wanglab/gogpt-training-data huggingface dataset:
Protein: Glutamate mutase sigma subunit (EC 5.4.99.1) (Glutamate mutase S chain) (Glutamate mutase small subunit) (Methylaspartate mutase) (P80078)
Organism: Clostridium cochlearium
Function: Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
Interaction partners:
- Glutamate mutase epsilon subunit
- methylaspartate ammonia-lyase
- Pyruvate-ferredoxin/flavodoxin oxidoreductase.
- Pyruvate-ferredoxin/flavodoxin oxidoreductase.
- Conserved hypothetical protein.
- 4-hydroxybutyrate CoA-transferase.
- Glutamate dehydrogenase
- glutamine synthetase
- GntR family transcriptional regulator
Sequence:
MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQEVFIKAAIETKADAILLSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE
Protein: Increased recombination centers protein 23 (Q08416)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Is probably involved in a pathway contributing to genomic integrity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein YIP4
- Bypass of stop codon protein 2
- ERAD-associated E3 ubiquitin-protein ligase HRD1
Sequence:
MIEALEIVLLLVIQSLQYICRTCIAFLLIPFLGLYAFDLFLYVYRMILYLSQMFNYKRKLGRSKTNNRPHSPRLHKIYSSGDCMDTLIGQVRDLRVFLLSTIHSHSKRFFSTRFQTKSGINSAIDANDVETTSDVSSFTNLHLTRSSEEGYYIAGSI
Protein: 26S rRNA (cytosine-C(5))-methyltransferase NOP2B (EC 2.1.1.-) (Nucleolar protein 2B) (tRNA methyltransferase 4d) (AtTRM4d) (Q8VYM6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ribosomal large subunit assembly (By similarity). S-adenosyl-L-methionine-dependent methyltransferase that probably methylates the C(5) position of cytosine 1586 (m5C1586) in mitochondrial 26S rRNA. May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation (By similarity). Seems involved in the regulation of cell proliferation (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P40991}.
Interaction partners:
- Ribosome biogenesis protein BOP1 homolog
- AT5g04600/T32M21_200
- Probable rRNA-processing protein EBP2 homolog
- Ribosome assembly factor mrt4
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Nucleolar complex-associated protein 3
- Ribosome biogenesis protein WDR12 homolog
- Pescadillo homolog
- Ribosome production factor 2 homolog
- Probable ribosome biogenesis protein RLP24
Sequence:
MAALTRNKKKGSNSQTPPLNKQTKASPLKKAAKTQKPPLKKQRKCISEKKPLKKPEVSTDEEEEEEENEQSDEGSESGSDLFSDGDEEGNNDSDDDDDDDDDDDDDDEDAEPLAEDFLDGSDNEEVTMGSDLDSDSGGSKLERKSRAIDRKRKKEVQDADDEFKMNIKEKPDEFQLPTQKELEEEARRPPDLPSLQMRIREIVRILSNFKDLKPKGDKHERNDYVGQLKADLSSYYGYNEFLIGTLIEMFPVVELMELIEAFEKKRPTSIRTNTLKTRRRDLADILLNRGVNLDPLSKWSKVGLIVYDSQVPIGATPEYLAGFYMLQSASSFLPVMALAPREKERVVDMAAAPGGKTTYVAALMKNTGIIYANEMKVPRLKSLSANLHRMGVTNTIVCNYDGRELTKVLGQSSVDRVLLDAPCSGTGVISKDESVKTSKSADDIKKFAHLQKQLILGAIDLVDANSKTGGYIVYSTCSVMIPENEAVIDYALKNRDVKLVPCGLDFGRPGFSSFREHRFHPSLEKTRRFYPHVHNMDGFFVAKLKKMSNAMQPSGNDEPAVTMEQAQVSSSDDDDEKAEAIEELEKPPVASGQPKRESNTKEDTNKRKNPRSKEIHKGKRNKNTKTESGNVEEPRKQKKKRSQWKNEIAQAREEKRKTMRENAKETPKHRG
Protein: 3-ketoacyl-CoA synthase 5 (KCS-5) (EC 2.3.1.199) (Eceriferum 60) (Very long-chain fatty acid condensing enzyme 5) (VLCFA condensing enzyme 5) (Q9C6L5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates mostly the synthesis of VLCFAs from 26 to 30 carbons in length (e.g. C20:1, C26, C28, C30).
