wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase ATG1 (EC 2.7.11.1) (Autophagy-related protein 1) (Q6CSX2)
Organism: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Function: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
Interaction partners:
- Autophagy-related protein 2
- Autophagy-related protein 8
- Autophagy-related protein 9
- Autophagy-related protein 13
- KLLA0F01166p
- Autophagy-related protein 29
- Autophagy-related protein 17
- Serine/threonine-protein kinase TOR
- Probable cysteine protease ATG4
- Autophagy protein 16
Sequence:
MSSESHDKVVAKAIRLPTENYSVEKEIGKGSFAVVYKGLSLRDGRNIAIKAVSRSKLKNKKLLENLEVEIAILKKIKHPHIVGLIDCERTSSDFYLIMEYCALGDLTFFIKKRKNLVLKHPLIKTVFEHYPPPSTEHNGLNRVLVVNYLQQLSSALKFLRSKNLVHRDIKPQNLLLCTPLLDYNDPKTFHELGFVGIYNLPILKIADFGFARFLPNTSLAETLCGSPLYMAPEILNYQKYNAKADLWSVGTVLYEMCCGRPPFKASNHLELFQKIKKANDEITVPSNCYIEPKLFNLIRGLLTFDPDSRMGFTDFFNNEVVTEDLTRYEQSYEPDLESKSKDVAESNMFVSEYLVKPLKQQESAHIPPTQTDENTSVQTGVRRTSGKERLATNHPPHQQIHPEDNSQNPEQSYQSASQKRLKSSYNDLILEKEYVVVEKKTVEVNSLADDFANNGPITNNQGAQVIKPLRYRTSSSSDASGGRRASLVERRLSISSLSPSNALSKALGLASVRLFGYQHNTKATSSPPQQTLLNPQIFQELTENAVLRADHKLNPFSEQMLDSNITPAVESLAAKAFVMYSFAEMKFSQILPTPPSSTDYDPLSDKRLSNGSCAIEDEEDLDQGRPPSNQTLTSATTKISSATNVDTQIPAPELKKLCTESLLLYLKALTILAASMKLTSKWWYENESKNCTLKLNILVQWIRDRFNECLDKAEFLRLKLHAINTSPNSQWSDDDPVIFVEKLIYDRALDISRNAARMEMESGNYNTCELAYATSLWMLEILLDENFQFNEVYDDEYASNITSLDESDKEMIKKYISSIANRLKALKSKMV
Protein: Homeobox protein Hox-C13b (Q6JIY4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis (By similarity). Plays a role in early embryonic development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MEGLSGNCPASHCRDFISHPALGRHSGSLASHQGTVYPDITTQDAGRQFPAPQASSGTSLGYGYAFGSPYYGCRLSYSHNVNLQQKSYHPAEKYMETSGALPAEELSSRSKEFAIYPSFASSYQTVPGYLDVPVVPGISAHPESRHEALFPMDSYQHWALSNGWDEQLYCSKEQTHFNHLWKSQFSDVVPHQAEMNGYRRGRKKRVPYTKIQLKELEKEYAASKFITKDRRRRISATTSLSERQVTIWFQNRRVKEKKFVCKSSKSSTNMHSV
Protein: Charged multivesicular body protein 2a (Chromatin-modifying protein 2a) (CHMP2a) (Putative breast adenocarcinoma marker BC-2) (Vacuolar protein sorting-associated protein 2-1) (Vps2-1) (hVps2-1) (O43633)
Organism: Homo sapiens (Human)
Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Peripheral membrane protein {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Cytoplasmic side {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}. Nucleus envelope {ECO:0000269|PubMed:28242692}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase (PubMed:28242692). {ECO:0000269|PubMed:28242692}.
