wanglab/gogpt-training-data huggingface dataset:
Protein: Major capsid protein (MCP) (F5HGT1)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04016}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04016}.
Interaction partners:
Sequence:
MENWSALELLPKVGIPTDFLTHVKTSAGEEMFEALRIYYGDDPERYNIHFEAIFGTFCNRLEWVYFLTSGLAAAAHAIKFHDLNKLTTGKMLFHVQVPRVASGAGLPTSRQTTIMVTKYSEKSPITIPFELSAACLTYLRETFEGTILDKILNVEAMHTVLRALKNTADAMERGLIHSFLQTLLRKAPPYFVVQTLVENATLARQALNRIQRSNILQSFKAKMLATLFLLNRTRDRDYVLKFLTRLAEAATDSILDNPTTYTTSSGAKISGVMVSTANVMQIIMSLLSSHITKETVSAPATYGNFVLSPENAVTAISYHSILADFNSYKAHLTSGQPHLPNDSLSQAGAHSLTPLSMDVIRLGEKTVIMENLRRVYKNTDTKDPLERNVDLTFFFPVGLYLPEDRGYTTVESKVKLNDTVRNALPTTAYLLNRDRAVQKIDFVDALKTLCHPVLHEPAPCLQTFTERGPPSEPAMQRLLECRFQQEPMGGAARRIPHFYRVRREVPRTVNEMKQDFVVTDFYKVGNITLYTELHPFFDFTHCQENSETVALCTPRIVIGNLPDGLAPGPFHELRTWEIMEHMRLRPPPDYEETLRLFKTTVTSPNYPELCYLVDVLVHGNVDAFLLIRTFVARCIVNMFHTRQLLVFAHSYALVTLIAEHLADGALPPQLLFHYRNLVAVLRLVTRISALPGLNNGQLAEEPLSAYVNALHDHRLWPPFVTHLPRNMEGVQVVADRQPLNPANIEARHHGVSDVPRLGAMDADEPLFVDDYRATDDEWTLQKVFYLCLMPAMTNNRACGLGLNLKTLLVDLFYRPAFLLMPAATAVSTSGTTSKESTSGVTPEDSIAAQRQAVGEMLTELVEDVATDAHTPLLQACRELFLAVQFVGEHVKVLEVRAPLDHAQRQGLPDFISRQHVLYNGCCVVTAPKTLIEYSLPVPFHRFYSNPTICAALSDDIKRYVTEFPHYHRHDGGFPLPTAFAHEYHNWLRSPFSRYSATCPNVLHSVMTLAAMLYKISPVSLVLQTKAHIHPGFALTAVRTDTFEVDMLLYSGKSCTSVIINNPIVTKEERDISTTYHVTQNINTVDMGLGYTSNTCVAYVNRVRTDMGVRVQDLFRVFPMNVYRHDEVDRWIRHAAGVERPQLLDTETISMLTFGSMSERNAAATVHGQKAACELILTPVTMDVNYFKIPNNPRGRASCMLAVDPYDTEAATKAIYDHREADAQTFAATHNPWASQAGCLSDVLYNTRHRERLGYNSKFYSPCAQYFNTEEIIAANKTLFKTIDEYLLRAKDCIRGDTDTQYVCVEGTEQLIENPCRLTQEALPILSTTTLALMETKLKGGAGAFATSETHFGNYVVGEIIPLQQSMLFNS
Protein: Kremen protein 2 (Dickkopf receptor 2) (Kringle domain-containing transmembrane protein 2) (Kringle-containing protein marking the eye and the nose) (Q8NCW0)
Organism: Homo sapiens (Human)
Function: Receptor for Dickkopf proteins. Cooperates with DKK1/2 to inhibit Wnt/beta-catenin signaling by promoting the endocytosis of Wnt receptors LRP5 and LRP6. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning and can also negatively regulate bone formation.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Dickkopf-related protein 1
- Endoplasmic reticulum lectin 1
- Low-density lipoprotein receptor-related protein 6
- Low-density lipoprotein receptor-related protein 5
- Dickkopf-related protein 2
- Fanconi anemia group M protein
- Dickkopf-related protein 4
- Proto-oncogene Wnt-1
- Kremen protein 1
- R-spondin-1
Sequence:
MGTQALQGFLFLLFLPLLQPRGASAGSLHSPGLSECFQVNGADYRGHQNRTGPRGAGRPCLFWDQTQQHSYSSASDPHGRWGLGAHNFCRNPDGDVQPWCYVAETEEGIYWRYCDIPSCHMPGYLGCFVDSGAPPALSGPSGTSTKLTVQVCLRFCRMKGYQLAGVEAGYACFCGSESDLARGRLAPATDCDQICFGHPGQLCGGDGRLGVYEVSVGSCQGNWTAPQGVIYSPDFPDEYGPDRNCSWALGPPGAALELTFRLFELADPRDRLELRDAASGSLLRAFDGARPPPSGPLRLGTAALLLTFRSDARGHAQGFALTYRGLQDAAEDPEAPEGSAQTPAAPLDGANVSCSPRPGAPPAAIGARVFSTVTAVSVLLLLLLGLLRPLRRRSCLLAPGKGPPALGASRGPRRSWAVWYQQPRGVALPCSPGDPQAEGSAAGYRPLSASSQSSLRSLISAL
