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Full Name
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147
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taxon
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46
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
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10
P09812
PYGM_RAT
Myophosphorylase
Rattus
MSRPLSDQDKRKQISVRGLAGVENVSDLKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVDRWIRTQQHYYAKDPKRIYYLSLELYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPPYFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDKFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELIRILVDLERLDWDKAWDVTVKTCAYTNHTVLPEALERWPVHLMETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEEYISDLDQLRKLLSYLDDQAFIRDVAKVKQENKLKFSAYLETEYKVHINPNSLFDVQVKRIHEYKRQLLNCLHIITLYNRIKREPNRFMVPRTIMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPAVGDRFRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEDNFFIFGMRVEDVERLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKDIVNMVMHHDRFKVFADYEEYIKCQDKVSELYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGLEPSRQRLPAPDEKI
Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
P09812
Q2QQA3
MAD20_ORYSJ
OsMADS20
Oryza sativa
MGRGKVQVRRIENEVSRQVTFSKRRPGLLKKAHEIAVLCDVDVAAIVFSAKGNLFHYASSHTTMERILEKYDRHELLSEGNNVIEEFPELEGSMSYDHIKLRGRIEALKKSQRNLMGQELDSLTLQDIQQLENQIDTSLNNIRSRKEKLLMEKNTILEKKITELETLHTCIRASPTKAAAPPACNTADAFVPNLNICCGDSGEPETVTAPLGWTSSNNGLPWWMLQSSSNGKS
Probable transcription factor.
Q2QQA3
Q65SV1
SUCC_MANSM
Succinyl-CoA synthetase subunit beta
Basfia
MNLHEYQAKQIFAQYGLPVSEGCACQSLEEAIQAVKKLGGGQWVAKCQVHAGGRGKAGGVKLVKSEEEVRSFFEKFLGQRLVTFQTDAKGQPVNAIYMEACANVKKELYLGAVLDRSSQRIVFMVSTEGGVNIEEVAEKTPHLLHKMPIDPLVGAMPYQGRELAFKLGLQGKQIQQFAQIFCQLGKMFVEKDLSLLEINPLVILDNDQLHCLDAKIVVDGNALYRQPELNAMRDPSQEDAREAAAEQWHLNYVALEGNIGCMVNGAGLAMGTMDIVKLHGGQPANFLDVGGGTTKERVAEAFKIILSDQSVKAILVNIFGGIVRCDLIAEGIVAAVNEVGVSVPVVVRLEGNNAPLGREILAQSGLNIIAATSLTDAAVQVVNAAEGK
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Q65SV1
Q88T65
LEPA2_LACPL
Ribosomal back-translocase LepA 2
Lactiplantibacillus
MKQSHIRNFAIIAHIDHGKSTLADQIMSLTQTVSAREQHAQLLDDMTVEQAHGVTVKARTVRNYYQADDGQEYEYNLIDTPGHVDFNYEVAKSLAATEGAILLVDATQGVQAQTIANYRIAKQRQLTLIPVLNKVDLPSADIDAALAQLNDLDSAFTPEQVLQISAKTGQGVPAVLEAIKQRLPAPQGDLHQPLKALVFDSLYDPYQGVIAYVRLIDGQLKSQQALCLMQGQQDFNGKAIGVFAPQMHPQESLSAGDVGYVVTGIKDPRKVRVGDTLTSVATPTQRPLAGYQPAKSMVFAGLYPKNNDYPALKEAVQKLNLNDPSFTYVEERSEALGVGFRCGFLGTFHLQIIRERLHDEYGVDVLTTAPNVTYHVTLTNGQQVIVNNPVQFPAFSLIKEVTEPFMKAEITMPADNLNAVLKLAEQHKGTLIDLANSGDLIVASLKIPLSEIAYHFFSELKSVSHGFASLSTAFMANEVSDLVKVEVDINYAPVDALTFIVHREDAPNMTQQLVANLKTTVPRQLYPTPVQARVEGKVIARVDVPPLRKNAAVNGEQHSTSKKAALLRRQSANKRRASKNTIKLPQSVFNAILSL
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Q88T65
P83468
PHP14_RABIT
Protein histidine phosphatase
Oryctolagus
MAAAGLAQIPDVDIDSDGVFKYVLIRVHAAPPSEAPGGESKDIVRGYKWAEYHADIYDKVSGELQKKGHDCECLGGGRISHQSQDRKIHVYGYSMGYGRAQHSVSTEKIRAKYPDYEVTWADDGY
May have a significant involvement in neuronal signaling.
P83468
A0KQA6
RL7_AERHH
50S ribosomal protein L7/L12
Aeromonas
MSITKDQIIEAVASMSVMEVVELIEAMEEKFGVSAAAAVMAGPAAAEAVEEKTEFDVVLTAAGANKVAVIKAVRGATGLGLKEAKDLVEAAPANLKEAVSKDEAEALKKELEAAGASVEIK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
A0KQA6
Q65V02
CCMA_MANSM
Heme exporter protein A
Basfia
MQSVNQLKIDRLACQRGDKILFTDLSFNLQSGDFVQIEGHNGIGKTSLLRILAGLAQPLSGKVRWNSEEISKCREEYYYDLLYLGHHAGIKPELTAWENLKFYQQAGHCRQGDEILWNVLEKVGLLGREDIVASQLSAGQQKRIALARLWISQAPLWILDEPFNAIDKNGVKVLTGLFEQQAEKGGIVILTSHQEVPSSALTVLNLAQYKFTDNE
Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system.
Q65V02
Q9N3S4
PUF60_CAEEL
60 kDa poly(U)-binding-splicing factor rnp-6
Caenorhabditis
MEENSADIENRPVAAFRPAVSVPMPVLPQDGEVFVGPGGKKDAQKIGLGLSKLSSKRKDDIQMAKKYAMDISIKQILLRQQKQQQENQQRQQMYSQALSIMSRIYVGSISFEIREDMLRRAFDPFGPIKSINMSWDPATGHHKTFAFVEYEVPEAALLAQESMNGQMLGGRNLKVNSMMFQEMRLPQNMPQAQPIIDMVQKDAKKYFRVYVSSVHPDLSETDLKSVFEAFGEIVKCQLARAPTGRGHRGFGYLEFNNLTSQSEAIAGMNMFDLGGQYLRVGKCVTPPDALTYLQPASVSAIPASVSVACAAITAKVMAAEAAAGSSPKTPSESGGSRAASPAPRAQSPATPSSSLPTDIENKAVISSPKKEPEEIEVPPLPPSAPDVVKDEPMEIEEEEEYTIPEEKPKPVAIVPPPGLAIPSLVAPPGLIAPTEIGIVVPNPSFLAQQQQKIEEKIEEEEEARTERVKLSTSQRKKMKREKLNQMTFEEKMAQVLGQQKAVQNQRMADPVTFGALDDTVAWKDPSNEDQTSEDGKMLAIMGPGRGGDNVASMALALMDGGSSLMLANNAKAKEAAAALALEPKKKKKVKEGKKIQPKLNTAQALAAAAKAGEMSDALKNEVMNSEDASLASQEGLEIRGNDARHLLMTKLMRTNRSNVIVLRNMVTPQDIDEFLEGEIREECGKYGNVIDVVIANFASSGLVKIFVKYSDSMQVDRAKAALDGRFFGGNTVKAEAYDQILFDHADYTG
DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation (Probable). Ensures the correct splicing of genes involved in immunity to promote longevity in response to infection by pathogenic bacteria such as S.aureus .
Q9N3S4
Q8BL95
CF298_MOUSE
Protein kurly homolog
Mus
MVVLHVKRGDESQFLLQAPGSTELEELTAQVARVYNGRLKVHRLCSEMEELAEHGVFLPPNMQGLTDEQIEELKLKDEWGEKCVPSGGSVFTKDEIGRRNGQAPNEKMKQVLKKTVEEAKAIVSKKQVEAGVFVTMEMVKDALDQLRGAVMIVYPMGLPPYDPIRMEFENKEDLSGTQAALEVIQESEAQLWWAAKELRRTKKLSDYVGKNEKTKIIVKIQQRGQGAPAREPVISSEEHKQLMLFYHRRQEELKKLEENDDDSCLNSPWADNTALKRHFHGVKDIKWRPR
Plays a role in motile cilium function, possibly by acting on outer dynein arm assembly. Seems to be important for initiation rather than maintenance of cilium motility. Required for correct positioning of cilia at the apical cell surface, suggesting an additional role in the planar cell polarity (PCP) pathway. May suppress canonical Wnt signaling activity.
Q8BL95
Q9M9Q6
SCP50_ARATH
Serine carboxypeptidase-like 50
Arabidopsis
MEQATTLFILLSTLLLAVSVESPQPPLFPDEALPTKSGYLPVKPAPGSSMFYAFYEAQEPTTPLPDTPLLVWLQGGPGCSSMIGNFYELGPWRVVSRATDLERNPGAWNRLFGLLFVDNPIGVGFSIAASQQDIPTNQRQVAEHLYAALVEFLEQNPSFENRPVYFTGESYAGKYVPAIGYYILKEKPNGKVNLKGLAIGNGLTDPVTQVQTHAVNVYYSGLVNAKQRVELQKAQEISVALVKSQKWREAADARTELLTLLSNMTGLATLYNTARAIPYRTDLVVDLLNQREAKRVLGVSETVRFEECSDEVEDVLRADVMKSVKFMVEYALERTQVLLYQGMLDLRDGVVSTEEWMKTMNWSGLGMFSTAERRVWKDEDGVVAGYVQRWGNLCHVAVTGAGHFVPTDKAVNSRDMIEGWVLGKGLFGGKDVKQTTSSSLYHSI
Probable carboxypeptidase.
Q9M9Q6
Q5LWJ6
DNAK_RUEPO
Heat shock protein 70
Ruegeria
MGKVIGIDLGTTNSCVAIMDGAQPKVIENSEGARTTPSIVAFTDEERLVGQPAKRQAVTNPSNTIFGVKRLIGRRVDDAEVTKDKKMVPFTIVNGGNGDAWVEAKGEKYSPSQISAVILGKMKETAESYLGEEVTQAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKNSQTIAVYDLGGGTFDVTILEIDDGLFEVKSTNGDTFLGGEDFDMRIVNYLADEFKKEHGVDLSGDKMALQRLKEAAEKAKIELSSTTQTEINQPFISMGANGQPLHLVMKLTRAKLESLVGDLIKKSMDPCKAALKDAGISPSDVDEVVLVGGMTRMPKVFEEVTKFFGKEPHKGVNPDEVVAMGAAIQAGVLQGDVKDVVLLDVTPLSLGIETLGGVFTRLIDRNTTIPTKKSQVFSTAEDNQNAVTIRVFQGEREMAADNKILGQFNLEDIPPAPRGMPQIEVTFDIDANGIVSVSAKDKGTGKEHKITIQASGGLSDEDIEKMVKDAEENAEADKARKELVEARNQAESLIHSTEKSVEEHGDKVDPTTVEAIELAIAALKDDLDKDGVSAEKIKSGLQNVTEAAMKLGEAIYKAQSEGGDDEPAAADARPSDDDIVDAEFEDLGEDKRK
Acts as a chaperone.
