wanglab/gogpt-training-data huggingface dataset:
Protein: Actin-1 (PfACT1) (EC 3.6.4.-) (Actin I) (P86287)
Organism: Plasmodium falciparum (isolate HB3)
Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm. Polymerizes into shorter and less stable actin filaments compared to ACT2/actin-2; this is thought to facilitate gliding motility and host cell invasion. Has ATPase activity (By similarity). ATP hydrolysis leads to the formation of a stable intermediate ADP-inorganic phosphate (Pi) actin, which is followed by the release of Pi (By similarity). ATP hydrolysis affects filament stability; ADP-bound actin depolymerizes much faster than ATP- or ADP-Pi-bound actin (By similarity). Plays an essential role during the asexual blood stage (By similarity). At the segmented schizont stage, required for apicoplast migration and segregation into individual daughter merozoites (By similarity). Also, required for the separation of daughter merozoites in the final stages of cytokinesis (By similarity). Essential for merozoite invasion of, but not adhesion to or reorientation towards, host erythrocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q4Z1L3}. Nucleus {ECO:0000250|UniProtKB:Q4Z1L3}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8I4X0}. Note=During host erythrocyte invasion, filamentous actin localizes close to the junction between merozoites and the host cell (By similarity). In schizonts, filamentous actin appears to connect apicoplasts (By similarity). Prior to gametocyte activation in the mosquito midgut, localizes to both the cytoplasm and the nucleus (By similarity). Following gametocyte activation, relocalizes completely to the cytoplasm, in an ACT2-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q4Z1L3, ECO:0000250|UniProtKB:Q8I4X0}.
Interaction partners:
Sequence:
MGEEDVQALVVDNGSGNVKAGVAGDDAPRSVFPSIVGRPKNPGIMVGMEEKDAFVGDEAQTKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRERMTQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMRLDLAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIEKSYELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNIVLSGGTTMYEGIGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWITKEEYDESGPSIVHRKCF
Protein: ANK_REP_REGION domain-containing protein (Q22290)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTDSQSTQMGRGRHAKRNKSTASVGSKKNRTQSTASGKFQPSVDGFTTFIVAVSRLGKQGQEFTWHDLRKVYHKETQRQLTAEELNAIFSSKNLTKREIFELPKVKRFMTSMDGSMMCRFRLIADPQEVYDDDLPPLMSTSVETDVITEDTSSDHSQAVSPSSGNPIAISTDCDDKAAGPTSDLSKSDNSPSQRSLAQQSSMTDDEGWVSGKDVRSENSSPVEDKDEVDGSKMEMEDDVFEEDQRIAAESDQVDSAMVADVIIVEEAKVEKLFKAQEIVAPIVLTESIDAAFEAVIQSVSHADATLSMTQNASEEAKVHATPPLPAERKTMVSAELANGKPIKHLIEKFDAGVNFAEHKPKSIYAQVLEEIGGSAPRVDEVFSASKKEEHAETEVTNVIFRSTSTHSSIIANGKEQLAEFVAEQEARQKVTTPNPVKEETENAFCAKEQSSMSSLDREYFASKTKLNEDLFAELGVKDTDGFQLKTVDSNGSGPGSSEIITVIETPLKDDHRKRADSVESDADVPYSLCSEDEAEPMTMIDKSMKVSQSAEQLSPVKEEQKAKTVVVNVELDGNRADPTIKDRIAALQAIVSKQHVPIAKVDSVDDDVRILSRTEELQHMALEAKPSPQALGALRRRHVRFMRGCCVVQ
