAGGDPSLLIWNPSTGKLLTSVPVWPAVLSHRRVRSHLRRHKPGSRKLKMDPVPEDMDEENQTFYTAPEGYMLPSGQGVCIKKIESVKIGGETVVLFFSEGASAIHSFILPTDPEGVKPTVHTLPLPHPLIDFTPIPSTSSADEKEVLLSLDTAWDVLKKNPGPGIEGRQDTIQRDDLSDEEKRNISKIFSVARISADGHLSLGDASVYDSLVSNLPSTDIKTLSNVNLYPLLCVLPRWPGFEEGDEELTVNTGTPDTPGTPGPADAVSLAPTSGAFLQKSYTQEELEKMNTKQLGRLKSAGIDVGSILLARQKKAKEEHKARKAAAKAKAEAQKNQKEGGRPAKKKKKVEMSEEELANA
|
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
|
P0CS52
|
Q13F13
|
Y086_RHOPS
|
Nucleoid-associated protein RPD_0086
|
Rhodopseudomonas
|
MADFLGMMKQAAQLQSKMKAMQAELDQIEVEGSSGGGLVQVRMSAKMEVRGVSIDPSLLKPDEGGVLEDLLVAAHADAHRKAEAAMQEKMQALTGGLGLPPGLGLG
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q13F13
|
O93233
|
PLIB_GLOBS
|
Phospholipase A2 inhibitor
|
Gloydius
|
MKSSVPSLLIACLVMSLNSYTQQVLYCPPTPAPENVTEFVCNSPSLHEFPTGFPARAKMISVEFTQVSSLGVEALQGLPNLQELHLSNNRLKTLPSGLFRNLPQLHTLDLSTNHLEDLPPEIFTNASSLILLPLSENQLAELHPSWFQTLGELRILGLDHNQVKEIPISCFDKLKKLTSLDLSFNLLRRLAPEMFSGLDNLEKLILESNPIQCIVGRTFHWHPKLTVLSLKNSSLTNIMGFFQPLEQLELLDLSDNELTTMEPPVYKTSANLSLDLSGNPWACDCRLDNLLTWVNEHNIHLYSKEEIVCASPKHFKGECATSLHKSQICPC
|
Inhibits the enzymatic activity of the basic phospholipase A2 (PLA2).
|
O93233
|
B0JWU7
|
ATPL_MICAN
|
Lipid-binding protein
|
Microcystis
|
MNPTVAAASVIAAALAVGLAAIGPGVGQGTASGEAVSGIARQPEAEGRIRGTLLLSLAFMESLTIYGLVIALVLLFANPFA
|
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
|
B0JWU7
|
C1D973
|
Y2029_LARHH
|
Nucleotide-binding protein LHK_02029
|
Laribacter
|
MQLILISGLAGSGKSIALNVLEDSGYSCIDNLPLTLVPDTVERLAPLGYEQLAISIDTRDGASRLLEVIHALETAGHNVRFLFLEARTDTLIRRFSETRRRHPLSRTALTIPEAIARERQLLQAIAGLGHRIDTSDLSPNQLRRYLRDVIAQAPGRMLVVIQSFGFKHGVPLDADFVFDVRCLPNPYYDPALRPFTGRDAPIINFLTAEPLVQAMADELSGLALRWIPVFRHDNRNYLTFAIGCTGGQHRSVYLAETLAARLRETGETVLLRHRELDR
|
Displays ATPase and GTPase activities.
|
C1D973
|
Q864F6
|
MSHR_EULFU
|
Melanocortin receptor 1
|
Eulemur
|
MPAQGSQRGLLGAVNFTPTATPHLRPAANQTGPQCLEVSVPDGLFLCLGLVSLVENTLVVAAIAKNRNLHSPMYCFICCLALSDLLVSVSNLLETAVLLLLEVGALAAQATVVQQLGNVIDVLICSSMVSSLCSLGAIAMDRYISIFYALRYHSIVTLARARRAIAAVWAASILSSTLFITYYDRTAALLCLVVFFLAMLVLMALLYVHMLIQACQHAQAIARLHKRQHPVQQGWGLKGAATLTILLGVFFLCWGPFFLHLTLIAVCPQHPTCSCIFKNFRLFLALIICNTIVDPLIYAFRSQELRRTLKEVLLFSW
|
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.