Q5LWJ6
Q6D0J6
COAE_PECAS
Dephosphocoenzyme A kinase
Pectobacterium
MTYIVALTGGIGSGKSTVADEFAKLGTTIVDADIIARQVVEPGKPALDAIRLRFGDAVLNADGSLNRSALRQRIFSSPEEKQWLNNLLHPLIHQETQAQFRAISTPYILWVVPLLVENGLQQRAQRILVVDVDRKTQLERTLARDGISLQQAENILAVQATREQRLACADDIIDNSRCPNALAQQVAELHRHYLELAASAADRMAKNE
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Q6D0J6
Q9UXS5
RL10_PYRAB
Acidic ribosomal protein P0 homolog
Pyrococcus
MAHVAEWKKKEVEELANLIKSYPVIALVDVSSMPAYPLSQMRRLIRENGGLLRVSRNTLIELAIKKAAQELGKPELEKLAEYIDRGAGILVTNMNPFKLYKFLQQNRQPAPAKPGAVVPKDVVIPAGPTPLAPGPIVGQMQAMGIPARIERGKVTIQKDTTVLKAGEVITPELANILNALGIQPLEVGLDVLAVYEDGIVYTPDVLAIDEQEYIDMVQKAYMHAFNLAVNIAYPTPETIEAIIQKAFLNAKAVAVEAGYITKETIQDILGRAFRAMLLLAQQLPDELLDEKTKELLSAQAQVAVAPQEVEEEKKEEEEKKEEEEEEASEEEALAGLSALFG
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Q9UXS5
Q7L266
ASGL1_HUMAN
Isoaspartyl peptidase/L-asparaginase beta chain
Homo
MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP
Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
Q7L266
Q0VC24
WDR12_BOVIN
WD repeat-containing protein 12
Bos
MAQLQTRFFTDNKKYAVDDVPFSIPAASEIADLSNLINKLLEAKNEFHKHVEFDFLIKGQFLRMPLFKHMELENISSEEVVELEYVEKYTAPQPEQCMFHDDWISAIEGTEEWILTGSYDKTSRIWSLEGKSIMTIVGHTDVVKDVAWVKKDSLSCLLLSASMDQTILLWEWNVERNKVKALHCCRGHAGSVDSIAVDSTGTKFCSGSWDKMLKIWSTVPTDEEDEMEESTNRPRKKQKTEQLGLTRTPIVTLSGHKEAISSVLWSDAEEICSASWDHTIKVWDVESGSLKSTLTGNKVFNCISYSPLCKRLASGSTDRHIRLWDPRTKDGSLVSLSLTSHTGWVTSVKWSPTHEQQLISGSLDNMVKLWDTRSCKAPLYDLAAHEDKVLSVDWTDSGLLLSGGADNKLYSYRYSPTTSHVGA
Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Q0VC24
A7MEQ8
CLPS_CROS8
ATP-dependent Clp protease adapter protein ClpS
Cronobacter
MSKDKSWLDFDHLAEDDLREALKPPSMYKVILMNDDYTPMEFVIDVLQKFFSYDVERATQLMLTVHYQGKAICGVFTAEVAETKVALVNKYARENDHPLLCTLEKA
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
A7MEQ8
B4UEK4
ISPH_ANASK
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
unclassified Anaeromyxobacter
MDVKIAKTAGFCWGVRRTVDKVMEVADQHRAPVVTLGPIIHNPQAVARFSEKGVGTVNGIGEVTDGTTVVVRTHGAVREELERAEARGLEVVDGTCPYVKYPQAMAQRLSREGYHIVIVGDANHAEIKGVISYSEQPCTVVKPGGPVPEIKAKKVAVIAQTTCIGAEFERVVGVLALRHKEVRAVNTICNDTEERQADARALASEVDAVVVVGGKNSANTRHLAEICRAIQPRTWHVETEAELGAAWFEGCRVVGLSAGASTPDWVVEGVAAWLRALR
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
B4UEK4
B8E9X6
FLGI_SHEB2
Basal body P-ring protein
Shewanella
MKYKLVLAVAVLVFSLPSQAERIKDIANVQGVRSNQLIGYGLVVGLPGTGEKTSYTEQTFMTMLKNFGINLPDNVKPKIKNVAVVAVHADMPAFIKPGQDLDVTVSSLGEAKSLRGGTLLQTFLKGVDGNVYAIAQGSLVVSGFSADGLDGSKVIQNTPTVGRIPNGAIVERSVATPFSTGDYLTFNLRRSDFSTAQRMADAINELLGPDMARPLDATSVQVSAPRDVSQRVSFLATLENLDVIPAEESAKVIVNSRTGTIVVGQNVRLLPAAITHGGMTVTIAEATQVSQPNALANGQTTVTSNSTITATESDRRMFMFNPGTTLDELVRAVNLVGAAPSDVLAILEALKVAGALHGELIII
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
B8E9X6
B5Z9N6
LUXS_HELPG
Autoinducer-2 production protein LuxS
Helicobacter
MKTPKMNVESFNLDHTKVKAPYVRIADRKKGVNGDLIIKYDVRFKQPNQDHMDMPSLHSLEHLVAEIIRNHANYVVDWSPMGCQTGFYLTVLNHDNYTEILEVLEKTMQDVLKATEVPASNEKQCGWAANHTLEGAKNLARAFLDKRAEWSEVGV
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
B5Z9N6
P26994
EXSB_PSEAE
Pilotin
Pseudomonas
MLLPLALLLGGCVSQPAPMSPKVTVGGSVGGVSLQARQAQLRLRLYAVVQGRMQTIAERRYRVSGLPLRYAFDLEVDRLEGEALYLRTELSWVGVAAVQASAWQQVAAGVDERVRLVRRDCFPNCTAARPEERSGND
Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells . Pilot protein that is required for the proper localization of the secretin PscC in the outer membrane . Necessary for full in vivo virulence .
P26994
Q8N442
GUF1_HUMAN
Ribosomal back-translocase
Homo
MWTLVGRGWGCARALAPRATGAALLVAPGPRSAPTLGAAPESWATDRLYSSAEFKEKLDMSRFPVENIRNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQVLDKLQVERERGITVKAQTASLFYNCEGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSDECIKISAKLGTNVESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVLNPNEQPTHKLYAGQVGYLIAGMKDVTEAQIGDTLCLHKQPVEPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKLIKEHREKEITIINPAQFPDKSKVTEYLEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAELVKMDILLNGNTVEELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLKRQAEGKKKLRKIGNVEVPKDAFIKVLKTQSSK
Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Q8N442
A3PMI6
PQQA_CERS1
Pyrroloquinoline quinone biosynthesis protein A
Cereibacter
MAWKTPRYDETPVGMEINMYACAKRK
Required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. PQQ is probably formed by cross-linking a specific glutamate to a specific tyrosine residue and excising these residues from the peptide.
A3PMI6
F4K2G3
MORC5_ARATH
Protein CRT1-homolog 5
Arabidopsis
MAESGSTNPKSPSVVPDSTLGGLKRDLRNYHDGDDSNNLSIKKSKTTKMENNCREIVPLDVTPLSIVPPDTPKLSRQFWKAGDDDEAAPVPLYCSNDAAVRVHPQFLHANATSHKWALGALAELLDNSLDEVSNGATYVHVDSTINKRDGKSSILIVEDNGGGMNPSTFRECLSLGYSRKRNMANRVGQYGNGFKTSTMRLGADAIVFSRSRGINGNNPTQSIGMLSYTFLYETRKCEAIVPTVDYELVDNKWKEIVYNSTNEWLDNLETILRWSPYLSQQDLLDQFNHLEEQGTRIVIYNLWEDDEGKMELDFDTDPHDIQLRGVNRDEKNIDMAKTYPNSRHFLTYRHSLRSYASILYLKRPDNFRIILRGEDVEHHSVLDDMMKIEEKTYKPMRSPEWPDQEEMVASLKLGFVKDAHHHIDIQGFNVYHKNRLIKPFWRVWNAAGSDGRGVIGILEANFIQPAHNKQGFERTVVLAKLESRLVTHQKNYWSSRCHEIGYAPRRKQKNYESSVTETPRPFNNINVVKGSSSSTPVPVRVFRPNVEPSGRNQIPQVETRERSFDINPEIGAKNRSYYGLGISSFKETGSVNLEAELQKVKQESAKLVSELQRQKQLLELQLQESKAKIQNLEKAQREKEVLELQLKESKARIQNLENRQEGVSTIFQQERARRDVTEDGLRKKLREASDVIDGLRKQVDTFKGKRIL
Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing.
F4K2G3
Q2NT72
CLSA_SODGM
Cardiolipin synthase A
Sodalis
MTTLYTVINWLLLFGYWLLIAGVTLRVMMKRRAVPSAMAWLLVIYILPLVGIITYLLFGELNLGKRRAERSKALWPSTAKWIEDLKGCRRIFASENSEVARALFQLCEHRQGMGGLKGNQMQLLTSSDDALRALVRDIGLAQKNIEIVFYIWQSGGLVDQVAEALMAVARRGVRCRLMLDSAGSVDFFRSPYPALMRAAGVHVVEALHVSLLRVFLRRMDLRQHRKMVLIDNYVAYTGSMNMVDPRFFKQDAGVGQWIDIMARMEGPVATAMGIIFSCDWEIETGERILPPLPDVNIMPFEQATGHTIQVIASGPGFPEGVIHQALLTSIYAAREQLVMTTPYLVPSDDLLQAICTAAQLGVEVHIIVPRHNDSMLVGWASRAFFAELLEAGVLIHQFEGGLLHTKSVLVDGQLSLVGTVNLDMRSLWLNFEITLVIDDDDFGSDLARVQEDYIARSRLIEPKVWSKRPYWQRIVERLFYFFSPLL
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Q2NT72
Q6EPF0
ROC5_ORYSJ
Protein RICE OUTERMOST CELL-SPECIFIC 5
Oryza sativa
MSFGGLFDGGGGGGMQFPFASGFASSPALSLALDNAGGGIGGRMLGGGAGAGSSAGGAMTRDTEAENDSRSGSDHLDAISAAGEDDVEDAEPSNSRKRKKRYHRHTPQQIQELEALFKECPHPDEKQRAELSRRLSLDARQVKFWFQNRRTQMKTQLERHENALLKQENDKLRAENMTIREAMRSPMCGSCGSPAMLGEVSLEEQHLRIENARLKDELNRVCALATKFLGKPISLLSPPPLLQPHLSLPMPNSSLELAIGGIGGLGSLGTLPGCMNEFAGGVSSPMGTVITPARATGAAIPSLVGNIDRSVFLELAISAMDELVKMAQMDDPLWVPALPGSPSKEVLNFEEYLHSFLPCIGMKPAGYVSEASRESGLVIIDNSLALVETLMDERRWSDMFSCMIAKATVLEEVSTGIAGSRNGALLLMKAELQVLSPLVPIREVTFLRFCKQLAEGAWAVVDVSIDGLVRDHNSGTAPTGGNVKCRRVPSGCVMQDTPNGYCKVTWVEHTEYDEASVHQLYRPLLRSGLAFGARRWLATLQRQCECLAILMSSATVTANDSTAISQEGKRSMLKLARRMTENFCAGVSASSAREWSKLDGATGSIGEDVRVMARKSVSEPGEPPGVVLSAATSVWVPVAPEKLFNFLRDEQLRAEWDILSNGGPMQEMTQIAKGQRDGNSVSLLRASAVSANQSSMLILQETCTDASGSIVVYAPVDIPAMQLVMNGGDSTYVALLPSGFAILPDGPRIGATGYETGGSLLTVAFQILVNNQPTAKLTVESVETVNNLISCTIKKIKTALQCDA
Probable transcription factor.