Protein: Immunoglobulin heavy constant alpha (A0A0A6YXW6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XSARNPTIYPLTLPRALSSDPVIIGCLIHDYFPSGTMNVTWGKSGKDITTVNFPPALASGGGYTMSSQLTLPAVECPEGESVKCSVQHDSNAVQELDVKCSGPPPPCPPCPPSCHPSLSLQRPALEDLLLGSDASLTCTLNGLRNPEGAVFTWEPSTGKDAVQKKAVQNSCGCYSVSSVLPGCAERWNSGASFKCTVTHPESDTLTGTIAKITVNTFPPQVHLLPPPSEELALNELVSLTCLVRAFNPKEVLVRWLHGNEELSPESYLVFEPLKEPGEGATTYLVTSVLRVSAELWKQGDQYSCMVGHEALPMNFTQKTIDRLSERQEPLSYVLLDQSEDILEEEAPGASLWPTTVTFLTLFLLSLFYSTALTVTTVRGPFGSKEVPQY
Protein: Pectate lyase H (EC 4.2.2.2) (Q5ATC7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pectinesterase A
Sequence:
MFIKNGLLLSLATSVLATHGARSHSQAATSKLSKRFTFPIPNSEGSVTLDEVYEIDGETFDGGMKTYGRGVSCTGQDEGGDSDAVFIVKNGGTLKNVIIGSDQIEGVHCEGSCTIENVWWEAVCEDALSLKTGDGPFNVVGGGAQGADDKVIQHNGGGTVSISDFTVYDFGKLYRSCGNCGDQYERHVVIEGVTAVDGKYLVGINSNYGDTATIDSATCATDVKTICAEYKGTDNNDEEPEEVSDGPSDYCIYTEPLSEC
Protein: Plant-specific TFIIB-related protein PTF2 (Protein POLLEN-EXPRESSED TRANSCRIPTION FACTOR 2) (TFIIB-related protein PTF2) (O81787)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant-specific TFIIB-related protein that plays important roles in pollen germination and embryogenesis, possibly by regulating gene expression through interaction with TBP2 and the subunits of RNA polymerases. Binds double-stranded DNA in vitro.
Subcellular location: Nucleus {ECO:0000269|PubMed:23713077}.
Interaction partners:
- TATA-box-binding protein 2
- Plant-specific TFIIB-related protein 1
- DNA-directed RNA polymerase III subunit RPC6
- Homeodomain-like superfamily protein
- Tetratricopeptide repeat
- DNA-directed RNA polymerase III subunit 2
- DNA-directed RNA polymerase III subunit 1
- Plant-specific TFIIB-related protein 2
- Transcription initiation factor IIB-2
- Transcription initiation factor IIB-1
Sequence:
MRCKRCNGSNFERDEDTGNSYCGGCGTLREYDNYEAQLGGIRGPQGTYIRVGTIGRGSVLDYKDKKIYEANNLIEETTERLNLGNKTEVIKSMISKLTDGEFGQGEWFPILIGACCYAVVREEGKGVLSMEEVAYEVGCDLHQLGPMIKRVVDHLDLELREFDLVGLFTKTVTNSPRLTDVDRDKKEKIIKQGTFLMNCALKWFLSTGRRPMPLVVAVLAFVVQVNGVKVKIDDLAKDASVSLTTCKTRYKELSEKLVKVAEEVGLPWAKDVTVKNVLKHSGTLFALMEAKSMKKRKQGTGKELVRTDGFCVEDLVMDCLSKESMYCYDDDARQDTMSRYFDVEGERQLSLCNYDDNISENQLSTKYNEFEDRVCGGTLAKRSQGSSQSMWQRRSVFGMVSTENWWKGKSELSKRLLLKDLLEKDVGLEALPPSYIKGCVAVERRREKIKAAKLRINAIQHPSDNVSEGALSLELEHSKKKRKKGSEIDWEDLVIQTLVLHNVNEEEIEKGHYKTLLDLHVFNSGEV
Protein: Cucurbitadienol synthase (EC 5.4.99.33) (Q6BE24)
Organism: Cucurbita pepo (Vegetable marrow) (Summer squash)
Function: Oxidosqualene cyclase involved in the biosynthesis of the highly oxygenated tetracyclic triterpenes cucurbitacins. Converts oxidosqualene to cucurbitadienol and does not produce lanosterol.