|
Q864F6
|
A5FA76
|
TRPA_FLAJ1
|
Tryptophan synthase alpha chain
|
Flavobacterium
|
MNRITQKLQEDKKILSIYFSAGYPNLNDTVQIIQDLEKNGVDLIEIGLPFSDPLADGPTIQASSTQALHNGMTTQILFDQLQNIRESVKIPLIIMGYFNPMLQYGVEAFCKKCAEIGIDGLIIPDLPVDVYADEYKAIFEKYGLINVFLITPQTSDERIRFIDSVSNGFIYMVSSASVTGSQSGFGNVQETYFERISNLNLKNPQIVGFGISNKETFNQATKYAKGAIIGSAFIKHLSESGSGKIQEFVGEIR
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
A5FA76
|
Q1KXU9
|
PSAI_HELAN
|
Photosystem I reaction center subunit VIII
|
Helianthus
|
MTTLNFPSVLVPLVGLVFPAIAMASLFLHVQKNKIV
|
May help in the organization of the PsaL subunit.
|
Q1KXU9
|
Q2NQN1
|
RS17_SODGM
|
30S ribosomal protein S17
|
Sodalis
|
MSDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNDSNIGDIVEISECRPISKTKSWTLVRVVEKAIL
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
Q2NQN1
|
A3CN43
|
DAPA_STRSV
|
4-hydroxy-tetrahydrodipicolinate synthase
|
Streptococcus
|
MAYADLKNCKIITAFITPFHEDGSINFEAIPDLIEHLLAHHTDGILLAGTTAESPTLTHDEELELFAAVQKVVKGRVPLIAGVGTNETRDSIEFVKEVDEFGGFAAGLAIVPYYNKPSQEGMYQHFKAIADASNLPIIIYNIPGRVVVEMTPETMLRLAEHPNIIGVKECTSLANMAYLIEHRPEEFLIYTGEDGDAFHAMNLGADGVISVASHTNGDEMFEMLDAIEHNDIKKAAAIQRKFIPKVNALFSYPSPAPVKAVLNYLGFAAGPTRLPLVPAPEEDAKRIIKVVVDGDYQATKETVKGVLRPDY
|
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
|
A3CN43
|
A6NI79
|
CCD69_HUMAN
|
Coiled-coil domain-containing protein 69
|
Homo
|
MGCRHSRLSSCKPPKKKRQEPEPEQPPRPEPHELGPLNGDTAITVQLCASEEAERHQKDITRILQQHEEEKKKWAQQVEKERELELRDRLDEQQRVLEGKNEEALQVLRASYEQEKEALTHSFREASSTQQETIDRLTSQLEAFQAKMKRVEESILSRNYKKHIQDYGSPSQFWEQELESLHFVIEMKNERIHELDRRLILMETVKEKNLILEEKITTLQQENEDLHVRSRNQVVLSRQLSEDLLLTREALEKEVQLRRQLQQEKEELLYRVLGANASPAFPLAPVTPTEVSFLAT
|
May act as a scaffold to regulate the recruitment and assembly of spindle midzone components. Required for the localization of AURKB and PLK1 to the spindle midzone.
|
A6NI79
|
Q61845
|
MEIG1_MOUSE
|
Protein expressed in male leptotene and zygotene spermatocytes 278
|
Mus
|
MATSDVKPKSISRAKKWSEEIENLYRFQQAGYRDEIEYKQVKQVAMVDRWPETGYVKKLQRRDNTFFYYNKERECEDKEVHKVKVYVY
|
Essential for spermiogenesis.
|
Q61845
|
P07902
|
GALT_HUMAN
|
UDP-glucose--hexose-1-phosphate uridylyltransferase
|
Homo
|
MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHYHLGQKDRETATIA
|
Plays an important role in galactose metabolism.
