wanglab/gogpt-training-data huggingface dataset:
Protein: Ribosome-associated molecular chaperone SSB (EC 3.6.4.10) (Heat shock protein SSB) (Hsp70 chaperone Ssb) (Q876N3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11484}. Note=Associated with translating ribosomes. {ECO:0000250|UniProtKB:P11484}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- L33
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
- Large ribosomal subunit protein uL3
- Candida glabrata strain CBS138 chromosome H complete sequence
Sequence:
MADGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPKNTVFDAKRLIGRRFDEESVQNDMKTWPFKVVDVDGAPVIEVEYLGENKQFSPQEISSMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSDKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKGEFKKKTGLDISNDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFEGEDFEASLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDYFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDIFGVVVPRNTTVPTIKRRTFTTVGDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPPMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSANITISNAVGRLSSEDIEKMVNQAEEFKAADEAFAKRHEAKQRLESYVASIEQTVTDPVLSSKLKRGSKTKIEAALADALSALQIEDGSAEEYRKAEVGLKRVVTKAMSSR
Protein: AMP deaminase 3 (EC 3.5.4.6) (AMP deaminase H-type) (AMP deaminase isoform E) (Heart-type AMPD) (O08739)
Organism: Mus musculus (Mouse)
Function: AMP deaminase plays a critical role in energy metabolism.
Interaction partners:
- Adenine phosphoribosyltransferase
- Adenylosuccinate lyase
- Adenylosuccinate synthetase isozyme 2
- Adenosine kinase
- Adenylosuccinate synthetase isozyme 1
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine-5'-monophosphate dehydrogenase 1
- Bifunctional purine biosynthesis protein ATIC
- GMP reductase 1
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MPRQFPKLNMSDLDEHVRLLAEKVFAKVLREEDSKDVMSLFTVPEDCPIGQKEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPTQQDWKGPPTASPAMSPATPLVPGATSKPGPAPYAMPEYQRVTISGDYCAGITVEDYEQAAKSLAKALMIREKYARLAYHRFPRTTAQYLAHQGESVPLEEGLPDFHPPPLPQEDPYCLDDAPPNLGYLVRMHGGVLFVYDNQTMLERQEPHSLPYPDLETYIVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKELKSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKLGRKITLRQVFDSLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENYLGGEYFARMVKEVARELEDSKYQYSEPRLSIYGRSPKEWSSLARWFIQHKVYSPNMRWIIQVPRIYDIFRSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESKHSDHMFSDKSPSPDLWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAGSITHLVSAFLTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREFLHKGLHVSLSTDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEKQKFLGQNYYKEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTK
Protein: TBC1 domain family member 19 (Q8N5T2)
Organism: Homo sapiens (Human)
Function: May act as a GTPase-activating protein for Rab family protein(s).
Interaction partners:
- Polyglutamylase complex subunit TTLL1
- Nicolin-1
- Leucine-rich repeat-containing protein 49
Sequence:
MLQEESDLSLIIAQIVQKLKGSNLYSQLERQAWASLQRPEIKLESLKEDIKEFFKISGWEKKLQNAVYSELSVFPLPSHPAAPPEHLKEPLVYMRKAQGSWEKRILKSLNSMCTELSIPLARKRPVGEQKELLNKWNEMGTDEPDLSLFRPVYAPKDFLEVLINLRNPNYENGDSLSFRTHLGLIQVPLKVKDIPELKECFVELGLNIGQLGIDDSTQVPPELFENEHVRIGQKVLAEQDSAAAQQYIRQGSPTALRAELWALILNISSQPEDVLYYEQLKTNVIQHDLLVDSLIYKDVKLTASNDDYYFVFEDYLYQVLLCFSRDTSVLSHFAFNSASPPKSYIRGKLGLEEYAVFYPPNGVIPFHGFSMYVAPLCFLYHEPSKLYQIFREMYVRFFFRLHSISSHPSGIVSLCLLFETLLQTYLPQLFYHLREIGAQPLRISFKWMVRAFSGYLATDQLLLLWDRILGYNSLEILAVLAAAVFAFRAVNLMEVTSLAAAEAVLADLSTLKVMPLLQIFLFATVT
Protein: Spliceosome RNA helicase Ddx39b (EC 3.6.4.13) (56 kDa U2AF65-associated protein) (DEAD box protein UAP56) (HLA-B-associated transcript 1 protein) (Q9Z1N5)
Organism: Mus musculus (Mouse)
Function: Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4 and the THO complex. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability.