Protein: Arfaptin-1 (ADP-ribosylation factor-interacting protein 1) (P53367)
Organism: Homo sapiens (Human)
Function: Plays a role in controlling biogenesis of secretory granules at the trans-Golgi network. Mechanisitically, binds ARF-GTP at the neck of a growing secretory granule precursor and forms a protective scaffold. Once the granule precursor has been completely loaded, active PRKD1 phosphorylates ARFIP1 and releases it from ARFs. In turn, ARFs induce fission. Through this mechanism, ensures proper secretory granule formation at the Golgi of pancreatic beta cells.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:22981988, ECO:0000269|PubMed:9038142}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21239483, ECO:0000269|PubMed:30917996}.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor 3
- ADP-ribosylation factor 1
- ADP-ribosylation factor 5
- RAC-alpha serine/threonine-protein kinase
- Arfaptin-2
Sequence:
MAQESPKNSAAEIPVTSNGEVDDSREHSFNRDLKHSLPSGLGLSETQITSHGFDNTKEGVIEAGAFQGSPAPPLPSVMSPSRVAASRLAQQGSDLIVPAGGQRTQTKSGPVILADEIKNPAMEKLELVRKWSLNTYKCTRQIISEKLGRGSRTVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQRQLGDAFADLSLKSLELHEEFGYNADTQKLLAKNGETLLGAINFFIASVNTLVNKTIEDTLMTVKQYESARIEYDAYRTDLEELNLGPRDANTLPKIEQSQHLFQAHKEKYDKMRNDVSVKLKFLEENKVKVLHNQLVLFHNAIAAYFAGNQKQLEQTLKQFHIKLKTPGVDAPSWLEEQ
Protein: Telomeric repeat-binding factor (D3ZJF7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|PIRNR:PIRNR038016}.
Interaction partners:
- Telomeric repeat-binding factor 2-interacting protein 1
- TERF1
- Protection of telomeres protein 1
- Telomeric repeat-binding factor
- Protection of telomeres protein 1
- Adrenocortical dysplasia protein homolog
- 5' exonuclease Apollo
- Nibrin
- Structure-specific endonuclease subunit SLX4
- Double-strand break repair protein MRE11
Sequence:
MAAGAGTAGPASGPGVVRDPMASQPRKRPGGEGARRSNTMAGGGGSSDNGGRAANRRASRSGGRARRGRHEPGLGGAAERGAGEARLEEAVNRWVLKFYFHEALRAFRSSRYRDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTDSMVESSRRLVKEAAVIICIKNKEFEKASKILKKYMSKDPTTQKVRTDLLNIIREKNLAHPVIQNFSYEIFQQKMLRFLESHLDDTEPYLLTMAKKALRSESAASSTMKEEKHTEPVEKPLREPPRQPRNPPTTIGLRTVKAAFKALSTAQDSEAAFAKLDQKDLVLPNLASPSSPTHKNKRPRKDENESSAPAEGEGGSERQPRNNRMTISRLVLEEDSQSSEPSPDLNSSRQALSASPSKPRALNQPHTGEKNPKASKDKWNSPNGLEEKEVWSEEDQLFEVRAPGEDKSSNLARKQKWTIEESEWVKDGVQKYGEGNWVAISKSYPFVNRTAVMIKDRWRTMKKLGLN
Protein: DnaJ heat shock protein family (Hsp40) member C7 (A0A6I8PUD4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSIGTCCFPGTNREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG
Protein: E3 ubiquitin-protein ligase ZNRF2 (EC 2.3.2.27) (Protein Ells2) (RING finger protein 202) (RING-type E3 ubiquitin transferase ZNRF2) (Zinc/RING finger protein 2) (Q8NHG8)
Organism: Homo sapiens (Human)