Subcellular location: Membrane {ECO:0000269|PubMed:15277688}; Multi-pass membrane protein {ECO:0000269|PubMed:15277688}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase-like protein At1g24470
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Very-long-chain
- Protein ECERIFERUM 26
- Very-long-chain enoyl-CoA reductase
- Protein ECERIFERUM 2
- At5g02890
- Protein ECERIFERUM 26-like
- Phosphoinositide phosphatase SAC4
- Very-long-chain aldehyde decarbonylase CER1
Sequence:
MSDFSSSVKLKYVKLGYQYLINNFLTLLLIPVIATVAIELLRMGPEEILSVLNSLHFELLHILCSSFLIIFVSTVYFMSKPRTVYLVDYSCYKPPVTCRVPFSSFMEHSRLILKDNPKSVEFQMRILERSGLGEETCLPPAIHYIPPTPTMESARNEAQMVIFTAMEDLFKNTGLKPKDIDILIVNCSLFSPTPSLSAMIINKYKLRSNIKSYNLSGMGCSASLISVDVARDLLQVHPNSNAIIISTEIITPNYYKGNERAMLLPNCLFRMGGAAILLSNRRSDRWRAKYKLCHLVRTHRGADDKSYNCVMEQEDKNGNVGINLSKDLMTIAGEALKANITTIGPLVLPASEQLLFLSSLIGRKIFNPKWKPYIPDFKQAFEHFCIHAGGRAVIDELQKNLQLSGEHVEASRMTLHRFGNTSSSSLWYELSYIEAQGRMKRNDRVWQIAFGSGFKCNSAVWKCNRTIKTPTDGAWSDCIERYPVFIPEVVKL
Protein: 60S ribosomal protein L38 (Q8II62)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Small ribosomal subunit protein eS30
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S5, putative
- 60S ribosomal protein L27
- Small ribosomal subunit protein eS12
- 60S ribosomal protein L3
- 40S ribosomal protein S15
- 40S ribosomal protein S11, putative
- 60S ribosomal protein L29
- 40S ribosomal protein S28e, putative
Sequence:
MPKQITDIRKFLKISRKPDTTAVIIMKKKSKTKKNTVITKLKLRTKKYLYTMVFADRKKAERIENSLLPSLKRIYYPQKKVGKTVKK
Protein: Endonuclease 4 (EC 3.1.21.2) (Endodeoxyribonuclease IV) (Endonuclease IV) (P0A6C1)
Organism: Escherichia coli (strain K12)
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin.
Interaction partners:
- Exodeoxyribonuclease III
- Endonuclease III lyase)
- Uncharacterized sugar kinase YeiI
- Formamidopyrimidine-DNA glycosylase
- Superoxide dismutase
- UvrABC system protein A
- Uracil-DNA glycosylase
- Adenine DNA glycosylase
- Endonuclease V
- Regulatory protein SoxS
Sequence:
MKYIGAHVSAAGGLANAAIRAAEIDATAFALFTKNQRQWRAAPLTTQTIDEFKAACEKYHYTSAQILPHDSYLINLGHPVTEALEKSRDAFIDEMQRCEQLGLSLLNFHPGSHLMQISEEDCLARIAESINIALDKTQGVTAVIENTAGQGSNLGFKFEHLAAIIDGVEDKSRVGVCIDTCHAFAAGYDLRTPAECEKTFADFARTVGFKYLRGMHLNDAKSTFGSRVDRHHSLGEGNIGHDAFRWIMQDDRFDGIPLILETINPDIWAEEIAWLKAQQTEKAVA
Protein: Ovarian-specific serine/threonine-protein kinase Lok (EC 2.7.11.1) (Protein loki) (dMNK) (O61267)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have a role in germline establishment.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:9507063}. Note=Speckled subnuclear compartment.