Interaction partners:
Sequence:
MWRLKVGAESVGEEDEKWVKSVSNHLGRQVWEFCADAAADTPHQLLQIQNARNHFHHNRFHRKQSSDLFLAIQYEKEIAKGAKGGAVKVKEGEEVGKEAVKSTLERALGFYSAVQTRDGNWASDLGGPLFLLPGLVIALHVTGVLNSVLSKHHRVEMCRYLYNHQNEDGGWGLHIEGTSTMFGSALNYVALRLLGEDADGGDGGAMTKARAWILERGGATAITSWGKLWLSVLGVYEWSGNNPLPPEFWLLPYSLPFHPGRMWCHCRMVYLPMSYLYGKRFVGPITPKVLSLRQELYTIPYHEIDWNKSRNTCAKEDLYYPHPKMQDILWGSIYHVYEPLFTRWPGKRLREKALQAAMKHIHYEDENSRYICLGPVNKVLNMLCCWVEDPYSDAFKLHLQRVHDYLWVAEDGMRMQGYNGSQLWDTAFSIQAIVATKLVDSYAPTLRKAHDFVKDSQIQEDCPGDPNVWFRHIHKGAWPLSTRDHGWLISDCTAEGLKASLMLSKLPSTMVGEPLEKNRLCDAVNVLLSLQNDNGGFASYELTRSYPWLELINPAETFGDIVIDYPYVECTAATMEALTLFKKLHPGHRTKEIDTAIGKAANFLEKMQRADGSWYGCWGVCFTYAGWFGIKGLVAAGRTYNSCLAIRKACEFLLSKELPGGGWGESYLSCQNKVYTNLEGNKPHLVNTAWVLMALIEAGQGERDPAPLHRAARLLMNSQLENGDFVQQEIMGVFNKNCMITYAAYRNIFPIWALGEYCHRVLTE
Protein: RH04289p (Q8MYW1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MYALSSSLIRSPALRQGLQMAAASRQVSMKVVSVAETQKDESFFEKNERLGRELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEGLQLSGATLTALKFIIAYPAGYHTANGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILALL
Protein: Protein indeterminate-domain 11 (Q9LRW7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- RING-H2 finger protein ATL75
- C2H2 and C2HC zinc fingers superfamily protein
- C2H2-like zinc finger protein
- C2H2-like zinc finger protein
- Vesicle-associated protein 2-1
- Sequence-specific DNA binding transcription factor
- Zinc finger
- FCS-Like Zinc finger 13
- Polyadenylation and cleavage factor homolog 4
- At4g35700
Sequence:
MMNKDMLLHQHQQPQQDENMSNLTSASGDQASVSSGNITEASGSNYFPHHQQQQEQQQQQLVVPDSQTQKKRRNQPGNPDPESEVIALSPKTLMATNRFVCEICNKGFQRDQNLQLHRRGHNLPWKLKQRSNKEVIRKKVYVCPEASCVHHDPSRALGDLTGIKKHFCRKHGEKKWKCDKCSKKYAVQSDCKAHSKTCGTKEYRCDCGTLFSRRDSFITHRAFCEALAEETAREVVIPQNQNNNQPNPLLIHQSASHPHHHHQTQPTINVSSSSSSSHNHNIINSLHFDTNNGNTNNSNNSNNHLHTFPMKKEQQSNDHIMNYHHSIIPPWLAPQPHALTSSNPNPSNGGGGGGSLFSLASPAMSATALLQKAAQMGSTKTPPLPPTTAYERSTHNNNLTTTMAAMMTSPSGFISSNNNNHVLFQDYNASGFDNHGREEAFDDTFGGFLRTNEVTAAAGSEKSTKSGGGEGLTRDFLGLRPLMSHNEILSFAGLGSCINSSASDQLHPKPWQG
Protein: Sal-like protein 1a (Spalt-like transcription factor 1a) (F1QI36)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- G protein-coupled purinergic receptor p2y 12
Sequence:
MSRRKQAKPQHFQSDSQLVLAEHNGDTETNPDDSPCKDSGAHVCSRCCAEFFELSDLEQHQKNCTKNQLVLIVNENPVSPSGTFSPGSSPHNPDEQMNDTTNNTDQAELTDLLEQNILDKEEAMDTEMSGVSAPHNDGNGRMAGSSPLSGVGTGHGTLGSTGSNLGSSVISASLPQLGNLTELGNFSMINSNVIIENLQSTKVAVAQFSQETRATGGQRVAVPALMEQLLALQQQQIHQLQLIEQIRHQILLLASQSPELQAPPSSSPVTLGSGTSPLTTLSSHLSQQLAAAAGLAQSIASQSASISSLKQMANVAQLPQSNSSVGESSQSLAAPGPAPVNAQPLEKRPGNAGSLHPPLGNPSLAKSSTPAFAMGNLLNPVANTLLPQPPPGNPIFSSALPSVGSTVEDLNSLAALAQQRKGKPPNVSSFEPKSSSEDTFFKHKCRFCGKVFGSDSALQIHLRSHTGERPYKCNICGNRFSTRGNLKVHFQRHKEKYPHIQMNPYPVPEHLDNIPTSTGIPYGMSMPPEKPVTSWLDSKPVLSTLTSSVGMLLPPTIPSLPPFIKKEENNSLAISSPSHSAKSDSGPADTPMKNTDSVLEEGESTTLPTSNGKAEENNQSSNLLSNMSSAVEGTIEYTTSNSPPMATNPLMPLMSEQFKAKFPFGGLLDPLQGSETSKLQQLVENIDRKVADPNECVICHRILSCQSALKMHYRTHTGERPFKCKVCGRAFTTKGNLKTHYSVHRAMPPLRVQHSCPICQKKFTNAVVLQQHIRMHMGGQIPNTPLPDNYPESMGSDAGSFDERNIDDLDNFSDDNMEGIEDGPDSSIPDTPKSVDASQDSLCSSPTLHESFGMDERIQEKSANHGAGEEVQYDQGKSVENGLVEGDRFTNDSSSLGGDIESQSAGSPAVSESTSSMQAPSPSNGIFQQQKSPSMEDRQQRALSLEHISASLMHSNSASPGALDLTSVNSSKDPISMLFPFRERGTLKNTACDICGKTFACQSALDIHYRSHTKERPFICTVCNRGFSTKGNLKQHMLTHQMRDLPSQLFEPNTSLASSLASSPTPSLLSVGPLSSMMKTEVNGFLHGLQPEVKDLPPALVTSSASTSPVLSAAPPRRTPKQHFCTTCGKTFSSSSALQIHERTHTGEKPFACTICGRAFTTKGNLKVHMGTHMWNSAPARRGRRLSVDGPMAFLGTNPVKFPELFQKDLSSRAGNGDPTSFWNQYAAAFSNGLAMKTNEISVIQNGGLPPPLSGSVGNGGSSPIGGLTGSMEKLHNSEPNPALAGLEKMANTENGTHFRFTRFMEDKEIVTN
Protein: Eukaryotic translation initiation factor 4E binding protein 2 (Q497A9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Regulatory-associated protein of mTOR
- Serine/threonine-protein kinase mTOR
- Eukaryotic translation initiation factor 4E-binding protein 1
- Similar to eukaryotic translation initiation factor 4E member 3
Sequence:
MSASAGGGHQPSQSRAIPTRTVAISDAAQLPQDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGALMEDSKVEVNNLNNLNNHDRKHAVGDEAQFEMDI
Protein: Autophagy-related protein 13 (O75143)
Organism: Homo sapiens (Human)
Function: Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19211835}. Preautophagosomal structure {ECO:0000269|PubMed:19211835}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation. {ECO:0000269|PubMed:19211835}.
Interaction partners:
- Autophagy-related protein 101
- RB1-inducible coiled-coil protein 1
- Serine/threonine-protein kinase ULK1
- Serine/threonine-protein kinase ULK2
- Beclin 1-associated autophagy-related key regulator
- GABA type A receptor associated protein like 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Beclin-1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Ubiquitin-like-conjugating enzyme ATG10
Sequence:
METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ
Protein: Arylsulfatase K (ASK) (EC 3.1.6.1) (Glucuronate-2-sulfatase) (EC 3.1.6.18) (Q9D2L1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of pseudosubstrates such as p-nitrocatechol sulfate and p-nitrophenyl sulfate (By similarity). Catalyzes the hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate. Acts selectively on 2-sulfoglucuronate and lacks activity against 2-sulfoiduronate (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q6UWY0}. Lysosome {ECO:0000250|UniProtKB:Q6UWY0}.
