wanglab/gogpt-training-data huggingface dataset:
Protein: Conserved oligomeric Golgi complex subunit 5 (COG complex subunit 5) (Component of oligomeric Golgi complex 5) (Q9C9V9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal Golgi function.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9VJD3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9VJD3}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 1
- Vacuolar protein sorting-associated protein 51 homolog
- Proline-rich family protein
- Vacuolar protein sorting-associated protein 54, chloroplastic
Sequence:
MALPPSSPSPSSPSLQRLSTFKNPPPSSLSSGAPPPQTPSSSSSSPLDSFATDPILSPFLSSSFSSASFSSAALASGSPASTAERLHQAIRLLDSQLRNDVISRHPELLAQLSSLSHADVSLSSLRSSVSSLQSSIRRVRSDLSEPIKSIRSKSVQLSNLHTATELLSHSVRTLRLSKKLRDLADFPDPDKIDLTKAAQFHFEILTMCKEYDLFGIDVIDEEIKFVTEIGEKLRSEAMKVLERGMEGLNQAEVGTGLQVFYNLGELKSTVDQLVNKYKGMAVKSVSVAMDMKAITSGSGGGFGPGGIRSSGSPHIGGGAKVREALWQRMASCMEQLCSLVVAVWHLQRVLSKKRDPFTHVLLLDEVIKEGDSMLTDRVWDALVKAFTSQMKSAYTASSFVKEIFTMGYPKLVSMIENLLERISRDTDVKGVLPAINLERKEQMVACIAIFQTAFLSLCFGRLSDLVNSIFPMSSRGSLPSKEQISQVLSHIQDEIEAVHPDARLTLLVLREIGKALSNLAQRAECQISTGPETRQISGPATSTQIRNFTLCQHLQGIHTHISSMVADLPSIATDVLSPYLAAIYDAACEPVTPLFKAMRDKLESCILQIHDQNFGADDADMDNNASSYMEELQRSILHFRKEFLSRLLPSAANANTAGTESICTRLTRQMASRVLIFYIRHASLVRPLSEWGKLRMAKDMAELELAVGQNLFPVEQLGAPYRALRAFRPLVFLETSQMGSSPLINDLPPSIVLHHLYTRGPDELESPMQKNRLSPKQYSLWLDNQREDQIWKGIKATLDDYAVKIRSRGDKEFSPVYPLMLQIGSSLTQENL
Protein: Cyclic GMP-AMP synthase (c-GAMP synthase) (cGAS) (EC 2.7.7.-) (3',3'-cGAMP synthase) (Cyclic AMP-GMP synthase) (c-AMP-GMP synthase) (Dinucleotide cyclase DncV) (CD-NTase) (Q9KVG7)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.
Interaction partners:
- cGAMP-activated phospholipase
- CD-NTase/cGAS isopeptidase
- ATP-dependent ubiquitin transferase-like protein Cap2
Sequence:
MRMTWNFHQYYTNRNDGLMGKLVLTDEEKNNLKALRKIIRLRTRDVFEEAKGIAKAVKKSALTFEIIQEKVSTTQIKHLSDSEQREVAKLIYEMDDDARDEFLGLTPRFWTQGSFQYDTLNRPFQPGQEMDIDDGTYMPMPIFESEPKIGHSLLILLVDASLKSLVAENHGWKFEAKQTCGRIKIEAEKTHIDVPMYAIPKDEFQKKQIALEANRSFVKGAIFESYVADSITDDSETYELDSENVNLALREGDRKWINSDPKIVEDWFNDSCIRIGKHLRKVCRFMKAWRDAQWDVGGPSSISLMAATVNILDSVAHDASDLGETMKIIAKHLPSEFARGVESPDSTDEKPLFPPSYKHGPREMDIMSKLERLPEILSSAESADSKSEALKKINMAFGNRVTNSELIVLAKALPAFAQEPSSASKPEKISSTMVSG
Protein: Olfactory receptor (Q920P2)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Receptor-transporting protein 1
- Receptor-transporting protein 2
- G protein-coupled receptor kinase 3
- Guanine nucleotide-binding protein G
Sequence:
MTLSDGNHSGAVFTLLGFSDYPELTIPLFLIFLTIYSITVVGNIGMIVIIRINPKLHIPMYFFLSHLSFVDFCYSSIVAPKMLVNLVTMNRGISFVGCLVQFFFFCTFVVTESFLLGVMAYDRFVAIRNPLLYTVAMSQRLCAMLVLGSYAWGVVCSLILTCSALNLSFYGFNMINHFFCEFSSLLSLSRSDTSVSQLLLFVFATFNEISTLLIILLSYVLIVVTILKMKSASGRRKAFSTCASHLTAITIFHGTILFLYCVPNSKNSRHTVKVASVFYTVVIPMLNPLIYSLRNKDVKDTVKKIIGTKVYSS
Protein: Acyl-CoA wax alcohol acyltransferase 2 (EC 2.3.1.75) (11-cis-specific retinyl-ester synthase) (11-cis-RE-synthase) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diacylglycerol O-acyltransferase 2-like protein 4) (EC 2.3.1.20) (Diacylglycerol O-acyltransferase candidate 4) (hDC4) (Long-chain-alcohol O-fatty-acyltransferase 2) (Multifunctional O-acyltransferase) (Wax synthase) (hWS) (Q6E213)
Organism: Homo sapiens (Human)
Function: Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters. Shows a preference for medium chain acyl-CoAs from C12 to C16 in length and fatty alcohols shorter than C20, as the acyl donors and acceptors, respectively. Also possesses acyl-CoA retinol acyltransferase (ARAT) activity that catalyzes 11-cis-specific retinyl ester synthesis. Shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis-retinol, 13-cis-retinol, and all-trans-retinol substrates.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6E1M8}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Retinol dehydrogenase 5
- Retinoid isomerohydrolase
- Retinol dehydrogenase 11
- Retinol dehydrogenase 10
- Cytochrome P450 26A1
- Retinol dehydrogenase 12
- Alcohol dehydrogenase 1A
- Retinol dehydrogenase 16
- 17-beta-hydroxysteroid dehydrogenase type 6
Sequence:
MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDWKTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHFATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMVIVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGGFVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIVAKYHTLYIDALRKLFDQHKTKFGISETQELEII
Protein: Protein virB9 (P17799)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Is essential for the biogenesis of the T-pilus, which is required for virulence and T-DNA transfer to plant cells. When is associated with virB7, might function as a nucleation center for recruitment of VirB proteins during assembly of the T-DNA transfer machine (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MTKKAFLTLACLLFAAIGARAEDTPTAGRLDPRMRYLAYNPDQVVRLSTAVGATLVVTFGANETVTAVAVSNSKDLAALPRGNYLFFKASKVLPPQPVVVLTASDAGMRRYVFSISSKTLPHLDKEQADLYYSVQFAYPADDAAARQKAAQEKAVADRIRAEAQYQQRAEGLLEQPATTVGAEDKNWHYVAQGDRSLLPLEVFDDGFTTVFHFPGNVRIPSIYTINPDGKEAVANYSVKGSYVEISSVSRGWRLRDGHTVLCIWNTAYDPVGRRPETGTVRPDVKRVLKEVRG
Protein: Poly(A) polymerase PAPalpha (EC 2.7.7.19) (Polynucleotide adenylyltransferase alpha) (O42617)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (By similarity).