Interaction partners:
- Serine/threonine-protein kinase ATR
- Serine/threonine-protein kinase grp
- M-phase inducer phosphatase
- Serine/threonine-protein kinase ATM
- Histone chaperone asf1
- Protein chiffon
- P53, isoform B
- Cdc25-like protein phosphatase twine
- Wee1-like protein kinase
- Crossover junction endonuclease MUS81
Sequence:
MARDTQGTQGTQSQASNIWTQVESQPMEKIVWGRLYGKNIKIKSLGTSSKYRIIYTHSSFSVDLNNDEFTAGRGEANDLILTLNDLPEKILTRISKVHFIIKRANCELTNPVYIQDLSRNGTFVNNEKIGTNRMRILKNDDVISLSHPTYKAFVFKDLSPNESIGLPEEINKTYYVNRKLGSGAYGLVRLVYDTRTCQQFAMKIVKKNMLSGARPSTNFSDPDRVLNEAKIMKNLSHPCVVRMHDIVDKPDSVYMVLEFMRGGDLLNRIISNKLLSEDISKLYFYQMCHAVKYLHDRGITHRDLKPDNVLLETNDEETLLKVSDFGLSKFVQKDSVMRTLCGTPLYVAPEVLITGGREAYTKKVDIWSLGVVLFTCLSGTLPFSDEYGTPAAQQIKKGRFAYGHPSWKSVSQRAKLLINQMLIVDPERRPSIDDVLQSSWLRDAPMLQKAKRLMKLDGMEIEEENFLEPPTKRSRR
Protein: Electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) (EC 1.5.5.1) (Q66I16)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein subunit beta.
- Hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit beta
- Acyl-CoA dehydrogenase very long chain.
- All trans-polyprenyl-diphosphate synthase PDSS1
- Trifunctional enzyme subunit alpha, mitochondrial
- Novel protein similar to human isovaleryl Coenzyme A dehydrogenase
- Ubiquinone biosynthesis protein
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- FAD synthase
Sequence:
MLPASRYTLQARRCIHALKVVKAEHVAPQIYSTRWFSSVPRITTHYTVYPRDKDSRWEGVEMERFADEADVVIIGGGPAGLSAAIRLKQLANQHEKELRVCVVEKASQIGAHTLSGACLEPTALNELIPDWKERGAPLNTPVTEDKFSILTEKYRIPVPILPGLPMNNHGNYLVRLGHFVRWLGEQAEELGVELYPGYAAAEVLFHEDGSVKGIATNDVGIAKDGSPKDVFERGMELHAKVTMFGEGCHGHLAKQLYKQFNLREKCEPQTYAIGLKELWVIDEKKWRPGRAEHSVGWPLNRNTYGGTFLYHLNEGEPLVALGFVVGLDYTNPYMSPFREFQRWKHHPSVMSTLEGGNRIAYGARALNEGGFQSIPQLTFPGGMLIGCSPGFMNVPKIKGTHTAMKSGMLAAETAFSKITDENLQSQTTGLYIPEYEEALKKSWVWKELRSVRNIRPSFHTYFGLYGGMVYTGIFYWIFRGKEPWTLKHSGSDYAQLKPAKDCSPIEYPKPDGKISFDLLSSVALSGTNHEHDQPAHLTLKDDSIPVSKNLAIYDGPEQRFCPAGVYEYVPLETGDGMRLQINAQNCVHCKTCDIKDPSQNINWVVPEGSGGPAYNGM
Protein: Protein ACTIVITY OF BC1 COMPLEX KINASE 3, chloroplastic (ABC1-LIKE KINASE 3) (EC 2.7.-.-) (EC 2.7.11.1) (Protein REPRESSOR OF BDR1) (Q9MA15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Kinase that can phosphorylate the tocopherol cyclase VTE1, a key enzyme of tocopherol (vitamin E) metabolism and involved in the recycling of oxidated alpha-tocopherol quinone, possibly stabilizing it at plastoglobules. Regulates also membrane prenylquinone composition. Required for photooxidative stress responses to prevent photosystem II core and chlorophyll degradations. Together with ABC1K1, contributes to plastoglobule (PG) function in prenyl-lipid metabolism, stress response, and thylakoid remodeling. Promotes photodamage of chloroplasts under continuous red light, thus working in opposition to ABC1K1.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}. Plastid, chloroplast {ECO:0000269|PubMed:25882344}. Note=Colocalizes with the chlorophyll autofluorescence of mature chloroplasts. In cotyledons of seedlings grown in continuous red light, only observed in the chloroplasts losing chlorophyll autofluorescence. {ECO:0000269|PubMed:25882344}.