Interaction partners:
- Charged multivesicular body protein 3
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 4a
- Charged multivesicular body protein 6
- Vacuolar protein sorting-associated protein 4B
- Vacuolar protein sorting-associated protein 4A
- RNF103-CHMP3 readthrough
- Charged multivesicular body protein 1b
- Vacuolar protein-sorting-associated protein 25
- Charged multivesicular body protein 4b
Sequence:
MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD
Protein: Kinesin-like protein (Q38FG7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAKWELKLVSLLEQHSLGHLAGKFMDSGITCEEFVALQHEQYGAYGVSSDEDTVNLYHAIKKLRGEPAVGSDSLQSEEESLLVPPILPSTSLPPPMEAATATGAVGDSDDILDEKVKERQYTTRGTTLLMRTDDSREVKRRKSRIVVAVRKRPISQCEQQRGFTDVMTTNDCDELVLAETRQKVDLTRYTHAHRFFFDEVFAETASNTDVYKRTAAALIDTVFEGGYATCFAYGQTGSGKTHTMLGTGGEPGIYALAAKEMLARLDPTKQMFVSFYEIYSGKLYDLLNGRQPLRCLEDGKQNVNICGLTEHPQSNVKSIMRLIEEGTRIRSSGTTGANDTSSRSHAILEVKLRNRGDKELFGKFTFIDLAGSERGADTMDCDRQTRIEGAQINKSLLALKECIRSLDLNHKHVPFRGSKLTEVLRDSFVGNCRTVMIGAVSPTSNSCEHTLNTLRYADRVKELKKSRSERKPLEENEQSEFIMEKKQTSPAARLSSHGRLSISPQGSLNLGCVSTHQNTSNKGNSVNTSSPSLPKRRSGTMRPSGMLCGRSTEQFISESTFKRSREDDEGRQSQQQQQQQGKEEAGRKSIDLDLGNRYDKVVDEIVQLERECVNTHRLYLDKDMALIKEEFSHIMSVEMPDSNIDTYVNNVLDILSVKLKAIHHFQGQMMRLRGLLDEEEKLCQRLEQNGI
Protein: Jitterbug, isoform I (E1JGS7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSPGLTALGESTRLVPANTPAVFEILPPPGQSLSKGECVATVLTPSKSKLNARVTHEAANGAARIEFVPTEVGTHVIDASINGTKIAGGPLIAKVYDSSLIQVTEVNGGVVGQACQFRVDASAAGEGQLEISINEGEVPNHVQVVGGGRCLVSFTPEQAKSHLIDIKFNGETVRGCPFVCAVADTSRVLLNLSNLELIPVNRPSSFHITVSGGGAAELAVSVRGPQGELPVRVTGDIHAGFTAEFTPTTVGGHSINVEYNGFAVQGTPFLAKSYDASKVVVGSVSRGTMGRPVQFTVDAGDAGEGNLEITISAKGQNIPTQVHPQGSARFSVSFVPTESCEHTINVSFNKMPVPGCPITVSISGGVAGPQVSLGGPGPVHQTNSFVINHNGGRLEDIEVNVEGPAGQSVPAQVHQSADGVFKAEFVPRVVGEHRVNVTVNGLPTAGSPYAAKVYDVSAIKVKNVSSGTVGKAVTFLVETSQAGPGNLEVTVNGGRVPTSAQAQGQHTYAISFTPREAESHTVELRFNSQDVPGSPFTCRVAAAARIQSPETMDKVSVGRLFEFVVESDTKPTVEVLGPARRSVPVKIDALGSSTLGYNVKFEPMEVGDHSVEVRLPGGGHVEGSPFLLKAYSAEKVIVTDIRAGVVNKSVSFGINASQAGAGNLEIIVAVNGKNVPNFVQSEGNARFKVNFKPTEAATHSLSVRFNGHPVPGSPFSCHIAAAAASPSMGLPRAMAMGECLKQAAVKMDNTFELEGFDGVEPQIFVTSPSGDNEHCQLSQHDGGSYSASFRPTTVGRHLISVTANDQHINGSPFSCNVFDVSRVSISGLEQQYGPANLGVPVTFSVDAAGAGEGTLELVVSTDSSTVKAEVVACARGLYDVTFVPQSTEPHYVNITFNEVAVDGSPFRVDIQQHTQHIQIGSLAAIDFPADDQIVEIFSPDQKSVPYSINRQTAEFRTHMTGNYTLRFIDRETRQHIGSRTLCVFDPTLVKITEVSEAFCHRPASIGVSLNEAGQGDLSALVRCGATEVPHTIRGPSKTGVYEIVYQPTRVAPHKISILFNEVPISLKPLEINVLPASAGKEISVSGLGLYQSRVGKTTSFAIDTVKRPAREFDVVVSGPGGQALPVRCYQTKNGHLQAEFTINKPGQCVIEVLHQSKPLPGSPFTCESFDSSKVSTQGVTKEPLALHSPNSFTVRTDNAGTAELEAFAISPSNQSIPVLISEQSDGVYNVEFVPSQPGNYKLTLMYGGETIPSSPLNFTASSSGVRNDARAAGHGLEVCHRNKEASFVVYCPIAPNVQIERLDEYGERIEPKIKALGNNEWRISYTILSVGKYEIRASCPNRGSLPGSPWHISCVESNKVTPVGGWGTLVDHDGRLILPARIIFDVENAGPGKLVCSIDGIEIPVDKLVDGKMCLNITGENLAAGEHDLDLTWSGLTITQCPRSAFVTGQQAADKVQLMGRGLAAAQAGEAAHFTIDASNAPAGRPEVILTSQDNTSLPVSLAQPRPSENIWLASYTPLKSTTGTLNLSVKWNGRLVKGCPLTVAVGSSMDASKVIVSGEGLRHGIVGKDIKSWIDTRRAGPGELTAHCAGVRKVAYCELYDHGDATFTLNIKPQESGRHILTIKYGGQNVPGSPFALKVAGAPDASKVRVYGPGIEHGVLATFQSRFICDTRGAGAGQLTVRVRGPKGAFRVEMQRESQKDRTILCKYDPTEPGDYRVEVKWAGEFVPGSPFPVMIFDTEEELRRYLQGI
Protein: Uncharacterized protein (O86326)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MRDFGQRSRSGGKAIAEHCRTHELHIRPRTGGESATTVQVGRSAANERADIAPRKTRCCVHVAKPNRIRLADQLARSSMGEKPGHDHQRNQRDQNQRDVRPRHPGYLGA
Protein: Myosin regulatory light chain 2, smooth muscle major isoform (MLC-2) (DTNB) (G1) (Isoform L20-A) (P02612)
Organism: Gallus gallus (Chicken)
Function: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity).
Interaction partners:
- Myosin-11
- Myosin light polypeptide 6
- Myosin light chain kinase, smooth muscle
- Myosin-9
- Actin, cytoplasmic 1
- Actin, aortic smooth muscle
- Rho associated coiled-coil containing protein kinase 2
- Rho-associated protein kinase
- Actin, cytoplasmic 2
- Protein phosphatase 1 regulatory subunit.
Sequence:
MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASMGKNPTDEYLEGMMSEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD
Protein: Beta-hexosaminidase subunit alpha (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit alpha) (Hexosaminidase subunit A) (N-acetyl-beta-glucosaminidase subunit alpha) (P06865)
Organism: Homo sapiens (Human)
Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A.
Subcellular location: Lysosome.
Interaction partners:
- Beta-hexosaminidase subunit beta
- Beta-galactosidase
- Alpha-N-acetylgalactosaminidase
- Alpha-galactosidase A
- N-acetylglucosamine-6-sulfatase
- Hexosaminidase D
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- Chitotriosidase-1
- Acidic mammalian chitinase
- Lactosylceramide alpha-2,3-sialyltransferase
Sequence:
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT
Protein: Two-component response regulator ORR29 (OsRRB7) (Q7XS69)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional activator that binds specific DNA sequence. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. May directly activate some type-A response regulators in response to cytokinins (By similarity). Functions as a response regulator in response to cytokinins.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22383541}. Nucleus {ECO:0000269|PubMed:22383541}.
