wanglab/gogpt-training-data huggingface dataset:
Protein: CBL-interacting serine/threonine-protein kinase 25 (EC 2.7.11.1) (SNF1-related kinase 3.25) (SOS2-like protein kinase PKS25) (Q8W1D5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Interaction partners:
- Calcineurin B-like protein 1
- Calcineurin B-like protein 9
- Calcineurin B-like protein 4
- SNF1-related protein kinase regulatory subunit gamma-1-like
Sequence:
MGSKLKLYPLLNHSSVFHPDSRYQSAPTMEEEQQQLRVLFAKYEMGRLLGKGTFGKVYYGKEITTGESVAIKIINKDQVKREGMMEQIKREISIMRLVRHPNIVELKEVMATKTKIFFIMEYVKGGELFSKIVKGKLKEDSARKYFQQLISAVDFCHSRGVSHRDLKPENLLVDENGDLKVSDFGLSALPEQILQDGLLHTQCGTPAYVAPEVLRKKGYDGAKGDIWSCGIILYVLLAGFLPFQDENLMKMYRKIFKSEFEYPPWFSPESKRLISKLLVVDPNKRISIPAIMRTPWFRKNINSPIEFKIDELEIQNVEDETPTTTATTATTTTTPVSPKFFNAFEFISSMSSGFDLSSLFESKRKLRSMFTSRWSASEIMGKLEGIGKEMNMKVKRTKDFKVKLFGKTEGRKGQIAVTAEVFEVAPEVAVVELCKSAGDTLEYNRLYEEHVRPALEEIVWSWHGDNHNNNIVKSNGNYVSDENSGSDC
Protein: Protein DUF642 L-GALACTONO-1,4-LACTONE-RESPONSIVE GENE 1 (DUF642 L-GalL-RESPONSIVE GENE 1) (Q9SSB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000303|PubMed:22323769}.
Interaction partners:
- TIP41-like protein
- Eukaryotic aspartyl protease family protein
- Putative glutamine amidotransferase GAT1_2.1
- Protein PELOTA 1
- Leucine-rich repeat
- Structural maintenance of chromosomes protein
- E3 ubiquitin-protein ligase ATL15
- Protein DETOXIFICATION 25
- At1g73120
- Endoglucanase 5
Sequence:
MMYQEAALLLALLFISSNVVLSAPVRDGLLPNGNFELGPKPSQMKGSVVKERTAVPNWNIIGFVEFIKSGQKQDDMVLVVPQGSSAVRLGNEASISQKISVLPGRLYSITFSAARTCAQDERLNISVTHESGVIPIQTMYGSDGWDSYSWAFKAGGPEIEIRFHNPGVEEHPACGPLIDAVAIKALFPPRFSGYNLIKNGNFEEGPYVFPTAKWGVLIPPFIEDDNSPLPGWMIESLKAVKYVDKAHFAVPEGHRAIELVGGKESAISQIVRTSLNKFYALTFNVGDARDGCEGPMIVEAFAGQGKVMVDYASKGKGGFRRGRLVFKAVSARTRVTFLSTFYHMKSDHSGSLCGPVIDDVRLVAVGKLRG
Protein: Beta-defensin 108B (Beta-defensin 8) (BD-8) (DEFB-8) (hBD-8) (Defensin, beta 108) (Defensin, beta 108B) (Q8NET1)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity.
Subcellular location: Secreted.
Interaction partners:
- Beta-defensin 106
- Beta-defensin 105
- Beta-defensin 107
- Beta-defensin 104
- Beta-defensin 103
- Beta-defensin 1
- Beta-defensin 121
- Beta-defensin 123
- Defensin beta 4A
- Beta-defensin 116
Sequence:
MRIAVLLFAIFFFMSQVLPARGKFKEICERPNGSCRDFCLETEIHVGRCLNSQPCCLPLGHQPRIESTTPKKD
Protein: Geranylgeranyl pyrophosphate synthase paxG (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Paxilline synthesis protein G) (Q9C446)
Organism: Penicillium paxilli
Function: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of paxilline, a mycotoxin that acts as an inhibitor of mammalian maxi-K channels. PaxG, the geranylgeranyl diphosphate (GGPP) synthase is proposed to catalyze the first step in paxilline biosynthesis. Condensation of indole-3-glycerol phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by epoxidation and cyclization of this intermediate (by paxM and paxB) to form paspaline. Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the latter being then converted to paxilline by paxQ. Finally paxilline can be mono- and di-prenylated by paxD.