Interaction partners:
- Tocopherol cyclase, chloroplastic
- Protein kinase superfamily protein
- At1g54500/F20D21_31
- Probable plastid-lipid-associated protein 11, chloroplastic
- non-specific serine/threonine protein kinase
- Thioredoxin family protein
- 31 kDa ribonucleoprotein, chloroplastic
- Alternative NAD
- Probable plastid-lipid-associated protein 1, chloroplastic
- Probable plastid-lipid-associated protein 13, chloroplastic
Sequence:
MSLVVGQSLGLTLVGDGLSLRNSKINVGKSKFFSVNRRRLARAALVQARPKEDGAAASPSPSSRPASVVQYRRADLADDLQAEARALGRAIDASIYSPELIARKHGSQPFKALRRSLEILGALGGFALKLGIDQKQGNLEKNMKKRAIELRRIFTRLGPTFVKLGQGLSTRPDLCPPDYLEELAELQDALPTFPDAEAFACIERELDLSLETIFSSVSPEPIAAASLGQVYKAQLRYSGQVVAVKVQRPGIEEAIGLDFYLIRGVGKLINKYVDFITTDVLTLIDEFACRVYQELNYVQEAQNARRFKKLYADKADVLVPDIFWDYTSRKVLTMEWVEGTKLNEQLAIESQGLKVLDLVNTGIQCSLRQLLEYGFFHADPHPGNLLATPDGKLAFLDFGMMSETPEEARFAIIGHVVHLVNRDYEAMARDYYALKFLSPDVDVTPIIPALRDFFDDALNYTVSELNFKTLVDGLGAVFYQYPFNVPPYYALILRSLTVLEGLALYADPNFKVLAASYPYFAKRLLTDPNPYLRDALIELLFKDGKFRWNRLENLLQQGSKDRDFSAKDALQPVLKLLLDPNGEELRLLVIKEAVRVSEAIALGTVVDTYNSLPEFLRSLVFNGNGNGPLTMSTAELQSTLELRDQVSRIWGLLQSSESFDPAILQPILQVLQQPEARRLGGRVAGGVGQRLAARFLQQLLRATTPSSAPSP
Protein: Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2 (P35206)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for calcium regulation. May regulate calcium accumulation by a non-vacuole organelle. Also regulates the activity of CSH1 and SUR1 during mannosyl phosphorylinositol ceramide synthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:7854312}; Multi-pass membrane protein {ECO:0000269|PubMed:7854312}.