Q6EPF0
Q6BKW8
H2A1_DEBHA
Histone H2A.1
Debaryomyces
MSGGKGKAGSSEKASTSRSAKAGLTFPVGRVHRLLRKGNYAQRVGSGAPVYLTSVLEYLAAEILELAGNAARDNKKSRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVLPNIHQNLLPKKSAKGKASQEL
Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.
Q6BKW8
B4TY46
AROB_SALSV
3-dehydroquinate synthase
Salmonella
MERITVTLGERSYPITIAAGLFNEPASFLPLKSGDQVMLVTNETLAPLYLDKVRGVLERAGVNVDSVILPDGEQYKSLTVLDTVFTALLKKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLKTLPARELASGLAEVIKYGIILDADFFTWLEENLDALLRLDGPAMAYCIRRCCELKAEVVAADEREAGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGIVMAARASERLGQFSSADTQRIIALLERAGLPVNGPCEMSAQDYLPHMLRDKKVLAGELRLVLPLAIGKSEVRGGVSHEVVLSAIADCQQA
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
B4TY46
B1JB30
SURE_PSEPW
Nucleoside 5'-monophosphate phosphohydrolase
Pseudomonas
MRILISNDDGVTAPGLAALHGALVDYAECVVIAPDQDKSGAGSSLTLDRPLHPQTLANGFISLNGTPTDCVHLGLNGLLPETPDMVVSGINLGANLGDDVIYSGTVAAALEGRFLGGTSLAFSLLSRLPDNLPSAAFIARRLVEAQSRLELPPRTVLNVNIPNLPLEHIRGIQVTRLGHRARAAAPTKVVNPRGKEGYWIAVAGDAEDGGPGTDFHAVMQGYVSITPLQLDRTFNDAFEQLHGWLEGVL
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
B1JB30
Q9KV40
MURB_VIBCH
UDP-N-acetylmuramate dehydrogenase
Vibrio
MQIQLGANLKPYHTFGIEQLAAQLVVAESIDDLKALYCSAEWASLPKLIIGKGSNMLFTCHYTGMIVVNRLNGIEHQQDDDYHRLHVAGGEDWPSLVSWCVEQGIGGLENLALIPGCAGSAPIQNIGAYGVEFKDVCDYVEYLCLETGTVKRLTMEECQFGYRDSIFKHQLYQKAVVTAVGLKFAKAWQPIIQYGPLKDLSSDCAIHDVYQRVCATRMEKLPDPAVMGNAGSFFKNPVISQQAFARLQIEHPDVVAYPAEQGVKVAAGWLIDQAGLKGHQIGGAKVHPKQALVIVNTGDASAQDVLMLAADIQQRVFNCYGIELEHEVRFIGESEETNLKQWMSEQA
Cell wall formation.
Q9KV40
B7GIU7
MTNN_ANOFW
S-adenosylhomocysteine nucleosidase
Anoxybacillus
MNIAIIGAMEEEVAILREKIANRTETTVANCSFYSGTLDGANVVLLKSGIGKVNAAMSTTILLERFAPDVVINTGSAGGFAPSLNVGDIVISTEVVHHDVDVTAFGYAYGQVPGMPARYAADERLIQAAETSAAHIRDIQVAKGLIATGDSFMHDPARVDFVRTQFPDLYAVEMEAAAIAQVCHQFNVPFVVIRALSDIAGKESNVSFEQFLQKAALHSSELVQLMVNELNK
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine.
B7GIU7
Q9FRH4
IDD16_ARATH
Protein indeterminate-domain 16
Arabidopsis
MELTQPIRENGDPQGHQLTDPDAEVVSLSPRTLLESDRYVCEICNQGFQRDQNLQMHRRRHKVPWKLLKRDKKDEEVRKRVYVCPEPTCLHHDPCHALGDLVGIKKHFRRKHSVHKQWVCERCSKGYAVQSDYKAHLKTCGSRGHSCDCGRVFSRVESFIEHQDTCTIRQPQPTNHRHLQQHTMGLDAPSRTTSTASFGPLLHGLPLLRPPRPSNQHSPAFAYPFNASSAPFESLELQLSIGMARTSAQARHNEKRETSLTKERANEEARKAEETRQEAKRQIEMAEKDFEKAKRIREEAKTELEKAHVVREEAIKRINATMMEITCHSCKQLFQLPVTADESTSSLVMSYVSSATTEGECE
Transcription factor regulating lateral organ morphogenesis and gravitropic responses . Has a redundant role with IDD14 in directing leaf and floral organ morphogenesis . Acts cooperatively with IDD15 to control silique and branche orientation . Involved in the establishment of auxin gradients through the regulation of auxin biosynthesis and transport .
Q9FRH4
Q6QLR2
GLL7_CHICK
Gallinacin-5
Gallus
MRILYLLLSVLFVVLQGVAGQPFIPRPIDTCRLRNGICFPGICRRPYYWIGTCNNGIGSCCARGWRS
Has bactericidal activity.
Q6QLR2
B1AIM3
RL2_UREP2
50S ribosomal protein L2
Ureaplasma
MAVKRIKNHSSGKRQTVVVDYKSILTTSKPEKSLLVTLPKKAGRNNQGKITIRHHGGGHKRKYRIIDFKRNKDNIYGTIKSIEYDPNRTSFISLVVYADGEKRYIIAPKGIKVGDKIISGNENIDILLGNSLPLEFIPEGTLVHNIELSPNAGGQITRSAGASAQILGFDETKKYILVKLNSGEVRKFRKECRATIGTVSNDEHILENLGKAGKSRHLGVRPTVRGSAMNPNDHPHGGGEGRSPVGMDAPRTPWGKRHMGVKTRNNKKSSTSMIVRRRK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
B1AIM3
P28324
ELK4_HUMAN
Serum response factor accessory protein 1
Homo
MDSAITLWQFLLQLLQKPQNKHMICWTSNDGQFKLLQAEEVARLWGIRKNKPNMNYDKLSRALRYYYVKNIIKKVNGQKFVYKFVSYPEILNMDPMTVGRIEGDCESLNFSEVSSSSKDVENGGKDKPPQPGAKTSSRNDYIHSGLYSSFTLNSLNSSNVKLFKLIKTENPAEKLAEKKSPQEPTPSVIKFVTTPSKKPPVEPVAATISIGPSISPSSEETIQALETLVSPKLPSLEAPTSASNVMTAFATTPPISSIPPLQEPPRTPSPPLSSHPDIDTDIDSVASQPMELPENLSLEPKDQDSVLLEKDKVNNSSRSKKPKGLELAPTLVITSSDPSPLGILSPSLPTASLTPAFFSQTPIILTPSPLLSSIHFWSTLSPVAPLSPARLQGANTLFQFPSVLNSHGPFTLSGLDGPSTPGPFSPDLQKT
Involved in both transcriptional activation and repression. Interaction with SIRT7 leads to recruitment and stabilization of SIRT7 at promoters, followed by deacetylation of histone H3 at 'Lys-18' (H3K18Ac) and subsequent transcription repression. Forms a ternary complex with the serum response factor (SRF). Requires DNA-bound SRF for ternary complex formation and makes extensive DNA contacts to the 5'side of SRF, but does not bind DNA autonomously.
P28324
B6IN25
YQGF_RHOCS
Putative pre-16S rRNA nuclease
Rhodospirillum
MAIRNLMELKASLPRNGRLMGLDLGEKTIGLAVSDPGLSVASPVGTIRRTKFTQDAQELARAMRDRDVRALVVGLPVNMDGTEGPRCQSVREFSRLLLQRPQLFGFEPEIAFWDERLSTSAVERMMIGWDMTRKRRDEVVDKMAAAYILQGALDRLRQGDAAPGGSDDERDEDGDTDGEDGGGDGGGE
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
B6IN25
Q9NES8
PPP5_CAEEL
Serine/threonine-protein phosphatase 5
Caenorhabditis
MAATITDDIVATVLESIEEKSYEDEKEKAGMIKDEANQFFKDQVYDVAADLYSVAIEIHPTAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDARAKFDECSKIVRRQKFEAAISTDHDKKTVAETLDINAMAIEDSYDGPRLEDKITKEFVLQLIKTFKNQQKLHKKYAFKMLLEFYNYVKSLPTMVEITVPTGKKFTICGDVHGQFYDLCNIFEINGYPSETNPYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLFKEDGVTLEDIRKTDRNRQPPDEGIMCDLLWSDPQPINGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGAFITITGDNLTPRFTPFDAVPHPKLPPMAYANSLFGFN
Serine/threonine-protein phosphatase . Dephosphorylates cdc-37 . Probably by dephosphorylating separase sep-1, may be involved in sep-1-mediated exocytosis of cortical granules during meiotic anaphase and mitotic cytokinesis .
Q9NES8
B2IMY3
RNZ_STRPS
tRNase Z
Streptococcus
MDIQFLGTGAGQPSKARNVSSLALKLLDEINEVWLFDCGEGTQNRILETTIRPRKVSKIFITHLHGDHIFGLPGFLSSRAFQANEEQTDLEIYGPQGIKSFVLTSLRVSGSRLPYRIHFHEFDQDSLGKILETDKFTVYAEELDHTIFCVGYRVMQKDLEGTLDAEKLKAAGVPFGPLFGKIKNGQDLVLEDGTEIKAADYISAPRPGKIITILGDTRKTDASVRLAVNADVLVHESTYGKGDEKIARNHGHSTNMQAAQVAVEAGAKRLLLNHISARFLSKDISKLKKDAATIFENVHVVKDLEEVEI
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
B2IMY3
Q4L888
RPOA_STAHJ
Transcriptase subunit alpha
Staphylococcus
MIEIEKPRIETIEISEDAKFGKFVVEPLERGYGTTLGNSLRRILLSSLPGAAVKYIEIEGVLHEFSAIDNVVEDVSTIIMNIKKLALKIYSEEDKTLEIDVRDEGEVTASDITHDSDVEVLNPELKIATVSKGGHLKIRLVANKGRGYALAEQNNTSDLPIGVIPVDSLYSPVERVNYTVENTRVGQSSDFDKLTLDVWTNGSITPQESVSLAAKILTEHLNIFVGLTDEAQNAEIMIEKEEDQKEKVLEMSIEELDLSVRSYNCLKRAGINSVQELADKSEADMMKVRNLGRKSLEEVKYKLEDLGLGLRKED
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q4L888
A4W9Y2
TUS_ENT38
DNA replication terminus site-binding protein
Enterobacter
MATYDLIERLNSTFRQIELELVTLTERLKGCRLLAARVFTLPDVAKGAEHDELNTIEVEQHIGQEAVALTLAHYRHLFIHQQSEKRSSKAAVRLPGVICLQCDGALREEIESQIAHINTLKMAFEKIITEESGLPPAARFEWVHRQLPGLITLNAYRSLTVLRQPATLRFGWANKHIIKNFTRDDVLSLLEKSLKSPRTVTPWSREQWIERLEEEYDNIAALPAETRLKIKRPVKVQPIARVWYAGQQKQVQYACPTPMIALFDAEQGAMVPDIGELLNYDADNIQHRYKPQAQPLRLIIPRLHLYVAE
Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.
A4W9Y2
Q9RW62
LGT_DEIRA
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Deinococcus
MPRRGPFLALFAGCVSRGASRSPPGHTLTRRPMDPVFLQIGNFTIAWYGVLMMLGIAAGYWLGLKLARERGLNADLFERMILWMLFWGFVGARLVFVLTSWHIFEGIPFPRVLLDIVNLRNGGISIHGGLIGGVLTLIYFARRYRLNFYQYADLAVPGVAFGIIGGRLGNIMNGTDTVGRVTGWPIGYHWPASARAFHEGMCRPNPNPDMDLSKYCHEVGGQIMMTAPVHFTQLYGVIIGIILAVASYFWLKSRVPGWAFWQFWLWYSILRAGWEETFRLNPLTIKTYLNQGLDAPGIGLWTDTQIFSVPLILVSLWMLWRLRQRRQVTVPTVPVQSQS
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Q9RW62
B4K7S5
EI3G2_DROMO
Eukaryotic translation initiation factor 3 subunit 4-2
Drosophila
MKPTITSWADEVEADYVDGLPPSKEHVDGDYKHVTEYKFNDEGKKIKVVRSFKIEKKIVSRAVAKRRNWTKFGDSKLDKPGPNSYTTKVADEILMNYMGSKDFEHTQDPLDASKPIAKCRICNGEHWSVKCPYKGTSMDIESKAIAAATAAVGETNKAGKYVPPFLKEGGKGRERDDSSAVRISNLSESMTEDDLEELVKKIGPHTKMYLAREKNSGLCKGFAYVHFKYRKDAAEAIEILNGHGYDHLILSVEWSKPQN
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA.
B4K7S5
P23890
CADC_ECOLI
Membrane-integrated pH sensor CadC
Escherichia
MQQPVVRVGEWLVTPSINQISRNGRQLTLEPRLIDLLVFFAQHSGEVLSRDELIDNVWKRSIVTNHVVTQSISELRKSLKDNDEDSPVYIATVPKRGYKLMVPVIWYSEEEGEEIMLSSPPPIPEAVPATDSPSHSLNIQNTATPPEQSPVKSKRFTTFWVWFFFLLSLGICVALVAFSSLDTRLPMSKSRILLNPRDIDINMVNKSCNSWSSPYQLSYAIGVGDLVATSLNTFSTFMVHDKINYNIDEPSSSGKTLSIAFVNQRQYRAQQCFMSIKLVDNADGSTMLDKRYVITNGNQLAIQNDLLESLSKALNQPWPQRMQETLQKILPHRGALLTNFYQAHDYLLHGDDKSLNRASELLGEIVQSSPEFTYARAEKALVDIVRHSQHPLDEKQLAALNTEIDNIVTLPELNNLSIIYQIKAVSALVKGKTDESYQAINTGIDLEMSWLNYVLLGKVYEMKGMNREAADAYLTAFNLRPGANTLYWIENGIFQTSVPYVVPYLDKFLASE
Regulates the lysine- and pH-dependent expression of the lysine decarboxylase CadA and the cadaverine-lysine antiporter CadB . At low external pH, and in the presence of external lysine, CadC activates transcription of the cadBA operon by binding directly to two sites, Cad1 and Cad2, within the cadBA promoter region (Pcad) . Preferentially binds to AT-rich regions within the Cad1 promoter .
P23890
A7DTF0
MRG1_CAEEL
Mortality factor related protein 1
Caenorhabditis
MSSKKNFEVGENVACIYKGKPYDAKITDIKTNSDGKELYCVHFKGWNNRYDEKIPVGEEKDRIFKGTASEYAEKHNAELPTTALKPKKKSLAAEAPRDDRDDTPGTSKGKKAKSVTIAPVMTADDMKVELPKPLRKILIDDYDLVCRYFINIVPHEYSVDQIIEDYIKTIPVSNEQMRTVDDLLIEYEEADIKITNLALICTARGLVDYFNVTLGSSYQLLYKFERPQYNDLVKKRAMEKGIDITNPTALQDSGFRPSQEYGIVHFLRMLAKLPDYLKLTQWNDHVINRIMIGVHDLIVFLNKNHGKYYRGSSDYQGASNDYYRRSLAADDGVGANQ
Protein involved in the remodeling of chromatin thereby regulating various processes including transcription, chromosome synapsis and genome integrity . Mainly binds genomic loci carrying trimethylated histone H3 'Lys-36' (H3K36me3) or 'Lys-4' (H3K4me3), and acetylated histone H3 'Lys-9' (H3K9ac), 'Lys-27' (H3K27ac) . During meiosis, required for the presynaptic pairing of homologous chromosomal regions outside of the pairing center and for the progression of chromosome synapsis . Essential maternal factor required in postembryonic germline development and in maintaining germ cell identity . Plays an important role in maintaining genomic integrity in primordial germ cells (PGCs) during meiosis by regulating DNA double-strand break (DSB) repair and synapsis . Also, required for chromatin-based transcriptional silencing in PGCs and for silencing of X-linked genes in the maternal germ line . By retaining histone acetyltransferase, cbp-1, in euchromatin, promotes the anchoring of heterochromatin at the inner nuclear membrane in intestinal and hypodermal cells .
A7DTF0
Q3KMC6
ACP_CHLTA
Acyl carrier protein
Chlamydia
MSLEDDVKAIIVDQLGVSPEDVKVDSSFIEDLNADSLDLTELIMTLEEKFAFEISEDDAEQLRTVGDVIKYIQERQN
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Q3KMC6
A7HQQ1
CH10_PARL1
Chaperonin-10
Parvibaculum
MKFRPLHDRVVVRRVEEESKTAGGIIIPDSAQEKPSQGEVVAVGPGARGDDGKLVALDVKVGDRVIFGKWSGTEVKIDGEELLIMKESDIMGVLEGAASKKKAAA
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.
A7HQQ1
A3NBM6
ASTB_BURP6
N-succinylarginine dihydrolase
pseudomallei group
MNAKEANFDGLVGPTHNYAGLSFGNVASLSNEKSDANPKAAAKQGLRKMKQLADLGFAQGVLPPQERPSLRLLRELGFSGKDADVIAKAARQAPELLAAASSASAMWTANAATVSPSADTGDARVHFTPANLCSKLHRAIEHESTRRTLAAIFADEARFAVHDALPGTPALGDEGAANHTRFCAEYGAPGVEFFVYGRAEYRRGPEPTRFPARQTFEASRAVAHRHGLREEATIYAQQRPDVIDAGVFHNDVIAVGNRDTLFCHEHAFVDPQAVYDALAASLGALGAQLNVIEVPDRAVSVADAVGSYLFNSQLLAREDGTQMLVVPQECRENANVAAYLDALVAGNGPIRDVRVFDLRESMKNGGGPACLRLRVVLNDAERAAVKPNVWIGDALFASLDAWIDKHYRDRLSPVDLADPALLDESRTALDELTQILGLGSLYDFQR
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
A3NBM6
A4VRJ2
METXS_PSEU5
Homoserine transsuccinylase
Pseudomonas
MPTAIPADSVGLVSPQVAHFAEPLTLACGRTLADYQLIYETYGELNAARSNAVLICHALSGHHHAAGYHSEDDRKPGWWDSCIGPGKAIDTDRFFVVSLNNLGGCNGSTGPSSTNPATGKPYGADFPVVTVEDWVHSQARLADRLGINQWAAVVGGSLGGMQALQWAISYPERVRHCLAIASAPKLSAQNIAFNEVARQAILSDPEFHGGHFQEMGVIPKRGLMLARMVGHITYLSDDAMGTKFGRGLKSEKLNYDFNSVEFQVESYLRYQGEEFSGRFDANTYLLMTKALDYFDPAAANDDDLARTFEVAQADFCVMSFTTDWRFSPERSREIVDALLAARKNVCYLEIDAPQGHDAFLIPNPRYLQAFRGYMNRIAV
Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
A4VRJ2
O79460
CYB_SORPA
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Sorex
MTNLRKTHPLMKIINNSFIDLPAPSNISSWWNFGSLLGVCLIVQILTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWLIRYLHANGASMFFICLFLHVGRGLYYGSYMFLETWNIGVLLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGSDLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAGVHLLFLHETGSNNPSGLCSDADKIPFHPYYTIKDILGILLFILILTSLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILVLAFIPFLHTSKQRSMMFRPFSQCLFWILVADLLTLTWIGGQPVEHPFIIIGQLASILYFLLILVLMPITSLLENNLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
O79460
Q5F6E8
GLUQ_NEIG1
Glutamyl-Q tRNA(Asp) synthetase
Neisseria
MYTGRFAPSPTGLLHIGSLLTAVASYADARSNGGKWLVRMEDLDPPREMPGAASHILHTLEAFGFKWDGEVTYQSRRYALYEETLYRLKTAGLVYPCHCNRKDWQAGARRGTDGFVYNGRCRHPGQRPALQGKQPSWRIRVPDRDIGFSDGIVGSYAQNLARDIGDFVLFRADGYWAYQLAVVADDAEQGVTHIVRGQDLLVSTPRQIYLQQCLGVPTPQYAHLPLLTNAQGQKWSKQTLAPALDLNRREQLLRQVFRYLKLPEAPETDRPAELLDWAVAHWDMDKVPKHAITAP
Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon.
Q5F6E8
Q9STX2
VEP1_ARATH
Protein VEIN PATTERNING 1
Arabidopsis
MSWWWAGAIGAAKKKLDEDEPSQSFESVALIIGVTGIVGNSLAEILPLSDTPGGPWKVYGVARRPRPTWNADHPIDYIQCDVSDAEDTRSKLSPLTDVTHVFYVTWTNRESESENCEANGSMLRNVLQAIIPYAPNLRHVCLQTGTKHYLGPFTNVDGPRHDPPFTEDMPRLQIQNFYYTQEDILFEEIKKIETVTWSIHRPNMIFGFSPYSLMNIVGTLCVYAAICKHEGSPLLFPGSKKAWEGFMTASDADLIAEQQIWAAVDPYAKNEAFNCNNADIFKWKHLWKILAEQFGIEEYGFEEGKNLGLVEMMKGKERVWEEMVKENQLQEKKLEEVGVWWFADVILGVEGMIDSMNKSKEYGFLGFRNSNNSFISWIDKYKAFKIVP
Involved in vascular strand development. Catalyzes the stereospecific conversion of progesterone to 5-beta-pregnane-3,20-dione. Can use progesterone, testosterone, 21-acetyl cortexone, 2-cyclohexenone, but-1-en-3-one, ethyl acrylate, ethylmethacrylate, cortisone and canarigenone as substrates, lower activity with 3-methyl-2-cyclohexenone and 3,5,5-trimethyl-2-cyclohexenone as substrate, and no activity with canarigenin, canarigenin digitoxoside and pregnenolone. May be involved in the formation of 5-beta phytoecdysteroids.