Subcellular location: Peroxisome {ECO:0000269|PubMed:19529962}.
Interaction partners:
Sequence:
MSYILAEALNFVRRGISHLNYWGASHSLSADNYWESNFQGFPRLLSDSSKAPSTIRTVQVLEDDVDDIAIQYNKIVRGPLDYLLAIPGKDIRSKLIDSFNIWLQLPEEKLSIVKDIINLLHTASLLIDDIQDASRLRRGKPVAHDVYGVAQTINSANYAYYLQQARLKEIGDPRAFEIFTRSLLDLHLGQGMDLYWRDMVVCPTEEEYTRMVMYKTGGLFNLALDLMRIQSRKNTDFSKLVELLGVIFQIRDDYMNLQSGLYAEKKGLMEDLTEGKFSYPIIHSIRASPESSELLDILKQRTEDEAVKIRAVKIMESTGSFQYTRETLSRLSAEARGYVKKLETSLGPNPGIHKILDLLEVEYPTNEKGRV
Protein: Probable aminoglycoside efflux pump (Acriflavine resistance protein D) (P24177)
Organism: Escherichia coli (strain K12)
Function: Participates in the efflux of aminoglycosides. Confers resistance to a variety of these substances.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Multidrug efflux pump subunit AcrA
- Multidrug resistance protein MdtA
- Outer membrane protein TolC
- Cation efflux system protein CusC
- Multidrug resistance protein MdtE
- Macrolide export protein MacA
- Multidrug resistance protein MdtB
- Multidrug resistance protein MdtC
- Multidrug export protein AcrE
- Probable multidrug resistance protein EmrK
Sequence:
MANFFIDRPIFAWVLAILLCLTGTLAIFSLPVEQYPDLAPPNVRVTANYPGASAQTLENTVTQVIEQNMTGLDNLMYMSSQSSGTGQASVTLSFKAGTDPDEAVQQVQNQLQSAMRKLPQAVQNQGVTVRKTGDTNILTIAFVSTDGSMDKQDIADYVASNIQDPLSRVNGVGDIDAYGSQYSMRIWLDPAKLNSFQMTAKDVTDAIESQNAQIAVGQLGGTPSVDKQALNATINAQSLLQTPEQFRDITLRVNQDGSEVRLGDVATVEMGAEKYDYLSRFNGKPASGLGVKLASGANEMATAELVLNRLDELAQYFPHGLEYKVAYETTSFVKASIEDVVKTLLEAIALVFLVMYLFLQNFRATLIPTIAVPVVLMGTFSVLYAFGYSVNTLTMFAMVLAIGLLVDDAIVVVENVERIMSEEGLTPREATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGTTGAIYRQFSITIVAAMVLSVLVAMILTPALCATLLKPLKKGEHHGQKGFFAWFNQMFNRNAERYEKGVAKILHRSLRWIVIYVLLLGGMVFLFLRLPTSFLPLEDRGMFTTSVQLPSGSTQQQTLKVVEQIEKYYFTHEKDNIMSVFATVGSGPGGNGQNVARMFIRLKDWSERDSKTGTSFAIIERATKAFNQIKEARVIASSPPAISGLGSSAGFDMELQDHAGAGHDALMAARNQLLALAAENPELTRVRHNGLDDSPQLQIDIDQRKAQALGVAIDDINDTLQTAWGSSYVNDFMDRGRVKKVYVQAAAPYRMLPDDINLWYVRNKDGGMVPFSAFATSRWETGSPRLERYNGYSAVEIVGEAAPGVSTGTAMDIMESLVKQLPNGFGLEWTAMSYQERLSGAQAPALYAISLLVVFLCLAALYESWSVPFSVMLVVPLGVIGALLATWMRGLENDVYFQVGLLTVIGLSAKNAILIVEFANEMNQKGHDLFEATLHACRQRLRPILMTSLAFIFGVLPMATSTGAGSGGQHAVGTGVMGGMISATILAIYFVPLFFVLVRRRFPLKPRPE
Protein: F-actin-capping protein subunit alpha-2 (CapZ alpha-2) (P47754)
Organism: Mus musculus (Mouse)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Interaction partners:
- F-actin-capping protein subunit beta
- Protein S100-B
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit alpha-3
- Capping protein, Arp2/3 and myosin-I linker protein 2
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Myotrophin
- Dynactin subunit 2
- Beta-centractin
- Cell division control protein 42 homolog
Sequence:
MADLEEQLSDEEKVRIAAKFIIHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNLDQFTPVKIEGYEDQVLITEHGDLGNGKFLDPKNRICFKFDHLRKEATDPRPYEAENAIESWRTSVETALRAYVKEHYPNGVCTVYGKKVDGQQTIIACIESHQFQAKNFWNGRWRSEWKFTVTPSTTQVVGILKIQVHYYEDGNVQLVSHKDIQDSLTVSNEVQTAKEFIKIVEAAENEYQTAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA
Protein: Prion-like-(Q/N-rich)-domain-bearing protein (O18118)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein T25E4.1
- Uncharacterized protein D2096.6
- MYOsin heavy chain structural genes
- Uncharacterized protein
- Neuronal Membrane GlycoProtein
- TLC domain-containing protein
Sequence:
MRCVIILFAVALAVAQASSIRETRQASCGCAQSVQPTCSCQQASQQYSCSCQPSTPCSCASSQQYQLQTSQCMPACQQSCSQQCQSNTNTQCQPTCQQSCQTSSCNPMTSTPIPASQSCLPECENRCMQQCTQQQTAQQCQPICQQQCQQECGSTGNMMYNNQDPYNQMQYGGYNQQGNQYQNQNQYQNPNQIQNQYNQNQYQNQNYYNPYQQTQCQQQCAPQCSQQTSTNCQQCQNSCQNSNTQTITIYVQASPQTSQCVPQCQQQCQQQCQTRTTASQQCAPACSTSCNQSCNQPAQMACQPMQNSQCGCQQNYSPCGNVSGQCCLKK
Protein: Pentatricopeptide repeat-containing protein At5g02830, chloroplastic (Q8GYL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MRDFVIVFGSSSAITNPHHHHRRCYATAPESNRKTKSNSSFTKLLPSLPQQHSPSPASVSATHSLSSHFSNVVRWIPDGSLEYYADFASKLAEDGRIEDVALIAETLAAESGANVARFASMVDYDLLSKGISSNLRQGKIESVVYTLKRIEKVGIAPLDLVDDSSVKLMRKQFRAMANSVQVEKAIDLMEILAGLGFKIKELVDPFDVVKSCVEISNPQLAIRYACLLPHTELLLCRIIHGFGKKGDMVSVMTAYEACKQILDTPNMYICRTMIDVCGLCGDYVKSRYIYEDLLKENIKPNIYVINSLMNVNSHDLGYTLKVYKNMQILDVTADMTSYNILLKTCCLAGRVDLAQDIYKEAKRMESSGLLKLDAFTYCTIIKVFADAKMWKWALKVKDDMKSVGVTPNTHTWSSLISACANAGLVEQANHLFEEMLASGCEPNSQCFNILLHACVEACQYDRAFRLFQSWKGSSVNESLYADDIVSKGRTSSPNILKNNGPGSLVNRNSNSPYIQASKRFCFKPTTATYNILLKACGTDYYRGKELMDEMKSLGLSPNQITWSTLIDMCGGSGDVEGAVRILRTMHSAGTRPDVVAYTTAIKICAENKCLKLAFSLFEEMRRYQIKPNWVTYNTLLKARSKYGSLLEVRQCLAIYQDMRNAGYKPNDHFLKELIEEWCEGVIQENGQSQDKISDQEGDNAGRPVSLLIEKVATHMQERTAGNLAIDLQGLTKIEARLVVLAVLRMIKEDYMRGDVVIDDVLIIIGTDEANTVSGKQEITVQEALVKLLRDELSLVVLPAGQRNIIQDAHCVDDADQENTKSFVSISSTRRPAILERLMVTKASLYQWLQRRK