Interaction partners:
- Mannosyl phosphorylinositol ceramide synthase SUR1
- Mannosyl phosphorylinositol ceramide synthase CSH1
- Serine palmitoyltransferase 2
- Inositolphosphotransferase 1
- Ceramide very long chain fatty acid hydroxylase SCS7
- Inositol phosphorylceramide synthase catalytic subunit AUR1
- 3-ketodihydrosphingosine reductase TSC10
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase-regulating protein TSC3
- Protein BCP1
Sequence:
MSTTLLWFSSVIGYVIQTKCLSNIQSKKEISVGPNGTIATPETNGDNGNSSSLTFYLTFMYFASWLLLVPASRLWEKMRPMFVSDSDSNRNSQFDNNNSGSVTNEDVDTFSHVLDDPQPRIPAQQQKQKIISVATFKYVAKLTVLALIMIVADLTYNMALSLSPAFDVALMQNTAIFEIVTLLYGVCGISRKNYVFRNFLIMMNAVIGILIISYTKATCDMLAGKLSVNPNTGELSDPFLFDRLKGALICGLGALIMGPFAVLWNRWFCSNISKNENSAVVLVKQSTHMALIGIIGMVILLPFIPKFPSRESVESISLFYNDKSFWFSLLGSIIFGSLPSLISILELNRKAPAEYLTTCNLGAIIFMGLAEWVCEPTQTTIVRWEVIGYIMLTVSLLVLSVTLGEGKYHH
Protein: Exportin-2 (Exp2) (Chromosome segregation 1-like protein) (Importin-alpha re-exporter) (Q9ERK4)
Organism: Mus musculus (Mouse)
Function: Export receptor for importin-alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the importin-alpha from the export receptor. CSE1L/XPO2 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P55060}. Nucleus {ECO:0000250|UniProtKB:P55060}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:P55060}.
Interaction partners:
- Importin subunit alpha-5
- Importin subunit alpha-4
- Importin subunit alpha-3
- Exportin-1
- Importin subunit beta-1
- Importin subunit alpha-1
- Exportin-4
- Importin-5
- GTP-binding nuclear protein Ran
- Transportin-1
Sequence:
MELSDANLQTLTEYLKKTLDPDPAIRRPAEKFLESVEGNQNYPLLLLTLLEKSQDNVIKVCASVTFKNYIKRNWRIVEDEPNKICEADRVAIKANIVHLMLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHVINGVLRTAHSLFKRYRHEFKSNELWTEIKLVLDAFALPLTNLFKATIELCSTHANDASALRILFSSLILISKLFYSLNFQDLPEFFEDNMETWMNNFHTLLTLDNKLLQTDDEEEAGLLELLKSQICDNAALYAQKYDEEFQRYLPRFVTAIWNLLVTTGREVKYDLLVSNAIQFLASVCERPHYKNLFEDQNTLTSICEKVIVPNMEFRAADEEAFEDNSEEYIRRDLEGSDIDTRRRAACDLVRGLCKFFEGPVTGIFSGYVNSMLQEYAKNPSVNWKHKDAAIYLVTSLASKAQTQKHGITQANELVNLTEFFVNHILPDLKSNNVNEFPVLKADGIKYIMIFRNQVPKEHLLVSIPLLISHLEAESIVVHTYAAHALERLFTMRGSNNTTLFTAAEIAPFVEILLTNLFKALTLPGSSENEYIMKAIMRSFSLLQEAIIPYIPTLITQLTQKLLAVSKNPSKPHFNHYMFEAICLSIRITCKANPAAVVNFEEALFLVFTEILQNDVQEFIPYVFQVMSLLLETHKNDIPSSYMALFPHLLQPVLWERTGNIPALVRLLQAFLERGSSTIATAAADKIPGLLGVFQKLIASKANDHQGFYLLNSIIEHMPPESVDQYRKQIFILLFQRLQNSKTTKFIKSFLVFINLYCIKYGALALQEIFDGIQPKMFGMVLEKIIIPEIQKVSGNVEKKICAVGITKLLTECPPMMDTEYTKLWTPLLQSLIGLFELPEDDSIPDEEHFIDIEDTPGYQTAFSQLAFAGKKEHDPVGQMVNNPKIHLAQSLHKLSTACPGRVPSMVSTSLNAEALQYLQGYLQAASVTLL