Q9STX2
Q2NVM8
CYSN_SODGM
Sulfate adenylate transferase
Sodalis
MNNAIAQQIAEQGGVEAYLHAQQHKSLLRFLTCGSVDDGKSTLIGRLLHDTRQIYEDQLSTLHTDSKRLGTQGDKLDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDVAILLIDVRKGVLDQTRLHSFISTLLGIRHLVVAVNKMDLVAFDEQIFQGIRQDYLRFAEQLPVDLDITFVPLSALEGDNVAALGKAMPWYNGPTLLDVLETVEVINLNEQQPARFPVQYVNRPNLDFRGYAGTVAAGVLRVGQAVKVLPSGVTSTISRIVTFDGDLTEAWAGEAVTLVLKDEVDISRGDLLVDAGETLTEVQNAQVDVVWMTEQPLVAGQSFDIKIAGKKTRARVDNIQYQVDINTLTQRVADSLPLNGIGLVELAFDEPMILDKYADNPTTGGMIFIDRLSNVTVGAGMVRQPLQDVYREPGAYGEFELALNALVRRHFPHWGARDLLGGK
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Q2NVM8
Q72QZ8
ENO_LEPIC
2-phosphoglycerate dehydratase
Leptospira
MSHHSQIQKIQAREIMDSRGNPTVEVDVILLDGSFGRAAVPSGASTGEYEAVELRDGDKHRYLGKGVLKAVEHVNLKIQEVLKGENAIDQNRIDQLMLDADGTKNKGKLGANAILGTSLAVAKAAAAHSKLPLYRYIGGNFARELPVPMMNIINGGAHADNNVDFQEFMILPVGAKSFREALRMGAEIFHSLKSVLKGKKLNTAVGDEGGFAPDLTSNVEAIEVILQAIEKAGYKPEKDVLLGLDAASSEFYDKSKKKYVLGAENNKEFSSAELVDYYANLVSKYPIITIEDGLDENDWDGWKLLSEKLGKKIQLVGDDLFVTNIEKLSKGISSGVGNSILIKVNQIGSLSETLSSIEMAKKAKYTNVVSHRSGETEDVTISHIAVATNAGQIKTGSLSRTDRIAKYNELLRIEEELGKSAVYKGRETFYNL
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q72QZ8
P14787
PRLR_RABIT
Prolactin receptor
Oryctolagus
MKENVASMIVFLLLLFLNIRLLKGQSPPGKPFIFKCRSPEKETFTCWWRPGADGGLPTNYTLTYHKEGETITHECPDYKTGGPNSCYFSKKHTSIWTIYIITVNATNQMGSSVSDPRYVDVTYIVEPDPPVNLTLEVKHPEDRKPYLWVKWLPPTLVDVRSGWLTLQYEIRLKPEKAAEWETHFAGQQTQFKILSLYPGQKYLVQVRCKPDHGFWSVWSPESSIQIPNDFTMKDITVWIFVAVLSTIICLIMVWAVALKGYSMVTCIFPPVPGPKIKGFDTHLLEKGKSEELLSAFGCQDFPPTADCEDLLVEFLEVDDSEDQQLMPAHSKEHSGPGMKPTDLDPDNDSGRGSCDSPSLLSEKCEEPQANPSTFHTPEVIEQPEKPKANVTHTWDPQTISLVGKMPYLSVNGSKSSTWPLLQPGQHNTNSPYHNIADMCKLATSLDKIDKDALQSSKTTEAAGEEKATKQREVESSHSKAEQDTGWLLPKEKPPFISPKPLDYVEIHKVNKDGALSLLLKQKENGDQTGKAGTPETSKEYAKVSRVMDNNILVLVQDPGAQNVALFEESTKEAPPSPSQNQAEKDLSSFSTAPSDCRLQQGGLDYLDPACFMHSLH
This is a receptor for the anterior pituitary hormone prolactin.
P14787
A1U2V8
LEPA_MARN8
Ribosomal back-translocase LepA
Marinobacter
MTELSRIRNFSIIAHIDHGKSTLADRFIQICGGLTDREMAEQVLDSMDLERERGITIKAQSVTLNYKAKDGETYKLNFIDTPGHVDFSYEVSRSLYACEGALLVVDAGQGVEAQSVANCYTAIEQGLEVVPVLNKMDLPQAEPERVAAEIEDIIGIDASDAVRCSAKSGLGVEDVLEDLIKKIPPPKGDRSAPLQALIIDSWFDNYLGVVSLVRVTEGVLRKGDKIVIKSTKKAWNADKVGVFNPKPTDTDVLEAGDVGFVVAGIKDIHGAPVGDTIVHQKFAEETPMLPGFKKVKPQVYAGLFPVSADDYDDFRDALEKLTLNDASLFFEPENSDALGFGFRCGFLGMLHMEIIQERLEREYDLDLITTAPTVIYEVVTKQGETLSVDNPSRLPDIGSIEEMREPIVEANILVPQEHLGNVIALCEEKRGVQKNMHFMSTQVQLTYELPMAEVVMDFFDRIKSASRGFASLDYHFVRFQSANLVRLDVLINGDRVDALALIVHRDLSHRKGRQLIEKMKELIPRQMFDIAIQAAIGTQVVSRVTVKALRKNVTAKCYGGDVSRKKKLLQKQKEGKKRMKQLGNVEVPQEAFLAVLKVDN
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
A1U2V8
A4WVI9
RL15_CERS5
50S ribosomal protein L15
Cereibacter
MKLNELRDNEGAARKKKRVARGPGSGKGKTAGRGIKGQKSRSGVALNGYEGGQMPLYRRLPKRGFSKPNRKEYAVVNLGLIQKFVDAGKLDASQPIDENAIVAAGVTSHKRDGIRVLAKGEITAKLTLTVAGASKSAVEAVEKAGGSITLTAPAAAASAE
Binds to the 23S rRNA.
A4WVI9
Q04641
SCTC_SHIFL
Outer membrane protein MxiD
Shigella
MKKFNIKSLTLLIVLLPLIVNANNIDSHLLEQNDIAKYVAQSDTVGSFFERFSALLNYPIVVSKQAAKKRISGEFDLSNPEEMLEKLTLLVGLIWYKDGNALYIYDSGELISKVILLENISLNYLIQYLKDANLYDHRYPIRGNISDKTFYISGPPALVELVANTATLLDKQVSSIGTDKVNFGVIKLKNTFVSDRTYNMRGEDIVIPGVATVVERLLNNGKALSNRQAQNDPMPPFNITQKVSEDSNDFSFSSVTNSSILEDVSLIAYPETNSILVKGNDQQIQIIRDIITQLDVAKRHIELSLWIIDIDKSELNNLGVNWQGTASFGDSFGASFNMSSSASISTLDGNKFIASVMALNQKKKANVVSRPVILTQENIPAIFDNNRTFYVSLVGERNSSLEHVTYGTLINVIPRFSSRGQIEMSLTIEDGTGNSQSNYNYNNENTSVLPEVGRTKISTIARVPQGKSLLIGGYTHETNSNEIISIPFLSSIPVIGNVFKYKTSNISNIVRVFLIQPREIKESSYYNTAEYKSLISEREIQKTTQIIPSETTLLEDEKSLVSYLNY
Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells . Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane . Necessary for the secretion of Ipa invasins .
Q04641
Q8NGC2
OR4E2_HUMAN
Olfactory receptor OR14-42
Homo
MDSLNQTRVTEFVFLGLTDNRVLEMLFFMAFSAIYMLTLSGNILIIIATVFTPSLHTPMYFFLSNLSFIDICHSSVTVPKMLEGLLLERKTISFDNCITQLFFLHLFACAEIFLLIIVAYDRYVAICTPLHYPNVMNMRVCIQLVFALWLGGTVHSLGQTFLTIRLPYCGPNIIDSYFCDVPLVIKLACTDTYLTGILIVTNSGTISLSCFLAVVTSYMVILVSLRKHSAEGRQKALSTCSAHFMVVALFFGPCIFIYTRPDTSFSIDKVVSVFYTVVTPLLNPFIYTLRNEEVKSAMKQLRQRQVFFTKSYT
Odorant receptor.
Q8NGC2
Q99795
GPA33_HUMAN
Glycoprotein A33
Homo
MVGKMWPVLWTLCAVRVTVDAISVETPQDVLRASQGKSVTLPCTYHTSTSSREGLIQWDKLLLTHTERVVIWPFSNKNYIHGELYKNRVSISNNAEQSDASITIDQLTMADNGTYECSVSLMSDLEGNTKSRVRLLVLVPPSKPECGIEGETIIGNNIQLTCQSKEGSPTPQYSWKRYNILNQEQPLAQPASGQPVSLKNISTDTSGYYICTSSNEEGTQFCNITVAVRSPSMNVALYVGIAVGVVAALIIIGIIIYCCCCRGKDDNTEDKEDARPNREAYEEPPEQLRELSREREEEDDYRQEEQRSTGRESPDHLDQ
May play a role in cell-cell recognition and signaling.
Q99795
P63054
PCP4_MOUSE
Purkinje cell protein 4
Mus
MSERQSAGATNGKDKTSGDNDGQKKVQEEFDIDMDAPETERAAVAIQSQFRKFQKKKAGSQS
Functions as a modulator of calcium-binding by calmodulin. Thereby, regulates calmodulin activity and the different processes it controls. For instance, may play a role in neuronal differentiation through activation of calmodulin-dependent kinase signaling pathways.
P63054
Q68W48
RMUC_RICTY
DNA recombination protein RmuC homolog
typhus group
MPGLLLLTTTMLLILFALIICFYIKTKTFKMQLQFLSEQNLEINNNNQLLNQEKITYLQKIEQLKCKLEYQERMIKDSEKIREESFASAKAALFDLGKDLSKQLIEIHKMENNTTRELAEKNIETASQKFNTELERLITMVGALNKDIEQSKGTVDLIKQSLLSPIGAGLLSEITLENILKSSGLRPNLDFIMQYSLTTSDSVKLRPDAIIFLPSGNLMVIDSKASKFLVDSQDNSVHLSKTMNYHLKTLTNKDYAENILTNLNKKTQNFNNVITLMFLPTEQAVEKVIAANPEFLQKAWGCNIFPVGPAGLMNMLSFAKFQITDNRRSENYKVIIEEVRKLLSSIGTIADYSKKIGYNLQNMVTNYDKFAASFNRNVMSRVKSIQKLGIDSGNKIIPATLERYQIVSAKSEIIEVDVENQHK
Involved in DNA recombination.
Q68W48
Q03NP0
NNRE_LEVBA
NAD(P)HX epimerase
Levilactobacillus
MSKAITIAEAQRYDAHATNVIGIPAMVLMERAALATFNNLLNDDFDLDRVVVVAATGNNGGDGIAVARLLKIRGIDVTIYLLGDPENATPQTSQQLKIANYYNIPVTADLNQIVNATLIVDAIFGVGLTRDVTGKFADAINAINAADAKTVAIDVPSGINADTGAVMGVAVVADSTTTMAYNKIGLLTTVGKQHAGTIHVADIGIYAQDRVEHAR
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Q03NP0
Q2T1Q4
BIOB_BURTA
Biotin synthase
pseudomallei group
MTEAQTACPTTETPVAAPVAPRWRVADVIALYELPFNDLLFRAQQTHREHFDANAIQLSTLLSIKTGGCEEDCGYCSQSAHHDTGLKAEKLMEVDAVLAAARTAKENGATRFCMGAAWRNPKDRHIEPIKEMIRGVKDMGLETCVTLGMLEEHQAKALAEAGLDYYNHNLDTSPEFYGQIISTRTYQDRLDTLERVRDAGINVCCGGIIGMGESRRERAGLIAQLANMNPYPESVPINNLVAIEGTPLENAQALDPFEFVRTIAVARITMPKAMVRLSAGREQLDDSMQALCFLAGANSMFYGDVLLTTGNPRAEADRKLLARLGMSATEATQLSA
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Q2T1Q4
Q2J4N0
PURQ_FRACC
Phosphoribosylformylglycinamidine synthase subunit I
Frankia
MTEADSPARIGIVTFPGSLDDQDTALAVRAAGAEPVSLWHGDSDLAGVDAVILPGGFSYGDYLRAGAIARFSPMVAALVPAARAGLPILGICNGFQVLCEAGLLPGALTRNVGLHFVCRDQRLRVEAPGTAWTRGYQDGEEIVIPVKHGDGRYVAAPDVLAELEAAGRVVVRYVGGNPNGSAADIAGICNESRTIVGLMPHPEHAVDDLTGPGVDGLRMFTSVLSGFLSAFSS
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Q2J4N0
Q7A2T0
FMTA_STAAM
Teichoic acid D-alanine esterase
Staphylococcus
MKFNKVKLVIHACVLLFIIISIALIFHRLQTKTHSIDPIHKETKLSDNEKYLVDRNKEKVAPSKLKEVYNSKDPKYKKIDKYLQSSLFNGSVAIYENGKLKMSKGYGYQDFEKGIKNTPNTMFLIGSAQKFSTGLLLKQLEEEHKININDPVSKYLPWFKTSKPIPLKDLMLHQSGLYKYKSSKDYKNLDQAVKAIQKRGIDPKKYKKHMYNDGNYLVLAKVIEEVTGKSYAENYYTKIGDPLKLQHTAFYDEQPFKKYLAKGYAYNSTGLSFLRPNILDQYYGAGNLYMTPTDMGKLITQIQQYKLFSPKITNPLLHEFGTKQYPDEYRYGFYAKPTLNRLNGGFFGQVFTVYYNDKYVVVLALNVKGNNEVRIKHIYNDILKQNKPYNTKGVIVQ
Catalyzes the liberation of D-alanyl moieties present on wall teichoic acid (WTA) and lipoteichoic acid (LTA) . Affects the methicillin resistance level and autolysis in the presence of Triton X-100 as well as the cell wall structure .
Q7A2T0
O09018
COT2_RAT
Ovalbumin upstream promoter beta nuclear receptor
Rattus
MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGSQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSGYISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITDQVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDVAHVESLQEKSQCALEEYVRSQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMAIQ
Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. May be required to establish ovary identity during early gonad development.
O09018
Q3SYS9
KBP_BOVIN
KIF1-binding protein
Bos
MADSPWDEIREKFQTALALSRVELHKNPEKEPYKSKYSARALLEEVKALLGPAPEDEDERPQADDSLGAGEHALGLPAELVEAEGPVAQGAVRRAVIEFHLGVNHIDTEELSAGEEHLVKCLRLLRKYRLSHDCVSLYIQAQNNLGILWSEREEIETAQAYLESSEALYNQYMKEIGSPPLDPTEHFLPEEEKLPEQERSKRFEKVYTHNLYYLAQVYQHMEMFEKAAHYCHSTLKRQLEHNAYHPMEWAINAATLSQFYINKQCFMEARHCLSAANVIFGQIGKIRTTEDTTEAEGDVPELYHQRKGEIARCWIKYCLTLMQNAQLSMQDNIGELDLDKQSELRALRKKELDEEESVRKKAVQFGTGELCDAISAVEEKVSYLRPLDFEEARELFLTGQHYVFEAKEFFQIDGYVTDHIEVVQDHSALFKVLAFFETDMERRCKMHKRRIAMLEPLIVDLNPQYYLLVNRQIQFEIAHAYYDMMDLKVAIADKLRDPDSHIVKKINNLNKSALKYYQLFLDSLRDPNKVFPEHIGEDVLRPAMLAKFRVARLYGKIITADPKKELENLATSLEHYKFIVDYCEKHPEAAQEIEVELELSKEMVSLLPTKMERFRTKMALT
Required for organization of axonal microtubules, and axonal outgrowth and maintenance during peripheral and central nervous system development.
Q3SYS9
C4KZV1
GLMU_EXISA
Glucosamine-1-phosphate N-acetyltransferase
unclassified Exiguobacterium
MERFAVILAAGKGTRMKSKLYKVLHPVLGKPMVEHVVDQLDQIGVSRQIVIVGHGAEAVQDTLGTRVEYAVQEEQLGTGHAVQMAEAELAGKSGATLVVCGDTPLLTAETLEALLAHHEAQQAKVTVLTAIADDATGYGRVVRGEDGNVTKVVEHKDASEAELAINEINTGTYVFDNELLFDALKQVGNNNAQGEYYLPDVISIAKEAGEVVAAHTAPTFDETIGVNDRVALSQAEAIMRKRTNERLMREGVTFMDPASTYISPDVVIGSDTVIYPGTVILGKTTIGSECVIGPNSDIRNSVIEDHAVVRQSVVTDSRIGEAAQVGPFAHLRQQAVLGANTRVGNFVEIKKSTFGDGAKASHLSYIGDASIGERVNLGCGSITVNYDGKNKFETVVEDDAFVGCNVNLIAPVKVGKGAIVAAGSTITSDVPEEALAIARERQTNKEGYTKR
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
C4KZV1
B7K085
PSAJ_RIPO1
Photosystem I reaction center subunit IX
Rippkaea orientalis
MEGLTKFLSTAPVLIMALLTFTAGLLIEFNRFYPDLLFHPLG
May help in the organization of the PsaE and PsaF subunits.
B7K085
B7UXE2
PDXH_PSEA8
Pyridoxal 5'-phosphate synthase
Pseudomonas
MTQSLADMRREYTRDGLSEANAPSDPFSLFRQWFDDAVKTERLPVEPNAMTLATVDADGYPHCRILLLKGLDERGFTFFTNYESAKGRQLAANPRAAMTFFWPALERQVRIEGSVEKVTPEESDAYYQVRPLGSRLGAWASPQSRVIADRAELERLLAETERRFADQPPSCPEHWGGYRLLPQRIEFWQGRPSRLHDRLDYRRQDGGWSRERLAP
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
B7UXE2
Q03UM2
LEUC_LEUMM
Isopropylmalate isomerase
Leuconostoc
MSKTLFDKIWEKHVITGEIGEAQLIYVDLHLVHEVTSPQPFDGLRSTNRRVRRPDLTFATMDHNVPTKDIFNVQDQMSRLQMDTLVKNTKEFDIPLASIGDDKQGIVHVVGPERGLTQPAKVIVCGDSHTATHGAFGAIAFGIGTSEVEHVLATQTIWQVKPKTMGIKVTGKLPKNTYAKDIIMGIIAKYGVSFGVGYAIEFYGETVENLSMEARMTMCNMSIEAGSRTGMVQPDQTTFDYIEGREQAPKDFESAKNYWSQFYTDDESDFDETLTFDVSNLKPMVTWGTNPGMATPVDQSLPAIKDDNDANAYEYIGLHPNMKPVDINLDYIFIGSCTNSRYEDLEIAANMMKGHHLAPNVTAWVVPGSRAIRNRAIKSGIAQIFEEAGCEWREPGCSACLAMNPDKIPAGKHVASTSNRNFIGRQGAGSRTHLASPAMVAAAGIAGHFVDITTDEFV
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Q03UM2
Q2GLX8
SFH5_CHAGB
Phosphatidylinositol transfer protein SFH5
Chaetomium
MYGRSVQDCAYTASIGMIAQGQNDFAANGRIWLGLLAPHDRGRGLGLGCECLRPIKMSAVEQKPSEQPAPTTVAPDTVSTPEPAVAAAADNATAAPAPSETPATPAAPAAPDASGAQDTPATAGADSEVPAPTETKELVETKEPAEKKEPAETKEAPVEKAPVDDKTPITQLWATAKATGHPEIWGVTLADPETHVPTRIILQKYLNANDADLDKAKDQLTKTLEWRAKTKPLELVKKAFSKTKFDGLGYVTKYVQDGSTEPEAKEVFTWNIYGGVKSIDETFGKLEEFLDWRVALMELALQELDLASATKLITAEYDPYKIFQVHDYKSISFLRQSPQVKSASAETIKVFAQNYPELLKEKFFVNVPAIMGFVYAFMKLFVAPKTIKKFHPMSNGGSLAVEFADSKVAALGEKLPANYGGKGAELEEQGKGPLLE
Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Q2GLX8
B0JX47
MTNX_MICAN
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase
Microcystis
MSKIVFCDFDGTITAVETFAGMLKEFAPDLSAQIMPQMYARTLTLRRGVRQLLESIPSQKYADILAYAESKPIRPGLAEFLAFLQEQSIPFIIISGGIQGMIETVLKREGLLDKVTAIYGVNLHTQGEYLQVHSDWENETELVAKALIMAKYSGVETIAIGDSVTDITMARRADLVFARDRLIDYLQAENQPYIPWDNFFEIREYLLLRD
Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
B0JX47
Q7FAY6
RGP2_ORYSJ
UDP-L-arabinose mutase 2
Oryza sativa
MSLEIQDSEVDIVIAALQPNLTTFFEAWRPFFSRFHIIVVKDPDMAEELQIPTGFDLKVYTKSDMGVLGATSIDFSGHSCRYFGYLVSRKKYVISIDDNCLPAKDNGGLTVDAVAQHMSNLKTPATPFFFNTLYDPFRKGADFVRGYPFSLREGVECMLSCGLWLHNADYDPMTHVVKRNQRNTTYVDAVMTVPLGAMMPVSGINVAFNREVLGPVMFPALRLRKEGKHRWDTLEDVWNGLCAKVVCDRLRYGVKTGLPYVMRSDAEAGKALESLKEWEGVKVMDVVLPFFESLKLSSTSVTVEDCVKELTSIVKEKLGPQNAIFAKAADAMEEWTKLWKSHGAQSA
Probable inactive UDP-L-arabinose mutase. Inactive in vitro, but associates with UAM1 and UAM3.
Q7FAY6
A6ZVS0
MPH1_YEAS7
Mutator phenotype protein 1
Saccharomyces
MASADDYFSDFEDDELDKLYEKAINKSVKETITRRAVPVQKDLHDNVLPGQKTVYEEIQRDVSFGPTHHELDYDALSFYVYPTNYEVRDYQYTIVHKSLFQNTLCAIPTGMGKTFIASTVMLNYFRWTKKAKIIFTAPTRPLVAQQIKACLGITGIPSDQTAILLDKSRKNREEIWANKRVFFATPQVVENDLKRGVLDPKDIVCLVIDEAHRATGSYAYTNVVKFIDRFNSSYRLLALTATPASDLEGVQEVVNNLDISKIEIRTEESMDIVKYMKKRKKEKIEVPLLLEIEDIIEQLGIAVKPVLQQAIELGIYEECDPSQINAFKAMQQSQKIIANPTIPEGIKWRNFFILQLLNNVGQMLKRLKIYGIRTFFNYFQNKCTEFTTKYNLKKSTNKIAAEFYYHPILKNIKNQCENYLSDPKFVGHGKLQCVRDELMEFFQKRGSDSRVIIFTELRESALEIVKFIDSVANDQIRPHIFIGQARAKEGFDEVKYTRKHAPKGRKKVERLHRQEQEKFLEAERTKRAANDKLERSARRTGSSEEAQISGMNQKMQKEVIHNFKKGEYNVLVCTSIGEEGLDIGEVDLIICYDTTSSPIKNIQRMGRTGRKRDGKIVLLFSSNESYKFERAMEDYSTLQALISKQCIDYKKSDRIIPEDIIPECHETLITINDENEIINEMEDVDEVIRYATQCMMGKKVKPKKAITKKKRVQENKKPKKFFMPDNVETSIVSASTLINKFLVNESGGKQLVTSNENPSKKRKIFKALDNLENDSTEEASSSLETEDEEFSDDNNVFIAEGQNGCQKDLETAIIRTGESLTTLKPLHNFERPNMALFVNDCGLPTKIEKNVKDIRGNQHNLEKEKNCTVDKNNMVLSLDDWNFFRDRYIPEGVSFDVEPNFVQYTKGVKVPHCHKVSKIITLFNDESNDNKKRTIDMNYTKCLARGMLRDEKKFVKVNDKSQVDNNSVNHDSSQSFTLSNAELDDILGSDSDF
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork.
A6ZVS0
Q9ZV28
C7104_ARATH
C-22 sterol desaturase
Arabidopsis
MVSSVSLFASLTPYLVSALLLFLLLEQLFYRVKKRNLPGPLFVFPIIGNVVALIRDPTSFWDKQSAMADTSVGLSVNYLIGKFIIYIKDAELSNKVLSNIRPDAFQLTGHPFGKKLFGDHSLIFMFGEDHKSVRRQVAPNFTRKPLSAYSSLQQIVILRHLRQWEESFSSGSRPVSMRQLIRELNLETSQTVFVGPYLDKEVKKTICDDYSLLTLGTMAIPIDLPGFTFGEARQAVSRLVNTMSVCVGKSKAKMAAGENPTCLVDFWTHSIIEENPPPPHSKDKEISCVLVDFMFASQDASTSSLLWAVVMLESEPEVLRRVREDVARFWSSESNELITADQLAEMKYTRAVAREVLRYRPPASMIPHVAVSDFRLTESYTIPKGTIVFPSLFDASFQGFTEPDRFDPDRFSETRQEDEVFKRNFLTFGNGSHQCVGQRYAMNHLVLFIAMFSSMFDFKRVRSDGCDDIVHIPTMSPKDGCTVFLSSRLVTSP
Required to form the C-22 double bond in the sterol side chain. Possesses C-22 desaturase activity toward beta-sitosterol and produces stigmasterol.
Q9ZV28
Q89J97
RS14_BRADU
30S ribosomal protein S14
Bradyrhizobium
MAKKSSIEKNNRRKRMVKNAAPKRERLKAIIADKTLPMEERFAATLKLAEMPRNSSATRVRLRCELSGRPRSNYRKNKLSRIALRELGSKGMVPGLVKSSW
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Q89J97
Q7U8I1
FUMC_PARMW
Iron-independent fumarase
Parasynechococcus marenigrum
MGQPMRQEHDSIGGVDVPAAALWGAQTQRSLNNFAIGHQKIPAELIHALARIKQCCAAVNGRHGLLNDQQVALIERAGQAIQTGQQDDHFPLSVWQTGSGTQTNMNVNEVISNLAAQESGENLGSHRPLHPNDHINRSQSTNDVFPAAIHVAAALQLQQELLPELKRLIASLDAKAVAWQDIIKIGRTHLQDAVPLRLGDEVSAWRDRLSDGAHWLTTAHQDLLALPLGGTAVGSGLNTPDRFAHEVCAELASRTGSDFQPADNLFAVMAGHDSLVQTMAQLRRLAVTLLTIANDIRLLACGPRAGLGELLLPANEPGSSIMPGKVNPTQCEAMAMVCTQVIGMDAAVAAAGAGGHLQMNVYKPLIGYNLIEGIRLLQDACRCFRLNLLTGMEADRDRIAFYVERSLMLVTALTPEIGYEKACAIAQHAHRDGLTLREAAMQSGAITDERFDQLIDPAAMASPHR
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Q7U8I1
Q9BZE2
PUS3_HUMAN
tRNA-uridine isomerase 3
Homo
MAYNDTDRNQTEKLLKRVRELEQEVQRLKKEQAKNKEDSNIRENSAGAGKTKRAFDFSAHGRRHVALRIAYMGWGYQGFASQENTNNTIEEKLFEALTKTRLVESRQTSNYHRCGRTDKGVSAFGQVISLDLRSQFPRGRDSEDFNVKEEANAAAEEIRYTHILNRVLPPDIRILAWAPVEPSFSARFSCLERTYRYFFPRADLDIVTMDYAAQKYVGTHDFRNLCKMDVANGVINFQRTILSAQVQLVGQSPGEGRWQEPFQLCQFEVTGQAFLYHQVRCMMAILFLIGQGMEKPEIIDELLNIEKNPQKPQYSMAVEFPLVLYDCKFENVKWIYDQEAQEFNITHLQQLWANHAVKTHMLYSMLQGLDTVPVPCGIGPKMDGMTEWGNVKPSVIKQTSAFVEGVKMRTYKPLMDRPKCQGLESRIQHFVRRGRIEHPHLFHEEETKAKRDCNDTLEEENTNLETPTKRVCVDTEIKSII
Formation of pseudouridine at position 39 in the anticodon stem and loop of transfer RNAs.
Q9BZE2
A4IJI7
EFTU_GEOTN
Elongation factor Tu
Geobacillus
MAKAKFERTKPHVNIGTIGHVDHGKTTLTAAITTVLAKQGKAEARAYDQIDAAPEERERGITISTAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLSRQVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDEVPVIKGSALKALEGDAQWEEKIVELMNAVDEYIPTPQREVDKPFMMPVEDVFSITGRGTVATGRVERGTLKVGDPVEIIGLSDEPKSTTVTGVEMFRKLLDQAEAGDNIGALLRGVSRDEVERGQVLAKPGSITPHTKFKAQVYVLTKEEGGRHTPFFSNYRPQFYFRTTDVTGIITLPEGVEMVMPGDNVEMTVELIAPIAIEEGTKFSIREGGRTVGAGSVSEIIE
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
A4IJI7
Q72ER6
PNP_DESVH
Polynucleotide phosphorylase
Desulfovibrio
MTNIFNAMRVTATVGGKEIVFETGRLANQADGAVWIQCGGTVVLVTACSQATDRDLGFFPLTVEYSEKMYAAGRIPGSFFRREIGRPSERETLVSRLIDRPIRPLFPKGLKDEVQVLANVISSDQNNDSDVLAVTGASTALGLSSIPFDGPVAGARIGRIDGQFVINPTIKEMERSDLNIVLAASRDAVVMVEGEASFVPEAVIVEALEWGHKEIQPLIDAQLKLREMAGKAKREFTAPVEDADLAARVAALATADLDVALRIPEKMARKDARKAVKEKVMEALVADPAYAEDTTPLRAVGDILSALEKRIVRERIVREGRRIDGRDTTTVRPILIEAGILPRAHGSALFARGETKSLVVATLGSSTDEQRMDSLTGDVTKRFMLHYNFAPYCVGEVKPVRVSRREIGHGALAEKALRPILPLGEDFPFTLRVVAETMESNGSSSMAAVCGGCLSLMDAGVPITAPVAGVAMGLIKEGDQYVVLTDILGDEDALGDMDFKIAGTSEGITAVQMDIKVKGLPTDVMARAMQQARDARLHILGEMGKVLEAPRAELSAYAPQHAEVFVNPDIIRIIIGPGGKNIKAITATTGASIDIEDSGRVSIFAPTLEAMEMAREMVQYYDQRADIGKNYTGKVRKVLEIGAIVEILPNLEALVHISQLDTNRVEQASDVARLGEDMVVKVIEINGDRIRASRKAVLLEEQGIEWKPEDTARPSGPREGGRRDGGRDGRRDGGRDGRRDGGRDGGRRDGGRRDGGRDRN
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Q72ER6
B2A4B2
ISPF_NATTJ
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Natranaerobius
MRIGHGVDVHKLVKGEDLVLGGVQIPSDLGLKGHSDADVLIHAIMDAMLGSLALGDIGKHFPDDDPRYHQIDSKVLLKKTYQLITSYGYQLINLDSTIMAEKPKLAPYIDEMRITISDVLDLYPSQIGIKATTFEKLGFVGSGQGIMAQAVVLMERLY
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
B2A4B2
Q73H97
RL24_WOLPM
50S ribosomal protein L24
unclassified Wolbachia
MSAKIKSGDDVIVLTGKDKGKIGKVIKVIARDAKKKVIVSGVNVHKRHTKPKAGSSGGILNKELAIDISNVATLDPKYKTPTRVGFKVIDGRKVRFAKVSGEVID
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
Q73H97
A6NJ46
NKX63_HUMAN
Homeobox protein Nkx-6.3
Homo
MESNLQGTFLLNNTPLAQFPEMKAPVCQYSVQNSFYKLSPPGLGPQLAAGTPHGITDILSRPVAAPNNSLLSGYPHVAGFGGLSSQGVYYSPQVGNFSKAGNEYPTRTRNCWADTGQDWRGGRQCSNTPDPLSDSIHKKKHTRPTFTGHQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKKSALEPSSSTPRAPGGAGAGAGGDRAPSENEDDEYNKPLDPDSDDEKIRLLLRKHRAAFSVLSLGAHSV
Putative transcription factor, which may be involved in patterning of central nervous system and pancreas.
A6NJ46
Q823T2
DNAJ_CHLCV
Chaperone protein DnaJ
Chlamydia
MDYYDVLGVSKTASPEEIKKSYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDPQKRESYDRYGKNGPFAGAGGFGGMGGMGNMEDALRTFMGAFGGEFGGGGSFFEGLFGGLGEAFGMRGDPAGARQGASKKVHITLTFEEAARGVEKELLVSGYKTCETCLGSGAASEQGIKCCDRCKGSGQIVQSRGFFSMASTCPECGGEGRVITDPCSNCRGQGRIKDKRNVHVQIPAGVDSGMRLKMEGYGDAGQNGAPSGDLYVFIDVEAHPVFERRGDDLILELPIGFVDAALGMKKEIPTLLKEGMCRLTVPEGIQSGTILKVKNQGFPNVHGRGRGDLLVRVSVETPQNLSEEQKELLRKFATTEKAENFPKKRGFLDKIKGFFSDFAV
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Q823T2
C5A333
VATE_THEGJ
V-ATPase subunit E
Thermococcus
MEGAELIIQEIHREAEQKIQYILSEAQREAEKLKEEARKRAQSQAEWILRKAKTQAEIEKQRIIANAKLEVRRKKLAVQEELIGEVLSAMREKLAALPDDEYFEALVSLTKEAIEELGTKKIVLRSNERTLKLIDSRMEEFSEKVGVEVSLGEPIECIGGVLVESPDGTVRVDNTFDARIERLESELRATVAKALFG
Produces ATP from ADP in the presence of a proton gradient across the membrane.
C5A333
C1DD40
NDK_LARHH
Nucleoside-2-P kinase
Laribacter
MAIERTLSIVKPDAVAKNVIGKIYDRFESNGLKIVAAKMKHLSRREAEGFYAVHKERPFFNDLVEFMISGPVMVQVLEGENAVLKNRELMGATDPKKADAGTIRADFAESIDANAVHGSDSLENAAIEIAYFFSATEVCPR
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
C1DD40
Q8X6V3
DGCI_ECO57
Probable diguanylate cyclase DgcI
Escherichia
MSRINKFVLTVSLLIFIMISAVACGIYTQMVKERVYSLKQSVIDTAFAVANIAEYRRSVAIDLINTLNPTEEQLLVGLRTAYADSVSPSYLYDVGPYLISSDECIQVKEFEKNYCADIMQVVKYRHVKNTGFISFDGKTFVYYLYPVTHNRSLIFLLGLERFSLLSKSLAMDSENLMFSLFKNGKPVTGDEYNAKNAIFTVSEAMEHFAYLPTGLYVFAYKKDVYLRVCTLIIFFAALVAVISGASCLYLVRRVINRGIVEKEAIINNHFERVLDGGLFFSAADVKKLYSMYNSAFLDDLTKAMGRKSFDEDLKALPEKGGYLCLFDVDKFKNINDTFGHLLGDEVLMKVVKILKSQIPVDKGKVYRFGGDEFAVIYTGGTLEELLSILKEIVHFQVGSINLSTSIGVAHSNECTTVERLKMLADERLYKSKKNGRAQISWQ
Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.
Q8X6V3
Q472B7
SELO_CUPPJ
Protein adenylyltransferase SelO
Cupriavidus
MSDTHPSQTTPRDAADSVATLSAPFPTMPGFAELGERFFTRLRPTPLPSAYLVSVAPNAAALLGMPVEAASEPDFIEAFVGNSVPDWADPLATVYSGHQFGVWAGQLGDGRAIRLAQAQTDTGPWEIQLKGAGLTPYSRMADGRAVLRSSIREYLCSEAMAALGVPTTRALSIIGSDAPVRRETIETAAVVTRLAPTFIRFGHFEHFAAHEDVAALRQLADFVINNFMPACREAAQPYQALLREVSLRTADMVAHWQAIGFCHGVMNTDNMSILGLTIDYGPFGFLDAFDANHICNHSDTQGRYAYSQQPQVAFWNLHCLAQALLPLWLEPGADEAARDGAVAQAREALDPFRDRYASEFFRHYRAKLGIHMPAGGDKEDEPLLTSLFQLLHEQHVDYTLFWRNLARISSADGSGDAPVRDLFLDRAAWDTWAESYRNRLRAEQSDDAARRVAMLAVNPKYVLRNHLAEIAIRRAREKDFSEVDRLLAVLSRPFDEQPEAEAYAALPPDWAGGLEVSCSS
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Q472B7
Q2Y752
ISPF_NITMU
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Nitrosospira
MFFAEIKQEEVIVGGFRIGQGFDVHQLVEGRKLVIGGVTIPYEKGLLGHSDADVLLHAICDAVLGAAALGDIGRHFSDTDPRYRNIDSRVLLQNVGNLLAERGYRVVNVDATIIAQAPRMASHIPAMVANIAQDLRMQPGDVNVKAKTAERLGPVGRGEGIEAEAVCLITHMNQTTD
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Q2Y752
A4X982
MURL_SALTO
UDP-MurNAc-L-Ala-L-Glu epimerase
Salinispora
MPNEQLRRMDAFTFPSYSFDLSTGEALFDYALTGPDGEQRFTEVITLPLPASPPSDERVATLGRVLELLHVIAGVSYYKTAAPHRLVLPAPLGPSAVALVTAVYTKGLAEYAYRNALPHVLRLRPEVPSGEVTPPVGYDTDGRRPLSAVGGGKDSIVSLEALRRDGLDPLPFSVNPNRVIEAVNVASGLPALAARRRIDPVLFDLNAAGALNGHIPVTAINSLIAVATSVLNGLGPVVMSNERSASDPNLIWDGHQINHQWSKGVEAEGLLRGALEEHAGLTDPYFSLLRQLSELHIARTFARIGGYDDVVTSCNAAFKLRGASDRWCRDCPKCRFVFLALAPFMPRERITRVFGGDLLADPAQLPGYRELLGVDGHKPFECVGEVEESVVALSLLGEQSGWRDAPVVSALIDAVPETAWKTAATSAVFTPGGPSFTPTRYADALGSLTEPARNLPG
Cell wall formation. Catalyzes epimerization of the terminal L-glutamate in UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate.
A4X982
Q2L1Z2
AROK_BORA1
Shikimate kinase
Bordetella
MTLSVNLCSGAEALPTEQEAASLAVECIEPLAQLPHDLPIFLVGMMGAGKTTIGRGLARALGREFIDLDHELEARCGVRVPVIFEIEGEAGFRKRESTALQECTQRRGIILATGGGAVLAEENRRLLRERGIVLYLRASVDELFRRTSRDRNRPLLATADPRGTLNDLMIKREPLYKEVADLVIETGAMPITTLIKAILPKLQAYEKKL
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Q2L1Z2
Q6C555
GET1_YARLI
Guided entry of tail-anchored proteins 1
Yarrowia
MDEAIIVDAEFVAPVGTTAGEFVPIDRAPAAGLLLLVAFVVLYAKVISKLGKPAIQEFLWEIITRIVPSKQLRRRKEAQLRAIEVHTQRSNTSSQDQFAKWAKLDREYGKLKVEIEDINNLLTASKARFFTIISSAIFLSTTGMKMFLRIKHRKAAIFWLPKNAFPYPIEYILSFSSAPLGSVSVSAWLMICDAAMDLIVTIFVALVVGVIGMLRSNKVKPKTA
Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with GET2, acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. The GET complex cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER.
Q6C555
Q72GD5
NUOH_THET2
NDH-1 subunit H
Thermus
MTWSYPVDPYWMVALKALLVVVGLLTAFAFMTLIERRLLARFQVRMGPNRVGPFGLLQPLADAIKSIFKEDIVVAQADRFLFVLAPLISVVFALLAFGLIPFGPPGSFFGYQPWVINLDLGILYLFAVSELAVYGIFLSGWASGSKYSLLGSLRSSASLISYELGLGLALLAPVLLVGSLNLNDIVNWQKEHGWLFLYAFPAFLVYLIASMAEAARTPFDLPEAEQELVGGYHTEYSSIKWALFQMAEYIHFITASALIPTLFLGGWTMPVLEVPYLWMFLKLAFFLFFFIWIRATWFRLRYDQLLRFGWGFLFPLALLWFLVTALVVALDLPRTYLLYLSALSFLVLLGAVLYTPKPARKGGGA
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.
Q72GD5
Q88XQ4
XPT_LACPL
Xanthine phosphoribosyltransferase
Lactiplantibacillus
MRELEERILKDGRVLPGEVLKVDGFLNHQVDPDLMFAMGTEFAHLFQDAGVTKILTVESSGIAPAVMAGLAMHVPVVFARKHKSVTLIDDLYTAEVYSYTKKTSNHISIAKKFLQADDQVLLIDDFLANGQAVQGMFEICDKAHVKIAGVGIVIEKVFQTGHQLIADRGVRLESLAQITSFDGDRVHFASEDTQA
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
Q88XQ4
Q31HA6
DNAJ_HYDCU
Chaperone protein DnaJ
Hydrogenovibrio
MSKRDYYEILEVSATASEGEIKKAYRKLAMRYHPDRNPDDEEAEDKFKEASEAYEVLSDAQKRQAYDQFGHAGVDGSAGQGGFGGGGFADFGDIFGDIFGGGFGGGHRGPQPGSDLQYELEVSLEDAVAGTTVDVRIPTKELCESCDGSGAEPGSDVQTCPTCQGIGQVRVQQGFFAVSRTCPNCHGTGKLVKTPCKTCRGEGYKHSSKTLSVKIPAGVDNGDRIRLQGEGEAGEPGAPHGDLYVRIRVKEHKIFQRDGNTLFCDMPLSFATATLGGTMDVPTLNGKANLKIPAGTQSGQRFKLAGKGVKSVRSSHVGDMIVEVHIETPVKLTSEQKELLKAFDESLQGKHHKQHSPKTHSFFDSVKAFFKGDDEDGGNDKKDGPWN
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Q31HA6
I3R7F2
PCCX_HALMT
Propionyl-CoA carboxylase, protein PccX subunit
Haloferax
MTEDLLSGLSIPDDADSEEAAAIAAAVGAHLHDQTAAAVAAAADEEETWDEKRWQYAGRLDSVTGCARRVPSGAPTNAWAASGRTDRF
Part of the propionyl coenzyme A carboxylase (PCC) complex involved in propionate utilization and in the production of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate)(PHBV), which is a water-insoluble biopolymer used as intracellular energy reserve material when cells grow under conditions of nutrient limitation. The complex catalyzes the carboxylation of propionyl-CoA to methylmalonyl-CoA. PCC is also able to catalyze the carboxylation of acetyl-CoA. PccX could be responsible for the interaction of the biotin carboxylase and carboxyltransferase subunits.
I3R7F2
Q2IKN1
FETP_ANADE
Probable Fe(2+)-trafficking protein
Anaeromyxobacter
MARMVMCKKLGRELPGLAYKPFPNELGQRIYDSISQDAWKLWLEHFKMILNEYRLSPADPRTTEILFQQAEQFFFGENAQLPPDYRPPPSKG
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
Q2IKN1
Q6QGC0
PDLI3_PIG
Alpha-actinin-2-associated LIM protein
Sus
MPQNVILPGPAPWGFRLSGGIDFNQPLIITRITPGSKAAAANLCPGDVILAIDGYGTESMTHADAQDRIKAAAHQLCLKIDRAETRLWSPQVTEDGKAHPFKINLESEPQDVNYFEHKHNIRPKPFIIPGRSSGCSTPSGIDGGSGRSTPSSVSTLSTICPGDLKVAAKMAPNIPLEMELPGVKIVHAQFNTPMQLYSDDNIMETLQGQVSTALGETPSMSEPTTASVPPQSDVYRMLHDNRNEPTQPRQSGSFRVLQELVNDGPDDRPAGTRSVRAPVTKIHGGAGGTQKMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFVEGELYCETHARARMRPPEGYDTVTLYPKA
May play a role in the organization of actin filament arrays within muscle cells.
Q6QGC0
Q3J9L3
RNH2_NITOC
Ribonuclease HII
Nitrosococcus
MLLDGGILSTSVLGQRVAGVDEVGRGPLAGPVIAGAVILDPECPISGVKDSKQLTAPARERLAALIQAQAVAWALGRAEAAEIDQFNILQASLLAMERAISALSVVPDLVLVDGKHCPPTVCPVRAIVKGDQQIMAIGAASIVAKVARDAEMIAFEESYPGYGFGIHKGYPTRAHLAALKALGPCSIHRRSFRPVRRFLEA
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q3J9L3
B2S5T1
HIS3_BRUA1
Phosphoribosyl-AMP cyclohydrolase
Brucella
MSIFPAQPSDKKAVEEGAAFMPRFDASGLITAIVTDARDGELLMVAHMNEEALRLTLETGIAHYWSRSRKTLWKKGETSGNLQSVVELRTDCDQDALWLKVHVAGDGPTCHTGRRSCFYRQVVSSGGKVALTMASDHDQ
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
B2S5T1