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MNTKTYGVTEPISTNGPTPKENILNDALIQELKNRGSFESEQATKKRVEVLTLFQRLVQEFVYTVSKSKNMSDSMAQDAGGKVFTFGSYRLGVYGPGSDIDTLVVVPKHVTRDDFFSVFADIIRKRPELEEIACVPDAYVPIIKLEFDGISIDLIMARLNIPRVPLDLTLDDKNLLKNLDEKDLRSLNGTRVTDEILQLVPKPTVFKHALRCIKLWAQQRAVYGNIFGFPGGVAWAMLVARICQLYPNAVSSAIVEKFFNIYTKWNWPEPVLLKSIEDGPLQVRVWNPRLYPHDRLHRMPVITPAYPSMCATHNITSSTQKVILAELSRGSSIMQEIHAGKKTWSDLFEKHSFFYKYKFYLCVVAASIDSAEEHKKWSGFIESKLRQLVLKLEVAEGVEIAHPYVKDFSNTFILDDKNAEDIINSYGTLSGEDFLRTLHSSDSDKDDEEFKKIRLTKYYIGLDLNLTKSSDGVRKLDIQYPCAEFYSICKGSTSFTEGVNFIQIKNVKLHELSNDVYEDGEERPKKSGKKRKKVIKEDGQKRVRNESPASSASVNGSS
Protein: Uncharacterized HTH-type transcriptional regulator YgfI (P52044)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator YiaU
- Uncharacterized HTH-type transcriptional regulator YbhD
- Putative outer membrane protein YiaT
- Uncharacterized HTH-type transcriptional regulator YcaN
- Uncharacterized HTH-type transcriptional regulator YbeF
- Putative frv operon regulatory protein
Sequence:
MDIFISKKMRNFILLAQTNNIARAAEKIHMTASPFGKSIAALEEQIGYTLFTRKDNNISLNKAGQELYQKLFPVYQRLSAIDNEIHNSGRRSREIVIGIDNTYPTIIFDQLISLGDKYEGVTAQPVEFSENGVIDNLFDRQLDFIISPQHVSARVQELENLTISELPPLRLGFLVSRRYEERQEQELLQELPWLQMRFQNRANFEAMIDANMRPCGINPTIIYRPYSFMAKISAVERGHFLTVIPHFAWRLVNPATLKYFDAPHRPMYMQEYLYSIRNHRYTATMLQHIAEDRDGTSH
Protein: Branched-chain amino acid ABC transporter, ATP-binding protein (Q5LSC0)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, periplasmic substrate-binding protein
- Branched-chain amino acid ABC transporter, permease protein
- ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, permease protein
Sequence:
MTEPILKIRNIESFYGPIMAIRGVSLEVRPGQIVSILGANGAGKTTLMKTISGVMDPEKGTITFDGEEIQGSEPHKVVQKGIVHVPEGREVFPLLTVDENLSLGAYTATDKAQIERDRDLVFTYFPILKERRNQEAGTLSGGQQQMLAIGRGLMANPRIMLLDEPSLGLSPLLVQEIFAILKRLNEEQNMTMMLVEQNASAALALADHGYVMEVGRIVMDGSAQSLMASEDIQNFYLGVQEEGARENRRWKRKKTWR
Protein: Aminomethyltransferase (EC 2.1.2.10) (Glycine cleavage system T protein) (P27248)
Organism: Escherichia coli (strain K12)
Function: The glycine cleavage system catalyzes the degradation of glycine.
Interaction partners:
- Serine hydroxymethyltransferase
- Glycine cleavage system H protein
- Glycine dehydrogenase
- Dihydrolipoyl dehydrogenase
- Bifunctional protein FolD
- 5,10-methylenetetrahydrofolate reductase
- Methionine synthase
- Thymidylate synthase
- Bifunctional purine biosynthesis protein PurH
- Phosphoribosylglycinamide formyltransferase
Sequence:
MAQQTPLYEQHTLCGARMVDFHGWMMPLHYGSQIDEHHAVRTDAGMFDVSHMTIVDLRGSRTREFLRYLLANDVAKLTKSGKALYSGMLNASGGVIDDLIVYYFTEDFFRLVVNSATREKDLSWITQHAEPFGIEITVRDDLSMIAVQGPNAQAKAATLFNDAQRQAVEGMKPFFGVQAGDLFIATTGYTGEAGYEIALPNEKAADFWRALVEAGVKPCGLGARDTLRLEAGMNLYGQEMDETISPLAANMGWTIAWEPADRDFIGREALEVQREHGTEKLVGLVMTEKGVLRNELPVRFTDAQGNQHEGIITSGTFSPTLGYSIALARVPEGIGETAIVQIRNREMPVKVTKPVFVRNGKAVA
Protein: Signal recognition particle subunit SRP68 (Signal recognition particle 68 kDa protein homolog) (P38687)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (By similarity). The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (By similarity). Binds the signal recognition particle RNA (7SL RNA), SRP72 binds to this complex subsequently (By similarity). The SRP complex possibly participates in the elongation arrest function.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O74436}. Nucleus, nucleolus {ECO:0000269|PubMed:11352936}.