Protein: Cytochrome P450 85A1 (OsCYP85A1) (3-dehydroteasterone synthase) (EC 1.14.14.-) (C6-oxidase) (Protein DWARF) (OsDWARF) (Teasterone synthase) (EC 1.14.14.-) (Typhasterol synthase) (EC 1.14.14.-) (Q8GSQ1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the C6-oxidation step in brassinosteroids biosynthesis. May convert 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) to 3-dehydroteasterone (3DT, 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY). Involved in the organization and elongation of the leaf and stem cells. Not able to convert 6-deoxocastasterone (6-deoxoCS) and castasterone (CS) to brassinolide (BL).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 734A5
- Cytochrome P450 734A6
- Os01g0388101 protein
- Os09g0441625 protein
- Os09g0441400 protein
- Cytochrome P450
- Os09g0441600 protein
- Os02g0503100 protein
- Os05g0200400 protein
- Os01g0521800 protein
Sequence:
MVLVAIGVVVAAAVVVSSLLLRWNEVRYSRKRGLPPGTMGWPLFGETTEFLKQGPSFMKARRLRYGSVFRTHILGCPTVVCMEAELNRRALASEGRGFVPGYPQSMLDILGRNNIAAVQGPLHRAMRGAMLSLVRPAMIRSSLLPKIDAFMRSHLAAWSSSSSSAVVDIQAKTKEMALLSALRQIAGVSAGPLSDALKAELYTLVLGTISLPINLPGTNYYQGFKARKKLVAMLEQMIAERRSSGQVHDDMLDALLTGVEGTREKLTDEQIIDLIITLIYSGYETMSTTSMMAVKYLSDHPKALEQLRKEHFDIRKGKAPEDAIDWNDFKSMTFTRAVIFETLRLATVVNGLLRKTTQDVEMNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLEKNMESHPHFMLFGGGSRMCPGKEVGTVEIATFLHYFVTQYRWEEEGNNTILKFPRVEAPNGLHIRVQDY
Protein: Teichoic acid glycerol-phosphate primase (EC 2.7.8.44) (CDP-glycerol:N-acetyl-beta-D-mannosaminyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenyl glycerophosphotransferase) (CDP-glycerol:glycerophosphate glycerophosphotransferase) (Major teichoic acid biosynthesis protein B) (Tag primase) (P27621)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the addition of a single glycerol phosphate residue to the prenoldiphosphate-linked disaccharide, as a primer for polymerisation by TagF.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16150696, ECO:0000269|PubMed:17660278}; Peripheral membrane protein {ECO:0000269|PubMed:16150696, ECO:0000269|PubMed:17660278}; Cytoplasmic side {ECO:0000269|PubMed:16150696, ECO:0000269|PubMed:17660278}.
Interaction partners:
- N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D-mannosaminyltransferase
- Glycerol-3-phosphate cytidylyltransferase
- Teichoic acids export ATP-binding protein TagH
- Teichoic acid translocation permease protein TagG
- Poly
- Probable undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase
- Uncharacterized glycosyltransferase EpsJ
- Teichoic acid poly
- Putative glycosyltransferase EpsH
- UDP-N-acetylglucosamine 2-epimerase
Sequence:
MKIRSLLANCYLYFLSAIAFFLQWVKPESKVTLLISFEANAKAILEEYEQGQYSYKLNILYTQQASAIAESFPNVDAYLLQEKNPIHLIKAVYLMFNSKVIITDNYFLLTSVLNKRKQTKCIQVWHANGSLKKFGLEDITNMQRTKTDIKRFQKVYSSYDYLTVGSEEMANIFKKSFGIKDNQLLKIGVPLTDPYYRENKKKISDTLNIQRKKIILYAPTFRDYNMQSIQLPFTEEQLIHQLKEEYVLFVKLHPAIQNNIDIKYSSDYIKDVSNYALFDLLMAADILITDYSSVPFEFSILNKPILFYTYDLKLYQQKRGLVDNYLSIIPGRACYDSESLINEIQTPFNYSKIKVFSDRWNKYSDGNSSQNLLNFIENLIS
Protein: Probable oxygen-dependent coproporphyrinogen-III oxidase (COX) (Coprogen oxidase) (Coproporphyrinogenase) (EC 1.3.3.3) (Q9UTE2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protoporphyrinogen oxidase