|
P07902
|
Q2VL90
|
C163A_PIG
|
Soluble CD163
|
Sus
|
MDKLRMVLHENSGSADFRRCSAHLSSFTFAVVAVLSACLVTSSLGGKDKELRLTGGENKCSGRVEVKVQEEWGTVCNNGWDMDVVSVVCRQLGCPTAIKATGWANFSAGSGRIWMDHVSCRGNESALWDCKHDGWGKHNCTHQQDAGVTCSDGSDLEMGLVNGGNRCLGRIEVKFQGRWGTVCDDNFNINHASVVCKQLECGSAVSFSGSANFGEGSGPIWFDDLVCNGNESALWNCKHEGWGKHNCDHAEDAGVICLNGADLKLRVVDGVTECSGRLEVKFQGEWGTICDDGWDSDDAAVACKQLGCPTAVTAIGRVNASEGTGHIWLDSVSCHGHESALWQCRHHEWGKHYCNHDEDAGVTCSDGSDLELRLKGGGSHCAGTVEVEIQKLVGKVCDRSWGLKEADVVCRQLGCGSALKTSYQVYSKTKATNTWLFVSSCNGNETSLWDCKNWQWGGLSCDHYDEAKITCSAHRKPRLVGGDIPCSGRVEVQHGDTWGTVCDSDFSLEAASVLCRELQCGTVVSLLGGAHFGEGSGQIWAEEFQCEGHESHLSLCPVAPRPDGTCSHSRDVGVVCSRYTQIRLVNGKTPCEGRVELNILGSWGSLCNSHWDMEDAHVLCQQLKCGVALSIPGGAPFGKGSEQVWRHMFHCTGTEKHMGDCSVTALGASLCSSGQVASVICSGNQSQTLSPCNSSSSDPSSSIISEENGVACIGSGQLRLVDGGGRCAGRVEVYHEGSWGTICDDSWDLNDAHVVCKQLSCGWAINATGSAHFGEGTGPIWLDEINCNGKESHIWQCHSHGWGRHNCRHKEDAGVICSEFMSLRLISENSRETCAGRLEVFYNGAWGSVGRNSMSPATVGVVCRQLGCADRGDISPASSDKTVSRHMWVDNVQCPKGPDTLWQCPSSPWKKRLASPSEETWITCANKIRLQEGNTNCSGRVEIWYGGSWGTVCDDSWDLEDAQVVCRQLGCGSALEAGKEAAFGQGTGPIWLNEVKCKGNETSLWDCPARSWGHSDCGHKEDAAVTCSEIAKSRESLHATGRSSFVALAIFGVILLACLIAFLIWTQKRRQRQRLSVFSGGENSVHQIQYREMNSCLKADETDMLNPSGDHSEVQ
|
After shedding, the soluble form (sCD163) may play an anti-inflammatory role.