Interaction partners:
- Signal recognition particle subunit SRP21
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP14
- Signal recognition particle subunit SRP54
- Signal recognition particle subunit SEC65
- Signal recognition particle receptor subunit beta
- Signal recognition particle receptor subunit alpha homolog
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL38
Sequence:
MVAYSPIIATYGNRAEQFLETDSDFAKYHAKLNKKLQHLRSRCHLVTKDTKKYSSKNKYGEINSEDYDNKTKLIGVLILLHAERDLALAETLKLRARQRGKLKKSEEKVLSTRLKKACKTADKLVNVTQNEQQWITRAQYLAFAKLVHSEYLINGKRFKRKDNAKISNNLALVFAALEHLKNLSLLAEEVVDNIVNKYQYSLKQYAGNLITTPEINNFIVERVQSDENKDDELVKLLLDNGFNMKKITTSTEDQKVTTNINWRSFNAKIIDAEVAQFLEQGLSIHPTQITQYTQRLSKLEKALDRHEFFIANHDDQDDIDEMVENSSENNQIILAYIKYNILLTSISRERDLFTHLWNQWLKLNTSLPSKLTKYKEMERIVKNLTKYLSDIMELPGVYSDDELLSQLDLCKLYFQLFLNTGCLSVLYQSKGRYMEALALYVDAYRRLENKLSEIESLDEILLPANLLSLNSVRSLQKRIENGGNSVITLAEYEKRNHGGSLGKYDLTVIEKLDSKKILPTDIQLKNLFPLKPKMLPIPSKPTLFDLAFNYITYDKQEPSASQVKDSVTETESISQTPISNEQTEGEPKKKRGFLGLFGR
Protein: OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 6 (OTU domain-containing protein 6) (EC 3.4.19.12) (Deubiquitinating enzyme OTU6) (Otubain-like deubiquitinase 1) (Q9XIP2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Binds chromatin (e.g. nucleosomes and histones) and has enzymatic histone deubiquitinase activity, specific for the H2B histone. Can both repress (e.g. OSR2) and promote (e.g. AN3) the expression of target genes by associating with chromatin, deubiquitinating H2B and regulating its euchromatic histone marks (e.g. H3ac and H3K4me). In association with LDL1/KDM1C, involved in transcriptional gene repression via histone deubiquitination and demethylation. Promotes the concerted epigenetic regulation and repression (e.g. the removal of euchromatic histone acetylation, ubiquitination, and methylation marks) of a set of genes (e.g. GA20OX, WUS, OSR2, ARL and ABI5) that collectively limit plant growth thus stimulating plant growth and increasing cell size.
Subcellular location: Nucleus {ECO:0000269|PubMed:21690391}. Cytoplasm {ECO:0000269|PubMed:21690391}.
Interaction partners:
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 4
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 3
- At2g28120/F24D13.9
- Putative OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 8
- Lysine-specific histone demethylase 1 homolog 1
- Ubiquitin carboxyl-terminal hydrolase 26
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 2
- Josephin protein-like protein
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin carboxyl-terminal hydrolase 27
Sequence:
MTRILVQRGSSGSSSNSSRPSSSSSSSSGSETQINNNIPVPPVTIDEEITDEKQEEVTVVEKAECSDAKDVAVDSDEPADREDDEGLVVAENVHVQSEGIDCDSPVSGGSNSDSPPVPAPPPKPSSTVNPGSNRSVLGSFGALRIGPTRRAAGPRSLVSSRSSPTGSHPSSPRSHSENEGYNSSDEHMPCYVPSHPGSGLEREHQFEAEIRYSKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQALAEMYNRPIHIYSYSTEPINIFQGNYSTDTPPIRLSYHHGNHYNSLVDPHRLTVGAGLGFSSLSGRHVDKEQVKAAIKAQQEHQIDNALLAEGRFYSDLELTEKEIERSVMEASRAEYLMEWSKPRIGPKESSTSNAETSSSGARPSGSDSKPAEAVKEKTVLSSSIEMVLSMGFSYAQAMEAYSIFGDDVDSMVCYVLETSCGGNNRRKGKATE