- Uroporphyrinogen decarboxylase
- Ferrochelatase, mitochondrial
- Porphobilinogen deaminase
- C-4 methylsterol oxidase erg25
- Prolyl 3,4-dihydroxylase ofd1
- Uroporphyrinogen-III synthase
- Delta-aminolevulinic acid dehydratase
- Lanosterol 14-alpha demethylase erg11
- Probable acyl-CoA desaturase
Sequence:
MSDITVEPIGKQMEKLILDVQQEIVAGLEAVDGQKFFQDKWTKGEGGYGISCVIQDGNVFEKGGVNTSIVQGKLNQDAVQRMRANHEGIDRTAKELPFFAAGISMVIHPRNPMAPTTHLNYRYFELVNSDGKKIWWFGGGADLTPSILFEEDGKHFHKLHKEACDRHDPTFYPRFKKWADEYFLIKHRKETRGIGGIFFDDLSEKDPQELFAFVKDCAHTFLPAYVPIMEKRKNMEFTEDDKEFQLIRRGYYAEFNVMYDRGTWFGLQAPEPRVESILMTLPLHASWRYKYEPKQERHKALLKVTHTPIEWC
Protein: DNA helicase MCM8 (EC 3.6.4.12) (Minichromosome maintenance 8) (Q9CWV1)
Organism: Mus musculus (Mouse)
Function: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity. Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs. The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression. However, may play a non-essential for DNA replication: may be involved in the activation of the prereplicative complex (pre-RC) during G(1) phase by recruiting CDC6 to the origin recognition complex (ORC) (By similarity). Probably by regulating HR, plays a key role during gametogenesis. Stabilizes MCM9 protein (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UJA3}. Chromosome {ECO:0000250|UniProtKB:Q9UJA3}. Note=Localizes to nuclear foci. Localizes to double-stranded DNA breaks. Binds chromatin throughout the cell cycle. {ECO:0000250|UniProtKB:Q9UJA3}.
Interaction partners:
- DNA replication licensing factor MCM4
- DNA helicase MCM9
- DNA replication licensing factor MCM7
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM2
- Protein MCM10 homolog
- DNA replication licensing factor MCM3
- Origin recognition complex subunit 2
- Cell division control protein 45 homolog
Sequence:
MSGAYRGRGFGRGRFQSWKRGRGGGNFSGRWRERENRVDLNEASGKHASAQASQPLLQQSTLDQFIPYKGWKLYFSEVYSNNSPFIEKIQAFEKFFTRHIDLYDKDEIERKGSILVDFKELTKADEITNLIPDIENALRDAPEKTLACMGLAIHQVLTKDLERHAAELQAQEGLSNGGETMVNVPHIYARVYNYEPLTHLKNIRATCYGKYISIRGTVVRVSNIKPLCTNMAFQCAACGEIQSFPLPDGKYTLPTKCPVPACRGRSFAPLRSSPLTVTLDWQLIKIQELMSDAQREAGRIPRTIECELVHDLVDSCVPGDTVTVTGIVKVSNSEEGSRNKNDKCMFLLYIEANSVSNSKGPKAQTAEDGCKHGTLMEFSLKDLYAIREIQAEENLLKLVVNSLCPVIFGHELVKAGLTLALFGGSQKYADDKNRIPIRGDPHVLIVGDPGLGKSQMLQAACNVAPRGVYVCGNTTTSSGLTVTLSKDSSSGDFALEAGALVLGDQGICGIDEFDKMGNQHQALLEAMEQQSISLAKAGVVCSLPARTSIIAAANPVGGHYNKARTVSENLKMGSALLSRFDLVFILLDTPNEQHDHLLSEHVIAIRAGKQKAVSSATVTRVLSQDSNTSVLEVVSEKPLSERLKVAPGEQTDPIPHQLLRKYIGYARQYVHPRLSTDAAQALQDFYLELRKQSQRVGSSPITTRQLESLIRLTEARARLELREEATREDAEDIIEIMKHSMLGTYSDEFGNLDFERSQHGSGMSNRSTAKRFISALNSIAERTYNNIFQYHQLRQIAKELNIQVADFENFIGSLNDQGYLLKKGPKIYQLQTM
Protein: Toll-like receptor 1 (E9PTL5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU363040}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU363040}.
Interaction partners:
- Toll-like receptor 2
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor
- Toll/interleukin-1 receptor domain-containing adapter protein
- Toll-like receptor 4
- T-cell surface glycoprotein CD4
- Interferon gamma
- Interleukin-6
- High mobility group protein B1
- High mobility group protein B1
Sequence:
MNSSSLKHVYCHTMTKTQSTIFYCIVVLGLILIKIQLSEESELIIKRPNANLTRVPKDLPLQTTTLDVSQNNISELQTSDILLLSKLRVFIMSYNRLQYLNISVFKFNTELEYLDLSHNELRLISCHATADLKHLDLSFNAFDALPICKEFGNLSQLQFLGLSGSQIQNSSVQLIAHLNISKVLLVLGDTYGEKEDPKCLQHISTETLHIVFPSKREFHFLLDMSVSTAISLELSNIKCVLEDKNCSYFLGTLERLRKTQRLSNLTLNNVDTTWNSFINILQLVWHTPVKSFSISNVKLKGHFNFRRFHYSDTSLRALSIHQVVTDVFSFPQSNIYSIFSNMNIQSFTVSGTRMVHMLCPDQISPFLYLDFTDNLLTDIVFEDCRNLIRLKTLSLQKNQLKTLENIILMSMEMTSLQKLDISQNSLRYSDAGSPCSWTQSLLVLNLSSNMLTDSVFRCLPPKVKVLDLHNNRIVSISKDVTHLQALQELNVASNFLTDLPGCGAFSSLSVLVIDHNSVSHPSSDFFQSCQNIRSITAGNNPFRCTCELREFVKNIGQASREVVEGWPDSYRCDYPDSIKGTPLQDFHMSPLSCDTILLTVTIGATLLLLAAIGASLCLYFDLPWYLRMLWQWTQTRHRARNIPLEELQRNLQFHAFVSYSGHDSAWVKNELLPNLEKDDIRVCLHERNFVPGKSIVENIIHFIEKSYKSIFVLSPHFIQSEWCHYELYFAHHNLFHEGSDNLILILLEPIPQYSIPTNYHKLKTLMARRTYLEWPTEKSKHGLFWANLRASINVKLVNQAEATCYTQQ
Protein: inorganic diphosphatase (EC 3.6.1.1) (Q7Z029)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MNNTHGVDSRSDRTSPQDLASAEVAGLPVSALHGTNISTGRGSEADVAEPIQEAVDRKVSELDLAAYDKDDFTQPMIKKIMSRLFSAFDVTHLGYLTPDKVEEVCRYLGRNMSDGDVKAMKAEINAIDGHVTFEKFWAWWCSHPVHSRTKCFSMVSADFSMPYHQQQLVVHEKGEMYTPSYRVLYFFRDLETGRERQVSPWHDIPLYVRDLVRTKPEATPMNRYNFICEIPKWTRAKFEIATGESFNPIKQDIKNGVPRFYKHGDMMWNYGAFPQTWESTEVLFEAGVTGDNDPVDAVEIGMTQFKVGQVSAVKVLGVLGMIDEGKMDWKVVCISHNDPICRFMKDIHDVPKFLPGCLDAIREWFRVYKICQGGEASHFAFDGEFKDKEYAMKVIDESHNMWHNLLKVNKMGEL