Interaction partners:
Sequence:
MAQKEGLPAGRLSAMVIDEDKCHADSTSYMLSAELNFSVTVFTSPIKALDFLQNHAEGVDLVLADVHMEEMNGFDFLKVARELHKSIQVIMMSTETTMYTMKRCVKLGAQFLVNKPLDAGTIKNLWQYVDLKVLRMEKIKDLLQGIGDESTCANETNSLAENPKNDTKKKYYLMWTPHLQKKFLHALQILGKDASPKNIKKIMGVDNIDCRQIAAHLQKHRLRLTKDLKKASFTTDTSKDESNSRIGPAESHHVCRNASTLQPRSNTQPTETTMQILSEDAEYDDVYAAMRRALQYGIVFDESKHSSDPSGDEDEQVVVGGDQDGCANEANDIDSSGDHHQVAAVVTKPCNANASQEIINKMTNSDGMQATKGSKAAVFRLVDYSESDSD
Protein: Pre-mRNA-splicing factor cwf11 (Complexed with cdc5 protein 11) (O94508)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mRNA splicing where it associates with cdc5 and the other cwf proteins as part of the spliceosome.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pre-mRNA-splicing factor cwf4
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor cwf3
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor cwf2
- Pre-mRNA-splicing factor spp42
- Pre-mRNA-splicing factor cwf7
Sequence:
MVLYKNKKKQIINYANSNWGQNEGVEFQETMLQCILEAVIVSKDAKQVLSLLHELKLFENFLWQRVNTEMSLNHINLTCMLLLYKSKYEYITWDLIDENRFQLFFEKVIEVSLSLNLSEVVYMIQFITLCFQFSNIEKLRKLVYQLTNISILNSLDNLDKVKYLLHDSSSLTKAFDSYKEKRPSIVEKFPLHNLLSRWIHSLLIKSISYAQTEKQEAKVTPLLAIINMSLVLLSAFPTRRFAHPVIEDSCFYTALRMSLYYDSNELFKKMTDDLNYVLKFPFDNTRGNEYEKEQKIRNDELVYYHLQLTLFSDFQKELGDLVFCTQTSLQQRQKLEEITSFLSFNSLKSLCSKCYLRTSFPEKYAIKVDFEFLKNVFINTYDRTRLVNDYDEIINFTLKDVLGERSVMDQENSLTNYFLLQNTAIQYLSISFFMRQQSKAYKKLLLRSLYAELLNFSEQYRRLSIKNATKNLTKDNFFSLNNFKVTSVAPPQIGQVLPQFVKCQMGLSRPGPFHSALRDLKNSIKSPFLCLIYISKDMEYKLLHGNALDPLEGVTDFTIATICNDDVGMFQSDMQSDSDNKSINVYLSPFYYHSLAGLGEYRPKQLKFNFALVLSPEANKYWLDLNILVSLLNRAKEFPKWFEDLFLGFGTPDICAFPNAGLNSIYARNLFNTVEQLQSVLPNCHVPSNLSTESLLIKFYTNQNKISADVTASDRHFLLPSNRLYTYNDKQLESILRGSQPGLTMVNGPTRCGKHVLVCKLLEVLQDTSPNDRTVVLSDSNFSMNTLFTLLEKARCFHQGHLLYLSDEGKDETLERYGTLSSWISKLPGLLREIGRLAASIQAPGSHDASPDTALYFRDAYIKRLWEKYLNTVDDKDSVDAYNRFPFHSYFGDKSKRPIETYNKDNFFDYATKLYGELEYMFQQLEEIRPFGLLRYYEDQELYALCQQSRIIGCTWTSLSTRLGTLKEKGFCFNNLIVMNSQNISESSITSILLSNCEPTGFDRLVLLGNQYLTSGNQDINNTSNGSLFKRLRYLKSRIIDLNTQYNVRESISSLCSSIYPLDIKTVDSSPNKRLDYGNSGFAHEVQFINVGAFKGSQETEPVSGYKQNLGEAEYAVALFQYMRMLGYPTNEIVICTLYESQVSLLNEIISVRCSHNSFFGQPAFVGTVEKLPSDKRVNFVIFTTVESKEASDHWNPKTFYKAFSACSYGLYVLCNRDLFRSTRGLEKLWNEIEKTPDKLLLTTGEIYPSSHKIGSSVETFEIENLLHLSNYVVEMTKKRLNTN
Protein: Preprotein translocase Sec, Sec61-beta subunit protein (Protein transport protein subunit-like) (Q9FKK1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Protein transport protein Sec61 subunit gamma-3