|
Q2VL90
|
P31204
|
TRPA_ANTSP
|
Tryptophan synthase alpha chain
|
unclassified Antithamnion
|
MNIISESLRSHPNSCALIPFITAGYPDINTTIQALYELDSQGADIIELGIPYSDALADGSVIQHSSLIALQGGTYIDQVLHILEVVSTKLNTPIIILPYYNPILKRGIEKFIKQISLMGAKGLIVPDLPLEETDELIVICNDNQIELVLFVAPTSSMKRINSISKKSPGCIYLVSSTGVTGVRDDIDIKVMELSNYIKKVSNKFIMLGFGISTPEHIKKIMKWNIDGVVVGSAFVKKLSALKIDDRISSISSLCKSLKKATIL
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
P31204
|
Q5WGQ3
|
MGSA_ALKCK
|
Methylglyoxal synthase
|
Alkalihalobacillus
|
MKIALIAHDKKKQELVDFCVAYEPILKEHELYATGTTGTRIMEATELVVTRFKSGPLGGDQQIGALVAENQFDLILFMRDPLTAQPHEPDVTALIRLCDVQSVPLATNMGTAEILIKGLERGDFAFRDIIHEQEKANPLKEG
|
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
|
Q5WGQ3
|
B8CW78
|
PNP_HALOH
|
Polynucleotide phosphorylase
|
Halothermothrix
|
MHKDWTIDVAGGKMKFETGKYAKQANGSVVARYGDTTVLVTATMSEPREGIDYFPLMVNYEERVYAIGKIPGSITRREGRPRDVATLAARLIDRPLRPLFPEGFRHDVQIIATVLSVDNDCEPDILALNGASVALTLSDIPFDGPIGGVKVGLVDGELVINPDEEEREKSKLDLTVAGTRDAVLMVEAGANEVSEDVMLDAIELAHQEIKRLVLLQEEIGEEAGKKKFEFTKDEITPELDEEIRKYISSDMENALRIPEKLERNAKVDEIKENTLQYFEDMFENNGLDNEEKNKQLKMVERTIEKVMKEKVRKMIIEEGIRPDGRKPDEIRPIWCEVGTLPRVHGSGVFTRGQTQALSVVTLGATSDEQILFGLGEEETKRYMHHYNFPPYSVGETSPLRSPGRREIGHGALGERALQPVIPDQEEFPYTIRVVSEVLESNGSTSQASICGSTLALMDAGVPIKEPVAGIAMGLLKEDEKVVILSDIQGLEDFYGDMDFKVAGTRNGITALQMDIKIHGISKEILKKALKRAREGRLYILDKMLQVIDKPRPELSPYAPLMITMKVSPDKIRHIIGPGGKIINKIIDETGVEIDIDDDGSVYILAQDQESGNRAKEIINKLTKEVEVGDIYEGRVKKITNFGAFVEILPGREGLVHISELADHHVKKVEDIVKIGDRIPVKVIEIDELGRINLSRKRALKEQKKE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
B8CW78
|
Q38870
|
CDPK2_ARATH
|
Calmodulin-domain protein kinase CDPK isoform 2
|
Arabidopsis
|
MGNACVGPNISGNGFLQTVTAAMWRPRIGAEQASSSSHGNGQVSKEAASEPATDQVQNKPPEPITMPSSKTNPETKLKPDLEIQPEEKKEKVLAEETKQKVVPEESKQEVPPEESKREVVVQPESAKPETKSESKPETTKPETTSETKPETKAEPQKPKHMRRVSSAGLRTESVLQRKTENFKEFYSLGRKLGQGQFGTTFLCLEKGTGNEYACKSISKRKLLTDEDVEDVRREIQIMHHLAGHPNVISIKGAYEDVVAVHLVMELCSGGELFDRIIQRGHYTERKAAELARTIVGVLEACHSLGVMHRDLKPENFLFVSREEDSLLKTIDFGLSMFFKPDEVFTDVVGSPYYVAPEVLRKRYGPESDVWSAGVIVYILLSGVPPFWAETEQGIFEQVLHGDLDFSSDPWPSISESAKDLVRKMLVRDPKRRLTAHQVLCHPWVQIDGVAPDKPLDSAVLSRMKQFSAMNKFKKMALRVIAESLSEEEIAGLKQMFKMIDADNSGQITFEELKAGLKRVGANLKESEILDLMQAADVDNSGTIDYKEFIAATLHLNKIEREDHLFAAFSYFDKDESGFITPDELQQACEEFGVEDARIEEMMRDVDQDKDGRIDYNEFVAMMQKGSIMGGPVKMGLENSISISLKH
|
May play a role in signal transduction pathways that involve calcium as a second messenger.
|
Q38870
|
P18970
|
HBA_AILME
|
Hemopressin
|
Ailuropoda
|
MVLSPADKTNVKATWDKIGGHAGEYGGEALERTFASFPTTKTYFPHFDLSPGSAQVKAHGKKVADALTTAVGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLASHHPAEFTPAVHASLDKFFSAVSTVLTSKYR
|
Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.
|
P18970
|
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