wanglab/gogpt-training-data huggingface dataset:
Protein: Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (ENR) (EC 1.3.1.9) (NADH-dependent enoyl-ACP reductase) (Q81GI3)
Organism: Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)
Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Interaction partners:
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- 3-oxoacyl-[acyl-carrier-protein] synthase
- (3R)-hydroxymyristoyl-[acyl carrier protein] dehydratase.
- Malonyl-CoA-[acyl-carrier-protein] transacylase.
- BioH protein.
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
- Beta-ketoacyl-[acyl-carrier-protein] synthase III 1
- Beta-ketoacyl-[acyl-carrier-protein] synthase III 2
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Acyl carrier protein
Sequence:
MELLQGKTFVVMGVANQRSIAWGIARSLHNAGAKLIFTYAGERLERNVRELADTLEGQESLVLPCDVTNDEELTACFETIKQEVGTIHGVAHCIAFANRDDLKGEFVDTSRDGFLLAQNISAFSLTAVAREAKKVMTEGGNILTLTYLGGERVVKNYNVMGVAKASLEASVKYLANDLGQHGIRVNAISAGPIRTLSAKGVGDFNSILREIEERAPLRRTTTQEEVGDTAVFLFSDLARGVTGENIHVDSGYHILG
Protein: Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Triose-phosphate isomerase) (Q6FRI3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Fructose-bisphosphate aldolase
- Phosphoglycerate kinase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Phosphoglycerate mutase
- Transaldolase
- Transaldolase
- mRNA 3'-end-processing protein RNA14
- Enolase 1
Sequence:
MARTFFVGGNFKLNGTKKSIKEIVDRLNTASLPENVEVVICPPATYLDYTVSLVSKKQVTVGGQNTYTKASGAYTGENSVDQLKDVGAKWVILGHSERRTYFHEDDKIVAEKTKFALDQGLGVILCIGETLEEKKAGVTLKVVERQLDAVIAEVKDWTNVVIAYEPVWAIGTGLAATAEDAQDIHHSIRSYLAEKLGKDTAEKTRILYGGSANGANAGTFKDKADVDGFLVGGASLKPEFVDIINSRN
Protein: Krueppel-like factor 6a (Kruppel-like factor 6a) (F1R7F0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDVLPMCSIFQELQIVHDTGYFSALPSLEEYWQQTCLELERYLQSEPYVSASDLKFEGQEDLWSKLILACGDKGDGNGSLPSVKEDDNQDCQILETNSMNSDASSEASDSSEELSPTHIFTSNPLGSVLTESAHHLSSSIISTPPSSPEMPQEPGVPQVWGSTQTDLHIPVKIRQNGLGKALDKTTTGGDASPDGRRRVHRCHFNGCRKVYTKSSHLKAHQRTHTGEKPYRCSWEGCEWRFARSDELTRHFRKHTGAKPFKCSHCDRCFSRSDHLALHMKRHL
Protein: Putative peripheral benzodiazepine receptor-related protein (B1AH88)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPHLLWCPTNGLGLGGSPAGQWGGGSHYRGLVPGEPAGRPPALPLPGLAGLHDHTQLLRMAGQPWLAWGTAAARVSARPTRDCSCTSRCHHACDVVAVTLS
Protein: Cell division protein ZapA (Z ring-associated protein ZapA) (P0ADS2)
Organism: Escherichia coli (strain K12)
Function: Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12368265}. Note=Localizes at mid-cell.
Interaction partners:
- Cell division protein ZapB
- Cell division protein FtsZ
- Cell division protein FtsA
- Cell division protein FtsQ
- Cell division protein ZipA
- Macrodomain Ter protein
- Cell division protein FtsN
- Cell division protein ZapC
- Probable peptidoglycan glycosyltransferase FtsW
- Cell division protein ZapD
Sequence:
MSAQPVDIQIFGRSLRVNCPPDQRDALNQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELAQEKAKTRDYAASMEQRIRMLQQTIEQALLEQGRITEKTNQNFE
Protein: Cytochrome c oxidase subunit 6A1, mitochondrial (Cytochrome c oxidase polypeptide VIa-liver) (Cytochrome c oxidase subunit VIA-liver) (COX VIa-L) (P12074)
Organism: Homo sapiens (Human)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}.