- Protein transport protein Sec61 subunit gamma-1
- SecY protein transport family protein
- F9K20.24 protein
- AT2G34250 protein
- Translocon-associated protein subunit beta
- Preprotein translocase subunit SCY1, chloroplastic
- Protein transport protein Sec61 subunit gamma-2
- DnaJ protein ERDJ2A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
Sequence:
MARGSSQSQQSTSTGSSTARPGLAAPRGSAAATAGMRRRRLGGGGGVSSGGGSGVGSGSSNMLRFYTDDAPGLKISPTVVLIMSLCFIGFVTALHVFGKLYLHKSGSQA
Protein: Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase (EC 2.5.1.145) (P9WK93)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01147}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01147}.
Interaction partners:
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- Indole-3-glycerol phosphate synthase
- Anthranilate synthase component 1
- Membrane protein insertase YidC
- Lipoprotein signal peptidase
- Decaprenyl-phosphate phosphoribosyltransferase
- Conserved protein
- Conserved protein similar to jag protein
- NADH-quinone oxidoreductase subunit L
Sequence:
MRMLPSYIPSPPRGVWYLGPLPVRAYAVCVITGIIVALLIGDRRLTARGGERGMTYDIALWAVPFGLIGGRLYHLATDWRTYFGDGGAGLAAALRIWDGGLGIWGAVTLGVMGAWIGCRRCGIPLPVLLDAVAPGVVLAQAIGRLGNYFNQELYGRETTMPWGLEIFYRRDPSGFDVPNSLDGVSTGQVAFVVQPTFLYELIWNVLVFVALIYIDRRFIIGHGRLFGFYVAFYCAGRFCVELLRDDPATLIAGIRINSFTSTFVFIGAVVYIILAPKGREAPGALRGSEYVVDEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAEPDGIRRQDDFSSRRRRWWRLRRRRQ
Protein: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (DiDHB-DH) (EC 1.3.1.28) (Trans-2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase) (P15047)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. Catalyzes the reversible NAD-dependent oxidation of the C3-hydroxyl group of 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), producing the transient intermediate 2-hydroxy-3-oxo-4,6-cyclohexadiene-1-carboxylate, which undergoes rapid aromatization to the final product, 2,3-dihydroxybenzoate (2,3-DHB). Only the compounds with a C3-hydroxyl group such as methyl 2,3-dihydro-2,3-dihydroxybenzoate, methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate, trans-3-hydroxy-2-cyclohexene-1-carboxylate, cis-3-hydroxy-4-cyclohexene-1-carboxylate, cis-3-hydroxycyclohexane-1-carboxylic acid are oxidized to the corresponding ketone products. The stereospecificity of the C3 allylic alcohol group oxidation is 3R in a 1R,3R dihydro substrate. It can also increase the DHB-AMP ligase activity of EntE by interaction EntE.