Function: May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:14561866}; Peripheral membrane protein {ECO:0000269|PubMed:14561866}. Lysosome membrane {ECO:0000269|PubMed:14561866}; Peripheral membrane protein {ECO:0000269|PubMed:14561866}. Presynaptic cell membrane {ECO:0000269|PubMed:14561866}; Peripheral membrane protein {ECO:0000269|PubMed:14561866}. Cytoplasm {ECO:0000269|PubMed:27244671}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D2
- Ubiquitin-conjugating enzyme E2 N
- E2 ubiquitin-conjugating enzyme
Sequence:
MGAKQSGPAAANGRTRAYSGSDLPSSSSGGANGTAGGGGGARAAAAGRFPAQVPSAHQPSASGGAAAAAAAPAAPAAPRSRSLGGAVGSVASGARAAQSPFSIPNSSSGPYGSQDSVHSSPEDGGGGRDRPVGGSPGGPRLVIGSLPAHLSPHMFGGFKCPVCSKFVSSDEMDLHLVMCLTKPRITYNEDVLSKDAGECAICLEELQQGDTIARLPCLCIYHKGCIDEWFEVNRSCPEHPSD
Protein: Kinesin like protein (Kinesin motor domain-containing protein) (G5ECC0)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Kinesin-like protein
- Protein regulator of cytokinesis 1
- Kinesin light chain
- Kinesin light chain
- Calponin-homology
- Kinesin-like protein
- Kinesin motor domain-containing protein
- Kinesin motor domain-containing protein
- Dynein heavy chain, cytoplasmic
- Kinesin motor domain-containing protein
Sequence:
MNVARRRSGLFRSTIGAPPKATRGRAAAPPIKEADPATIPRQSAPGGITIGAAACRPPSRLPGATISATGRASLPERSAMAKTSTSSHSRPALQSTASRNTTLTAASTSRQLRTGRPPPPSTQRSTATFSLKPSVARARPVAQKPILPSKVTLLEERNAQLEREMAEATDFAEHQKSKIQFLDGKLEGADRKLISLQDQLSTLKEVHKSKMEECEEYRVHNNDLRDLLNEKEAELRKLHNDVVDLRGQIRVAVRVRPLIKSEVDTSSSAIEYPAVDAIKINEGSKPGNVVKFENVFTPVFSQKEVFANVEEFIRSSLHGYNVGLIAYGQTGSGKTHTMRGGNGEEEGIIPRAAAFLFAESKKLESLGWKFDFSLSFLEVYNNVAYDLLSGRDVVQLRLNDQTVSMIGLSEHTISNVSDVARLLRVADGGRKTAATKCNGSSSRSHAVYMWKIKAHQPSTGISTTCQLKLVDLAGSERAKESGVSGDQFKEMTNINQSLSILQMCISQQRSQKGHVSYRDSKLTQVLMDCLGRGSSKTMVVVNLNPCNEQATESKRSIEFASKMRSTHIGSAVQQRTLLGDVSQMSMN
Protein: Uncharacterized protein (Q383E8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVWKGSRERGVQEYRKKSKGNKPTKGEKVSKKGVSSSRQPKQRELLSAKQQQQQNRKNEELRAALAGAFSTEVSSSNAGPAFDGYGKGSPTDRLQFGYAPAVAAEAVAYHSTISTDAWIEARRTRYRTAIVEQKKLRRPNCEPITSILKLQGHWRSTELFEREVHGSHAVAQDKVDDILDTFVSRQRVA
Protein: Actin-like protein 6A (Q54UQ7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- SWI/SNF complex component SNF12 homolog
- Myb domain-containing protein
- RuvB-like helicase 2
- RuvB-like helicase
- Probable transcription-associated protein 1
- Actin-related protein 8
- Enhancer of polycomb-like protein
- NuA4 complex subunit EAF3 homolog
- Chromatin modification-related protein EAF6
- Histone H4
Sequence:
MYSGDDVSAIVIDVGTFSTKGGYAGEDSPKAVFPTDIGVVYKNENETVGTGDSEMGEKDDSEPKRTYYCGTNGITYRRPHMEIINPLSDGLIKNWDAMEQIWNHTFYERLHINPIEHPILLAEPTYNTRAIREKVTEIMFEKYHAPALFIAKNAVLSSFASSKASSLVLDSGGGMTSVTPVFEGFVVKNGIVKSNLAGNRLTEEYYRILSSKNITVNPINLIKKVEIKTGEFGITPYNIPTLTESYKRYVTLETIRDLKETSCRVSDTKDLGEDINIAQVPYELPDGNLLEIGSDRFQIPELLFNPTPLNEQILNNNNNNSNGENTTTSSVVQQPQYQGLGRMIIESLEKSDTDIRKELISNLIITGGNTLFAGFQERLVRDISEISYNKPKIVANQTEKKNSVWIGGSVLGSLGTFQQMWMSKSEWEEFGRPLVEKKCP
Protein: Probable ATP synthase 24 kDa subunit, mitochondrial (Q9SJ12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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 (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit delta', mitochondrial
- ATP synthase subunit beta-3, mitochondrial
- ATP synthase subunit beta-2, mitochondrial
- ATP synthase subunit O, mitochondrial
- ATP synthase protein YMF19
- ATP synthase subunit a-2
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit d, mitochondrial
- ATP synthase gamma chain 2, chloroplastic
- Probable mitochondrial-processing peptidase subunit beta, mitochondrial
Sequence:
MAYASRFLSRSKQLQGGLVILQQQHAIPVRAFAKEAARPTFKGDEMLKGVFFDIKNKFQAAVDILRKEKITLDPEDPAAVKQYANVMKTIRQKADMFSESQRIKHDIDTETQDIPDARAYLLKLQEIRTRRGLTDELGAEAMMFEALEKVEKDIKKPLLRSDKKGMDLLVAEFEKGNKKLGIRKEDLPKYEENLELSMAKAQLDELKSDAVEAMESQKKKEEFQDEEMPDVKSLDIRNFI
Protein: Uncharacterized protein (Q57UK9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLSPQWSQHSVVVHSEGQAIVQQSQPHSFTPSSIGRPIIVRQRDPRVFTATPTASTSSIAAEGGGSVFALTSLVRPQDISETFWVPDATRNEVGLLEAIQKRTAANRTYVLVHSRPLAELQCNFSTCTGDNIDISHDVFRLSKASAALLQMERNLFDGGSAYLHGDAPKAGTGADADSFKSNVRMPRGPTGFKGNVPSKTFKEQLRMGLCSINEEEYYLVRYRDYSLWAVQRYADIAKKDGFWGKKYVEQCFAVHVGKEPGELIPITEAQFLFGVELLQRQILEYVGVYDSLDINYCALSRDQFRSLGVILGDGMRAVEVEGEEIRRRREEEEESKDSRANAHSDAYVPPSIWDWRPSAIKKRINHQLQLQYHAIGRLVVRVVMFGTATYIVCSYAQRFLPQAGSGNGATSQRRGKGYRGQGGNYDRNDTPFVSRGFLRSVMLGPKEVFDYLLAPSA
Protein: Cytochrome P450 2B6 (EC 1.14.13.-) (1,4-cineole 2-exo-monooxygenase) (CYPIIB6) (Cytochrome P450 IIB1) (P20813)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of endocannabinoids and steroids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of arachidonoylethanolamide (anandamide) to 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling. Hydroxylates steroid hormones, including testosterone at C-16 and estrogens at C-2. Plays a role in the oxidative metabolism of xenobiotics, including plant lipids and drugs. Acts as a 1,4-cineole 2-exo-monooxygenase.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 3A5
- Cytochrome P450 3A7
- Cytochrome P450 4A11
- Peptidyl-prolyl cis-trans isomerase G
- Cytochrome P450 1A2
- Aldehyde oxidase
- Cytochrome P450 3A4)
- Cytochrome P450 1A1
- Sulfotransferase 2A1
- Epoxide hydrolase 1
Sequence:
MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFREKYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNRWKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIICSIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQEINAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGTETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFSDLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGALKKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKIPPTYQIRFLPR
Protein: Bradykinin inhibitor peptide (BIP) (P85025)
Organism: Agkistrodon bilineatus (Cantil) (Tropical moccasin)
Function: Bradykinin inhibitor peptide antagonizes the vasodilatory actions of bradykinin at the B2 bradykinin receptor (BDKRB2).
Subcellular location: Secreted {ECO:0000269|PubMed:16277978}.
Interaction partners:
Sequence:
TPPAGPDVGPR
Protein: 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC 4.1.2.55) (O54288)
Organism: Saccharolobus solfataricus (Sulfolobus solfataricus)
Function: Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal). It is equally active with both D- and L-glyceraldehyde.
Interaction partners:
Sequence:
MPEIITPIITPFTKDNRIDKEKLKIHAENLIRKGIDKLFVNGTTGLGPSLSPEEKLENLKAVYDVTNKIIFQVGGLNLDDAIRLAKLSKDFDIVGIASYAPYYYPRMSEKHLVKYFKTLCEVSPHPVYLYNYPTATGKDIDAKVAKEIGCFTGVKDTIENIIHTLDYKRLNPNMLVYSGSDMLIATVASTGLDGNVAAGSNYLPEVTVTIKKLAMERKIDEALKLQFLHDEVIEASRIFGSLSSNYVLTKYFQGYDLGYPRPPIFPLDDEEERQLIKKVEGIRAKLVELKILKE
Protein: Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial (EC 2.8.3.5) (3-oxoacid CoA-transferase) (Q9W058)
Organism: Drosophila melanogaster (Fruit fly)
Function: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BYC2}.
Interaction partners:
- hydroxymethylglutaryl-CoA lyase
- Acetyl-CoA acetyltransferase 1, isoform A)
- Acetyl-CoA acetyltransferase 2
- Hydroxymethylglutaryl-CoA synthase
- RE15974p
- acetyl-CoA C-acyltransferase
- Short-chain dehydrogenase/reductase)
- HL08109p)
- Vanin-like protein 3
- Adenylosuccinate lyase
Sequence:
MLCRLVGNRSLGARYTASIKAIACYSTSGKQRNGKIYESAIDAVADVQDGAQILFGGFGICGIPEKMINALKQKGVKNITGVSNNGGVDDTGLGVLIKQKQVSKVIGSYVGENTELVRQYLEGELAVELTPQGTLAEKIRAGGAGIPAFYTPTGYATLVQEGGAPIKYSKDGKVEISSEKKPVKEFNGKNYVMEESIFADFAFVKAQKADPLGNLVFNKAARNFNAPMCRAAKITVAEVEEIVPIGALSPDEIHVPGIYINRIFKGTNYNKRVERLRITEPKDPSKPAPPPNPAQVLRERIARRVALEFHDGMYANLGIGIPVLSSNYIPKGMNVMLQSENGILGLGPFPTKDKVDPDLINAGKESVTVVPGASYFGSDDSFAMIRGGHVDITILGAMEVSATGDLANWMIPGKLVKGMGGAMDLVAAPGTKVIITMEHNARDGSPKILDTCSLPLTGKGVIDMIISEKAVFTVEKGVGLTLIEVAEGYTVDDIIASTGAKFTVSPNLKKMGQIPV
Protein: Serine/threonine-protein kinase, putative (EC 2.7.1.-) (Q582V7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- BTB domain-containing protein
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Small GTPase, putative
- GTP binding protein
Sequence:
MLNRLFGRGKSKKDKDKDKDKSKEKEKRDGESSNTKSGNSHKSGSERKDENTTEKVTKEDFETIDTLGKGSFAYVVLVRRVGTNNLYAMKVVNKQGLLDHNRCRDVFIERNVLSRINHPFLLKLYWTFQSEHKLFFVMEYMAGGDLDKYMNSVPNKQLDLPTSKLYGAEILMAILTLHEQSVIYRDLKPENILLTGDGHCVLADFGLSKDFYDAKMGENASVTDMRANSFVGSPFYVAPDVLKQREYTNAVDFWSFGILLYRMLCGRTPFSGKNMKEVFDNILYSDLRFPSTVSIPSEAKDLISRLLVKDAAHRIKGPEVKAHPFWTGINFDEVMQKKVKPPRWVPAPSVDKLIAERSAAQSGNNSSKNPAQVVNTPAHSSQLNARQQQLFNGFSCTTDNHLGGGS
Protein: Bifunctional cysteine synthase/O-acetylhomoserine aminocarboxypropyltransferase (Q59US5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Cysteine synthase 1
- assimilatory sulfite reductase
- Cysteine synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Sulfite reductase subunit beta
- Cystathionine beta-synthase
- cystathionine gamma-synthase
- cystathionine gamma-lyase
- Transaminase A
- S-adenosylmethionine-homocysteine S-methyltransferase
Sequence:
MPSHFDTLQLHAGQPVEKPHQPRAPPIYATTSYVFNDSKHGAQLFGLETPGYIYSRIMNPTNDVFEQRIAALEGGIGALATSSGQSAQFLAIAGLAHAGDNIISTSYLYGGTYNQFKVAFKRLGIETKFVNGDAAEDFAKLIDDKTKAIYIETIGNPKYNVPDFEKITKLAHEHGIPVVVDNTFGAGGFLVNPIAHGADIVVHSATKWIGGHGTTIAGVIVDSGNFPWTEYPEKYPQFSKPSEGYHGLVLSDALGKAAYIGHLRIELLRDLGPALNPFGSFLLLQGLETLSLRVERQSENALKLAQWLEKNPNVESVSYLGLPSHESHELSKKYLNNDAKYFGGALAFTVKDITNTSSDPFNEASPKLVDNLEIASNLANVGDSKTLVIAPWFTTHQQLSDEEKLASGVTKGLIRVSTGTEYIDDIINDFEQAFKKVYNN
Protein: Translation factor GUF1, mitochondrial (EC 3.6.5.-) (Elongation factor 4 homolog) (EF-4) (GTPase GUF1) (Ribosomal back-translocase) (P46943)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: 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.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03137, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18442968}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03137, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18442968}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03137, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18442968}.
Interaction partners:
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL23
Sequence:
MLKFRIRPVRHIRCYKRHAYFLRYNHTTTPAQKLQAQIEQIPLENYRNFSIVAHVDHGKSTLSDRLLEITHVIDPNARNKQVLDKLEVERERGITIKAQTCSMFYKDKRTGKNYLLHLIDTPGHVDFRGEVSRSYASCGGAILLVDASQGIQAQTVANFYLAFSLGLKLIPVINKIDLNFTDVKQVKDQIVNNFELPEEDIIGVSAKTGLNVEELLLPAIIDRIPPPTGRPDKPFRALLVDSWYDAYLGAVLLVNIVDGSVRKNDKVICAQTKEKYEVKDIGIMYPDRTSTGTLKTGQVGYLVLGMKDSKEAKIGDTIMHLSKVNETEVLPGFEEQKPMVFVGAFPADGIEFKAMDDDMSRLVLNDRSVTLERETSNALGQGWRLGFLGSLHASVFRERLEKEYGSKLIITQPTVPYLVEFTDGKKKLITNPDEFPDGATKRVNVAAFHEPFIEAVMTLPQEYLGSVIRLCDSNRGEQIDITYLNTNGQVMLKYYLPLSHLVDDFFGKLKSVSRGFASLDYEDAGYRISDVVKLQLLVNGNAIDALSRVLHKSEVERVGREWVKKFKEYVKSQLYEVVIQARANNKIIARETIKARRKDVLQKLHASDVSRRKKLLAKQKEGKKHMKTVGNIQINQEAYQAFLRR
Protein: cGMP-dependent protein kinase (EC 2.7.11.12) (TgPKG) (Q8MMZ7)
Organism: Toxoplasma gondii
Function: Serine/threonine protein kinase which acts as a downstream effector of the second messenger cGMP. Plays an essential role in tachyzoite invasion of and egress from host cells. During invasion of host cells, regulates the apico-basal flux of F-actin probably via Ca(2+)-mediated activation of CDPK1. In tachyzoites, required for microneme secretion. Required for tachyzoite gliding motility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31235476}. Membrane {ECO:0000269|PubMed:31235476}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:11834729, ECO:0000269|PubMed:28465425}; Lipid-anchor {ECO:0000269|PubMed:11897122}. Note=Membrane localization is essential to regulate parasite invasion, egress and microneme secretion. {ECO:0000269|PubMed:28465425}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:11897122, ECO:0000269|PubMed:28465425}.