Interaction partners:
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6C
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 7A2, mitochondrial
Sequence:
MAVVGVSSVSRLLGRSRPQLGRPMSSGAHGEEGSARMWKTLTFFVALPGVAVSMLNVYLKSHHGEHERPEFIAYPHLRIRTKPFPWGDGNHTLFHNPHVNPLPTGYEDE
Protein: PXA domain protein 1 (O14200)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for required for normal vacuolar morphology and for vacuolar protein transport. Also required for endosome-to-Golgi protein transport.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:18256467}; Multi-pass membrane protein {ECO:0000269|PubMed:18256467}.
Interaction partners:
- Sorting nexin-12
- Meiotically up-regulated gene 122 protein
Sequence:
MAKLSSLLNPIISKILEIYVYSWYSGISKDALFPSQCEQVGGSIVHELEKRLSRQDAMDLLFYEIPFLLIKHIENTEEAKLRFALPQGQILEIDTIYHSLHPHIALEKEENELVYCRLLVEDILKYLLPATNSKSEIECVILREALAVQIHKSIQVASSPETMYKFIIYLSKAILQPSRRPWKESITTAVRWVWHAFRILLITRGVPYFSTAWFQFYLKLFSQKDNVSSSDLTRWFFFYTLLYPWIALVSAFVAETMTLCCIVTIFYDKNVNRQWKQYILTSVSNMDKGNPSGGSQSTNVTTFRRFSQSSYPRRSNYRRRISTSSKSLYELSPSKFKSIPITSNPPPMLNLSKGSTSVEPTFCETNASVALSTVTSTPVFSTDSSPLSSRTRENLLSLIPSAVSSPTKANTNKSHQRSFSIPKATKDSQTPSENSAATLKQAAIDAYSQIPVIPFFLPSDKLIMLVESEYRNKHIFYSLLNSFTMVMFPELRHTK
Protein: tryptophan 5-monooxygenase (EC 1.14.16.4) (A2VCX5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLSNKLDGPRRGRSFDSINKNYEEKLLSNELRKTTFHKTDENKDKKLSSKREHAAIVFSLKNEVGGLVKALKLFQDNQVNLLHIESRKSRRRNSELEVLVDCDSDRETLKEIVQLLRKQTSIIAMNSPDKFWTPASDLTEVPWFPKKISDLDKSACRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMSYKHGDPIPHVEFTEEEVKTWGVVFRELNKLYPTHACREYLQNLPLLSQFCGYREDNIPQLEDVSNFLRERTGFTIRPVAGYLSPRDFLAGLAFRVFHCTQYVRHSSDPLYTPEPDTCHELLGHVPLLAEPSFAQFSQELGLASLGASDDAVQKLATCYFFTVEFGLCKQEGSLRAYGAGLLSSISELKHSLSDSAKILPFEPKVTCKQECLITTFQDVYFVSESFEEAKCRMREFAKTIQRPFSLRYNPYTQSVCVLKDMPSINDVVEELRHELDIVGDALCRLSTHLGV
Protein: HXXXD-type acyl-transferase family protein (Hypersensitivity related protein-like) (Q9LYQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGSQGMSSPSPLVVKKSQVVIVKPSKATPDVSLSLSTLDNDPYLETLAKTIYVYAPPSPNDHVHDPASLFQQALSDALVYYYPLAGKLHRGSHDHRLELRCSPAEGVPFVRATADCTLSSLNYLKDMDTDLYQLVPCDVAAPSGDYNPLALQITLFACGGLTLATALSHSLCDGFGASQFFKTLTELAAGKTQPSIIPVWDRHRLTSNNFSLNDQVEEGQAPKLVDFGEACSSAATSPYTPSNDMVCEILNVTSEDITQLKEKVAGVVTTLEILAAHVWRARCRALKLSPDGTSLFGMAVGIRRIVEPPLPEGYYGNAFVKANVAMKAGELSNSPLSHVVQLIKEAKKAAQEKRYVLEQLRETEKTLKMNVACEGGKGAFMLLTDWRQLGLLDEIDFGYGGSVNIIPLVPKYLPDICIFLPRKQGGVRVLVTLPKSVMVNFKEHINPLNT
Protein: laccase (EC 1.10.3.2) (R4JRR8)
Organism: Cerrena sp. HYB07
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKRHASVGFVTLGLALGVLGAIGPVTDLPIVNKDIAPDGFTRAAVLAGGTFPGPLITGQKGDEFKINVVNQLTDADMLKSTSIHWHGFFQKGTNWADGPASVNQCPVATNHSFLYQFSSQGQPGTFWYHSHLSTQYCDGLRGAFVVYDPEDPHKLLYDVDDESTVITLADWYHTLARKLKGPPVPDTTLINGLGRDKLGDLDASLAVITVQAGKRYRFRLVSISCDPNYVFAIDGHDMTIIEVDSVSSQPHTVDSIQIFAGQRYSFVLNANQPVNNYWIRANPNAGMKGFDGGINSAILRYEGAPVAEPTTVEKTSTKPLNEVDLHPLVPMPVPGKPFPGGADVTHNLEFGFANGHFTINNATFVPPNVPVLLQILSGAQNAQDLLPSGSVIELPLNKDIELTLAATRKAVGGPHPFHLHGHNFHVIRSAGQTQPNYIDPIVRDVVNIGAPPDNVTIRFRTDNPGPWFLHCHIDWHLEIGFAMVFAEGLGQTAVANPVPESWNNLCKIYDALDPGDQ
Protein: Serpin family G member 1 (Serpin peptidase inhibitor clade G member 1 isoform 2) (Serpin peptidase inhibitor clade G member 1 isoform 3) (E9PK97)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASRLTLLTLLLLLLAGGLGRTPKQTWRASSLTPRTSPVSTRP
Protein: Uncharacterized protein SPBC1E8.03c (O42968)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MVVIANKGALWAYYCKRLLNSVTYMMYPLIRKRTMKKLLLIVGLLLACSTVMRRIPLFHESFHLPSLDPRASTTTSQKFQEYRSDFLEKLETAEPPEDVIMFTAYGLGVHTHNLFMLACDMAKTSDSQIRFLLLTDGTILPEALYDYNRETVSTCPLSFLSYSTGVERLSKELILKDLLSLQFQQALLAISPSVIVTSEHSPLVMFQAINPYLNNNYYTHDTVDTNALEENSWITKLDMQSLQHFRTPRINVVLIVEDGTYKYLLNLMRDLGRDFKNSEEYPHLFIHLFMSENIPNLSSIRANWPQHRLFINLHFNQKDLNLIEVWTPPNDYTYALVVDLQPDSPPQLSSNLITWLKYKILLIYYHKSSSTYKNNIAAIVPSFDFSNEEAVILSQTINSNIVLFAPVVFQKFQEYMAVRLLNPNFELPESNGIEFAHEDSVLGHSKPSLTEFHAILGLYSLVISYNHFEGSLSNELRLDNLIAYFLKNPSVINFEEISEKNLYFTYDSKRLSFQGAKNESKKLYNSVTSCPYYGSLSSFPIRSIFCEPLM
Protein: Origin recognition complex subunit 2 (Q13416)
Organism: Homo sapiens (Human)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3.
Subcellular location: Nucleus.
Interaction partners:
- Origin recognition complex subunit 1
- Origin recognition complex subunit 3
- Origin recognition complex subunit 5
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM2
- DNA replication factor Cdt1
- Origin recognition complex subunit 6
- Cell division control protein 6 homolog
- Origin recognition complex subunit 4
- Protein DBF4 homolog A
Sequence:
MSKPELKEDKMLEVHFVGDDDVLNHILDREGGAKLKKERAQLLVNPKKIIKKPEYDLEEDDQEVLKDQNYVEIMGRDVQESLKNGSATGGGNKVYSFQNRKHSEKMAKLASELAKTPQKSVSFSLKNDPEITINVPQSSKGHSASDKVQPKNNDKSEFLSTAPRSLRKRLIVPRSHSDSESEYSASNSEDDEGVAQEHEEDTNAVIFSQKIQAQNRVVSAPVGKETPSKRMKRDKTSDLVEEYFEAHSSSKVLTSDRTLQKLKRAKLDQQTLRNLLSKVSPSFSAELKQLNQQYEKLFHKWMLQLHLGFNIVLYGLGSKRDLLERFRTTMLQDSIHVVINGFFPGISVKSVLNSITEEVLDHMGTFRSILDQLDWIVNKFKEDSSLELFLLIHNLDSQMLRGEKSQQIIGQLSSLHNIYLIASIDHLNAPLMWDHAKQSLFNWLWYETTTYSPYTEETSYENSLLVKQSGSLPLSSLTHVLRSLTPNARGIFRLLIKYQLDNQDNPSYIGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGTDGVEYLLIPVDNGTLTDFLEKEEEEA
Protein: Adenine phosphoribosyltransferase 5 (AtAPT5) (EC 2.4.2.7) (Q9LFP0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. May contribute to the recycling of adenine into adenylate nucleotides and the inactivation of cytokinins by phosphoribosylation. Possesses low activity toward adenine, but can efficiently convert cytokinins from free bases (active form) to the corresponding nucleotides (inactive form).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Adenine phosphoribosyltransferase 3
- AMP deaminase
- GMP synthase
- Adenosine kinase 1
- Guanylate kinase 3, chloroplastic
- Guanylate kinase 1
- Guanylate kinase 2
- Adenosine kinase 2
- Inosine triphosphate pyrophosphatase
- Adenylosuccinate lyase
Sequence:
MFAAENGLKGDPRLEAISAAIRVVPNFPKKGIMFQDITTLLLDHKAFKHTIDIFVDRYKDMQISVVAGVEARGFLFGPSIALAIGAKFIPLRKPGKLPGKVISESYELEYGHDRLEMHVGAVEPRERVIIIDDLVATGGTLSAAMSLLESQGAEVVECACVIGLPEVKGQHKLKGKPLYVLVEPSGLDEFC
Protein: 26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8) (26S proteasome regulatory subunit S12) (Mov34 protein) (Proteasome subunit p40) (P26516)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 5
- Proteasome subunit alpha type-5
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-1
- Ubiquitin carboxyl-terminal hydrolase 14
Sequence:
MPELAVQKVVVHPLVLLSVVDHFNRIGKVGNQKRVVGVLLGSWQKKVLDVSNSFAVPFDEDDKDDSVWFLDHDYLENMYGMFKKVNARERIVGWYHTGPKLHKNDIAINELMKRYCPNSVLVIIDVKPKDLGLPTEAYISVEEVHDDGTPTSKTFEHVTSEIGAEEAEEVGVEHLLRDIKDTTVGTLSQRITNQVHGLKGLNSKLLDIRSYLEKVASGKLPINHQIIYQLQDVFNLLPDASLQEFVKAFYLKTNDQMVVVYLASLIRSVVALHNLINNKIANRDAEKKEGQEKEESKKERKDDKEKEKSDAAKKEEKKEKK
Protein: PRKCH upstream open reading frame 2 (uORF2) (Protein uPEP2) (C0HM02)
Organism: Homo sapiens (Human)
Function: Product of an upstream open reading frame (ORF) of PRKCH which regulates translation of the downstream protein kinase C eta (PKC-eta) ORF. Functions as a repressive element that maintains low basal levels of PKC-eta in growing cells but enhances its expression during stress conditions induced by amino acid starvation in a EIF2AK4/GCN2-dependent manner. In addition to its role in regulating PKC-eta translation, also inhibits the kinase activity of PKC-eta as well as other protein kinases including PRKCD, PRKCQ and PRKCE but not PRKCA, PRKCG or PRKCZ.
Interaction partners:
Sequence:
MASRGALRRCLSPGLPRLLHLSRGLA
Protein: Vinculin (Metavinculin) (A0A0S2I7K2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004278}. Cell projection, podosome {ECO:0000256|ARBA:ARBA00004188}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MPVFHTKTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLSAPVLAVQAAVSNLVRVGKETVQTTEDAIMRRDMPPAFIKVENACTKLVQAAQMLKADPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVESMEDLITYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISGIKIFVTTRTSQGKGVEEALKNRNFTVEKMNTEINEIIRVLQLTSWDEDAWANKDTEAMKRALALIDSKMAQAKNWLRDPQGQPGGPGEQAIRQILDEAEKVGELCAGKERRDIVGTAKTLGQLTEQVSDLRARGQGANPVAMQKAQQVSQGLDVLTGKVENAARKLEAMTGSKQAIAKRIDAAQSWLADPHSGPEGEENIRALLGEARKIADLCEDPKEREDILRSMSEIAALSGKLAELKRAGKGDTPEARALAKQIATALQNLQSKTSKAVANTRPAKAAVHLAGKMEQAGRWIDNPTLDDSGVGQAAIRGLLAEGRRLANALPAAQRQELLGKCEQVEHLMAQLAELAARGEGDSPQARAIAQQLQHTLKELEGKMQDAMTQEVSDIFSDTTTPIKLLAVAATAPSDSPNREEVFKERASNFENHASRLGATAEKAAAVGTANKSTVEGIQAAVKSARDLTPQVVSAARILLKNPGNQAAFEHFETMKNQWIDNVEKLTGLVDEAIDTRSLLAASEDAIKKDLDKCQVAMANHQPQMLVAGATSIARRANRILLVAKREIENSEDPKFRETVKAASDELSRTISPMVMDAKAVAANIKDQGLQRGFLDSGFKILGAVANVRDAFQPQEPEFPPPPPDLESLQISDTAAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQQAGEMVSEPMMVAARQLHDEARKWSSKGNDIIGAAKRMALLMAEMSRLVRGSGGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISEEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLHWVRKTPWYQ
Protein: Energy-coupling factor transporter ATP-binding protein EcfA2 (ECF transporter A component EcfA2) (EC 7.-.-.-) (Q9WY65)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake; uptake does not occur in the absence of RibU or the EcfA1A2T complex.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:23359690}; Peripheral membrane protein {ECO:0000305|PubMed:23359690}.
Interaction partners:
- Energy-coupling factor transporter ATP-binding protein EcfA1
- Energy-coupling factor transporter transmembrane protein EcfT
- Biotin transporter BioY
- Phosphate import ATP-binding protein PstB
- ABC transporter, ATP-binding protein
- ABC transporter, ATP-binding protein
- Oligopeptide ABC transporter, ATP-binding protein
- Uncharacterized ABC transporter ATP-binding protein TM_0288
- ABC transporter, ATP-binding protein
- Oligopeptide ABC transporter, ATP-binding protein
Sequence:
MRIEVVNVSHIFHRGTPLEKKALENVSLVINEGECLLVAGNTGSGKSTLLQIVAGLIEPTSGDVLYDGERKKGYEIRRNIGIAFQYPEDQFFAERVFDEVAFAVKNFYPDRDPVPLVKKAMEFVGLDFDSFKDRVPFFLSGGEKRRVAIASVIVHEPDILILDEPLVGLDREGKTDLLRIVEKWKTLGKTVILISHDIETVINHVDRVVVLEKGKKVFDGTRMEFLEKYDPRFFTSKMLVMRRLVLKGEDPFSMSDDELLERVCNS
Protein: SPI-2 type 3 secretion system translocon protein SctE (SPI-2 T3SS translocon protein SctE) (Secreted effector protein SseC) (Secretion system effector C) (O84947)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. May act as a translocator that mediates translocation of SPI-2 TTSS effector proteins from intraphagosomal bacterial cells into the host cells.
Subcellular location: Secreted {ECO:0000269|PubMed:11159962, ECO:0000269|PubMed:11567004}. Cell surface {ECO:0000269|PubMed:11159962, ECO:0000269|PubMed:11567004}. Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Note=Secreted via the type III secretion system 2 (SPI-2 T3SS) (PubMed:11159962, PubMed:11567004). After secretion, localizes mainly on the surface of the bacterial cell (PubMed:11159962, PubMed:11567004). {ECO:0000269|PubMed:11159962, ECO:0000269|PubMed:11567004}.
Interaction partners:
- SPI-2 type 3 secretion system translocon protein SctB
- Secretion system chaparone
- Secretion system effector
- Secretion system chaparone
- Secretion system apparatus protein SsaL
- Secretion system apparatus lipoprotein SsaJ
- Secretion system effector
- Secretion system apparatus protein
- Secreted effector protein SseB
- Type 3 secretion system secretin
Sequence:
MNRIHSNSDSAAGVTALTHHHLSNVSCVSSGSLGKRQHRVNSTFGDGNAACLLSGKISLQEASNALKQLLDAVPGNHKRPSLPDFLQTNPAVLSMMMTSLILNVFGNNAQSLCQQLERATEVQNALRNKQVKEYQEQIQKAIEQEDKARKAGIFGAIFDWITGIFETVIGALKVVEGFLSGNPAEMASGVAYMAAGCAGMVKAGAETAMMCGADHDTCQAIIDVTSKIQFGCEAVALALDVFQIGRAFMATRGLSGAAAKVLDSGFGEEVVERMVGAGEAEIEELAEKFGEEVSESFSKQFEPLEREMAMANEMAEEAAEFSRNVENNMTRSAGKSFTKEGVKAMAKEAAKEALEKCVQEGGKFLLKKFRNKVLFNMFKKILYALLRDCSFKGLQAIRCATEGASQMNTGMVNTEKAKIEKKIEQLITQQRFLDFIMQQTENQKKIEQKRLEELYKGSGAALRDVLDTIDHYSSVQARIAGYRA
Protein: Histone acetyltransferase type B catalytic subunit (HAT B) (EC 2.3.1.48) (Q9FJT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acetylates soluble but not nucleosomal H4 (By similarity). Acetylates 'Lys-12' of histone H4.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Histone H4
- Tetratricopeptide repeat
- Origin of replication complex subunit 3
- Origin of replication complex subunit 5
- Origin of replication complex subunit 2
- WD-40 repeat-containing protein MSI4
- WD-40 repeat-containing protein MSI2
- Histone-binding protein MSI1
- WD-40 repeat-containing protein MSI3
- WD-40 repeat-containing protein MSI5
Sequence:
MVQKQQASAGPGTEPKKRRRVGFSPADTGVEANECIKIYLVSSKEEVDSSDISSVKPVDLNDFFDGDGKIYGYQGLKINVWINSISLHSYADITYQSTINGDKGITDLKSALQNIFAETIVDTKDEFLQTFSTQRDFIRNMVSNGEVMHAGATDGSSKNAEVVPSDPQVIRMEIGSPNAGLLYSRLVPLVLLFVDGSNPIDVTDPDWHLYLLIQKKEEKEDPLYRIVGFTAIYKFYRYPDRLRMRLSQILVLPSFQGKGLGSYLMEVVNNVAITENVYDLTVEEPSEKFQHIRTCIDINRLRSFDPIKPDIDSAVQTLTKGKLSKKAQIPRFTPPLNAIEKVRESLKINKKQFLKCWEILIYLALDPIDKYMEDYTSVITNHVRTDILGKDIETPKKQVVDVPSSFEPEASFVVFKSVNGEEANTNVQVDENKPDQEQQLKQLVEERIREIKLVAEKVSKSGQTLKV
Protein: ECF sigma factor, FemI (Q9I2J2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Sigma factor regulator, FemR
- Anti-sigma factor FoxR
- Probable transmembrane sensor
- Probable transmembrane sensor
- Ferric-mycobactin receptor, FemA
- Probable transmembrane sensor
- Probable transmembrane sensor
- FpvR
- Probable transmembrane sensor
- Probable transmembrane sensor
Sequence:
MPPADASLHDAVSHLYQDHHGWLQGWLRRRLGCAENAADLAQDTFARLLASRRVLDAREPRAYLTTVAKGLMINWFQRQSLERAYLDALANLPEDLAPPPEQRLMVLETLHEVDALLGSLPDRVRQAFLLAQIEGLKYEAIAERLGVSLGSVKRYMQQAFRQCLELME
Protein: Metal transporter Nramp4 (AtNramp4) (Q9FN18)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vacuolar metal transporter involved in intracellular metal homeostasis. Can transport iron (Fe), manganese (Mn) and cadmium (Cd). Regulates metal accumulation under Fe starvation. Acts redundantly with NRAMP3 to mobilize vacuolar Fe and provide sufficient Fe during seed germination. In association with NRAMP3, required for optimal growth and photosynthesis under Mn deficiency. Exports Mn from vacuoles in leaf mesophyll cells, making Mn available for functional photosystem II in chloroplasts.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16270029}; Multi-pass membrane protein {ECO:0000269|PubMed:16270029}.
Interaction partners:
- Vacuolar iron transporter 1
- Oligopeptide transporter 3
- Ferric reduction oxidase 3, mitochondrial
- Protein ZINC INDUCED FACILITATOR 1
- Fe
- Ferric reduction oxidase 2
- Solute carrier family 40 member 2
- Transcription factor bHLH47
- Putative metal tolerance protein C3
- Metal tolerance protein A2
Sequence:
MSETDRERPLLASEERAYEETEKVLIVGIDEEEDADYDDDPGNSPKFSWKKLWLFTGPGFLMSIAFLDPGNLESDLQAGAIAGYSLIWLLMWATAIGLLIQLLSARLGVATGRHLAELCREEYPTWARMVLWIMAEIALIGADIQEVIGSAIAIKILSNGLVPLWAGVVITALDCFIFLFLENYGIRKLEAVFAILIATMALAFAWMFGQTKPSGTELLVGALVPKLSSRTIKQAVGIVGCIIMPHNVFLHSALVQSREVDPKKRFRVKEALKYYSIESTGALAVSFIINVFVTTVFAKSFYGTEIADTIGLANAGQYLQDKYGGGFFPILYIWAIGVLAAGQSSTITGTYAGQFIMGGFLNLKMKKWVRALITRSCAIIPTMIVALVFDSSDSMLDELNEWLNVLQSVQIPFAVIPLLCLVSNEQIMGSFKIQPLVQTISWIVAALVIAINGYLMVDFFSGAATNLILLVPVIIFAIAYVVFVLYLISRGLTYTPWQLVASSHKEPQRDDE