Interaction partners:
- Enterobactin synthase component B
- Enterobactin synthase component F
- Isochorismate synthase EntC
- Enterobactin synthase component E
- Proofreading thioesterase EntH
- Enterobactin synthase component D
- Ferrienterobactin receptor
- Ferric enterobactin-binding periplasmic protein FepB
- Iron
- Enterobactin exporter EntS
Sequence:
MDFSGKNVWVTGAGKGIGYATALAFVEAGAKVTGFDQAFTQEQYPFATEVMDVADAAQVAQVCQRLLAETERLDALVNAAGILRMGATDQLSKEDWQQTFAVNVGGAFNLFQQTMNQFRRQRGGAIVTVASDAAHTPRIGMSAYGASKAALKSLALSVGLELAGSGVRCNVVSPGSTDTDMQRTLWVSDDAEEQRIRGFGEQFKLGIPLGKIARPQEIANTILFLASDLASHITLQDIVVDGGSTLGA
Protein: Succinate dehydrogenase flavoprotein subunit (EC 1.3.5.1) (O53370)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- succinate dehydrogenase
- Succinate dehydrogenase 2 membrane subunit SdhC
- Probable succinate dehydrogenase SdhD
- Fumarate reductase iron-sulfur subunit
- Probable succinate dehydrogenase [iron-sulfur subunit]
- Fumarate hydratase class II
- Fumarate reductase subunit C
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
- Fumarate reductase subunit D
Sequence:
MICQHRYDVVIVGAGGAGMRAAVEAGPRVRTAVLTKLYPTRSHTGAAQGGMCAALANVEDDNWEWHTFDTVKGGDYLADQDAVEIMCKEAIDAVLDLEKMGMPFNRTPEGRIDQRRFGGHTRDHGKAPVRRACYAADRTGHMILQTLYQNCVKHDVEFFNEFYALDLALTQTPSGPVATGVIAYELATGDIHVFHAKAVVIATGGSGRMYKTTSNAHTLTGDGIGIVFRKGLPLEDMEFHQFHPTGLAGLGILISEAVRGEGGRLLNGEGERFMERYAPTIVDLAPRDIVARSMVLEVLEGRGAGPLKDYVYIDVRHLGEEVLEAKLPDITEFARTYLGVDPVTELVPVYPTCHYLMGGIPTTVTGQVLRDNTSVVPGLYAAGECACVSVHGANRLGTNSLLDINVFGRRAGIAAASYAQGHDFVDMPPNPEAMVVGWVSDILSEHGNERVADIRGALQQSMDNNAAVFRTEETLKQALTDIHALKERYSRITVHDKGKRFNTDLLEAIELGFLLELAEVTVVGALNRKESRGGHAREDYPNRDDVNYMRHTMAYKEIGADKEGPELRSDVRLDFKPVVQTRYEPKERKY
Protein: Actin-1 (PfAct1) (EC 3.6.4.-) (Actin I) (PfActI) (Q8I4X0)
Organism: Plasmodium falciparum (isolate 3D7)
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. ATP hydrolysis leads to the formation of a stable intermediate ADP-inorganic phosphate (Pi) actin, which is followed by the release of Pi (Probable). ATP hydrolysis affects filament stability; ADP-bound actin depolymerizes much faster than ATP- or ADP-Pi-bound actin (Probable). Plays an essential role during the asexual blood stage. At the segmented schizont stage, required for apicoplast migration and segregation into individual daughter merozoites. Also, required for the separation of daughter merozoites in the final stages of cytokinesis. Essential for merozoite invasion of, but not adhesion to or reorientation towards, host erythrocytes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q4Z1L3}. Nucleus {ECO:0000250|UniProtKB:Q4Z1L3}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28810863}. Note=During host erythrocyte invasion, filamentous actin localizes close to the junction between merozoites and the host cell (PubMed:28810863). In schizonts, filamentous actin appears to connect apicoplasts (PubMed:28810863). 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:0000269|PubMed:28810863}.
Interaction partners:
- Myosin-A
- Cofilin/actin-depolymerizing factor homolog 2
- Cofilin/actin-depolymerizing factor homolog 1
- Glyceraldehyde-3-phosphate dehydrogenase
- Tubulin alpha chain
- Profilin
- Coronin
- Tubulin beta chain
- Histone H3-like centromeric protein CSE4
Sequence:
MGEEDVQALVVDNGSGNVKAGVAGDDAPRSVFPSIVGRPKNPGIMVGMEEKDAFVGDEAQTKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRERMTQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMRLDLAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIEKSYELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNIVLSGGTTMYEGIGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWITKEEYDESGPSIVHRKCF