Datasets:
habdine
/
Prot2Text-Data

Dataset card Data Studio Files
xet
Community
1
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
B7MNC1
RSMC_ECO45
rRNA (guanine-N(2)-)-methyltransferase RsmC
Escherichia
MSAFTPASEVLLRHSDDFEQSRILFAGDLQDDLPARLDTAASRAHTQQFHHWQVLSRQMGDNARFSLVATADDVADCDTLIYYWPKNKPEAQFQLMNLLSLLPVGTDIFVVGENRSGVRSAEQMLADYAPLNKVDSARRCGLYFGRLEKQPVFDAEKFWGEYSVDGLTVKTLPGVFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVLSVAFARHSPKIRLTLCDVSAPAVEASRATLAANGVEGEVFASNVFSEVKGRFDMIISNPPFHDGMQTSLDAAQTLIRGAVRHLNSGGELRIVANAFLPYPDVLDETFGFHEVIAQTGRFKVYRAIMTRQAKKG
Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
B7MNC1
Q01W95
RL2_SOLUE
50S ribosomal protein L2
Candidatus Solibacter
MPIKSYRPTTPTRRFQTVVSREDITKQTPEKSLVESKKRSGGRNSTGRVTSRFIGGGAKKAYRVVDFKRDKAGIPAVVAAIEYDPNRSSRIALLNYVDGEKRYILQPDGLKVGMKIMSGPNADILIGNALPLKNIPAGTIVHNIELKPGKGGQMARSAGSQAQLVSREGGLALLKLPSGEIRRVAVECMATVGQVGNVDHENVSLGKAGRKRWMGKTPHNRGVSMNPVDHPHGGGEGKTSGGRHPVTPWGQPTRGFKTRNNKRTDKWIVNRKSKKR
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.
Q01W95
B0UUN2
NAGB_HISS2
Glucosamine-6-phosphate isomerase
Histophilus
MRLIPLKTAQQVSKWAAKYIVDRINTFAPTAERPFVLGLPTGGTPLQTYKELIKLYQAEEVSFKYVVTFNMDEYVGLPKEHPESYHSFMYNNFFNHIDIQPQNINILDGNTDDHDEECRRYEEKIKSYGKINLFMGGVGVDGHIAFNEPASSLASRTRIKTLTEDTLIANSRFFDNDVTKVPKYALTIGVATLLDAEEVMLLVTGHNKALALQAGVEGNVNHFWTISALQLHRHAIFVCDEPATQELKVKTVKYFTELEQRAIHSVLD
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
B0UUN2
Q1DCG7
FMT_MYXXD
Methionyl-tRNA formyltransferase
Myxococcus
MSRPRIVFMGTPEFAVSSLAACFELGDVVAVVTQPDKPKGRGNTVTAPPVKELALSRGVPVLQPTKLRTPPFAEELRQYAPDVCVVTAYGRILPKDLLELPTHGCVNVHGSLLPRFRGAAPIQWAIAHGDTETGVSLMVMDEGLDTGPVLAMKRMAIAPDETSASLYPKLAALGGEVLREFLPAYLSGELKPVPQPSEGMVLAPIIEKDQGRLDFTKPAVELERRLRAFTPWPGAFTTLGGKLLKVHRAQARGGSGAPGTVLASGPDGIEVACGEGSLVLLDLQPEGKRVMRAADFLQGHKLAPGSQPFVAG
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Q1DCG7
A0KRH2
PCKA_SHESA
Phosphoenolpyruvate carboxykinase (ATP)
Shewanella
MADGLNRVHYNPSTAQLVEFALLRGEGELTANGALVAKTGTRTGRSPGDRFIVKEDSSAADIEWGPVNQAFEPGAFEGLWARVEAFLADKELFVSDLEVGADPEHYQPVRVTTQYAWHQLFARNLFIIPEEFNRQDKPVWQIINAPDFVCVPERDGTNSDAAVILNFAERKVLLAGLKYAGEMKKSMFSVQNFLLPAQGVLPMHCSANVGKDGDTTLFFGLSGTGKTTLSADPKRFLIGDDEHGWAPGGVFNIEGGCYAKCIDLSQKNEPVIWDAIRFGTVLENVVMDEHRVPNYKDSSLTENTRAAYPLEHIAQRKEDNRGAEPHAVVFLTCDVSGVLPPVSILSKEQAAYHFLSGYTAKVGSTEIGSTSAIQSTFSTCFGAPFFPRPAGVYAELLMKRIESFGSQVYLVNTGWTGGPHGIGKRFDIPTTRAIVDAIVSGELKNVETVHLETLNLAVPVAVPGVDTNLLNPVNTWSDKALYAEYAQKLAEAFTKNFAKYQVSDAIRNAGPKA
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
A0KRH2
A1ADD0
NUOH_ECOK1
NDH-1 subunit H
Escherichia
MSWISPELIEILLTVLKAVVILLVVVTCGAFMSFGERRLLGLFQNRYGPNRVGWGGSLQLVADMIKMFFKEDWIPKFSDRVIFTLAPMIAFTSLLLAFAIVPVSPGWVVADLNIGILFFLMMAGLAVYAVLFAGWSSNNKYSLLGAMRASAQTLSYEVFLGLSLMGVVAQAGSFNMTDIVNSQAHVWNVIPQFFGFITFAIAGVAVCHRHPFDQPEAEQELADGYHIEYSGMKFGLFFVGEYIGIVTISALMVTLFFGGWQGPLLPPFIWFALKTAFFMMMFILIRASLPRPRYDQVMSFGWKICLPLTLINLLVTAAVILWQAQ
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.
A1ADD0
Q08751
NEPU2_THEVU
TVA II
Thermoactinomyces
MLLEAIFHEAKGSYAYPISETQLRVRLRAKKGDVVRCEVLYADRYASPEEELAHALAGKAGSDERFDYFEALLECSTKRVKYVFLLTGPQGEAVYFGETGFSAERSKAGVFQYAYIHRSEVFTTPEWAKEAVIYQIFPERFANGDPSNDPPGTEQWAKDARPRHDSFYGGDLKGVIDRLPYLEELGVTALYFTPIFASPSHHKYDTADYLAIDPQFGDLPTFRRLVDEAHRRGIKIILDAVFNHAGDQFFAFRDVLQKGEQSRYKDWFFIEDFPVSKTSRTNYETFAVQVPAMPKLRTENPEVKEYLFDVARFWMEQGIDGWRLDVANEVDHAFWREFRRLVKSLNPDALIVGEIWHDASGWLMGDQFDSVMNYLFRESVIRFFATGEIHAERFDAELTRARMLYPEQAAQGLWNLLDSHDTERFLTSCGGNEAKFRLAVLFQMTYLGTPLIYYGDEIGMAGATDPDCRRPMIWEEKEQNRGLFEFYKELIRLRHRLASLTRGNVRSWHADKQANLYAFVRTVQDQHVGVVLNNRGEKQTVLLQVPESGGKTWLDCLTGEEVHGKQGQLKLTLRPYQGMILWNGR
Hydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose.
Q08751
A7H576
PAND_CAMJD
Aspartate 1-decarboxylase alpha chain
Campylobacter
MNIALLKSKIHRASVTEARLDYVGSISIDEKLLQASGILEYEKVQVVNINNGARFETYTIATQEEGVVCLNGATARLAEVGDKVIIMSYADFNEEEAKTFKPKVVFVDENNTATKITNYEKHGSIF
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
A7H576
Q1KVR1
RK14_TETOB
50S ribosomal protein L14, chloroplastic
Tetradesmus
MIQPQSYLNVADNSGARKLMCIRVLGGGRQTATIGDVIIAVVKDALPNMPLKKSDVVRAVIVRTSKGVRRENGMMLCFDDNAAVVINKEGNPRGTRVFGPIARELRDRNFTKIVSLAPEVV
Binds to 23S rRNA.
Q1KVR1
B3EPH6
THIC_CHLPB
Thiamine biosynthesis protein ThiC
Chlorobium
MSTSPDNLFCPEQNFYGPDSEKIYIDGSLHPVKVGMRRIKLSKTYTLHGTDFSSFPLYDTSGPYSDPSVTIDLHKGLPSTRDFWQKNRTDIEVCPGKNPSPMNNRTPVRAKQGKSVTQMHYARKGIITPEMEYVAIRENQQLEEWIERFSSNGSSVKPVTPEFVRDEIAKGRAIIPANINHPELEPMAIGRNFRVKINANIGNSALASSISEEVEKSVWACRWGADTVMDLSTGKNIHQTREWILRNSPVPIGTVPIYQALEKVGGKAEELNWNIYRDTLIEQAEQGVDYFTIHSGILLDFLPAAQRRTTGIVSRGGSIIAKWCRAHKQENFLYSHFDDICDILRSYDIAISIGDALRPGSIADANDEAQFSELKTLGELTLKAWKYDVQVMIEGPGHVPLNLVEENMRKQLEYCHEAPFYTLGPLVTDIAAGYDHVNSAIGGTLLASLGCAMLCYVTPKEHLGLPDKNDVREGVIVHKLAAHAADIAKGSPSALLHDKLMSSARYSFAWNDQFNLSLDPVKTRQVHAESSQQNTGDGTDDHFCTMCGPDFCSMKKSQEVTGK
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
B3EPH6
Q6GHJ9
Y1212_STAAR
UPF0122 protein SAR1212
Staphylococcus
MGQNDLVKTLRMNYLFDFYQSLLTNKQRNYLELFYLEDYSLSEIADTFNVSRQAVYDNIRRTGDLVEDYEKKLELYQKFEQRREIYDEMKKHLSNPEQIQRYIQQLEDLE
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
Q6GHJ9
Q6NYR8
NPL_DANRE
Sialic acid lyase
Danio
MSQRVKKLTGLVAATFTPLTAEGEINLSVIAAYVDYLIEKQNVKSVFVNGTTGEGCSLTVDERKHLAAAWCQHGKGKLEQLIVHVGCMSIKDSQELARHAASIGADGISVISPSYFKPINADALRLFIKEVSASAPDLPMYYYHLPGMTGVALEAADVLNGIEREIPSFQGVKYSGTDLRDLGQCVCYSQSRDWSVLYGVDEQLLGALVLGVHGAVGSTYNYLGHIVNQMLSAFNNGNHTQTRDLQFGFMEVITFARTLGFDVSVNKQVMSEVSGLPMGPPRLPLLPCPVSKAQAIAQKIHNFTQGL
Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
Q6NYR8
A0A075TXZ8
PATL_PENEN
Patulin biosynthesis cluster protein L
Penicillium
MYSTFSANFDTTIDASRDRSATPVTAPRPKRNQVARACDWCRLNRVRCDDKQPCQNCQNRGGSCSNTKPQEATSLPAANREMQRLRNKVKDLQDQIAKLKEGAEIQAQTGFATPPLSDAAHTSFDFAELTNTTEGWQGLQQTGQIHYGPLSSSYFVSRISRYLSQALNEPIEDAKLEACMARFHYIAPSHQPSRWDASPASQADQPQDGTEEAEDLTRSQEEHFLNLLWQSFHCVYPILDEREFQQYYESLWSSSPDGMSTRKPSALVDVLLAVCMQYSSTFFVSDDNQQGDTDSEWQAKHANLASRTYYQRAQRLLQSELENPTIMVVQSHIYSIVYLYNTSLLNTAHINLGATLRIAHALRLHIRPLDGTSPEQQELQRRIWWALYRIDSQLSMTLGRPPLIQLSHVSCGLPGDDREHARLSGTVLLTNHEDISWLSFHVQCTKLIFLVQGVQTAFNRKCSQLLNGDKVKDLYEDPRLLETLAEFLGQEMTAIHNWVQNVPQSLCNPRKGGSDPFSTNRDALNLSAYSPLWLQRQRLLLELHYHHLVISTLRPFIRFPPVSSSMTPLTDGYNISCLNHAMAITSILNQVLSETDLLRGWSPIFQYQWDAILCTLGFVLANSVCPPTPSARKSLQTAIRTLDLVSDHFLAAKNAAQVVREVSCQADRLVKNVQQGLTRRQAPRASQALSTRAQNPRQASNQTSFVAPAQPGVRSNSLKRALPPTTLEVSQHQPMPNFEARMQLMDMMPIGSLSELSPSLGTTESMSMPSVTSADMVIGTEAQWLHASAMILDSWTTNS
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria.
A0A075TXZ8
Q9BVJ6
UT14A_HUMAN
Serologically defined colon cancer antigen 16
Homo
MTANRLAESLLALSQQEELADLPKDYLLSESEDEGDNDGERKHQKLLEAISSLDGKNRRKLAERSEASLKVSEFNVSSEGSGEKLVLADLLEPVKTSSSLATVKKQLSRVKSKKTVELPLNKEEIERIHREVAFNKTAQVLSKWDPVVLKNRQAEQLVFPLEKEEPAIAPIEHVLSGWKARTPLEQEIFNLLHKNKQPVTDPLLTPVEKASLRAMSLEEAKMRRAELQRARALQSYYEAKARREKKIKSKKYHKVVKKGKAKKALKEFEQLRKVNPAAALEELEKIEKARMMERMSLKHQNSGKWAKSKAIMAKYDLEARQAMQEQLSKNKELTQKLQVASESEEEEGGTEDVEELLVPDVVNEVQMNADGPNPWMLRSCTSDTKEAATQEDPEQLPELEAHGVSESEGEERPVAEEEILLREFEERRSLRKRSELSQDAEPAGSQETKDSGSQEVLSELRVLSQKLKENHQSRKQKASSEGTIPQVQREEPAPEEEEPLLLQRPERVQTLEELEELGKEECFQNKELPRPVLEGQQSERTPNNRPDAPKEKKKKEQMIDLQNLLTTQSPSVKSLAVPTIEELEDEEERNHRQMIKEAFAGDDVIRDFLKEKREAVEASKPKDVDLTLPGWGEWGGVGLKPSAKKRRRFLIKAPEGPPRKDKNLPNVIINEKRNIHAAAHQVRVLPYPFTHHWQFERTIQTPIGSTWNTQRAFQKLTTPKVVTKPGHIINPIKAEDVGYRSSSRSDLSVIQRNPKRITTRHKKQLKKCSVD
May be required for ribosome biogenesis.
Q9BVJ6
Q9ZFE1
CH10_BURCE
Chaperonin-10
Burkholderia cepacia complex
MNLRPLHDRVIVKRLDQETKTASGIVIPDAAAEKPDQGEVLAIGPGKRDDKGAPIALDVKVGDRVLFGKYAGQTVKVDGQELLVMREEDIMAVVNAK
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.
Q9ZFE1
Q0T7A9
AES_SHIF8
Acetyl esterase
Shigella
MKPENKLPVLDLISAEMKTVVNTLQPDLPSWPATGTIAEQRQYYTLERRFWNAGAPEMATRAYMVPTKYGQVETRLFCPQPDSPATLFYLHGGGFILGNLDTHDRIMRLLASYSQCTVIGINYTLSPEARFPQAIEEIVAACCYFHQQAEDYQINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKIAGVLLWYGLYGLRDSVTRRLLGGAWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTREVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQFFTAQL
Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity.
Q0T7A9
Q9SIU8
P2C20_ARATH
AtPPC3;1.2
Arabidopsis
MAGREILHKMKVGLCGSDTGRGKTKVWKNIAHGYDFVKGKAGHPMEDYVVSEFKKVDGHDLGLFAIFDGHLGHDVAKYLQTNLFDNILKEKDFWTDTKNAIRNAYISTDAVILEQSLKLGKGGSTAVTGILIDGKTLVIANVGDSRAVMSKNGVASQLSVDHEPSKEQKEIESRGGFVSNIPGDVPRVDGQLAVARAFGDKSLKIHLSSDPDIRDENIDHETEFILFASDGVWKVMSNQEAVDLIKSIKDPQAAAKELIEEAVSKQSTDDISCIVPCFLRREALSERYCR
May be involved in defense signaling.
Q9SIU8
Q891Z8
RUVB_CLOTE
Holliday junction ATP-dependent DNA helicase RuvB
Clostridium
MIILDNRFVTPLSIEEDIDIEYNLRPTQLEEYIGQSKVREKLRIFIKAAKNRGESLDHVLLYGPPGLGKTTLANIIAKEMKGNLKITSGPAIERAGDLAAILTTLNEHDVLFIDEIHRLNRAVEEILYPAMEDYALDIVIGKGAAAKSIRLDLPHFTLIGATTRVGLLTAPLRDRFGVLCPMEFYNEEELKDIIVRSSKILNVKTEEEAAYELARRSRGTPRIANRILKRVRDYSEVMGDGIIDLNMTNKALNLLEIDKEGFDSIDTKILKAILDNFNGGPVGLETLAYFIGEELDTIEDVYEPYLLQKGFIMRTPRGRVATEKTYKHFKREIKKENINQYKFKI
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
Q891Z8
P0CP51
PAN3_CRYNB
Poly(A)-nuclease deadenylation complex subunit 3
Cryptococcus neoformans species complex
MLPPPKSAAVQIVRPPSPSSEKAKEKEKKHSPEKRETAQRICRNVMIYGYCKYQDQGCIYYHPPAGADPSTPQNSSPVAHAPTPSAPTPLAGTPAREKPTLSIEHLAAPVFVPKGLDSSPRASTPSVPTPSAPTPPVWPSLPSTGLLPRQDVQVSAQPSHAQLSATASPMAYDDPSHIALSAAHAHAQAQALTHGILDPHAHAPPVDQSMYLPPRQPLDYNLYAAPLPSIGGNPLYPTHPHAFFVSDDLRRAIQAKQEAVYAGANGASAPGLPQELGVYHSLIPLPLPAPTAQCPPTQSQPSKVYGLPSPVYRATSEVDGNTYCLRRVEGFKLVNQLAFASMDTWRRMRHPNIVGLKEAFTTKTFGDNSLIMVYDYHPLSTTLYDEYLSPNPPEPSPASALANQPPKRRSSPPERILWSYVTQIANALKAIHSSGLAVRNLDASKILLTGKNRIRLNGCGVWDVLAFDNKTPVQAFQQEDLLSFGKLIISLTCDFFQPTLPFSLPLEHISRHYSSDLSNLILYLISKPAQGQIKSIDEVVKMMGPRILNELDAVQSYADVLENELGAEVENGRIVRLLTKLGFINERAEFELDPRWSDTGDRYILKLFRDYVFHSVGVDGKPILDLSHVLVCLNKLDAGLDERVMLVSRDDQSCLVVSYREIKHCIEAAFNELKNAGNNHRVHR
Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
P0CP51
B5YE18
AROB_DICT6
3-dehydroquinate synthase
Dictyoglomus
MEELRVELKDKKYPIYIGYDILKKFLKNYRDNYSFSFIITHSFLYDLYKEDLEISQEGIIYVPVGEKSKSFKEVIRISRELAQRGADRKSAIFAFGGGVIGDLTGFVASIYMRGIRYIQIPTTLLAQVDSSIGGKTGINIKEGKNLIGTFYHPDAVIIDIKTLNTLPEREYRSGIAEVIKYGMIMNQSLFNFLEKNTTSILNKDIDILSHIIRESLICKKYVVEKDEKESSLRMILNFGHTFGHAIEAKGGYKRFLHGEAVAIGMFLATYLAYKIGFCDYSVLKRLQDTLLSFGFDLNNPYRIEDLVGYIKRDKKAYGGKIRLILPKEIGKVEIVENLEEKDIIKALKAGDGYGK
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
B5YE18
Q6YPD0
HOX27_ORYSJ
OsHox27
Oryza sativa
MELGLSLGDAVTVADGGRLELVLGLGVGVGAGVRRGEEEERGRREDVVGAGRWAAMAAASPEPSVRLSLVSSLGLHWPSETGRSEAAARGFDVNRAPSVAAGAPGMEDDEEGPGAAPALSSSPNDSGGSFPLDLSGQGLRGHAEAAAQGGGGGGGGERSSSRASDDDEGASARKKLRLSKEQSAFLEESFKEHSTLNPKQKVALAKQLNLRPRQVEVWFQNRRARTKLKQTEVDCEYLKRCCETLTEENRRLHKELAELRALKTARPFYMHLPATTLSMCPSCERVASNPATASTSAPAAATSPAAAPTAAARTAVASPEPHRPSSFAALFAAPLGFPLTAAQPRPPPPASNCL
Probable transcription factor.
Q6YPD0
Q9Y315
DEOC_HUMAN
Phosphodeoxyriboaldolase
Homo
MSAHNRGTELDLSWISKIQVNHPAVLRRAEQIQARRTVKKEWQAAWLLKAVTFIDLTTLSGDDTSSNIQRLCYKAKYPIREDLLKALNMHDKGITTAAVCVYPARVCDAVKALKAAGCNIPVASVAAGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEIRQFRKACGEAHLKTILATGELGTLTNVYKASMIAMMAGSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTGNKIGFKPAGGIRSAKDSLAWLSLVKEELGDEWLKPELFRIGASTLLSDIERQIYHHVTGRYAAYHDLPMS
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. Participates in stress granule (SG) assembly. May allow ATP production from extracellular deoxyinosine in conditions of energy deprivation.
Q9Y315
A5WB34
UBIA_PSEP1
4-HB polyprenyltransferase
Pseudomonas
MYLQLLKSLNRLHPRAWDFVQLSRMDRPIGIYLLLWPTLSAVWIAGNGSPTLANVLIFGLGVVLMRAAGCCINDFADRKVDGHVKRTADRPLASGRVRPREALTLFAILVGVSFLLVLCTNSRTVWLSFGAVALAFCYPFMKRYTYYPQVVLGAAYSWGIPMAFTAAGGELPAGAWLLYIANLLWTVGYDTYYAMVDRDDDLKIGVKSTAILFGDADRSIILTLQLLSLGCLLLAGSRFDLGGWFHLGLLGAAACFAWEYWSTRKLDRESCFKAFLHNHWAGMLVFIGVVLDYALR
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
A5WB34
A9H9A8
ATPB_GLUDA
F-ATPase subunit beta
Gluconacetobacter
MSETTQNEAPVAAQGASQHSNIVGRVTQVRGAVVDVQFEGTLPHILDALHVTFNGQTVVLEVAQEIGEHEVRCIAMDTTDGLMRGTEVVATGGQITVPVGPGTLGRILNVIGEPIDERGPVKSDKRYPIHRKAPSFDEQAAATEILVTGIKVVDLLCPYLKGGKVGLFGGAGVGKTVIIQELINNIAKAHGGVSVFAGVGERTREGNDLYYEMQDAGVIKLGEDTTEGSKVALVYGQMNEPPGARARIALSGLSLAEYFRDEEGQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPAATFAHLDATTVLNRSIAEMGIYPAVDPLDSTSRSLDPKIVGEEHYQVARDVQRILQTYKSLQDIIAILGMDELSEDDKQVVARARRIQRFLSQPFHVAEVFTGAPGKLVSLEDTVRSFKAIVAGEYDHLPEGAFYMVGSIEEAVAKAEKMKETA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
A9H9A8
Q8Z377
ILVD_SALTI
Dihydroxy-acid dehydratase
Salmonella
MPKYRSATTTHGRNMAGARALWRATGMTDSDFGKPIITVVNSFTQFVPGHVHLRDLGKLVAEQIEASGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMASLRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDDQSNQVERSACPTCGSCSGMFTANSMNCLIEALGLSQPGNGSLLATHADRKQLFLNAGKRIVELTKRYYEQDDESALPRNIANKAAFENAMTLDIAMGGSTNTVLHLLAAAQEAEIDFTMSDIDKLSRKVPQLCKVAPSTQKYHMEDVHRAGGVLGILGELDRAGLLNRNVKNVLGLTLPQTLEQYDITVTQDEAVKKMFRAGPAGIRTTQAFSQDCRWDSLDDDRAAGCIRSLEYAYSKDGGLAVLYGNFAENGCIVKTAGVDDSILKFTGPVKVYESQDDAVEAILGGKVVEGDVVVIRYEGPKGGPGMQEMLYPTSFLKSMGLGKACALITDGRFSGGTSGLSIGHVSPEAASGGTIALIEDGDTIAIDIPNRSIQLQLSEAEIAARREAQEARGDKAWTPKNRQRQVSFALRAYASLATSADKGAVRDKSKLGG
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Q8Z377
Q9SL92
HCS1_ARATH
Biotin--[acetyl-CoA-carboxylase] ligase
Arabidopsis
MEAVRSTTTLSNFHLLNILVLRSLKPLHRLSFSFSASAMESDASCSLVLCGKSSVETEVAKGLKNKNSLKLPDNTKVSLILESEAKNLVKDDDNSFNLSLFMNSIITHRFGRFLIWSPRLSSTHDVVSHNFSELPVGSVCVTDIQFKGRGRTKNVWESPKGCLMYSFTLEMEDGRVVPLIQYVVSLAVTEAVKDVCDKKGLPYIDVKIKWPNDLYVNGLKVGGILCTSTYRSKKFNVSVGVGLNVDNGQPTTCLNAVLKGMAPESNLLKREEILGAFFHKFEKFFDLFMDQGFKSLEELYYRTWLHSEQRVIVEDKVEDQVVQNVVTIQGLTSSGYLLAVGDDNQMYELHPDGNSFDFFKGLVRRKI
Plays a major role in biotin-dependent carboxylase biotinylation . Catalyzes the addition of biotin to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase . Can also biotinylate methylcrotonyl-CoA carboxylase . Is responsible for most, if not all, biotin--protein ligase activity in Arabidopsis . Is essential for plant viability and required for ovule development .
Q9SL92
Q0KEQ3
COAD_CUPNH
Pantetheine-phosphate adenylyltransferase
Cupriavidus
MVIAVYPGTFDPMTRGHEDLVRRASNIFDELVVGVAHSPNKRPFFSLEERIGIAREVLGHYPNVRVEGFSGLLKDFVRNNNARVIVRGLRAVSDFEYEFQMAGMNRYLLPDVETMFLTPSDQYQFISGTFVREIAVLGGDVSKFVFPSVERWLQEKIGKPE
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Q0KEQ3
Q5LPV9
KTHY_RUEPO
dTMP kinase
Ruegeria
MSGTGLFLTFEGIDGSGKSTQARLLAETLRAAGHDVVLTREPGGSPGAEEIRRLVLEGDPDRWSAETEILLFTAARRDHLERTIEPALAAGRVVICDRFADSTRMYQGLSRGDLRQLVDQLHALMIGREPDLTLLVDMDPETGLSRAKGRQGSEERFEDFGPELQQRMRAGFLDLAREYAHRFRIIDGNRDMDSVAADVTEIVLTHLNRTR
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Q5LPV9
H1A981
C7263_MEDTR
Cytochrome P450 72A63
Medicago
MEVFMFPTGTTVIISVLSVLLAVIPWYLLNKLWLKPKRFEKLLKAQGFQGEPYNLSVLKDKSKQNYMLKLQQEDKSKSIGLSKEAAPSIFTPVHQTVRKYGNNSFLWEGTTPRVIITDPDQIKDVFNKIDDFPKPKLRSIAKYLSVGILDHEGKKWAKHRKIANPAFHLEKLKVMLPAFSHSCNEMISKWKELLSSDGTCEIDVWPSLQNFTCDVISRTAFGSSYAEGTKLFQLLKKQGFLLMTGRHTNNPLWGLLATTTKTKMKEIDREIHDSLEGIIEKREKALKNGETTNDDLLGILLQSNHAEKQGQGNSKNIGMTTQDVIDECKLFYLAGQETTSSLLVWTMVLLGRYPEWQARAREEVLQVFGNQNPNNEGLSQLKIVTMILYEVLRLFPPLIYFNRALRKDLKLGNLLLPEGTQISLPILLIHQDHDLWGDDAKEFKPERFAEGIAKATKGQVSYFPFGWGPRICLGQNFALLEAKIAVSLLLQNFSFELSPNYVHVPTTVLTLQPKNGASIILHKL
Involved in the biosynthesis of triterpenoid saponins. Catalyzes three sequential oxidation steps at C-30 of 11-oxo-beta-amyrin. Also able to catalyze sequential C-30 hydroxylation of beta-amyrin to produce 30-hydroxy-beta-amyrin and 11-deoxoglycyrrhetinic acid.
H1A981
Q85A51
CCSA_ANTAG
Cytochrome c biogenesis protein CcsA
Anthoceros
MILINLEHILAHISFFLPFLATLVFWGRIVCIDNKRIGSLGNKSIIIAYICITGLLLTRWFHSRHLLLSNLYESFMFLSWSFCLIHIVSEIGSKNDWLGIIIVLIAMLTHGFATVGLPIEMQQSTVLVPALQSHWLIMHVSMMIPSYATLPCGSLLVIALLITTLNKNKNFPILKFNVNSFIWSLILEKKFYLGGSGGDISSRNSSSGNGSDNDSNNNNNKKTFHSLSIDCRKLQLTQQLDYWSYRIISLGSLFLTIGILSGAVWVNEAWGSYWSWDPKETWALITWLLSAIHIHIRMIRGWQGEKPAIIASSGSSIVWFRYLGVNSPEKGLHSYGWLN
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Q85A51
P51148
RAB5C_HUMAN
RAB5L
Homo
MAGRGGAARPNGPAAGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNTDTFARAKNWVKELQRQASPNIVIALAGNKADLASKRAVEFQEAQAYADDNSLLFMETSAKTAMNVNEIFMAIAKKLPKNEPQNATGAPGRNRGVDLQENNPASRSQCCSN
Protein transport. Probably involved in vesicular traffic.
P51148
C5DDK8
MTC6_LACTC
Maintenance of telomere capping protein 6
Lachancea
MNRVVYGLLLTLVLNVVRGQSFWPALSSDSLIALRSQRDVLSNISIDKVPMVGVQLNEVAFRGTSNETESLEILASLLNVGVQAYMMDIEFDESYNLTISGSDTSLGTTLSTFKRFISSSNNYLNADMLVLLLRLKQNTNTSTKGAPSNFPNITAILDLYLGSSTLYTPSQLAYDRSSGNVAPSYGNLNSPDWPSLNYFLYSIQKRAVVFYVDTASSDALQSPAIFNASNLNYETSNTPIVCPLTNNAQVLNTSSLSWRFLQKDYSPSDIREYTMCGYSPIIDNKYNPNSINTISNVLENSLLWSWASNEPNTSDDTRSNSTSLVARRCAVVHYTKSNSSSYWTVANCYDRKRALCKRDGNDFEWAVTQEGASYFSHHDQDGNGFCPDNFSLSLPQTALQEKSLDNYLSQLSPEGWEIWIDLNSVSVPDCWVPDGPYASCPYQKEVSTRNFVSMITPVSVFAAVTILMLIMLSWRRVPIQDNRKRWKRVINSHLGSKAEGVPA
May be involved in telomere capping.
C5DDK8
A3PNS6
MNMG_CERS1
Glucose-inhibited division protein A
Cereibacter
MKHFDVVVIGGGHAGCEAAATAARMGVQVALITLRKSGLGVMSCNPAIGGLGKGHLVREIDALDGIMGRAADEAGIQFRLLNRKKGPAVQGPRAQADRRLYREAVQRLLAEQPGLTIIEGEVVDLQVNGGRVQGVSLADGTSVGAGRVILTSGTFLNGVIHIGDQRRPGGRMGDDPSQRLAAVLGELSLARGRLKTGTPPRLDGRTIRWAELEMQPGDEDPVVFSFLNRVPKARQIACGITHTNARTHQIVRDNLSRSAMYGGHIEGVGPRYCPSIEDKIVRFADKEEHQVFLEPEGLDDDTVYPNGISTSLPAEVQEAYVRTIAGLEDVRILQPGYAIEYDYFDPRELRPTLEVKALGGLYFAGQINGTTGYEEAAAQGLAAGLNAALSIREREPLHFSRSGSYLGVMIDDLTSRGVTEPYRMFTSRAEFRLSLRADNADQRLTPIGLDLGCVSDARRESFNKKRELLEKGRALLEGSSFTPSQLNELGIQVSQDGMRRTAFAVMAFGEEAASAVARGVEGYGDLPEEIRQQLAKDGLYAQFILRQEEEAAALKRDEAIRIPADFDYAPLSGLSSELKAKLMRARPSTIAQAAQLEGMTPSALTLILARLRRAGRDAAAV
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
A3PNS6
B5EFN9
RL11_CITBB
50S ribosomal protein L11
Citrifermentans
MAKKITGYIKLQVPAGKANPSPPIGPALGQHGVNIMEFCKAFNAKTQADEGTITPVVITVYADRSFTFITKTPPAPVLIKKALGLQSGSAVPNKTKVGKLTKDQVREIATKKMPDLNAASLEAAMKTIEGTARSMGVEIV
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
B5EFN9
A6UQM0
BIOW_METVS
Pimeloyl-CoA synthase
Methanococcus
MFSLKMRASKDGVHVSGAERISTENKIEEIANSLIKRALFHENGTPDTINLKLEKITSEITYLKHIPIKTLISNNKETSRNISRNILRKELEVYFLKNGKDFGKIDILIDTAFEIIDKGNMRGAAVLDLDGNRLEEDTEKGVRVKNIDTSEELKSKILADSKLTDRTIDAIAIATKVLNFGFIAEICTSDNYSYNIGYVATKSGYFRIPNLKNEGEFGGRVFFIENSANIEEIFEKIEKTPVIVY
Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
A6UQM0
D0NYP1
RXLRX_PHYIT
RxLR effector protein PITG_18609
Phytophthora
MRMHSVLMMVVATLAIANGSVSAAGGSNLRKAKATSSINSFNTVQTEAKNSRMLRNTDVATGENGHVYYYPAKKGERKPFIEVRLKKALSNSKKVNRLYEDWYKSGFSTKKVAKELNQSENRELKETYKTLAIGYTAFVKGKQSQQQLQ
Effector that enhances P.infestans colonization of Nicotiana benthamiana leaves.
D0NYP1
Q31DD5
GATB_PROM9
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Prochlorococcus
MNNLESWEAVIGLETHVQLNTKSKIFTSASTAFGDAPNTHIDPVVCGLPGTLPVLNETVLEYAVKTSLALNLNVAEHCKFDRKQYFYPDLPKNYQISQFDEPLAENGWLEVEIIEKDKDPYTKKIGIERLHMEEDAGKLVHSGSDRLAGSKYSLVDYNRAGIALCEIVSKPDIRTGREAAEYASEIRRTVRYLGVSDGNMQEGSLRCDVNISVRKGPNAPFGTKVEIKNMNSFSAIQKACDYEIARQIEVYENGGEIFQETRLWDEAKQLTKSMRLKEGSSDYRYFPDPDLGPIEITKAQKEIWFNELPELPSKKRNKYVNEFGLSAYDARVISDEINMANFFEETVANGAEAKLASNWVTSDIVGYLKANKLSFSELKLSPENLAEMINMILKNTISGKIAKEILPELIKKNISPKKLVEEKGLAMISDSSSILPIINELINEYPNEVQAFRNGKTKLLGFFIGQLMKRTKGKADPKLANKLLAEKLNG
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Q31DD5
B9KDV7
MIAA_CAMLR
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Campylobacter
MFFEFALIGTTASGKTELANKLAYEFNASILSLDSLCVYKQINIASAKTEQKTLDELDYFGINLLNVNEHFNIALFFEEYKKAKTFAQKNNQILIITGGTSFYLKALMDGLSENFKESQSTLSNDEIYHLMIKIDPQAKIEKNDTYRLKKWLGIYEQTNKIPSEVLKETKQEALIKKLDIFEISWQKDLLEKRIIKRTKNMLNEGLIEEAKMLFDNYDHHLKALNSIGLKECKDFLDKKINLNKLEELIIIHTRQLAKRQRTFNKKFNKENLDFQSAYENLKAYILKKYQG
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
B9KDV7
Q9ZCS8
RS11_RICPR
30S ribosomal protein S11
typhus group
MNQTIKVKKKKKTITLGVVHIRASFNNTIVTFTDIQGNTISSASAGGNGFKGARKATPYAAQVTIDKASEKAKECGLKTISIRIGGPGAQRESAMRALFGQNFVVTSILDVSSIAHNGVRPPKRRRV
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Q9ZCS8
A3CK79
RL6_STRSV
50S ribosomal protein L6
Streptococcus
MSRIGNKVIVLPAGVEISNKDNVVTVKGPKGELTREFSKDIEIRVEGTEVTLHRPNDSKEMKTIHGTTRALLNNMVVGVSEGFKKELEMRGVGYRAQLQGKKLVLSVGKSHPDEVEAPEGITFELPNPTTIVVSGISKEVVGQTAAYVRSLRAPEPYKGKGIRYVGEFVRRKEGKTGK
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.
A3CK79
Q2IL14
NUOI2_ANADE
NDH-1 subunit I 2
Anaeromyxobacter
MPQTVRAYTGAIRDTVKSFWHGLSITLSYLARRPTTVQYPDRTPMPVRDMLPPRYRGFLEVDSGICTGCQACERACPIGCIQISLEKDAANPKQRVVTQFDIDEAKCMFCGLCVEPCPTGSIQHTREFEGTHKHIRNLVFRWADPMNPFPVYKVDKNAEYYPRVPLGSLVRQRLETMAWDRSAPQFLPPEPPKPAEAKPAAKAAPAAKPAAAAPAAPAAAAPAAAPAPAKPAAAPAPAAAAAPAAPAAEAPAAPAAPAANPESK
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.
Q2IL14
Q6CKE8
PRP46_KLULA
Pre-mRNA-processing protein 46
Kluyveromyces
MNTSSRSSEPSKVADDVYVQTRWNNEFKHADYLPESLQKCLDQEKTVLERYSELVEVSKTVANESSQALVKHTTKPGDQLVRRVFQQPHQQISLMERYEKTRSYKPQWHAPWKLSKVINGHTGWVRCVCVDPVDNEWFATGSNDTTIKIWDLAAGKLKITLIGHVMSVRDIAISKRHPYMFSASEDKLVKCWDLERNTAIRDFHGHLSGVHTVDVHPSLDIIATAGRDAVVRLWDIRSRSEIMVLPGHKSPINKVKCLPVDPQIISCSGDATVRLWDIIAGKASKVLTHHSRNIRDLTLHPAEFSFASVSTNDVRSWKLPEGQLLTNFQSQNTGILNTVSINHDNVLLAGGDDGTLCFYDYKTGHKYQSMMTTEVAGSLESERSILCSTFDVTGTRLITGEGDKSIKIWKQVPDATEDTFPGLPWNPTLISQRF
Involved in pre-mRNA splicing and required for cell cycle progression at G2/M.
Q6CKE8
P0CT90
OMT2_PHACR
3-O-methyltransferase 2
Phanerodontia chrysosporium
MSDYPKTPQAAHLTALVELISSSVNEVISVYSAAGRDIPSLDSLEEGFLETPATTPPGLRHARQIIEAACAQLCVTIAQPGDCIVNKAFAYTESACLQVAANAKISDFLADKPDGLHTEELAKLSGVDAGKLGQVLRFLATKHVYREVRPNVYANNRLSVKLMSSDPVSCNVGVCTGELFQAATAAWDTLSDKEYGPSYLPTKTAFRKVHGATFFEYYETHVRLNLPRFSGAMVGWGNITDRGLLPQMYEWQRLEPGATICDVGGNNGHATLDLVKEYPMISVIVQDLESLRPRWSDLWARELPDAIQDGRTSFVPIDFFRDIPVRNCDVYYIRHILHDWPDASCVQILRNVKEAMQPSSRVLIHEYVLQQTTRDDVTVENDSAPEPLLPNYGNGRIRRYYQDITMLLGLNSKERTLQEFIDIGAQAGLKFVKLWDGGQTALVEFSC
S-adenosyl-L-methionine-dependent methyltransferase that preferentially catalyzes the methylation of 3-OH phenolic compounds like isovanillic acid and 3-OH-4-Met cinnamic acid. May play a role in promoting lignin degradation by methylating and inactivating free-hydroxyl phenolic compounds, products of lignin cleavage which are known inhibitors of lignin peroxidases.
P0CT90
B2A5V2
CH10_NATTJ
Chaperonin-10
Natranaerobius
MNLKPLGDRIVIKILEAEEKTESGIVLPEKAKEKPQEGEVVAVGSGKTLDDGSKVEPEVKAGDKVVYSKFAGNEVEVDGEEYLIMRQDDILAVIE
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.
B2A5V2
Q74IV0
ENO3_LACJO
2-phosphoglycerate dehydratase 3
Lactobacillus
MLKSVIENVHALEIFDSRGNPTVEVFVTLSNGVVGKAEVPSGASTGENEAVELRDGGSRLGGKGVMNAVNNVNTEINDALKGLDPHDQPNIDATMIALDGTPNKGRLGANAILGVSMATAAAAAKDNHQPLYRYLGGTDLEMPQTFHNVINGGEHADNGIDIQEFMITPVAKTSFRDGFEKIVNVYHTLKKVLEDMGYETGLGDEGGFAPNMKNSEEALKALHESIIKAGYKPGEDIAIACDCAASYFYNKEDGKYHLEGKVLTDEELADYYDKLLDEFPELISMEDPYDENDVEGMVKFTQSHKDRIQIVLDDFICTNPKLLNKAIHEGAGNASLIKLNQIGTVTETLETIRLSRKNGYNTMISHRSGETGDTFIADFAVAVNGGQLKTGAPARSERVEKYNRLLEIEEELGKGERLAFFPDNVDLD
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Q74IV0
Q3ZX56
COBD_DEHMC
Cobalamin biosynthesis protein CobD
Dehalococcoides
MEILLIFLLALVIDMVFGDPPNAFHPVAYMGKVISLFERAGFKGGKGYQFVYGIVMVIFTMALFFVPVYFLLDWLQGINSIVYIIVSAILFKMCFTVTGLRKAALLIKRLLEKDDIAQARFELRSLVSRDTSKLPQPKLVAAAVESVAESIGDGFVAPLFFFLIFGVPGVMAYRVVSTFDSMVGYRGKYEYLGKFAARFDDVLNFIPARLSALCILVASFFGRYSPAGAWRIMWRDHGKTQSPNAGWPMATAAGALEVCLEKVGHYSLGDDIRPLLPQTISCSLVLINNAGCIWVLISVGVIYFARIA
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Q3ZX56
O26949
THIN_METTH
Thiamine-phosphate pyrophosphorylase
Methanothermobacter
MMIMEIENVRRALEMISSAEDFGILIPEVRSNIVMARSNPCGPEDVVAVPGRITEFQGRAFACRDPEYGASSHMARFIIALNEHLPGRRSALNIKFDESIISICEDMGLVVSSYDRSREPDSVRDTEGGSIPWGVEEALRNSESPPDVIYHRGAWGKEPMIVLTGRDAVEVAELAIKILRKYKSLKGDTR
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
O26949
Q14AW5
NSUN7_MOUSE
NOL1/NOP2/Sun domain family member 7
Mus
MLDPTSERDLFDQENMEEISQLASLEMSGDVVANTNSTVVLEKPSYPDSVYVTAANIFQGIRIQRSPDKVIINYGSEPLQPSSSRSEDESFQRLSYELAFSTLKYQDILESILIDSYIFSSTTIASQLNSLIIVMLYDFQDRKFQPRILSENEETIPEVQEVENLLNGFKTKLAAALARCRIKHDALSIYHILPETVRKQEQRASTLPLYAWINTSKISLEEVYNNLRRKGYSKVKSITSVNEKVYAVDQHCFNVLIFPAHLKTDLLNIDLIKDYKLIFQDKSRSLAVHSVKALINIDDDVLMVNTGSWYTVAHMSILTSGHTSKIFVCGIQQEEKDFNARKLFTRMGCQNIEILHETFLSIESKDHRLQNVKVILLLPRCSSLGVSNPVEFILNEHEDKSLLQDLSQGGLPKDKLETLVQQQFEQLTHAMKFTKVQAIVYCTCSVSKEENEDVVEKALEYQSSGVKMQPYRLSPPVLPLCTLKEIELSMDRFFRLEPSDMNNGCFLSILTRERDPSETVSVKDVLARAAAKGLLEGVEVGKTLKRDKKRKKSKALPSRAPHHGDPLRDHLAVDGNDTSNVQMKISELLHRESKISTSTKMSAPAKTVSQAGTSSQVRKPSKPLSTPLVRNFSRPVERPTNFVRARPEGKVIPLKPIEIVLPPVIFPLSSQGPRVQMPATHFYYRFIGSKVGVPRYLTSSTSRRKEKVKESTTSSHVRHPRPWL
May have S-adenosyl-L-methionine-dependent methyl-transferase activity.
Q14AW5
B3QPW9
GRPE_CHLP8
HSP-70 cofactor
Chlorobaculum
MTKKHHKEQEEIQETIKTEAAEENVGDETVAIPAATESDIEAEIAARDAEIQKLRDEVMRRAAEFENFRKQKEREAAQSGKRMLENTVRDLLPLLDDLKRLMEHIPAELQEMAEAKPFVEGVELIRKNFKSLLESKGVKEIEALGKVLDVNFHEAITQIDVPDTEPDTIVQEYQTGYTLGDRVIRHAKVIVAK
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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.
B3QPW9
Q6G014
HFQ_BARQU
RNA-binding protein Hfq
Bartonella
MAERSQHLQDVFLNTVRKQKISLTIFLVNGVKLTGIVTSFDNFCVLLRRDGHAQLVYKHAISTIMPGQPVQMFEGESSE
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
Q6G014
Q9SRQ2
CHAT_ARATH
(Z)-3-hexen-1-ol acetyltransferase
Arabidopsis
MDHQVSLPQSTTTGLSFKVHRQQRELVTPAKPTPRELKPLSDIDDQQGLRFQIPVIFFYRPNLSSDLDPVQVIKKALADALVYYYPFAGRLRELSNRKLAVDCTGEGVLFIEAEADVALAELEEADALLPPFPFLEELLFDVEGSSDVLNTPLLLVQVTRLKCCGFIFALRFNHTMTDGAGLSLFLKSLCELACGLHAPSVPPVWNRHLLTVSASEARVTHTHREYDDQVGIDVVATGHPLVSRSFFFRAEEISAIRKLLPPDLHNTSFEALSSFLWRCRTIALNPDPNTEMRLTCIINSRSKLRNPPLEPGYYGNVFVIPAAIATARDLIEKPLEFALRLIQETKSSVTEDYVRSVTALMATRGRPMFVASGNYIISDLRHFDLGKIDFGPWGKPVYGGTAKAGIALFPGVSFYVPFKNKKGETGTVVAISLPVRAMETFVAELNGVLNVSKG
Acyltransferase involved in the production of green leaf volatiles (GLVs). Uses acetyl-CoA as substrate, but not malonyl-CoA or benzoyl-CoA. Prefers primary, medium-chain-length, aliphatic alcohols.
Q9SRQ2
P55026
TYRO_PELSI
Monophenol monooxygenase
Pelodiscus
MCLLALGFLLGILQPASGQFPRACASSESLLRKECCPLWAGDGSPCGELSGRGSCQEILLSRAPLGPQFPFTGVDDREDWPAVFYNRTCQCNSNFMGFNCGECRFGFSGPNCAERRMRMRRSIFQLSTREKNKFLAYLNLAKHTPSQDYVIATGTYAQMNNGLTPMFRNISVYDLFVWMHYYVSRDTLLGDASVWRDIDFAHEAPGFLPWHRLFLVLWEHEIQKITGDENFTIPYWDWRDAEGCDVCTDELMGDRHPTNPQLLSPASFFSSWQ
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.
P55026
B5FG09
RL3_ALIFM
50S ribosomal protein L3
Aliivibrio
MIGLVGRKVGMTRIFTEEGVSIPVTVVEVEANRVSQVKTVETDGYNAIQVTCGSKKANRVSKPEAGHFAKAGVEAGRGLWEFRLENGEEFAVGAELTVEVFNEIKKVDVTGTSKGKGFQGAVKRWNFRTQDMTHGNSLSHRAPGSIGQCQTPGRVFKGKKMAGHMGAERVTTQNLEIVRVDAERNLLLIKGAVPGSTGGNVIVKPAVKA
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
B5FG09
Q8Z3K5
TDCD_SALTI
Propionate kinase
Salmonella
MNEFPVVLVINCGSSSIKFSVLDVATCDVLMAGIADGMNTENAFLSINGDKPINLSHSNYEDALKAIAFELEKRDLTDSVALIGHRIAHDGELFTQSVIITDEIIDNIRRVSPLAPLHNYANLSGIDAARRLFPAVRQVAVFDTSFHQTLAPEAYLYGLPWEYFSSLGVRRYGFHGTSHRYVSRRAYELLDLDEKNSGLIVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMAWIAKETGQTLSDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERARLAIKTFVHRIARHIAGHAASLHRLDGIIFTGGIGENSVLIRQLVIEHLGVLGLTLDVEMNKQPNSHGERIISVNPSQVICAVIPTNEEKMIALDAIHLGNVKAPVEFA
Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP.
Q8Z3K5
Q1BRX9
ENGB_BURCA
Probable GTP-binding protein EngB
Burkholderia cepacia complex
MAFLLHQARFYTTVNHLRDLPPTVQPEIAFAGRSNAGKSTAINVLCNQKRLAFASKTPGRTQHINYFSVGPAAEPVANLVDLPGYGYAEVPGAAKAHWEMLLSSYLATRSQLCGLILMMDSRRPLTDLDRRMIEWFAPTGKPIHTLLTKCDKLTRQESINALRNTQKGLDAYRDQGVKGKLTVQLFSALKRTGLDEAHELIESWLRPSVADEKSEPVAQ
Necessary for normal cell division and for the maintenance of normal septation.
Q1BRX9
Q95150
NTF3_CEREL
Neurotrophin-3
Cervus
MSILFYVMFLAYLRGVQGNSMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEDSARESAKSEFQPVMVMGPELLWYQRRYNSSRFLLSDSIPLESPPLFLIEVHLANPMVNSRSPRRKRYAEHKSHRGEYSVCDSESLW
Seems to promote the survival of visceral and proprioceptive sensory neurons.
Q95150
B0KKB9
SELA_PSEPG
Selenocysteinyl-tRNA(Sec) synthase
Pseudomonas
MSSSLASDTPRLPSIDTLLRHQACLPLIDRHGREGVLATLRQLLDDLRNLVRNGELTPAELAPEILLGRTGERLAAQQRSQVRRVFNLTGTVLHTNLGRALLPEAAIEAMQTAARYPLNLEFDLATGKRGDRDDLIEGLIRELTGAEAVTVVNNNAAAVLLALNSLGARKEGIISRGELIEIGGAFRIPDIMARAGVKLHEIGTTNRTHARDYEAAIGPRTGLLMRVHCSNYSIQGFTTQVPTAELASIAHQRDLPLLEDLGSGSLLDLTRWGLPAEPTVRQALADGADIVTFSGDKLLGGPQAGIIVGRKDLIARIKKNPLKRALRVDKITLAALEAVLALYRNPDRLAERLPTLRLLTRSQAEIQAQAERLAPEVKAHLGEQWAVSVAPALGMIGSGSQPVARLPSAALCLRPQVSKKLRGRSLHVLERALRDLPVPVLGRLDDDALWLDLRQLDDEAQWLAQLPALQLGPVQ
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
B0KKB9
B9EA92
UPPP_MACCJ
Undecaprenyl pyrophosphate phosphatase
Macrococcus
MTFFELVKALILGIVEGLTEFAPVSSTGHQILVDDMWLQTKYVLNSQESANTFKIVIQLGSIFAAAWIFRHRFLEVLHIEKTKTEGPRLNLLHIFIGLIPAGIMGLLFDDFIDKHLFSVPTVLIGLALGALLMIAADLFNKKVTHTTTVDEMTYKQALIIGVAQCLALWPGFSRSGSTISAGVLLKMNHKAASDFTFIMAVPIMFAASAKSLASNIQYIHSDQILFYIVGFIAAFIFGVLSIRLFLSLINRVKLMPFAIYRLILVAVIAVLYFGFGIGKGI
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
B9EA92
A6TAH1
SELO_KLEP7
Protein adenylyltransferase SelO
Klebsiella
MTLSFTTHWRDELPDFYTSLSPTPLDNARLIWRNAPLAQQLGVPDALFAPESGAGVWGGEALLPGMSPLAQVYSGHQFGAWAGQLGDGRGILLGEQQLADGRRYDWHLKGAGLTPYSRMGDGRAVLRSTIRESLASEAMHALGIPTTRALAMVTSDTPVYRERVEPGAMLMRVAESHVRFGHFEHFYYRREPQKVQQLADYVIRHHWPQLQDEADKYLLWFRDIVMRTAQTIASWQTVGFAHGVMNTDNMSILGLTIDYGPYGFLDDFQPDFICNHSDYQGRYSFENQPAVGLWNLQRLAQSLSPFISAEALNAALDEYQHALLTAYGQRMRDKLGLFSQQKGDNDLLDGLFALMIREKSDYTRTFRLLSHSEQLSAASPLRDEFIDRAAFDSWFAGYRARLRDEQVDDAQRQQRMQGVNPALVLRNWLAQRAIEQAEAGDMGELERLHAALADPFTDREDDYVRRPPDWGKRLEVSCSS
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
A6TAH1
D8RLD3
MTS17_SELML
Microbial Terpene synthase-like protein 17
Selaginella
MAVSSIASIFAAEKSYSIPPVCQLLVSPVLNPLYDAKAESQIDAWCAEFLKLQPGSEKAVFVQESRLGLLAAYVYPTIPYEKIVPVGKFFASFFLADDILDSPEISSSDMRNVATAYKMVLKGRFDEATLPVKNPELLRQMKMLSEVLEELSLHVVDESGRFVDAMTRVLDMFEIESSWLRKQIIPNLDTYLWLREITSGVAPCFALIDGLLQLRLEERGVLDHPLIRKVEEIGTHHIALHNDLMSLRKEWATGNYLNAVPILASNRKCGLNEAIGKVASMLKDLEKDFARTKHEIISSGLAMKQGVMDYVNGIEVWMAGNVEWGWTSARYHGIGWIPPPEKSGTFQL
Sesquiterpene synthase converting farnesyl diphosphate to eight sesquiterpenes, with (+)-germacrene D and an unidentified oxygenated sesquiterpene as the major products. Has no diterpene synthase activity.
D8RLD3
C4JHR8
RTC5_UNCRE
Restriction of telomere capping protein 5
Uncinocarpus
MGAGQSTTTTEGRSSPEEMSHLLAQRFASKCFTPLELTHLEDNFNSQALDEHGLRYWNEEILSRFLGIPDGAGEKASPQTDATLDAGPVLFRMVSYLGAFPFHNTLAPSVLTYDAIVKVIVLLTERYGRVLKRGRKDRMKLLFGSLADVGRTQTEKQRETSQVDTKMSSDEAYSTDGASSNITGFSIDAPANDGEEEDDDDDLALAALESLDAIEVFKHDQRLDRSVYKARISVSTFRRLLALLLVIAPLHPMGRRQMIQTDAESIDAVQPSWIASCSLGDEANGDGHYLSDFSRVITTSLPFLFDPLTPLFEHFLFSKNLDLSKRKDSHQSHEESNSPSPPPSPHLECVFLPGHFETNILNSAILSHLSFFLSTSYPIPNLFRNQTRLHPVFSSDFHGESLTAFSHHVLTWHAPSLLLLKGVTGSSSSKQETVLAGAYLPEPWKRSTSPLSTPMSDFLDTSRFPCLFQLLPTHTVLQAAPAFKSLKSNMPVVSFSTNSGIAVGCMIPPSSRTSLNNELQPRPSGGGSLIIDPALENATFYVSDGLHGDGVFLPPGLSPSSSLSLSASATSSTMSISIHSIEVWGVVPTPAELDANLDPNSPKDAISMQKAMWDFEAREAERRKTIHLNVGGGDSEAQTGRALLEMAGIIGDSQYSPRRR
May be involved in a process influencing telomere capping.
C4JHR8
A1KAY2
DSBB_AZOSB
Disulfide oxidoreductase
Azoarcus
MIALPRNRRPLFLAVFAYCAALLAFGLYLQHYQGIEPCPMCIMQRYAFALVGVIALVAGLHGPRGAGVRVYGGLLLLTALAGGSVAARQTWMQLYPPEIPECGPGLEYMLESFPLTSALPMIFRGAGDCSAIDWTFLGLSLANWSLLNFGAAALLALWLLFGRRVR
Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
A1KAY2
P34475
TBG_CAEEL
Gamma-tubulin
Caenorhabditis
MSGTGALMTVHVGQCGNQLAQAFWKSMVDEHGINERGQTTHEDDMNDKKDLLFYQADDDHYVPRAVLVDLEPRVINGMMQSPNFSNLFNTDNIFMSDHGGGAGNNWASGYCQGQEVQEKIMDIIIREAENTNNLDGILFTHSVSGGTGSGTGSLLLERLREAFPKKVIQTYSVFANSDTSTDVVVHPYNWVLSMQRLIENPDHVVVLDNAALHRLAAGKFKTDTPTFDHINSLVARIMSTSTAPYRFNSAMCPSIRYLDLAPFPPMHFIQSAISPVVDPNENFTRKTSVADVTRFLLKPTSMMVSTASRVRPNDCMLSAYMFLQGQIEAHTIMTAEQNVDFAIRRPPFYMLKPLRMMHAPLSPYVRPQYKVSGLLLNNSTSVAPLFESLLSKYDKLRSKRAFIDKFEKIDNFSLDMMDDAMHIVQDLLDEYKAVVQKDYLTRGL
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
P34475
Q865S0
RCAS1_CANLF
Estrogen receptor-binding fragment-associated gene 9 protein
Canis
MAITQFRLFKVCTCLATVFSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGNGNVATQQNALEQLEPDYFKDMTPTIRKTQKIIIKKREPLNFGIPDGSTGFSSRLAATQDMPFIHQSPELGDLDTWQENTNAWEEEEDAAWQAEEVLRQQKIADREKRAAEQQRKRMEKEAQRLMRKEQNKIGVKLS
May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
Q865S0
Q4UN61
TSAD_RICFE
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
spotted fever group
MIKILGIESSCDDTAVSIITENREILSNIIISQNTEHAVFGGVVPEIAARSHLSNLDKALKNVLKESNTKLTEISAIAATSGPGLIGGVIVGSMFARSLSSAFKKPFIAINHLEGHALTARLTDNIPYPYLLLLASGGHCQFVAVLGLGKYKILGSTIDDAIGEAFDKVAKMLNLAFPGGPEIEKRAKLGDPHKYKFPKPIINSGNCNMSFSGLKTAVRTLIMSLKELNDAVINDIAASFQFTIGEILSSKVQDAIIAYERVVNDYYENIDYTTQLNLKSFRQDEFKEEPAEHTKVREHRLYPQNSLGSSFLNDAIVIAGGVAANKYLQEILSNCAKTYGYQLIYPPIRLCTDNAAMIAYAGLERYNNKLFTPLNFCPKARWSLEDISK
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Q4UN61
Q8Z316
MURB_SALTI
UDP-N-acetylmuramate dehydrogenase
Salmonella
MTHSLKPWNTFGIDHCAKHIVCAENEQQLLSAWQQATREGLPVMILGEGSNVLFLENYAGTVILNRLKGIEVNETADAWHLHVGAGENWHQLVRYALDNNMPGLENLALIPGCVGSSPIQNIGAYGVELHRVCDYVDCVELETGKRLRLSAAECRFGYRDSIFKNEYQDRVAIVAVGLRLSKQWQPVLTYGDLTRLDPKTVTAQQVFDAVCHMRTTKLPDPKVNGNAGSFFKNPVVAADIAMELLERFPNAPHYPQADGSVKLAAGWLIDQCQLKGVTIGGAAVHRQQALVLINANDATSKDVVALAHHVRQKVGEKFNVWLEPEVRFIGQFGEVNAVESIA
Cell wall formation.
Q8Z316
Q1H1P1
RS18_METFK
30S ribosomal protein S18
Methylobacillus
MARDMFKRRRYCRFSAEGIKQVDYKDVDLLKDFINENGKIIPARITGTKAKYQRQLTTAVKRARFLALLPYTDKH
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Q1H1P1
Q553P5
STX8A_DICDI
Syntaxin-8A
Dictyostelium
MNNNNNFNSNFNSNRISSTQPYLSDDARNALFEGKDRKWGNNNNNNYDTLSNQDVFEKQKRDMEEQDKMLDALSGSISRVKDTAITINKTAQEQTDMLDELDVHVDSTSARMRNTTKNLITLTQQSKTTGYCSAICFLLLVLLVIIILASVL
Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for fusion of late endosomes with lysosomes and homotypic lysosomal fusion.
Q553P5
Q21WM7
FETP_ALBFT
Probable Fe(2+)-trafficking protein
Rhodoferax
MARTVNCIKLGKEAEGLDFPPYPGELGKRIWESVSKQAWADWLKHQTMLVNENRLNLADARARQYLARQMENHFFGGGADAAQGYVPPSA
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.
Q21WM7
Q9VJ83
GRND_DROME
Protein grindelwald
Sophophora
MSVRKLSALSLSIGGVPLIPSVSLVAAANGESRDCHGTICHPVNEFCYVATERCHPCIEVCNNQTHNYDAFLCAKECSAYKTFEPLKAEMLDIQNTQQLILLLLTILLVLIALRCAFQFLRWLIGNRCFQKLMRRLQSKAYPHPATANGKDLNATTIQNLNAINHPGSDLERAQSQIYSVAGAAEGSVVTMTTPVSTRYPAENSTTPTTVMTEIGYGYDNQAMVVTPVSEKPSAATIPVAF
Acts as a receptor for egr. Plays a role in activation of JNK signaling and is required for egr-induced apoptosis. May also play an egr-independent role in cell proliferation.
Q9VJ83
Q108T9
CTTB2_LOXAF
Cortactin-binding protein 2
Loxodonta
MATDGASCEPDFSRASEDAAEATAEATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAREKEKKPVCTNPLSILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKHVVLMLVKECKQLSGKVIEEAQKVEEVMAQLEEEKKRTNELEEELSTEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMKKMIEQLKRGNDSKPSLSLPRKVKDRRLVSVSVGTEGPVTRSVACQTDLVVESTDHVKKLPLTVPVKPSAGSPLVSASAKGNVVRPSVDRQASHGDLILSSVPTVPPPSVNKTEENGPSTGSTPDLPSSTPPLPNNTAPPAVQPPSIASQNYSQASSLHSLHSPCANASLHPGVNPRIQAVRFRFQGNANDQDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTGPQVGASARPGAPTTGDISTHPPVGRTSLKTSGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIMDSSRASNAGAKVDKTVASPPTSLPQGNRVINEENLPKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWRAETPGLNQPACSDSSLVIPTTIAFCSSINPVSASSCRPGASDSLLVTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVNAADKNGFTPLCAAAAQGHDKCVELLIAYRANINHAADGGQTPLYLACKNGNKECIKLLLEAGTDRSVKTRDGWTPVHAAVDTGNVDSLKLLMYHRAPACGDRLNEEEPESDVFDLDGGGERPEGTVKPVVPADLINHADREGWTAAHIAASKGFKNCLEILCQHGGLEPERNDKCNRTVHDVATDDCKHLLENLNALKIPLRISMSETQRDSFGSDDFECENTIWALTIRRQTSWDDFSKGVIQALTNHFQAISSDGWWSLEDVTFNNTTESSIGLGASSVLSIMLGSVSWSPGQSFAQSPWDFLKKNKAEQVTVLLSGPQEGCLSSVTYASMIPLPMLQNYLRLVEQYHNVIFHGPEGSLQDYIAHQLALCMKHRQMAVGFSCEIVRAEVDAAFCKEQLVDLFIRNACLIPVKQSPGNKKVIVILENLEKSSLSELLGDFLAPLENRSTESPCTFQKGNGTSECYYFHENCFLMGTIAKACLQGSDLLVQQHFRWVQLRWDGEPMQGLLQRFLRRKAVNKFRGKLSSPRDPVCKTVDWALSVWRQLNSCLARLGTPEALLGPKYFLSCPVVPGHAQATVKWMSKLWNAVIAPRVQEAILSKASVKRQPGLGQTNAKKHPSQGQQAVVKAALSILLNKAVLHGCPLPRAELDQYIAEFKGGSFPLSIVSSYSSCGKKKGENGAWRKVSTSPRKKSGRFPSPTWSKPDLSDEGIKNKTVSQLNCNRNASLSRQKCLENDLSLTLNLDQRLSLGSDDEADLVKELQSMCSSKSESDISKIADSRDDLRRFDSSRNSPAFSATVNNPRMPVSQKEVSPLSSHQTTECSNSKLKTELGVSRVKSFLPVPRSKVAQCSQNTRRSSSSSNTRQIEINNNSKDEIWNLRKNEQVEKPNK
Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, thus controls dendritic spinogenesis and dendritic spine maintenance.
Q108T9
C1KWA4
RNC_LISMC
Ribonuclease III
Listeria
MNQWEELQESVGFDFKDVELLKQAFTHSSYVNEHRRENVKDNERLEFLGDAVLELTVSNYLFNKYPDMAEGHMTKMRAAIVCEPSLVEFAEAVHFSKYVRLGKGEEKAGGRTRPALLADVFESFIGALYLDNGIDKVVTFLERVIFPKIDAGAYLQTVDYKTQLQEIVQRDRDVLIEYDILGETGPAHNKAFDAQVIVNGQVLGKGSGRTKKQAEQSAAQFAINQLTHR
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
C1KWA4
Q6N2R1
GMHBB_RHOPA
D,D-heptose 1,7-bisphosphate phosphatase
Rhodopseudomonas
MTASAPRRPAAFLDRDGVINYNDHYVGTRERLRWMPGIAAAIRQLNAAGYYVFIITNQSGVARGMFSEDDVRALHRWMLDELNTQGARIDDVRFCPHHVEGTLDAYRVACEHRKPGPGMILDLAKTWPVDMTRSFVIGDSASDVEAAKAAGIPGFRFEGEDIDVFVKQVLIEMQRAAVSN
Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position. Also catalyzes the dephosphorylation of D-glycero-alpha-D-manno-heptose 1,7-bisphosphate in vitro.
Q6N2R1
C4L5J5
HPRK_EXISA
HPr(Ser) kinase/phosphorylase
unclassified Exiguobacterium
MQNIVRTAQVVERFKLQVIAGEEGLHRPVATPDLSRPGLVLAGYYTHYAKNRLQVLGKTELTFYASLSEEKRRERAKILCTEQTPGILITRGFDIPKEIEEEAEAANVPLMRTNAVTTSIESQITNFLEMELAPMTAMHGVLVDIYGVGVLIKGQSGVGKSETALELVKRGHRLVADDSVEIRQTGDQLLVGSAPKLIRHLLEIRGIGIIDVMTLFGAGAVRSHKKISLIVNLENWDAGKVYDRVGLDHNTMKIIDSEVPLLTIPVRPGRNLAVIIEVAAMNYRLQNMGINTAEEFAERLANAIQDTEGDL
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Therefore, by controlling the phosphorylation state of HPr, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
C4L5J5
Q1H0D2
SELO_METFK
Protein adenylyltransferase SelO
Methylobacillus
MLTFDNRFLRELPGDPETSNQLRQVYGACWSRVMPTSVSSPKLLAYSHEMLEALELSEEEIRSPAWVDALAGNGLMPGMEPYAACYGGHQFGHWAGQLGDGRAISLGEVVNRQGQRWELQLKGAGVTPYSRMADGRAVLRSSVREFLCSEAMHHLGIPTTRALSLVQTGDVVIRDMFYDGHPQAEKGAIVCRVSPSFIRFGNFEIFAMRDDKQTLQKLVDFTIDRDFPELRNYPEEERLAEWFAIICVRTARLIAQWMRVGFVHGVMNTDNMSILGLTIDYGPYGWVDNFDPGWTPNTTDAAGRRYCFGRQPDIARWNLERLAQALYTLKPEREIYDEGLMLYDQAYNNEWGAVLAAKFGFSAWRDEYEPLLNEVFGLMTQAEIDMTEFFRKLALVDAAQPDLGILQSAAYSPALWETFKPRFSDWLGQYAQATLADGRDPAERREAMNRVNPRYVLRNYLAQQAIDLADTGDTSMIEALMDVLRKPYDEQPGKERFAALRPDWARHKAGCSMLSCSS
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Q1H0D2
Q6BW46
MTC6_DEBHA
Maintenance of telomere capping protein 6
Debaryomyces
MISYTYITALSILVLNVLNVACTSVDDWPNLSPQIEIALRSQRDIGKYISIDQVTGMGVSLNTLVFDKDGYTLDALNDVSTLLDVGVQTLMINLYWNEFTQKWQLCPAPFPANISSDITTSKELYWDGRTYKCEASLTVDSLVRTINTYLAETNTNIKVNMVHLLFHLKSIRIDPPSGNVSSSEIKDYISTFQPTDSHFVALNNATLNDTVSSFGTSLFTPSDLSSYRKSNYRKGDKVGFYNETRKSFPNLNTFLLLDYKRVMTTVIANDLVKSQYTYNVTSSDKKSVFLEGSGVDTTVASLSDPDAVSQCNELIHYNQDNIEVFDNISLKEHFRIVVDDNGTSFTNVTFSDFVRCGFSPILNASYYNVYNDEEGVSEIDGSLSDIVDNFIPLSFWSWAENQLIEPNRGLNISDSTDTDNDEERDDNDNDDPLVRRDMDYKSSHTAFKCVVLDENGWKVSDCYSRQPIACQKSGSPNDWHIDVKTKREYFTAYKDDSCPDDYNFGIPSSSIEMLALMSYIERENISYPVWIDMNDITVPDCFVTGGPYATCPYQMTVTRLKLAGLIAPSFIVAVVILALILCEKIFRTNPIQSNRKRHWKKAINKYVEKYDYEGVPS
May be involved in telomere capping.
Q6BW46
Q8XU74
ATPA_RALSO
F-ATPase subunit alpha
Ralstonia
MQLNPSEISDLIKTRIEGLKAGADAKNTGTVISVTDGICRIHGLSGVMQGEMLEFPGNTFGLALNLERDSVGAVVLGDYEHISEGNEVKCTGRILEVPVGPELLGRVVNALGQPIDGKGPINAKKTDVIEKVAPGVIARQSVSQPVQTGLKSIDAMVPIGRGQRELIIGDRQTGKTAVAVDAIINQKGKGIFCVYVAIGQKASTIANVVRKLEEHGALEYTIVVAAAASDSAAMQYLSAYAGCTMGEYFRDRGEDALIVYDDLTKQAWAYRQVSLLLRRPPGREAYPGDVFYLHSRLLERAARVNAEHIEKITNGEVKGKTGSLTALPVIETQAGDVSAFVPTNVISITDGQIFLETDLFNAGIRPAINAGISVSRVGGAAQTKVVKKLSGGIRTDLAQYRELAAFAQFASDLDEATRKQLERGRRVTELLKQPQYQPLQVWQLAASLYAANNGFLDNVDVKDILAFEKGLHDQLKTKYADLINRIEDTKDLSKDDEAALRAAIEDFKKSAAF
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Q8XU74
Q35994
CYB_TADBR
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Tadarida
MTNIRKSHPLIKIINDAFIDLPAPSNISSWWNFGSLLGVCLAVQILTGLFLAMHYTSDTATAFNSVTHICRDVNYGWLLRYLHANGASMFFICLYLHVGRGLYYGSYTYTETWNVGIILLFAVMATAFMGYVLPWGQMSFWGATVITNLLFAIPYIGTDLVEWIWGGFSVDKATLT
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.
Q35994
B0KLJ7
SOTB_PSEPG
Probable sugar efflux transporter
Pseudomonas
MNGPTPTHISPATGSGSWLSVIALALAAFIFNTTEFVPVALLSDIGRSFDMSTAQVGLMLTIYAWVVALASLPMMLLTRNIERRRLLLFVFLVFIVSHLLSWLSQSFAMLLVSRIGIALAHAVFWAITASLAVRVAPPGQQAKALGLLATGTTLAMVLGIPLGRVVGEALGWRITFLSIAGVALATMLCLMKSLPLLPSQNSGSLRSLPILFKRPALVITYLLVTLVITAQFTAYSYIEPFALHVAQIGGERTTLVLLLFGGAGVFGSLLFSRYSDRFPHGFLVGSIGLLAACLLLLLPLSGNFYAFAALSMFWGVAILSFSLSLQSKTLKLASDATDVAMALFSGIYNIGIGGGALLGSIVSSQMDVANIGLVGGSVAVVGLVLAVASTRRFREALTR
Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites.
B0KLJ7
Q0S219
IF2_RHOJR
Translation initiation factor IF-2
Rhodococcus
MAGKARVHELAKELGVTSKELLATLKEQGEFVKSASSTVEAPVARRLRESFPSAKSADSAARPAAKPGAPAPSTPATAAKPGGPRPGPKPAAPAPAPVAPAAAAPAATPEAQAPAPAAPAARAVTPAAPATNAPKPGRPTPAAPAPAAPAPAAPAAPAAPAASAPAAPSTGAKPGGPRPGPKPPRVGNNPYSSAPAERPAPRPAPGAPRPGAPRPAPGQGGPRPAPGQGGPRPAPGQGGPRPAPGQGGPRPAPGQGGPRPSPGSMPPRPNPGAMPARSARPAPGGRPGRPGGAPGGRPGGGGGGYRGGGAPGAGAGAPGGGAPAGGFRGRPGGGGRPGQRGAAAGAFGRPGGAPRRGRKSKRQKRQEYDSMQAPAVGGVRLPRGNGETIRLARGASLSDFAEKIDANPAALVQALFNLGEMVTATQSVNDETLELLGGEMNYVVQVVSPEDEDRELLDSFDLTYGEDEGGEEDLESRPPVVTVMGHVDHGKTRLLDTIRKANVREGEAGGITQHIGAYQVLTELDGNERLVTFIDTPGHEAFTAMRARGAKATDLAILVVAADDGVMPQTVEAINHAQAADVPIVVAVNKIDKEGANPDKIRQQLTEYGLVAEEYGGDTMFVDISAKLGTNIDALLEAVLLTADAALDLRANPDMDAQGVAIEAHLDRGRGPVATVLIQRGTLRVGDSIVAGDAYGRVRRMVDEHGDDVLEALPSRPVQVVGFTSVPGAGDNLLVVDEDRIARQIADRRNARKRNALAAKSRKRISLEDLDSALKETSQLNLILKGDNSGTVEALEEALHGIEIDDEVQLRVIDRGVGGVTETNVNLAAASNAIIIGFNVRAEGKATELANREGVDIRYYSVIYQAIDEVEKALKGMLKPIYEEVELGKAEIRAMFRSSKVGNIAGCLVTSGTIRRNAKARLLRDNTVVAETVTISSLKREKEDVVEVREGYECGLTVTYSDIKVGDVIEAYELREKPRD
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Q0S219
Q6D842
EX7S_PECAS
Exodeoxyribonuclease VII small subunit
Pectobacterium
MPKKTEQPVSFESSLNELEKIVTRLESGELPLDDALNEFEHGIQLARQGQQKLQQAEQRVQILLSDDPDAPLSPFTPDNDTL
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q6D842
C6DHM7
HSLV_PECCP
ATP-dependent protease subunit HslV
Pectobacterium
MTTIVSVRRNGQVVIGGDGQATLGNTVMKGNVRKVRRLYHDRVIAGFAGGTADAFTLFELFERKLELHQGHLVKAAVELAKDWRTDRMLRKLEALLAVADENASLIITGNGDVVQPENDLIAIGSGGPYAQAAARALLENTELGARDIVEKSLGIAGDICIYTNQFHTIEELASKA
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
C6DHM7
Q9UVG6
VPS15_PICPA
Vacuolar protein sorting-associated protein 15
Komagataella
MGAELSLLAPTAQPIALSVYVDFLSNIQYNKPLGTSRFLKTVKGLNDQGSIVVKVLVKPNSGLDLSEWVEKLEFLRLKLLDVPNVIPYNLVIDSVRAGYLIRPFQQRTLYERVSIQPYLEPIEKKWIAFQLIHAVMECHERGQYHGDIKSENVLLTSWDMVFLTDFAPFKPIYLPGNNPSQFSFYFDTSRRNVCYVAPERFLGEGTPTQYQEVDKLTSSMDIFSLGCTVAELFLEGSVLFTLPQLFKYKKGEYTPSLSGIVDNDLRNMIQEMIDLDPRKRISAHDCLRKHRGKVFPEYFYSFLYDYMLELSTPSDHSVGNWRFDECDRRIERIYNDMGMICDKLDVNLDLNIVHSFTEEPSQNVIPMTLRLPGVEPHIPQSSKTPYDSALIILNILLHSMRNTTHSSYRIKSCDLILMISEMLSDEQKLDRCLPYLVHLLNDPSIDVQAAALKYMTQLLLLVDYLTPVNVLIFPEYILPKLASFLSTTKGSYMRMIFATILPHLAKTALKFYEMAILLGSHVEKFELLKNFENLTIQLLIDPDSSAKISLLKNILPLASVFGKDKTNDIILSHMITYLNDPDENLRVAFIESILGLSIFVGITSLENYILPLLVQTLTDNSEIVVVNVLRSFAELNNLGLIKKRYKFDLIKVSSKLLLHPNSWIRLGTLRLLISVVKDLSLTDFYCLLYPLVRPFFEYEVTNFDWATLYPCIIKPIPRSIYTLSITWALKAEKTLFWQQVKLAKPDPFGSRNSTFLLNRNSKIGESGVVSNNQIPTSPEDIGWLGKLKASGFDEKDLWKIATLRDYIFRVARSRSNIPTQENNEVTMQQMGIYPRIVFFEKGSMYETEGFVTGSSMMANYRILVNSEYSPESLTKRKTVGGVNTNHTYSGANPYILKFLECIKFRHVLDDSEEFGPSIPSATVEEGHWKFEGVLVSHLTEHTGSITSLALSPDQQYFLTGDSKGIIRLWDVLQLERNGYATSHVTVSMSSSVKDIKFIENRNSFCAVTADGEIKIFRVEINSTSSSVRSNGSPHRHESISLLREHSLEGEHISDMKFIGPNLAVTTLSCKLILFDLRDMQIAEEIQNPVSHGFITSFDLDSSQSWLLIGTSKGILDFYDLRFELLVKSWKLKSTSYPIKHITVPPAGFTCNRKSERFALINGGTNDSVTIVFDVSKGQCSELYFTETVNLNTAIDNYEVLEVDNGEERTRTSVLATEVEDRSITSLTMLGSNQFLTATFDKRVILWDTGNKANSSALISKLDDFTSSFSSVQVRPHLMAINEKIVEKDPQDIGGPKRNMASANSSTFDLHSDIITGIAVIQKPLKMLILVDRAGVINIYK
Involved in glucose-induced micropexophagy and ethanol-induced macropexophagy. Required for ATG2 recruitment to a perivacuolar compartment.
Q9UVG6
B5Y0W8
THII_KLEP3
tRNA 4-thiouridine synthase
Klebsiella
MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKNYDETLAVVRHWDHIEVRAKDENQRPAIRDALTRIPGIHHILEVEDVPFTSLHDIFEKTLPLWREALEGKTFCVRVKRRGKHEFTSIEVERYVGGGLNQHIETARVKLTDPDVTVNLEIENDRLLLVKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEILEKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHDKEHIIDLAREIGTEDFARTMPEYCGVISKSPTVKAVKAKIEAEEEHFDFSILDKVVEEASNIDIRDIAQQTEAAVVEVETVTGFGANDAILDIRSIDEQEDKPLKVEGVEVVSLPFYKLSTKFGDLDQSKTWLLWCERGVMSRLQALYLREQGFSNVKVYRP
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
B5Y0W8
Q9QXD8
LIMD1_MOUSE
LIM domain-containing protein 1
Mus
MDKYDDLGLEASKFIEDLNMYEASKDGLFRVDKGAGNNPEFEETRRVFATKMAKIHLQQQQQQQLLQEEALPRAGRSPVNGGNRQGASGKLAADGAAKPPLAVPTVAPGLATTTAAAQPSYPSQEQRIRPSAHGARPGSQNCGSREGPVSSQRPALHGLSPSCEDPSCLTHGDYYDNFSLASPQWGDKPEGCPSVSLGVGSGWPGCPGNDSTLPKSCGDHHPYQPQLSTVCSGRSFESGISGQDGGIGGHSSEKPTGLWSTASSQRVNLGFSSMGLENGTSAQPKGTTVSAPMVPSSASQGACPKRDSGLGYEASGRVFKPLVDTQPWLQDGPKSYLSVSAPLSSTAGKDSTQPGMTTGLDPKFGCVESGTSPKPSPTSNVHPVMSTPSELSCKESSPSWSTDSSLEPVLPGSPTPSRVRLPCQTLAPGPELGPSTAELKLEALTQRLEREMDAHPKADYFGSCVKCSKGVFGAGQACQAMGDLYHDACFTCAACSRKLRGKAFYFVNGKVFCEEDFLYSGFQQSADRCFLCGHLIMDMILQALGKSYHPGCFRCVICNECLDGVPFTVDSENKIYCVRDYHKVLAPKCAACGLPILPPEGSDETIRVVSMDRDYHVECYHCEDCGLELNDEDGHRCYPLEDHLFCHSCHVKRLEKGPSPAPLHQHHF
Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation.
Q9QXD8
Q58337
GCH1L_METJA
GTP cyclohydrolase 1 type 2 homolog
Methanocaldococcus
MKAKEIIEFIETFAPKDLAIEGDNIGLQVGDNLDKEIKKLGIALDPSLSVIKKAEKEGVDFLFTHHPLLKDPIRNFTGVIYKKLKILMENDIILYSAHTNLDICKNGLNDALAELYNLENPKPLYDNGLGRVGIFKGSFEEFLEITKKYIHKNPIVVKSKEVDDNFKLAVLSGYGLSQSSIKYVAEKADVYLSGDLTHHSKILAEELGLVVVDATHYSTEVFGLKKFKEFLSSNLDLEIISLDF
DNA-binding protein exhibiting the ability to bind to both single-stranded and double-stranded DNA.
Q58337
Q32JU2
GLND_SHIDS
[Protein-PII]-UMP uridylyl-removing enzyme
Shigella
MNTLPEQYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVDVWPRLPSPELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLDLIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPNDKG
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Q32JU2
Q3ZWX7
RECO_DEHMC
Recombination protein O
Dehalococcoides
MTKPHDFKTKAIIVRKTKCGEADRILSLLTPDLGLIQGFAKSVRKTKSKLSGHLELLCYSEVSLARGKAIDTITGSQTIQSFLNIRNSLQLSAMAFYACELAYHFSPEEAANPAMFQLLLSTLEELDNGSQPELCLKYFEINLLASSGYKPELRECANCHKKLQATINYYSPESGGVICPNCRNTQIGMPVSVNTVKVLRYIQENSFSSICRLKINREILSELELAIRANIRFVLEKEPKALLWLDSLRLADL
Involved in DNA repair and RecF pathway recombination.
Q3ZWX7
Q9BAB9
RRP3_EUGVI
Probable 30S ribosomal protein 3, chloroplastic
Euglena
MQKFVLKFLWLQRSVAVSLDQKIGDNVSPLTEFYFWPQCDAWEEMRNFLESKSWINSSESILLLNQVTEIINDWQEKDDSQRKDIFDLKEKFPFVDFIGFD
Probably a ribosomal protein or a ribosome-associated protein.
Q9BAB9
Q2Y7P0
SYM_NITMU
Methionyl-tRNA synthetase
Nitrosospira
MNKRKILVTSALPYANGSIHLGHLVEYIQTDIWVRFQKMQEHEVHYVCADDAHGTPIMLRAEQEGITPRQLIDRVWHEHKTDFDGFHIGFDHYYTTDSPENQAFCEDIYRQLRAGELIAKRSVEQFYDPVKQMFLPDRYIKGECPRCHAGDQYGDSCEACGATYLPTDLISPYSAVSGARPERRTSNHYFFKLSDVRCEAFLKNWIFESIPAQPGVALETRPRLQPEAANKMNEWLSAGLVDWDISRDAPYFGFPIPRTGGKKFFYVWLDAPVGYFGSFKNYFKQNQRTQAEIDEFLRPGGNTEMVHFIGKDILYFHALFWPAMLEFSGYRTPTQIYAHGFLTVNGQKMSKSRGTFITAESYLKQGLNPEWLRYYYAAKLNDSMEDIDLSFEDFVARVNSDLVGKYVNIASRCAGFITKKFGGELTHNVSEASRKWFNQFLFCELGEGDTFLGRHMSIANFYERREYSKAIKEIMSAADVANQYVDRMKPWVLAKDSRNDRELHEVCSVALNMFRMLTVYLKPVLPKLAMEAEQFLGLDPLTWKDANSQHRLLPDGHRINDYQHLMTRIDPKQIEMLTHANKESLAPAKSQQVAQAVETMEKNSSTTPAPAKEGEAGQASASTISIEDFGKIDLRVAKILDAEHVPGADKLLKLTLDVASEQRTVFAGIKSAYDPGQLKGRLTVMVANLAPRKMKFGISEGMVLAAGDGEGPYLLSPDEGARPGMKVK
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Q2Y7P0
Q3AC78
NUOB_CARHZ
NDH-1 subunit B
Carboxydothermus
MEIKTIQSEEEKLIGKNVFLTTLDAVFNWARGNSLWPLTFGLACCAIEVMAAGGPKYDFSRFGYEVWRPSPRHADLMIVAGTITKKMQPLVLRLYEQMAEPKYVIAMGSCAISGGPFVDSYHVVPGANTFLPVDVYIPGCPPRPEALLYGWLELKRKIQNPRVVKR
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 a menaquinone. 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.
Q3AC78
Q21H90
PSD_SACD2
Phosphatidylserine decarboxylase beta chain
Saccharophagus
MKDDLFIALQRIIPHHAFSRLVGWFAATKIRWIKHLFITKFINAYNVNMAEALEPNPENYANFNDFFVRALKPDARPIASEANAIVSPADGAVSQLGEISGDKIFQAKNHWFSIKELLACDDELAEQFMGGSFATIYLSPSDYHRVHMPAAGLLTQMNYIPGDLFSVNPVTTENVAGLFARNERIAAIFDTEFGPMAVVMVGAMIVASIETVWDGQITPASREVKRNVYSKPREIKLGKGDEMGRFKLGSTAVLLFPKGAIKWKEDIKAETTLRMGEMIAELQTQA
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Q21H90
A6VCY0
OADC_PSEA7
Oxaloacetate decarboxylase
Pseudomonas
MHRASHHELRAMFRALLDSSRCYHTASVFDPMSARIAADLGFECGILGGSVASLQVLAAPDFALITLSEFVEQATRIGRVARLPVIADADHGYGNALNVMRTVVELERAGIAALTIEDTLLPAQFGRKSTDLICVEEGVGKIRAALEARVDPALTIIARTNAELIDVDAVIQRTLAYQEAGADGICLVGVRDFAHLEAIAEHLHIPLMLVTYGNPQLRDDARLARLGVRIVVNGHAAYFAAIKATYDCLREERGAVASDLTASELSKKYTFPEEYQAWARDYMEVKE
Catalyzes the decarboxylation of oxaloacetate into pyruvate. Seems to play a role in maintaining cellular concentrations of bicarbonate and pyruvate.
A6VCY0
Q8FZV1
CRCB1_BRUSU
Putative fluoride ion transporter CrcB 1
Brucella
MTREFIMLMMPPLTDGFPLDILVANVVACFLLGTVTALYARKIHSRDVHTIIGMGMMGGVSTFSSFAYGSVVLASASMSAFLIAAAYVTVSVVAGYVAVLAGMKFGEKSADILHRYPPMASIIDSGLVTVESRHSVAETIERVAAKAKSMGMNVFTRVDHGAGAKEAGLGLPPTELIIFGNPQNGTVLMQDKRTIGLDLPIRALAWEDGSGKVWLTVNDPAWLAQRHSLGLSSDVAIKAMVTGTGTVTKYAAGD
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q8FZV1
Q7ZT99
CRVP_CROAT
Catrin-2
Crotalus
MIAFIVLPILAAVLQQSSGSVDFDSESPRKPEIQNKIVDLHNFLRRSVNPTASNMLKMEWYPEAAANAERWAYRCIESHSPRDSRVLGGIKCGENIYMSPVPIKWTEIIHAWHGENKNFKYGIGAVPPNAVTGHFSQVVWYKSYRIGCAAAYCPSSKYSYFYVCQYCPAGNIIGKTATPYKSGPPCGDCPSACDNGLCTNPCTKEDKYTNCKSLVQQAGCQDKQMQSDCPAICFCQNKII
Catrin-2 weakly blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffeine-stimulated contraction. Catrin-1 has no significant effect. May target voltage-gated calcium channels on smooth muscle.
Q7ZT99
P25972
PYRE_BACSU
Orotate phosphoribosyltransferase
Bacillus
MGGNQILKQIIAKHLLDIQAVFLRPNEPFTWASGILSPIYCDNRLTLSFPEVRNDVASGISKLVKEHFPEAEMIAGTATAGIPHAALAADHLNLPMCYVRSKPKAHGKGNQIEGAVQEGQKTVVIEDLISTGGSVLEACAALQAAGCEVLGVVSIFTYGLPKAEEAFAKAELPYYSLTDYDTLTEVALENGNIHSDDLKKLQTWKRNPESKDWFKK
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
P25972
Q9K706
GNGF_HALH5
Gluconeogenesis factor
Halalkalibacterium (ex Joshi et al. 2022)
MKKKNVVVFGGGTGLSVLLRGLKTFPVSITAIVTVADDGGSSGRLRKELDIPPPGDVRNVLVALSEVEPLLEQLFQHRFENGNGLSGHSLGNLLLAGMTSITGDFARGISEMSKVLNVRGKVLPASNRSIILHGEMEDGTIVTGESSIPKAGKKIKRVFLTPKDTKPLREGLEAIRKADVIVIGPGSLYTSVLPNLLVPGICEAIKQSTARKVYICNVMTQNGETDGYTASDHLQAIMDHCGVGIVDDILVHGEPISDTVKAKYAKEKAEPVIVDEHKLKALGVGTISDYFVLEQDDVLRHNASKVSEAILEGKPRTSSSIQ
Required for morphogenesis under gluconeogenic growth conditions.
Q9K706
Q04TV4
DER_LEPBJ
GTP-binding protein EngA
Leptospira
MAKAVRKSNSEETVPIKAPRKAPGEKIPVVSIVGRQNVGKSTLFNSLLKKKLAITEDYPGVTRDVLSARVYQEEKDLDFYLCDTPGLDIENPDSLSQSILEAAYRQLNESDVIIFLLDKNLVTVADHTLLDYLRKKYGPVDKPIIYCVNKADKELDEFDLEEFYRMGLPEVLPISATGRKNLGLLLEKIKFFLSSKPGKVWIEKISASKKKDAQPLPLAEEDYEFRLAIVGKPNSGKSSLLNAVCGYERAVVSDVAGTTRDSVDTLLEFGNRKLLLTDTAGIRKHSKTAEALEYYSYQRTLKAIESSDLVIHLLDAKKGFGDFDKKITSLLQEKGKPFLIAVNKWDSIEDKTDKTFREYKEKLYSRFPLLNEVPIVTISATERLRVQKLIDLSFDLASRSRRKVSTSELNKNLKNWMSQAGRSFSAHQPPKMLYCTQVSTSPFHLILFVNHVEYFKSNLISFLKKKLTEAYDLQGIPVRLEFRSDRK
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Q04TV4
O95780
ZN682_HUMAN
Zinc finger protein 682
Homo
MELLTFRDVTIEFSLEEWEFLNPAQQSLYRKVMLENYRNLVSLGLTVSKPELISRLEQRQEPWNVKRHETIAKPPAMSSHYTEDLLPEQCMQDSFQKVILRRYGSCGLEDLHLRKDGENVGECKDQKEIYNGLNQCLSTLPSKIFPYNKCVKVFSKSSNLNRENIRHTTEKLFKCMQCGKVFKSHSGLSYHKIIHTEEKLCICEECGKTFKWFSYLTKHKRIHTGEKPYKCEECGKAFNWCSSLTKHKRIHTGEKPYKCEECGKAFHWCSPFVRHKKIHTGEKPYTCEDCGRAFNRHSHLTKHKTIHTGKKPYKCKECGKAFNHCSLLTIHERTHTGEKPYKCEECGKAFNSSSILTEHKVIHSGEKPYKCEKCDKVFKRFSYLTKHKRIHTGEKPYKCEECGKAFNWSSILTEHKRIHTGEKPYNCEECGKAFNRCSHLTRHKKIHTAVKRYKCEECGKAFKRCSHLNEHKRVQRGEKSCKYKKCGEAFNHCSNLTT
May be involved in transcriptional regulation.
O95780
B0BBR1
NQRD_CHLTB
NQR-1 subunit D
Chlamydia
MTTNKSYLTYFTDALWINNQPLIAILGICSALAVTTTVTTALTMGFAVSFVTGCSSFVVSLLRKITPESVRMIAQLIIISLFVILIDQFLKAFFFTISKTLSVFVGLIITNCIVMGRAESMARHVSPIPAFLDGLGSGLGYGWVLVCISIIRELFGFGTILGFRVIPEILYASAAHPDGYENLGLMVLAPSAFFLLGIMIWIVNIIRAPKTKR
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
B0BBR1