Interaction partners:
Sequence:
MGACISKNSSARVSRSSALSASKQTVAASAPPGAAGDETSATGAAEEASRNSLARVDGTRASAAELERAPDGVCPDREEPGTANAEQGGVTEKKDTRETLAGMNSPKTLEAEAQEDDPKREAPNQDVPSEAPEGPKEKPGGDRKPAQKAILKQDDSHTEEEKLNAHLAYREKTPADFALIQDSLKANLVCSSLNEGEIDALAVAMQFFTFKKGDVVTKQGEPGSYFFIIHSGTFDVLVNDKRVNAMDKGKAFGEIALIHNTERSATVVASSTEGALWGVQRHTFRETLKQLSSRNFAENRQFLASVKFFEMLTEAQKNVITNALVVENFKPGQPIVKEGDAGDVLYILKSGKAKVSIGGREIRMLRKGDYFGERALLYKEPRSATITAEEFTVCVSIGRELLDRVLGNLQHVLFRNIMVEALQQSKVYELFQGDQLSKLIEAAVVKDYGADYVILDKENKTKGIRFFFVLEGELSVYAYTQNPATKEEERKLAATLKRGQAFGEEYVLNPTRPFNHYVKSVGPCKLALFTSSVLTATLGGEDIDETLDFNNKRAIIRKMYIFRYLSDHQMTMLIKAFKTVRYMSGEYIIKEGERGTRFFIIKAGEVAILKNNKRLRTLGRHDYFGERALLYDKPRTASVCANSAGVDLWVVDKSVFNEIIKGPMLAHLEERIRMQDTKVEFQDLQVVRVVGRGTFGTVKLVRHVPTDIRYALKCVSRRSVIALSQQQHIRLEREIMAENDHPFIIRLVRTFRDKEFLYFLTELVTGGELYDAIRKLGLLARSQAQFYLASIVLAIEYLHERNIAYRDLKPENILLDSQGYVKLIDFGCAKKMQGRAYTLVGTPHYMAPEVILGKGYTLTADTWAFGVCLYEFMCGPLPFGNDAEDQLEIFRDILTGKLVFPHYVTDQDAINLMKRLLCRLPEVRIGCSINGYKDIKEHAFFGDFDWDKLAGRGLPPPLAPKGETYAEDTEQSSFELDEDDTIVLEDEYDWDKDF
Protein: Dipeptidase (EC 3.4.13.19) (E7FBC7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU341113}; Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU341113}.
Interaction partners:
- Cytosolic non-specific dipeptidase
- Dipeptidase
Sequence:
MLIHKEAGISGAWLQWFICISLSLLHGVISETSRALDMMTKYPLIDGHNDWALHLRKHDDNKLTKVNLYNYPQGATDITRLIAGHVGGQVFSAYVLCTAQDKDAVRLTLEQIDVIRRMCTEKPELELVTTSEGMKKSTKIACLISVEGGHSIDSSLAALRMFYQLGVRSMSLTHTCNTPWAKSSSSFYQHYQWVNNSLTEFGKEVVHEMNRLGMLVDLSHSSWETARAVLKHTAAPVIFSHSSAYAVCNNVRNVPDDLLLLLKRNGGLIMVNLYNNFIACSSNKANVSIVADHFDHIKRVIGAESIGIGADYDGAQGFPEGLEDVSKYPALIEELIARNWTEQELAGVLRLNFLKVFEMVEKIRDDMLDTSPSEVEIPFLEANNSCRAMLIHPTKVSKMVKNGNAPQTMPAGAFAWFILFLIQSI