Subcellular location: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Can translocate to the cytoplasm in the presence of MX1. {ECO:0000250}.
Interaction partners:
- THO complex subunit 4
- Aly/REF export factor 2
- SAP domain-containing ribonucleoprotein
- THO complex subunit 1
- THO complex subunit 3
- Chromatin target of PRMT1 protein
- THO complex subunit 2
- THO complex subunit 5 homolog
- THO complex subunit 6 homolog
- THO complex subunit 7 homolog
Sequence:
MAENDVDNELLDYEDDEVETAAGADGTEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRCIALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIAFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELPDEIDISSYIEQTR
Protein: ADP-ribosylation factor-like protein 16 (Q0P5N6)
Organism: Homo sapiens (Human)
Function: May suppress the RNA sensing activity of RIGI in a GTP-dependent.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21233210}.
Interaction partners:
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- ADP-ribosylation factor-like protein 9
Sequence:
MRVAGGRALSRGAELRVPGGAKHGMCLLLGATGVGKTLLVKRLQEVSSRDGKGDLGEPPPTRPTVGTNLTDIVAQRKITIRELGGCMGPIWSSYYGNCRSLLFVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIIACAKQNITTAEISAREGTGLAGVLAWLQATHRAND
Protein: Esterase CG5412 (EC 3.1.2.-) (Q9VDL1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform C
- 2-
Sequence:
MTNNDAAVEAAGSSRASSSKQQLKLEITEKVRVLCLHGYRQNGEAFKNKLGSFRKFANKYAEFVFITAPHVAKALESAAEPVPEQRSWWANKDDGSFKGTNKGGPAFGFQESLRCVEEAWRTQGPFQGLLGFSQGACFVGLICGLAKKKLTSIRPEFAVLASGFLSGSLVHMSAYEEAISIPTLHIYGQTDEIIPKEMSESLAARFKNAEVLEHSGGHYFPATAQQKQTFINFFQDRLQEYLEHEELQQSGNASFVDSGAEDDNDAEVAAMTAELDESD
Protein: 2-phosphoxylose phosphatase 1 (EC 3.1.3.-) (Acid phosphatase-like protein 2) (Xylosyl phosphatase) (epididymis luminal protein 124) (Q8TE99)
Organism: Homo sapiens (Human)
Function: Responsible for the 2-O-dephosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature glycosaminoglycan (GAG) chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-dephosphorylation during completion of linkage region formation is a prerequisite for the initiation and efficient elongation of the repeating disaccharide region of GAG chains.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:24425863}; Single-pass type II membrane protein {ECO:0000255}. Note=Colocalizes to Golgi apparatus in a B3GAT3-dependent manner. {ECO:0000269|PubMed:24425863}.
Interaction partners:
- Galanin-like peptide
- Serine/threonine-protein kinase A-Raf
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
Sequence:
MLFRNRFLLLLALAALLAFVSLSLQFFHLIPVSTPKNGMSSKSRKRIMPDPVTEPPVTDPVYEALLYCNIPSVAERSMEGHAPHHFKLVSVHVFIRHGDRYPLYVIPKTKRPEIDCTLVANRKPYHPKLEAFISHMSKGSGASFESPLNSLPLYPNHPLCEMGELTQTGVVQHLQNGQLLRDIYLKKHKLLPNDWSADQLYLETTGKSRTLQSGLALLYGFLPDFDWKKIYFRHQPSALFCSGSCYCPVRNQYLEKEQRRQYLLRLKNSQLEKTYGEMAKIVDVPTKQLRAANPIDSMLCHFCHNVSFPCTRNGCVDMEHFKVIKTHQIEDERERREKKLYFGYSLLGAHPILNQTIGRMQRATEGRKEELFALYSAHDVTLSPVLSALGLSEARFPRFAARLIFELWQDREKPSEHSVRILYNGVDVTFHTSFCQDHHKRSPKPMCPLENLVRFVKRDMFVALGGSGTNYYDACHREGF
Protein: UDP-D-apiose/UDP-D-xylose synthase 2 (EC 4.1.1.35) (Q9SGE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of UDP-D-glucuronate to a mixture of UDP-D-apiose and UDP-D-xylose. D-Apiose (3-C-hydroxymethyl-d-erythrose) is the only plant cell wall monosaccharide with a branched carbon skeleton and is found in rhamnogalacturonan II (RG-II), apiogalacturonan, and several apioglycosides (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32662159}.
Interaction partners:
- UDP-glucose 6-dehydrogenase 4
- UDP-glucose 6-dehydrogenase 3
- UDP-glucose 6-dehydrogenase 2
- UDP-glucose 6-dehydrogenase 1
- Probable UDP-arabinose 4-epimerase 3
- Putative UDP-glucose 6-dehydrogenase
- Putative UDP-arabinose 4-epimerase 4
- Putative UDP-arabinose 4-epimerase 2
- UDP-glucuronate 4-epimerase 4
- UDP-glucuronate 4-epimerase 2
Sequence:
MANGADRLDLDGKPIKPMTICMIGAGGFIGSHLCEKLMTETPHKVLALDVYNDKIKHLLEPDTVQWAGRIQFHRINIKHDSRLEGLIKMADLTINLAAICTPADYNTRPLDTIYSNFIDALPVVKYCSENNKRLIHFSTCEVYGKTIGSFLPKDHPLRQDPEFYVLKEDISPCIFGSIEKQRWSYACAKQLIERLVYAEGAENGLEFTIVRPFNWIGPRMDFIPGIDGPSEGVPRVLACFSNNLLRREPLKLVDGGESQRTFIYIKDAIEAVLLMIENPERANGHIFNVGNPNNEVTVRQLAEMMTEVYAKVSGETAIESPTIDVSSKEFYGEGYDDSDKRIPDMTIINRQLGWNPKTSLWDLLESTLTYQHTTYAEAIKKATSKPVAS
Protein: Aerobic respiration control protein ArcA homolog (P44918)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Member of the two-component regulatory system ArcB/ArcA. Represses a wide variety of aerobic enzymes under anaerobic conditions (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phosphate regulon sensor protein PhoR
- Sensor protein QseC
Sequence:
MTTPKILVVEDEIVTRNTLKGIFEAEGYDVFEAENGVEMHHILANHNINLVVMDINLPGKNGLLLARELREELSLPLIFLTGRDNEVDKILGLEIGADDYLTKPFNPRELTIRARNLLHRAMPHQEKENTFGREFYRFNGWKLDLNSHSLITPEGQEFKLPRSEFRAMLHFCENPGKLQTREELLKKMTGRELKPQDRTVDVTIRRIRKHFEDHPNTPNIIMTIHGEGYRFCGDIE
Protein: Penicillin-binding protein 1A (PBP-1a) (PBP1a) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] (O66874)
Organism: Aquifex aeolicus (strain VF5)
Subcellular location: Cell inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Probable peptidoglycan glycosyltransferase FtsW
- Penicillin binding protein 2
- Penicillin binding protein 2
- Putative 8-amino-7-oxononanoate synthase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- D-alanine--D-alanine ligase
Sequence:
MKKLVIGILGIVIALFVGLLVFLIPIYKNLPDPKLLESWTPPQASEVYDAKGRLYGTIGIQKRFYVSIDKIPEHVINAFVATEDRNFWHHFGIDPVAIVRAAIVNYRAGRIVQGGSTITQQLAKNLFLTRERTLERKIKEALLAIKIERTFDKKKIMELYLNQIYLGSGAYGVEAAAQVYFGKHVWELSLDEAALLAALPKAPAKYNPFYHPERALQRRNLVLKRMLEEGYITPEQYEEAVNKPLTVKKENKYKFSDYFLDMVKSYVFNKYGEIAYKGRLKIYTTIDLDYQKIAQKSLEEGLKRVAKIIGLPFLPKSEEDMELAYEKEAQLKRLKRGKIYVAKILKYDGNFMKVEIHGKKLKGEIKGLNTEGHKYVFVKYLGGNRAEIIPDLEGSLVSIDVKTGEIKAIVGGRSYAYSQFNRAVKALRQPGSAIKPVIYLSALLKGMTQISTIDASSKPYYDPSKGEDWIPKNYDEKEYGNVTLRYALAHSINTAAVNLLDKVGFELVLEVGKKVGLDNLKPYYSLALGTVEVTPLQLTAAYQVFANLGTECKPFFIKKIVDENGEVLEENVPECEEVLPKPETRVPVDMLRAVVLEGTARRASVLDRIVAGKTGTTDDFQDAWFVGFSPYIVTGVWVGYDVKKSLGKHMSGSRVALPIWIDYMKVVTRMYPNEDFELPPENIVVNINPKDLVLADETCEGVPMVFVKGTEPHITCSDLNAILGLR
Protein: ATP synthase peripheral stalk subunit F6, mitochondrial (ATPase subunit F6) (ATP synthase peripheral stalk subunit F6) (P18859)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MILQRLFRFSSVIRSAVSVHLRRNIGVTAVAFNKELDPIQKLFVDKIREYKSKRQTSGGPVDASSEYQQELERELFKLKQMFGNADMNTFPTFKFEDPKFEVIEKPQA
Protein: ESX-3 secretion system protein EccC3 (ESX conserved component C3) (Type VII secretion system protein EccC3) (T7SS protein EccC3) (P9WNA9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ESX-3 specialized secretion system, which is important for iron and zinc uptake or homeostasis.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:B2HST4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ESX-3 secretion system protein EccE3
- ESX-3 secretion system protein EccD3
- ESX-3 secretion system ATPase EccB3
- ESX-3 secretion system protein EccA3
- Mycosin-3
- PPE family protein PPE4
- ESX-5 secretion system ATPase EccB5
- ESX-5 secretion system protein EccD5
- Putative S-adenosyl-L-methionine-dependent methyltransferase Rv0281
- ESX-3 secretion-associated protein EspG3
Sequence:
MSRLIFEARRRLAPPSSHQGTIIIEAPPELPRVIPPSLLRRALPYLIGILIVGMIVALVATGMRVISPQTLFFPFVLLLAATALYRGNDKKMRTEEVDAERADYLRYLSVVRDNIRAQAAEQRASALWSHPDPTALASVPGSRRQWERDPHDPDFLVLRAGRHTVPLATTLRVNDTADEIDLEPVSHSALRSLLDTQRSIGDVPTGIDLTKVSPITVLGERAQVRAVLRAWIAQAVTWHDPTVLGVALAARDLEGRDWNWLKWLPHVDIPGRLDALGPARNLSTDPDELIALLGPVLADRPAFTGQPTDALRHLLIVVDDPDYDLGASPLAVGRAGVTVVHCSASAPHREQYSDPEKPILRVAHGAIERWQTGGWQPYIDAADQFSADEAAHLARRLSRWDSNPTHAGLRSAATRGASFTTLLGIEDASRLDVPALWAPRRRDEELRVPIGVTGTGEPLMFDLKDEAEGGMGPHGLMIGMTGSGKSQTLMSILLSLLTTHSAERLIVIYADFKGEAGADSFRDFPQVVAVISNMAEKKSLADRFADTLRGEVARREMLLREAGRKVQGSAFNSVLEYENAIAAGHSLPPIPTLFVVADEFTLMLADHPEYAELFDYVARKGRSFRIHILFASQTLDVGKIKDIDKNTAYRIGLKVASPSVSRQIIGVEDAYHIESGKEHKGVGFLVPAPGATPIRFRSTYVDGIYEPPQTAKAVVVQSVPEPKLFTAAAVEPDPGTVIADTDEQEPADPPRKLIATIGEQLARYGPRAPQLWLPPLDETIPLSAALARAGVGPRQWRWPLGEIDRPFEMRRDPLVFDARSSAGNMVIHGGPKSGKSTALQTFILSAASLHSPHEVSFYCLDYGGGQLRALQDLAHVGSVASALEPERIRRTFGELEQLLLSRQQREVFRDRGANGSTPDDGFGEVFLVIDNLYGFGRDNTDQFNTRNPLLARVTELVNVGLAYGIHVIITTPSWLEVPLAMRDGLGLRLELRLHDARDSNVRVVGALRRPADAVPHDQPGRGLTMAAEHFLFAAPELDAQTNPVAAINARYPGMAAPPVRLLPTNLAPHAVGELYRGPDQLVIGQREEDLAPVILDLAANPLLMVFGDARSGKTTLLRHIIRTVREHSTADRVAFTVLDRRLHLVDEPLFPDNEYTANIDRIIPAMLGLANLIEARRPPAGMSAAELSRWTFAGHTHYLIIDDVDQVPDSPAMTGPYIGQRPWTPLIGLLAQAGDLGLRVIVTGRATGSAHLLMTSPLLRRFNDLQATTLMLAGNPADSGKIRGERFARLPAGRAILLTDSDSPTYVQLINPLVDAAAVSGETQQKGSQS
Protein: Bifunctional dethiobiotin synthetase/adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Includes: Dethiobiotin synthetase (DTB synthetase) (DTBS) (EC 6.3.3.3); 7,8-diamino-pelargonic acid aminotransferase (DAPA AT) (DAPA aminotransferase) (EC 2.6.1.62) (7,8-diaminononanoate synthase) (DANS) (Adenosylmethionine-8-amino-7-oxononanoate aminotransferase) (Diaminopelargonic acid synthase)] (Q5AYI6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Bifunctional enzyme; part of the cluster involved in the biosynthesis of biotin (also known as vitamin B8 or vitamin H), a water-soluble vitamin that functions as a prosthetic group of many carboxylases, such as acetyl-CoA carboxylase and pyruvate carboxylase. Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. Catalyzes also the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:B0F481}.
Interaction partners:
- Acetylglutamate kinase
- Biotin synthase, mitochondrial
- 8-amino-7-oxononanoate synthase
- argininosuccinate lyase
- Arginine biosynthesis bifunctional protein ArgJ
- Ornithine carbamoyltransferase, mitochondrial
- Argininosuccinate synthase
- Amino-acid acetyltransferase, mitochondrial
Sequence:
MAPVGAALWRSLRAHQVYGANTDVGKTIVSTFLCNAVNRLKNQGKSAFLKPVSTGPLDEADDRHLQRHAPNTLTKCLYQFDEPVSPHIAAKTFAIPRDDEILSSVHRTLSDWANDGVGFALVETAGGVHSPGPNGNSQADLYRPLRLPIILVADSRLGGISSSISAYESLLLRGYDVHSVLLFKDDYYQNHEYLGNYFRGKSIPLVPVPAPPRRPQEQDPDSRARDLEALDKYYSSVTKSTDVVSLLDELVLKNKQRVEYLDEMASRAQKTIWYPFTQHHGMAAKDITPIDSAYDDFFQTYVTADRSAQQGRLQATFDGSASWWTQGLGHGNPGLALSAAYAAGRYGHVMFPGNIHEPALALAESLLKTVDNPRLQKVFYTDNGSTGMEVALKMGLRAACDRYGWDASKEQINILGLKGSYHGDTIGVMDCSEPSTYNQRVEWYRGRGHWFDFPLVKMSQGVWQVEVPATLQASLGGNQQFSSLDAVFDVESRVRSDAGQRYRKYILETIERLVTQEGKKFGALIMEPIILGAGGMLFCDPLFQRCLADVVRGNPQLFNRGRLTEPQPQTDLSWSGLPVIFDEVFTGLYRLGRKSSASFLGVNPDIAVNAKLLTGGLVPLCTTLASNEIFNAFTSPEKRDALLHGHSYTAHAVGCQVALDSLRTMNNMDEDGSWNDFKNDWKQPHAGDTARVWSVWSHKLLHNLSHAESVDGVFAIGSVLSISLKDAEGAGYTSTAAKGLQTRLAAGGPQFNVHSRVLGNVLYLMSSVTSKQETLRTIEGILREALL
Protein: Short coiled-coil protein homolog (Q9U377)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MSQKTEQDDIPLADDDDTVTIISGGKTPRAAQPLPKEEPPEDPEEKARMITQVLELQNTLDDLSQRVESVKEESLKLRSENQVLGQYIQNLMSSSSVFQSSQPSRPKQ
Protein: Phosphate butyryltransferase (EC 2.3.1.19) (Phosphotransbutyrylase) (Q05624)
Organism: Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
Function: Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate.