Interaction partners:
- Arylsulfatase I
- Arylsulfatase J
- Arylsulfatase B
Sequence:
MLLLLVSVVAALALAAPAPRTQKKRMQVNQAPNVVLVASDSFDGRLTFQPGSQVVKLPFINFMRAHGTTFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNFKGLDPNYTTWMDIMEKHGYQTQKFGKVDYTSGHHSISNRVEAWTRDVAFLLRQEGRPIINLIPDKNRRRVMTKDWQNTDKAIEWLRQVNYTKPFVLYLGLNLPHPYPSPSSGENFGSSTFHTSLYWLEKVAYDAIKIPKWLTLSQMHPVDFYSSYTKNCTGKFTENEIKNIRAFYYAMCAETDAMLGEIILALHKLDLLQKTIVIYTSDHGEMAMEHRQFYKMSMYEASVHVPLLMMGPGIKANLQVPSVVSLVDIYPTMLDIAGIALPPNLSGYSLLTLLSNASANEQAFKFHRPPWILSEFHGCNANASTYMLRTGQWKYIAYADGASVQPQLFDLSLDPDELTNIATEFPEITYSLDQKLRSIVNYPKVSASVHQYNKEQFIMWKQSVGQNYSNVIAHLRWHQDWQRDPRKYENAIQHWLTAHSSPLASSPTQSTSGSQPTLPQSTSG
Protein: Calcium/calmodulin-dependent protein kinase type IV (CaMK IV) (EC 2.7.11.17) (CaM kinase-GR) (Calspermin) (P13234)
Organism: Rattus norvegicus (Rat)
Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. In the thymus, regulates the CD4(+)/CD8(+) double positive thymocytes selection threshold during T-cell ontogeny. In CD4 memory T-cells, is required to link T-cell antigen receptor (TCR) signaling to the production of IL2, IFNG and IL4 (through the regulation of CREB and MEF2). Regulates the differentiation and survival phases of osteoclasts and dendritic cells (DCs). Mediates DCs survival by linking TLR4 and the regulation of temporal expression of BCL2. Phosphorylates the transcription activator CREB1 on 'Ser-133' in hippocampal neuron nuclei and contribute to memory consolidation and long term potentiation (LTP) in the hippocampus. Can activate the MAP kinases MAPK1/ERK2, MAPK8/JNK1 and MAPK14/p38 and stimulate transcription through the phosphorylation of ELK1 and ATF2. Can also phosphorylate in vitro CREBBP, PRM2, MEF2A and STMN1/OP18 (By similarity).
Subcellular location: Cytoplasm. Nucleus. Note=Localized in hippocampal neuron nuclei. In spermatids, associated with chromatin and nuclear matrix. {ECO:0000250}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Cyclic AMP-responsive element-binding protein 1
- Histone lysine acetyltransferase CREBBP
- Calcium/calmodulin-dependent protein kinase kinase 2
- Calcium/calmodulin-dependent protein kinase kinase 1
- Histone deacetylase 4
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Histone deacetylase
Sequence:
MLKVTVPSCPSSPCSSVTSSTENLVPDYWIDGSKRDPLSDFFEVESELGRGATSIVYRCKQKGTQKPYALKVLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVEHQVLMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGIITYILLCGFEPFYDERGDQFMFRRILNCEYYFISPWWDEVSLNAKDLVKKLIVLDPKKRLTTFQALQHPWVTGKAANFVHMDTAQKKLQEFNARRKLKAAVKAVVASSRLGSASSSHTNIQESNKASSEAQPAQDGKDKTDPLENKMQAGDHEAAKAAADETMKLQSEEVEEEEGVKEEEEEEEEEEETSRMVPQEPEDRLETDDQEMKRNSEETLKSVEEEMDPKAEEEAAAVGLGVPPQQDAILPEY
Protein: Archaeal flagellar ATPase motor FlaI (EC 3.6.4.-) (Q4J9L0)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Subcellular location: Archaeal flagellum {ECO:0000269|PubMed:23129770, ECO:0000269|PubMed:24103130}. Cell membrane {ECO:0000269|PubMed:21506936, ECO:0000269|PubMed:23416110}; Peripheral membrane protein {ECO:0000269|PubMed:21506936, ECO:0000269|PubMed:23416110}; Cytoplasmic side {ECO:0000269|PubMed:21506936, ECO:0000269|PubMed:23416110}. Note=Localizes to the membrane via a three-helix bundle domain (amino acids 61-127) present in the N-terminal region of FlaI. {ECO:0000269|PubMed:23416110}.