Protein: Sesquiterpene synthase 31 (SlTPS31) (Viridiflorene synthase TPS31) (EC 4.2.3.88) (G5CV46)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Sesquiterpene synthase involved in the production of viridiflorene from (E,E)-farnesyl diphosphate (FPP). Has no activity with (Z,Z)-FPP. Can act with a low efficiency as a monoterpene synthase with geranyl diphosphate as substrate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MAPAAALMSKCQEEEEIVRPVADFSPSLWGDRFHSFSLDNQVAEKYVEEIETLKEQTRSMLMSGKTLAEKLNLIDIVERLGIAYHFEKQIDDMLNHIFNIDPNFEAHEYNDLCTLSLQFRILRQHGYYISPKIFSRFQDANGKFKESLCDDIRGILNLYEASHVRTHGEDTLEEALAFSTAHLESAAPHLKSPLSKQVTHALEQSLHKSIPRVETRYFISIYEEEELKNDVFLRFAKLDFNLLQMLHKQELSEVSRWWKDLDFVTTLPYARDRAVECYFWTMGVYAEPQYSQARVMLAKTIAMISIVDDTFDAYGIVKELEVYTDAIQRWDVSQIDRLPEYMKISYKALLDLYNDYETELSNDGRSDVVQYAKERMKEIVRNYFVEAKWFIEGYMPPVSEYLSNALATSTYYLLTTTSYLGMKSATKKDFEWLAKNPKILEANVTLCRVIDDIATYEVEKGRGQIATGIECYMRDYGVSTQVAMDKFQEMAETAWKDVNEGILRPTPVSAKILTRILNLARIIDVTYKHNQDGYTHPEKVLKPHIIALLVDSIEI
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FLU9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Transcription factor
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Peptidyl-prolyl cis-trans isomerase D
- Hsp90 chaperone protein kinase-targeting subunit
- Candida glabrata strain CBS138 chromosome L complete sequence
- Serine/threonine-protein phosphatase
- Candida glabrata strain CBS138 chromosome E complete sequence
- Heat shock protein homolog SSE1
- Heat shock transcription factor
Sequence:
MSETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDAIDKIRYQALSDPKQLETEPELFIRITPRPEEKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKNNDDEQYIWESNAGGSFTVTLDTVNEKIGRGTILRLFMKEDQLEYLEEKRIKEVVKKHSEFVAYPIQLMVTKEVEKEVPVTEEEKKDEEKKDEDDKKPKLEEVDEDEEKKDEKKTKTVKETVKELEELNKTKPLWTRNPSEITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFKAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEELIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIESFNEIAEDSEQFDKFYSAFAKNIKLGIHEDTQNRAALAKLLRYNSTKSVDELTSLSDYVTRMPEHQKNIYFITGESLKAVQNSPFLDALKAKDFEVLFLVDPIDEYAFTQMKEFEGKQLVDITKDFELEETEEEKAEREKEIKEYEPLTKALKEVLGEQVEKVVVSHKLVDSPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKIFEISPKSPIIKELKKRVDEGGAQDKTVKDLTNLLFETALLTSGFTLEEPSSFASRINRLISLGLNIDEDEEEQAAPEVKAEAEVEEVPADTEMEEVD
Protein: Major inner protein P1 (P11126)
Organism: Pseudomonas phage phi6 (Bacteriophage phi-6)
Function: P1 is the major inner capsid (core) protein of the polyhedral procapsid, which is responsible for genomic replication and transcription. Forms a dodecahedral shell from 60 asymmetric dimers. Binds to RNA and may be involved in genomic packaging.
Subcellular location: Virion. Note=Inner capsid protein (120 copies).
Interaction partners:
Sequence:
MFNLKVKDLNGSARGLTQAFAIGELKNQLSVGALQLPLQFTRTFSASMTSELLWEVGKGNIDPVMYARLFFQYAQAGGALSVDELVNQFTEYHQSTACNPEIWRKLTAYITGSSNRAIKADAVGKVPPTAILEQLRTLAPSEHELFHHITTDFVCHVLSPLGFILPDAAYVYRVGRTATYPNFYALVDCVRASDLRRMLTALSSVDSKMLQATFKAKGALAPALISQHLANAATTAFERSRGNFDANAVVSSVLTILGRLWSPSTPKELDPSARLRNTNGIDQLRSNLALFIAYQDMVKQRGRAEVIFSDEELSSTIIPWFIEAMSEVSPFKLRPINETTSYIGQTSAIDHMGQPSHVVVYEDWQFAKEITAFTPVKLANNSNQRFLDVEPGISDRMSATLAPIGNTFAVSAFVKNRTAVYEAVSQRGTVNSNGAEMTLGFPSVVERDYALDRDPMVAIAALRTGIVDESLEARASNDLKRSMFNYYAAVMHYAVAHNPEVVVSEHQGVAAEQGSLYLVWNVRTELRIPVGYNAIEGGSIRTPEPLEAIAYNKPIQPSEVLQAKVLDLANHTTSIHIWPWHEASTEFAYEDAYSVTIRNKRYTAEVKEFELLGLGQRRERVRILKPTVAHAIIQMWYSWFVEDDRTLAAARRTSRDDAEKLAIDGRRMQNAVTLLRKIEMIGTTGIGASAVHLAQSRIVDQMAGRGLIDDSSDLHVGINRHRIRIWAGLAVLQMMGLLSRSEAEALTKVLGDSNALGMVVATTDIDPSL
Protein: Transcription elongation factor (TFIIS) family protein (Q8VZM2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00649}.
Interaction partners:
- Transcription factor IIS family protein
- Transcription factor IIS family protein
- Transcription factor IIS protein
- Transcription factor IIS family protein
- Transcription elongation factor
- Probable mediator of RNA polymerase II transcription subunit 26c
- Probable mediator of RNA polymerase II transcription subunit 26b
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit
Sequence:
MTLEDFFTLTEIKDGLTVTSRVEELVSVMQSNKDSVLKNSGDAFRQWTAVASTIAATKNRDCLDVFVNLDGLVYLSSWLAEAQMLDNDSVDRSVEESILALLEAVENLGVDSSKLVSSGLWVAVKKLVDHGSSRVQDQARKLFGSWKDKDDYDHSEHDSESCNKIHEDEMRVVAASIESSGQKSAVTLCSMQSTSEKHCPEIADEALLSGCSEGNIPDQDKGLGLQNDKAGFVSNVNSHCSNSMTETFNGSCTDDIMKEVQEKLSVKEKSSMGETSGPTTFGTMPTGSSSLLYLERDSAEGPSNAPLDAEIPKEKQMANYFLEKLGEAGTSSAAGHVAVSSDSIVASMELEKNSLLQSSLDSNEVSKNVSGTICGSHDVSVAHNSKQVSSLTHMTDNQDSDNSSRLSGGLGRSRKFESDNLTGLADNEGKDDMGHSDKKRRVKRRKKRISSRSMTISQRLGAIDKTTTDIDLGILDALEVATKVAQEVAREVDSGEPSHSSSEELSDESGQSGSQYSRDDDVHTGSPSKGLSVTENHSFEEPHVGDDDLMDEKDDKPESGDVEERHLATAAKSEVGREKSPCGFDLNQDICPDETDVIMSSTSTTPAPMSVSFSVSSSAMPAAAPWHLERSLSGKGSAATSVFHSALPHKVPSGDLREKQVISRGIDLNVAEVGDDQVEDLTPWKQFPFSSSNSRGGESSHEASLRGSSKFNLDLNCMNEDDEMPPPSESKMETRLFLSHNGQQSASPVSSSSVAQQSGKEVNFDLNDRPQFFIDSRDQGPYYGRHPWSTASYGGHKLEEPGISILGTKVEADRKDSVPQMASFLSNGKSLEPATGLHMGRTGNSLGLAPGVSFSPAPMYGYNGLTGPPGLSMSSPMYVPGTAIPYMVDSRGTPVMMPQIIGSAPYVQPPFPQQHMFMSLAGGSPSTNGSMRPNFDQNSGFGLEIGNRESLNLRQFLSPSQSGAMGEHSGANVEPSSSSSISIGGKRKEPEPRWEFPPWR
Protein: Cytochrome c (Q9I238)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Cytochrome c domain-containing protein
- Short-chain fatty acid transporter
- DUF7660 domain-containing protein
- Uncharacterized protein
- Probable transcriptional regulator
- Ubiquinol-cytochrome c reductase iron-sulfur subunit
Sequence:
MTLSRLSLAILSVLAGAPAFADDSGVDLDQGWNQTQKTAWLEAGQGSRMLPLAWLVALEQRASEEPLMSDALIRQYGYVPHTLGGSSVKVVQGYAVDRSDDSDLTFTKLRWKALQGSREPWVGPTCSMCHTSHISYQGTQLTVYGGQTMGDLAGFQLEILGALQSTRADTAKFERFARKVLGADGLVSGYNDANKARLQAALDATIVRLRDGSHFNLPHDPEFGPGRLDAIGSIFNSVGYELHADEQIYGAEDAPVSYPFLWNVPQLDRVQWTGFNPNHINVVDIDNRKFDVGALARNAGEAVGVFADVKVLSPIQSALHIGYPSSINVDNLIRIEDQLGQLKPPAWPNQLFGAPEPTRVAEGRELYRQHCSSCHTPLDRNDLRTPVKTVLTHLQARGEVAPIGTDPWTACNSIAQLKTGYVRGKPYLSFVGTGQRGFYGKQAYAVDVLQEVVVQALAARGLSVALGAFQTAALGIFDGQLPPLISPVPDSPDADSAEATAADAPGALLLAENVAADSDKARRLEQCLAMTSDLMAYKARPLNGIWASPPYLHNGSVATLYDLLLPPDLRPRTFYTGSVEFDPVNVGYITDAGGANRFLFDSGKPGNANGGHDYGNAQFNEQQRRALVEYMKTL
Protein: Autophagy-related protein 18 (O16466)
Organism: Caenorhabditis elegans
Function: Component of the autophagy machinery that is recruited to phosphatidylinositols on preautophagosomal structures, which are early autophagic structures, to promote autophagosome formation, and the subsequent degradation and clearance of engulfed apoptotic cells and P-granules in somatic cells. In particular, binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), and more weakly to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Plays a role in mitophagy, which is the autophagic consumption of mitochondria, in response to dietary restriction. Involved in xenophagy, the autophagy-mediated degradation of pathogens and pathogen products, such as toxins. Also plays a role in membrane-pore repair. In a daf-18/PTEN- and daf-16/FOXO-dependent manner, required for the proliferation of germ stem cell progenitors in the gonad during the late phases of larval development. By regulating the release of neurotransmitters and neuropeptides, involved in the control of lifespan in response to dietary restriction and daf-2 signaling. Probably through its involvement in autophagy, required for dauer formation.
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:22451698}; Peripheral membrane protein {ECO:0000305|PubMed:22451698}; Cytoplasmic side {ECO:0000305|PubMed:22451698}. Cytoplasm {ECO:0000269|PubMed:25124690}. Note=Partially localizes to the phagosome membrane of engulfed apoptotic cells. {ECO:0000269|PubMed:22451698}.
Interaction partners:
- Autophagy-related protein 2
- Autophagy-related protein 9
- Autophagic-related protein 16.2
- Autophagic-related protein 16.1
- Autophagy-related protein 5
- Serine/threonine-protein kinase unc-51
- Ubiquitin-like protein atg-12
- Ubiquitin-like modifier-activating enzyme ATG7
- Protein lgg-1
- Beclin homolog
Sequence:
MSATTSEENPDSINYIGFNQDSKVICVGHKDGYMFYKTADILENNTLTYEGENLTHLGLNNCLIIERLFSSALMVVISQKDPRVLHVYHFTSRNIICDHRFNKSVLTVRLNRDRIVVCLEDCIYIYNLKDMKMMHNIMDTPTNKLGVLDLTSNPGNALIAYPGSTDTGSVHLFDAINLSSVSTFNAHEGTIACLKFNQEGNMIATASTKGTVIRVYSVPNGHRLFEFRRGVTRCVNIYSLCFSSDSKYLTSSSNTETVHVFKLEKTEGVDNKPEASTEGGGWFDAINKTFSAYMPSQVLQVGELMTTERSFATAKLPGAARSNQVSLVSHKNQQYVMAATSDGFVYAYRLDPEGGELDLIKQHNIGPKSDTSRASPTSTGSGGAAKSAEASNQSVPNMDDPDDFPPMSHTSG