Interaction partners:
Sequence:
MSKNFDELLSRLKEVPTKKVAVAVAQDEPVLEAIKEATENNIAQAILVGDKQQIHEIAKKINLDLSDYEIMDIKDPKKATLEAVKLVSSGHADMLMKGLVDTATFLRSVLNKEVGLRTGKLMSHVAVFDVEGWDRLLFLTDAAFNTYPEFKDKVGMINNAVVVAHACGIDVPRVAPICPVEVVNTSMQSTVDAALLAKMSDRGQIKGCVIDGPFALDNAISEEAAHHKGVTGSVAGKADILLLPNIEAANVMYKTLTYFSKSRNGGLLVGTSAPVILTSRADSFETKVNSIALAALVAARNK
Protein: Alpha-1,3/1,6-mannosyltransferase ALG2 (EC 2.4.1.132) (EC 2.4.1.257) (Asparagine-linked glycosylation protein 2) (GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase) (GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase) (GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase) (Q6FJJ9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P43636}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- GDP-Man:Man
- Crossover junction endonuclease MUS81
Sequence:
MVPAKKLKIAFVHPDLGIGGAERLVVDAALGLQEAGHEVIIYTSHCDKTHCFEEVKNGTLKVEVFGDFLPTDLGKRFFIVFANLRQLYLTAKVVLSGRSKDKDVFIIDQLSTCVPFFKLANNKVLFYCHFPDQLLAIRTNWIKSLYRIPFDLLEQFTMYCSDEVVVNSNFTKSMYKKTFKYLQKNPNVIYPCVDTDTETLINDRDMQIGNLLVGKCPNFYLSINRYERKKNIELAIQAFAKASVENTNLVVCGGYDPRIHENVQYLQELTCLCKELDLSYTVNHYSDFIEDSYSVNEIEKLFGAKVIFLTSISSSLKEFLIQNMQLLLYTPSYEHFGIVPLEAMKYGKPVLAVNNGGPVETVVSYQKEDNEKSTTGWLRSADADEWASALIESKEVLNQNPELFKNNGPKRVIELFSRKAMTQEFETNIKLALRHTSNISIIYVVSIIFAVLLKVFVF
Protein: Cag pathogenicity island protein (Cag3) (O25258)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Cag pathogenicity island protein
- Cag pathogenicity island protein
- Cag pathogenicity island protein
- CAG pathogenicity island protein 12
- Ribosomal silencing factor RsfS
- Cag pathogenicity island protein
Sequence:
MFRKLATAVSLIGLLTSNTLYAKEISEADKVIKATKETKETKKEAKRLKKEAKQRQQIPDHKKPQYVSVDDTKTQALFDIYDTLNVNDKSFGDWFGNSALKDKTYLYAMDLLDYNNYLSIENPIIKTRAMGTYADLIIITGSLEQVNGYYNILKALNKRNAKFVLKINENMPYAQATFLRVPKRSDPNAHTLDKGASIDENKLFEQQKKMYFNYANDVICRPDDEVCSPLRDEMVAMPTSDSVTQKPNIIAPYSLYRLKETNNANEAQPSPYATQTAPENSKEKLIEELIANSQLVANEEEREKKLLAEKEKQEAELAKYKLKDLENQKKLKALEAELKKKNAKKPRVVEVPVSPQTSNSDETMRVVKEKENYNGLLVDKETTIKRSYEGTLISENSYSKKTPLNPNDLRSLEEEIKSYYIKSNGLCYTNGINLYVKIKNDPYKEGMLCGYESVQNLLSPLKDKLKYDKQKLQKALLKDSK
Protein: RNA-binding protein pos-1 (Posterior segregation protein pos-1) (Zinc-finger protein pos-1) (G5EF15)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9834181}. Note=Localized to P granules in the germline blastomeres P1, P2, P3 and P4. {ECO:0000269|PubMed:9834181}.
Interaction partners:
- C-type lectin domain-containing protein 91
- Uncharacterized protein EEED8.3
- CCCH-type zinc finger protein oma-2
- G2/mitotic-specific cyclin-B
- Chondroitin proteoglycan 1
- glucosamine-phosphate N-acetyltransferase
- Embryonic mRna
- Transmembrane protein
- C-type lectin domain-containing protein 87
- RING-type domain-containing protein
Sequence:
MADNDFLSGEAIMVFKKEILDSHSDFTRSLSHQSASPEAYDQENVFSQDFQPFMKQDKETQNSASQPTSEQSLANRDPCTVPDDLREEMMRQRRKEDAFKTALCDAYKRSQACSYGDQCRFAHGVHELRLPMNPRGRNHPKYKTVLCDKFSMTGNCKYGTRCQFIHKIVDGNAAKLASGAHANTSSKSPARNAAAHNHSLFVPQGSTDRSMDLNQSLPIRQSDLVRAFARATRLDVSGYNSTAQLAQYFESQFQRIQQLSSHHH