Interaction partners:
- Archaeal flagellar ATP-binding protein FlaH
- Flagella-related protein J
- Flagellar protein FlaG
- Archaeal flagellar motor scaffold protein FlaX
- Conserved flagellar protein F
- Flagellin
Sequence:
MSFVEDYLTKLQERPTIIENPNILKGSKIFNAIYRVDDFVYIHIQSIKSEDGYNQYNVIEPPRPTHDEMEEIEEKFALSIGDKEPPEDTKEKEKLIRSILDKILLRMRLSVPKEYVIYHFIRDKLYTGSLEPLIRDPYIEDISIPGLGHVYIVHKVFGPMRTSIKFENYEELDNLIVSLSEKSYRPVSHNRPVVDASLPDGSRVNFVYGVDISRRGSNLTVRKFSRVPTSITQLIMFGTLSSMMAAYIWTMLDEGMNLFVCGETASGKTTTLNAITAFIPPNLKIVTIEDTPELTVPHSNWVAEVTRETGGEGTIKLFDLLKAALRQRPNYILVGEIRDKEGNVAFQAMQTGHSVMATFHAANITTLIQRLTGYPIEVPKSYINNLNIALFQTALYDKKGNLIRRVVEVDEIIDIDPVTNDVVYIPAFTYDSVQDKMLFAGKGSSYLIENKIAVKRGIDRRNIGLLYDELQMRSRFLNLLVEKKIFNYYDVWDYILRARQMGLEEAIKYVSNI
Protein: ATP-dependent 6-phosphofructokinase isozyme 1 (ATP-PFK 1) (Phosphofructokinase 1) (EC 2.7.1.11) (6-phosphofructokinase isozyme I) (Phosphohexokinase 1) (Sedoheptulose-7-phosphate kinase) (P0A796)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. In addition, is involved in the utilization of D-sedoheptulose 7-phosphate, an intermediate of the pentose phosphate pathway, via the sedoheptulose bisphospate bypass pathway. Catalyzes the phosphorylation of D-sedoheptulose 7-phosphate to D-sedoheptulose 1,7-bisphosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000305|PubMed:17895580}.
Interaction partners:
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase isozyme 2
- Fructose-bisphosphate aldolase class 2
- Enolase
- Triosephosphate isomerase
- Fructose-1,6-bisphosphatase class 1
- Pyruvate kinase I
- Pyruvate kinase II
- Transaldolase B
- Fructose-bisphosphate aldolase class 1
Sequence:
MIKKIGVLTSGGDAPGMNAAIRGVVRSALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFVVVPEVEFSREDLVNEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIDLLLAGYGGRCVGIQNEQLVHHDIIDAIENMKRPFKGDWLDCAKKLY
Protein: Beta-1,6-galactosyltransferase GALT29A (EC 2.4.1.-) (GT29 family galactosyltransferase 1) (AtGALT29A) (Sialyltransferase-like protein GT29A) (Q9SGD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Galactosyltransferase involved in the biosynthesis of type II arabinogalactan. Possesses galactosyltransferase (GalT) activity in vitro, transferring galactose from UDP-galactose to a mixture of various oligosaccharides derived from arabinogalactan proteins. Forms a complex with GALT31A that can work cooperatively to enhance the activities of adding galactose residues at O6 positions to beta-1,6-galactan and beta-1,3-galactan.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:24693939}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,6-galactosyltransferase GALT31A
- Beta-glucuronosyltransferase GlcAT14A
- Hydroxyproline O-galactosyltransferase GALT2
- Fucosyltransferase 6
- Probable fucosyltransferase 4
- Beta-arabinofuranosyltransferase RAY1
- Beta-glucuronosyltransferase GlcAT14C
- Beta-glucuronosyltransferase GlcAT14B
- Probable xyloglucan galactosyltransferase GT14
- Sialyltransferase-like protein 2
Sequence:
MKRSVRPLFSALLFAFFAATLICRVAIRRSSFSFASAIAELGSSGLMTEDIVFNETLLEFAAIDPGEPNFKQEVDLISDYDHTRRSHRRHFSSMSIRPSEQQRRVSRDIASSSKFPVTLRSSQAYRYWSEFKRNLRLWARRRAYEPNIMLDLIRLVKNPIDVHNGVVSISSERYLSCAVVGNSGTLLNSQYGDLIDKHEIVIRLNNAKTERFEKKVGSKTNISFINSNILHQCGRRESCYCHPYGETVPIVMYICQPIHVLDYTLCKPSHRAPLLITDPRFDVMCARIVKYYSVKKFLEEKKAKGFVDWSKDHEGSLFHYSSGMQAVMLAVGICEKVSVFGFGKLNSTKHHYHTNQKAELKLHDYEAEYRLYRDLENSPRAIPFLPKEFKIPLVQVYH
Protein: T. brucei spp.-specific protein (Q388A5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGGGACKMERHDVQPRVSSSRVSDCSTPRQQGVTSDSSETVKKEEEQQQQPILIPRQPLGPGATTPPRPMGVVKIGDPLDIRSGVGSPQCDVTLTTNNTWNHSTSAFTTRLPHFVNTEGFDASTGVRWTDNDTAPNRPRSRRTSILVEKESAAYHNGYPATYDGDRHQRSYSRGGSWYKNAENSVFLRSTDMPSFAGNSARYPGDENRNKSFASAANSSYFFGASCSRRSVARSGTCVVNLAESTKTLRGAMATLRKHVQQGAKPLSLRSSYRDVGGSMGCSYNDDVPRSRLPSIFTANNAITPAPDGSMYGEYNAFNRDYDAPGVLGGGRGAMFPNVPINGGFKKSSVPAPHVGSLLELVDTSTVSVFAADSRAESTDDANKQQLRRVANNVGCSPVVKVASPPRQAQRNCRVVVREDLDGVEWHTKNVEFPVVGSDEGNKSREVSTTFALPGSICTFGATTDVSEDSGPRGWVGVGGDFGVSSSDWYARQRSKLMSDESDVNSKDGAGEVDSSGDAAEEM
Protein: General transcriptional corepressor CYC8 (Glucose repression mediator protein CYC8) (P14922)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.
Subcellular location: Nucleus.
Interaction partners:
- General transcriptional corepressor TUP1
- Regulatory protein MIG1
- CRE-binding bZIP protein SKO1
- Glucose transport transcription regulator RGT1
- Histone deacetylase complex subunit CTI6
- DNA damage response protein kinase DUN1
- Large ribosomal subunit protein uL3
- Transcriptional regulator NRG1
- RFX-like DNA-binding protein RFX1
- Carbon catabolite-derepressing protein kinase
Sequence:
MNPGGEQTIMEQPAQQQQQQQQQQQQQQQQAAVPQQPLDPLTQSTAETWLSIASLAETLGDGDRAAMAYDATLQFNPSSAKALTSLAHLYRSRDMFQRAAELYERALLVNPELSDVWATLGHCYLMLDDLQRAYNAYQQALYHLSNPNVPKLWHGIGILYDRYGSLDYAEEAFAKVLELDPHFEKANEIYFRLGIIYKHQGKWSQALECFRYILPQPPAPLQEWDIWFQLGSVLESMGEWQGAKEAYEHVLAQNQHHAKVLQQLGCLYGMSNVQFYDPQKALDYLLKSLEADPSDATTWYHLGRVHMIRTDYTAAYDAFQQAVNRDSRNPIFWCSIGVLYYQISQYRDALDAYTRAIRLNPYISEVWYDLGTLYETCNNQLSDALDAYKQAARLDVNNVHIRERLEALTKQLENPGNINKSNGAPTNASPAPPPVILQPTLQPNDQGNPLNTRISAQSANATASMVQQQHPAQQTPINSSATMYSNGASPQLQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAHAQAQAQAQAQAQAQAQAQAQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQPLPRQQLQQKGVSVQMLNPQQGQPYITQPTVIQAHQLQPFSTQAMEHPQSSQLPPQQQQLQSVQHPQQLQGQPQAQAPQPLIQHNVEQNVLPQKRYMEGAIHTLVDAAVSSSTHTENNTKSPRQPTHAIPTQAPATGITNAEPQVKKQKLNSPNSNINKLVNTATSIEENAKSEVSNQSPAVVESNTNNTSQEEKPVKANSIPSVIGAQEPPQEASPAEEATKAASVSPSTKPLNTEPESSSVQPTVSSESSTTKANDQSTAETIELSTATVPAEASPVEDEVRQHSKEENGTTEASAPSTEEAEPAASRDAEKQQDETAATTITVIKPTLETMETVKEEAKMREEEQTSQEKSPQENTLPRENVVRQVEEDENYDD
Protein: Toxin FitB (Ribonuclease FitB) (RNase FitB) (EC 3.1.-.-) (Trafficking protein B) (Q5F882)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. FitAB binds to its own promoter better than FitA alone. The expected nuclease activity was not observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.
Interaction partners:
- Antitoxin FitA
Sequence:
MILLDTNVISEPLRPQPNERVVAWLDSLILEDVYLSAITVAELRLGVALLLNGKKKNVLHERLEQSILPLFAGRILPFDEPVAAIYAQIRSYAKTHGKEIAAADGYIAATAKQHSLTVATRDTGSFFAADVAVFNPWHD