Protein: Type 4 fimbrial biogenesis protein PilX (Q9HVM9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Type 4 fimbrial biogenesis protein PilW
- Type 4 fimbrial biogenesis protein PilV
- Type IV pilus biogenesis factor PilY1
- Type II secretion system protein H
- Type IV pilus non-core minor pilin PilE
- Type 4 fimbrial biogenesis protein PilY2
- Type II secretion system protein H
- Fimbrial assembly protein PilQ
- Type IV pilus inner membrane component PilO
- Type IV pilus retractation ATPase PilT
Sequence:
MNNFPAQQRGATLVIALAILVIVTLLAVSSMREVVLESRITGNVIEQTRLQNAAESGLREGERRFVNTLRPPEPGTGCTADNVARPCLLDLAALNLKLADTHQNPVGVLKGIANTWMSYRGSDISSATTAGTLYSVQWNNLPIPSGGQVNEAESPEYGNLMRGIGTFYYETNSVARNQTNSETVLQTVLARLYTN
Protein: Nicotinamide N-methyltransferase (D4A605)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Aldehyde oxidase 4
- Aldehyde oxidase 2
- Aldehyde oxidase 3
- Aldehyde oxidase 1
- Nicotinamide phosphoribosyltransferase
- NAD-dependent protein deacetylase sirtuin-1
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- NAD-dependent protein deacetylase
- Sirtuin 6 6
Sequence:
MESGFTSKDTYLSHFNPRDYLEKYYSFGSRHCAENEILRHLLKNLFKIFCLDGVKGELLIDIGSGPTIYQLLSACESFTEIIVTDYTDQNLWELQKWLKKEPGAFDWSPVVTYVCDLEGNRTKGPEKEEKLRRAIKQVLKCDVSQSQPLGGVSLPPADCLLSTLCLDAACPDLPAYRTALRNLGSLLKPGGFLVMVDALKSSYYMIGEQKFSSLSLDREAVRDAVEEAGYTIEQFEVISQSYSSTTSNNEGLFSLVGRKPVGSE
Protein: 11-beta-hydroxysteroid dehydrogenase type 2 (11-DH2) (11-beta-HSD2) (EC 1.1.1.-) (11-beta-hydroxysteroid dehydrogenase type II) (11-HSD type II) (11-beta-HSD type II) (Corticosteroid 11-beta-dehydrogenase isozyme 2) (NAD-dependent 11-beta-hydroxysteroid dehydrogenase) (Short chain dehydrogenase/reductase family 9C member 3) (P80365)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids. Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (By similarity). Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen. Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone. Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro. 7-beta-25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration. May protect ovulating oocytes and fertilizing spermatozoa from the adverse effects of cortisol (By similarity).
Subcellular location: Microsome {ECO:0000269|PubMed:17314322}. Endoplasmic reticulum {ECO:0000269|PubMed:10497248, ECO:0000269|PubMed:17314322}.
Interaction partners:
- Cytochrome P450 11B1, mitochondrial
- Cytochrome P450 11B2, mitochondrial
- Steroid 21-hydroxylase
- Aldo-keto reductase family 1 member D1
- 11-beta-hydroxysteroid dehydrogenase 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Hydroxysteroid 11-beta-dehydrogenase 1-like protein
- Mineralocorticoid receptor
- GDH/6PGL endoplasmic bifunctional protein
Sequence:
MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALAVLAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDSMGFTVLATVLELNSPGAIELRTCCSPRLRLLQMDLTKPGDISRVLEFTKAHTTSTGLWGLVNNAGHNEVVADAELSPVATFRSCMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPCLGAYGTSKAAVALLMDTFSCELLPWGVKVSIIQPGCFKTESVRNVGQWEKRKQLLLANLPQELLQAYGKDYIEHLHGQFLHSLRLAMSDLTPVVDAITDALLAARPRRRYYPGQGLGLMYFIHYYLPEGLRRRFLQAFFISHCLPRALQPGQPGTTPPQDAAQDPNLSPGPSPAVAR
Protein: Envelope small membrane protein (E protein) (sM protein) (Q84706)
Organism: Porcine epidemic diarrhea virus (strain CV777) (PEDV)
Function: Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Counteracts the production of type I interferon by interacting with host IRF3 component and preventing its translocation to the host nucleus.
Subcellular location: Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04205}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04205}. Host endoplasmic reticulum {ECO:0000269|PubMed:33486326}. Note=The cytoplasmic tail functions as a Golgi complex-targeting signal. {ECO:0000255|HAMAP-Rule:MF_04205}.
Interaction partners:
Sequence:
MLQLVNDNGLVVNVILWLFVLFFLLIISITFVQLVNLCFTCHRLCNSAVYTPIGRLYRVYKSYMRIDPLPSTVIDV
Protein: Vitrin (Akhirin) (Q8VHI5)
Organism: Mus musculus (Mouse)
Function: Promotes matrix assembly and cell adhesiveness. Plays a role in spinal cord formation by regulating the proliferation and differentiation of neural stem cells.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}.
Interaction partners:
- Ubiquitin-like protein FUBI
Sequence:
MGIVVPTMKASVIEVLLVLLVTGIHSNKETPKKTKRPKLTVPQINCDVKAGKIINPEFMVKCPAGCQDPKYHVYGTGVYASYSSVCGAAIHSGVLDNSGGKILVRKVAGQSGYKGSYSNGVQSLSLPRWRESFIVAESKPQKGVAYPSTLTYSSSKTAAAKAGETTKAYEKPSIPGTTIQPVTLTQAQATPVAEVTHRSTSKPFAASVTNSPRPQPVGHRSQEMEEVDGWKPGPVLLDSGFVPKEELSTQSSEPVPQGDPNCKIDLSFLIDGSTSIGKRRFRIQKQFLADVVQALDIGPAGPLVGVVQYGDNPATQFNLKTHMNSQDLKTAIEKITQRGGLSNVGRAISFVTKTFFSKANGNRGGAPNVAVVMVDGWPTDKVEEVSRVARESGINVFFITVEGAAERDIQHVVEPGFASKAVCRTNGFYSFNVQSWLSLHKTVQPLVKRVCDTDRLACSKTCLNSADIGFVIDGSSSMGTSNFRTVLQFVANLSKEFEISDTDTRVGAVQYTYEQRLEFGFDKYNSKADILSAIRRVGYWSGGTSTGAAIQYALEQLFKKSKPNKRKVMIIITDGRSYDDVRIPAMAAYQKGVITYAIGIAWAAQDELEVMATHPAKDHSFFVDDFDNLYKIAPRIIQNICTEFNSQPRN
Protein: Variant surface glycoprotein (VSG)-related, putative (B2ZWB3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MKVWKTVRFIVGAVLVMADASNAEGSLANEREFATLCGFVSLTHQIRESLYKVREKSEVDVILLQKKVADILFGTGISDVGSMKWKQYRQQDCGQDSGGRTFPGGETLVKDLICLCDGTDLQPRRDALCYAENTEQSRYTGWKNTLNHEKTWSRLQGKCEADHREGTPTRAEFEKKKEQLRSGIKGRKDKEGTYYTYGGNAKNGLQICNGIATTEADGICVLYKRGSDGDNTSGIEWLNKLEELVKIVEGMDQSTNSDAKTVVETETKEKPKENPKENPPSGRRDESTQGGSRYTPTATSTEANVSPARPAGEQKSYSQVISIPLRVLFSLIL
Protein: Cytochrome f (Q6ENG0)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00610}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00610}.
Interaction partners:
- Cytochrome b6-f complex subunit 4
- Cytochrome b6
- Cytochrome b6-f complex subunit 5
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- Photosystem II CP47 reaction center protein
- Uncharacterized protein
- Photosystem I reaction center subunit II
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Uncharacterized protein
Sequence:
MENRNTFSWVKEQMTRSISVSIMIYVITRTSISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVLRIPYDMQLKQVLANGKKGGLNVGAVLILPEGFELAPPDRISPELKEKIGNLSFQSYRPNKKNILVIGPVPGKKYSEIVFPILSPDPAMKKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATSTGVVRKILRKEKGGYEISIVDASDGRQVIDLIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFFASVILAQVFLVLKKKQFEKVQLYEMNF
Protein: Nuclear transcription factor Y subunit nfyc-1 (CAAT box DNA-binding protein subunit nfyc-1) (O17072)
Organism: Caenorhabditis elegans
Function: Component of sequence-specific heterotrimeric transcription factor (nfya-1-NF-Y and nfya-2-NF-Y) complexes which specifically recognize a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types. In association with the components in the NF-Y complexes, represses the expression of the T-box transcription factor tbx-2 throughout larval development, which most likely restricts its expression to certain tissues. May act to repress txb-2 expression in conjunction with tbx-2 itself, which has an autoregulatory role (Probable). In association with the components in the nfya-1-NF-Y complex, negatively regulates the expression of the homeobox protein egl-5 to spatially restrict its expression in tissues such as the head. May regulate egl-5 expression in association with the mes-2-mes-3-mes-6 complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:17574230}. Cytoplasm {ECO:0000269|PubMed:15704008, ECO:0000269|PubMed:17574230}. Perikaryon {ECO:0000269|PubMed:15704008}. Note=Localizes to the cytoplasm of secretory cells and cell bodies of the small ganglia surrounding the pharynx. {ECO:0000269|PubMed:15704008}.
Interaction partners:
- Nuclear transcription factor Y subunit nfyb-1
- Nuclear transcription factor Y subunit nfya-1
- Nuclear transcription factor Y subunit nfya-2
- DNA polymerase epsilon subunit 3
Sequence:
MSQFPEVLDNNLLHAENNETAEYIQNDGTNQSEVFMEHPYTPNMHPINMPSIVEGAVHPYNNLIHHNDAIPPAKYASMRQMTEDFWREKKQKMTEISEEDMLNKSKNMSVPMARVKKIMRIDDDVRNFMIASDAPIFMAQAAEFFIEEMTAMGWQYVSEARRRILQKADIASAVQKSDQFDFLIDFLPPKTVPTTSTNGPGHMSEDSFQDPNMHSDFHQRTSNSSVNRSHHN
Protein: NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 5) (NADH-plastoquinone oxidoreductase subunit 5) (P0C327)
Organism: Oryza sativa subsp. indica (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- 4Fe-4S ferredoxin-type domain-containing protein
- NAD
Sequence:
MEHTYQYAWVIPLLPLPVIMSMGFGLFLVPTATKNLRRIWAFPSVLLLSIAMVFSVHLSIQQINGSSIYQYLWSWTVNNDFSLEFGYLIDPLTSIMLILITTVGILVLIYSDDYMSHDEGYLRFFVYISFFNTSMLGLVTSSNLIQIYFFWELVGMCSYLLIGFWFTRPIAASACQKAFVTNRVGDFGLLLGILGFFWITGSLEFRDLFKIANNWIPNNEINSLLTILCAFLLFLGAVAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLIARLLPLFISLPLIMSFISLIGTLTLFLGATLALAQRDIKRSLAYSTMSQLGYMMLALGIGSYQAALFHLITHAYSKALLFLGSGSVIHSMEPLVGYSPDKSQNMVLMGGLRKYIPITRTCFLWGTLSLCGIPPLACFWSKDEILSNSWLYSPFFGIIASFTAGLTAFYMFRIYLLTFDGYLRVHFQNYSSTKEDSLYSISLWGKRISKGVNRDFVLSTAKSGVSFFSQNLSKIHVNTGNRIGSFSTSLGTKNTFVYPHEPGNTMLFPLLILLLCTLFIGSIGIHFDNEIGELTILSKWLTPSINFFQESSNSSINSYEFITNAISSVSLAIFGLFIAYMFYGSAYSFFQNLDLINSFVKGGPKKYFFHQLKKKIYSWSYNRGYIDIFYTRTFTLGIRGLTELTQFFDKGVIDGITNGVGLASFCIGEEIKYVGGGRISSYLFFFLCYVSVFLFFFLS
Protein: Neuronal PAS domain-containing protein 1 (Neuronal PAS1) (Basic-helix-loop-helix-PAS protein MOP5) (Class E basic helix-loop-helix protein 11) (bHLHe11) (Member of PAS protein 5) (PAS domain-containing protein 5) (Q99742)
Organism: Homo sapiens (Human)
Function: May control regulatory pathways relevant to schizophrenia and to psychotic illness. May play a role in late central nervous system development by modulating EPO expression in response to cellular oxygen level (By similarity). Forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) leading to transcriptional repression on its target gene TH (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator
- Aryl hydrocarbon receptor nuclear translocator 2
Sequence:
MAAPYPGSGGGSEVKCVGGRGASVPWDFLPGLMVKAPSGPCLQAQRKEKSRNAARSRRGKENLEFFELAKLLPLPGAISSQLDKASIVRLSVTYLRLRRFAALGAPPWGLRAAGPPAGLAPGRRGPAALVSEVFEQHLGGHILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVEMTGSSVFDYIHPGDHSEVLEQLGLRTPTPGPPTPPSVSSSSSSSSSLADTPEIEASLTKVPPSSLVQERSFFVRMKSTLTKRGLHVKASGYKVIHVTGRLRAHALGLVALGHTLPPAPLAELPLHGHMIVFRLSLGLTILACESRVSDHMDLGPSELVGRSCYQFVHGQDATRIRQSHVDLLDKGQVMTGYYRWLQRAGGFVWLQSVATVAGSGKSPGEHHVLWVSHVLSQAEGGQTPLDAFQLPASVACEEASSPGPEPTEPEPPTEGKQAAPAENEAPQTQGKRIKVEPGPRETKGSEDSGDEDPSSHPATPRPEFTSVIRAGVLKQDPVRPWGLAPPGDPPPTLLHAGFLPPVVRGLCTPGTIRYGPAELGLVYPHLQRLGPGPALPEAFYPPLGLPYPGPAGTRLPRKGD
Protein: Iron-sulfur cluster repair protein YtfE (Regulator of cell morphogenesis and NO signaling) (RCMNS) (P69506)
Organism: Escherichia coli (strain K12)
Function: Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Flavohemoprotein
- NADH oxidoreductase HCR
- HTH-type transcriptional repressor NsrR
- Uncharacterized protein YgbA
- Hydroxylamine reductase
- Uncharacterized protein YeaR
- Anaerobic nitric oxide reductase flavorubredoxin
- Protein YoaG
- Probable Fe
Sequence:
MAYRDQPLGELALSIPRASALFRKYDMDYCCGGKQTLARAAARKELDVEVIEAELAKLAEQPIEKDWRSAPLAEIIDHIIVRYHDRHREQLPELILQATKVERVHADKPSVPKGLTKYLTMLHEELSSHMMKEEQILFPMIKQGMGSQAMGPISVMESEHDEAGELLEVIKHTTNNVTPPPEACTTWKAMYNGINELIDDLMDHISLENNVLFPRALAGE