wanglab/gogpt-training-data huggingface dataset:
Protein: HTH-type transcriptional repressor NsrR (P0AF63)
Organism: Escherichia coli (strain K12)
Function: Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress, such as ytfE, hmpA and ygbA. May require iron for activity. Does not regulate its own transcription.
Interaction partners:
- Flavohemoprotein
- Iron-sulfur cluster repair protein YtfE
- Anaerobic nitric oxide reductase transcription regulator NorR
- Redox-sensitive transcriptional activator SoxR
- Anaerobic nitric oxide reductase flavorubredoxin
- Uncharacterized protein YgbA
- Ribonuclease R
- NADH oxidoreductase HCR
- Cytochrome c-552
- Hydroxylamine reductase
Sequence:
MQLTSFTDYGLRALIYMASLPEGRMTSISEVTDVYGVSRNHMVKIINQLSRAGYVTAVRGKNGGIRLGKPASAIRIGDVVRELEPLSLVNCSSEFCHITPACRLKQALSKAVQSFLTELDNYTLADLVEENQPLYKLLLVE
Protein: DNA polymerase epsilon subunit D (DNA polymerase II subunit D) (Q04603)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair. Also functions as component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:11024162}.
Interaction partners:
- Imitation switch two complex protein 1
- Protein DLS1
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit B
- DNA polymerase epsilon subunit C
- ISWI chromatin-remodeling complex ATPase ISW2
- DNA polymerase delta small subunit
- DNA polymerase alpha catalytic subunit A
- DNA polymerase delta catalytic subunit
- DNA polymerase alpha subunit B
Sequence:
MPPKGWRKDAQGNYPTTSYIKEQENITIQDLLFPKSTIVNLAREVPQQSGKKLLINKDASLALQRGATVFVNHLLLFAREIAKSQDKKSCSVDDVLSALDHIGHSALKGPVRDKLDEYQAAVEQRKKEKLDSGEVDADGDIDMGEDKENVPVEKVKEHDEIEEQGDALQDVEESSEKKQKTESQDVETRVQNLEQT
Protein: Vacuolar fusion protein CCZ1 homolog B (C0Z274)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in membrane trafficking through the secretory apparatus. In complex with MON1, acts as a guanine exchange factor (GEF) for RABG3F of the RAB7 protein family. Promotes the exchange of GDP to GTP, converting RABG3F from an inactive GDP-bound form into an active GTP-bound form. The RABG3F active form is involved in protein trafficking from prevacuolar compartments (PVCs) to vacuoles. May serve as a linker between Rab5 and Rab7 protein families in PVCs and mediate PVC maturation.
Subcellular location: Endosome {ECO:0000250|UniProtKB:F4I2S4}. Prevacuolar compartment {ECO:0000250|UniProtKB:F4I2S4}.
Interaction partners:
- Vacuolar fusion protein MON1 homolog
- Vacuolar protein-sorting-associated protein 11 homolog
- Vacuolar sorting protein 18
- Protein VACUOLELESS1
- C18orf8
- Vacuolar protein-sorting-associated protein 33 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- GDSL esterase/lipase At1g54790
- Vacuolar sorting protein 39
- Vacuolar sorting protein 3
Sequence:
MGMASMSSGTESLRLCVFDLRRGQHEGQELDKILFFYPPDLTFSTQLSVIGLSEGLITFTRLFSPEAACEVIEAERHSHVFYEAEPDIWMVMIVEKNKEIEAVWRIDALRRVLKEVHSLFVMFQGSIRALLEKEPTGGLVRSHLYPFITDYLNDLFVGKKQQLPSFRDTLKERGTVQMLTLARDAALEVQSLVGVLDSCAGTVRCHSVILFHDLLVSTTLSPDDTVDLFAFSVMRLTTNALSSGTSSWSYLRKGSGSPQISSRSTTVPPLGSGGTLPSGNGSSTGRVIRPLQHDKWSKGKDGFLVTDIWGLDATPTILIQKTQESFYLLTYQYKSLTLVLLVPIAAIVNGELDISFVKQQVIENASTKILKVEEKLSKGWGGENAYHVSGYRYLLVDNDMEVSRASPPGKVATLAKESLLALNKLREEVDTEKNRSKQEKDMEICIRAKNNTWVIARLNRGKELYMALEKASETLLDATDSVQRFSNRYCSGAFPMD
Protein: Apolipoprotein B-editing catalytic subunit 2b (C->U-editing enzyme APOBEC-2b) (D2D565)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MADKKDSKTPSKGGFIKKKEKKVEKVESKPEKEKEKSKNKDEKTTKKPEKTPENQPKNEEMPQGNGEIPEEAKGPVKNEEFELEPMELPPFEIIVGDRMNPTFFKFQFKNVEYSSGRNKTFLCYQVDIQGGAAETDGVRGYLEDEHSGSHAEEAFFQQVLAYYDKSLRYTVTWYTSSSPCVACAAKLVEILKARKALRLNIHCSRLFEWEEPEIQAGLQALVRAGCKLRMMRPVDFVYVWSTFVENEEDNFTPWEDCQDNFEYYDERLQDILK
Protein: Uncharacterized protein (Q385K4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEIERYHHIAPLLREMGPYNCDSKKQPGSTLSNSQQQQWNRDEPFHNNPDARTNEMKRTRDRGLRYTMNTASTPPPPPPETLSPIEDPLERPREEMKPTRRRYTSPAPTKSPLLSSERKRQPPTYDDQDEKPITHRIRRRQAYSAERLRPPKSNTSRGRPLSPANPRGYAGQQRARSYDRKPPPPSSRRISPQDECPNGLGKSPSSYSYFRPAATAKPAWRGVKNAQRYMDLFAPPAANPSENRSPLRRIKGGYIAPLPPPDGQSRRTLSARKRPLSPPVPGRRLTPPVDRYFPLSSGISRWGRMDNGYDSELTDASEDVHPSDDALQGYAGYDNYVVIPPRVVERERCVRNRVPTMSPARSSILVSPCRCFSSPCERSGSSDAQRMWRSPQRTQRGTRSPQVRLSPAVDDSRESEKNKSTRVKNEDLSRKNTCDAGISFPSPRQRFKPPDMVTKKGNHRETQTSPPQPSHKEVKNAALSPRTLPDEKTPRPDGTTEQPSTKSPSLPASTRGSNISVSSSEGGGKDEVPIVDISKENKSCDNSHSPDSVTHTYKNVGNKILDRKTAVSPRVHDKDKRERKGKRQKRIKRRKNNAPDSSTDQSSTSDSSSSSNFSSGTPFDESRTTERKRRHRRTHQKSGGDSHRQQKGKSALSSDNSPLRDDTAHAQVPKVYPPLTSSPQRIRKPICLQQDPVVRPQVQSASRPPFAQTVQRPVCTPEPFISFSSPPKSKTDVNGIQRSDNAGQGVPSVSIRVVPPPSPGPRREPPSPTAPKMGGVKIPYMSYLHTSSPTSVRASQLGPAQPQQTQSAASAATPRNGTGEPVWRSSGHDSVGRSNTREPHLRRKWAICGHTQIRSPPRGGRCSSQPPHLQAHEWTANGQRMTTTRQITEPPLPITPRRSGATTPQRPNGSCVKIISSPSRVAQH
Protein: Cortactin (O96046)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWKASAGHQIQATSAASAEDDDWETDPDFVNDVSEQEQRWGSKTIDGSGRTAGTIDMDKLREETEQADLDKKKQLLKDQNAGYGYGGKFGVEKDRMDKSAVGHDYQGKVGKHASQKDYSDGFGGKFGVQEDRKDKSAVGWDHVEKVEKHASQKDYATGFGGKFGVQSDRVDKSAVGWDHIEKVEKHESQKDYSKGFGGKFGVQEDRKDKSAVGWDHKEAPQKHASQVDHKVKPVIEGAKPSNLRAKFENLAKNSEEESRKRAEEQKRLREAKDKRDREEAAKKTVAENTPRTSTEAPPPKGSRAAIQTGRTGGIGNAISAFNQMQSPVSETPPARKEPIIIPKAQPVKIEVEAKEEPTASTTSAAVAPTPTVVPAREPETAPVAKATAPPPDVVPQIEVETVDTPPRSEPQSPVYVPTPQPEVLAQVQVQPEPQPQADPEPVVEEEPLYQNQAEIKAASPLPPTNGTVSEAVAPSGTATVPEEAIYANSDNLADYLEDTGIHAIALYDYQAADDDEISFDPDDVITHIEKIDDGWWRGLCKNRYGLFPANYVQVVGQNS
Protein: P-type Ca(2+) transporter (EC 7.2.2.10) (Q9UUY2)
Organism: Neurospora crassa
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MDPIASHWTPSHQHSNSLGQRSEMRQSTSFDSRDSRPTSPHNVSSPVTYRPMDPQNFLSVPGAAGRSRQNSVNSNDETRSIASSQGETVIGGSSHQGDKIGRPLSSNTSDNAQIMNDPDALKPDQGREADFEVVDNPFAYTPGQLNKMFNPKSLSAFWKLGGLAGLEKGLRTDRKAGLSMDEVEVDGRVTFDEATARPSGNPPAQPKAATETVLAKTDSHAAADHHKKHHGDDHYTSRKRVFSDNRLPEKKGKSLLELMWITYNDKVLILLSIAAVVSLAIGLYQTFGQAHKPGEAKVEWVEGVAIIVAIVIVVMVGSLNDYQKERQFAKLNKKKQDRLVKAIRSGKTVEISVFDVLVGDVLHLEPGDMIPVDGILIEGYNVKCDESQATGESDIIRKRPADEVYAAIENNENVKKMDPFIQSGARVMEGMGTYLVTSTGIYSSYGRTLMALDEDPEMTPLQSKLNVIAEYIAKLGGAAGLLLFIVLFIIFLVKLPKSQHTPAEKGQQFLNIFIVVVTIIVVAVPEGLPLAVTLALAFATTRMLRDNNLVRHLKACEVMGNATTICSDKTGTLTQNKMQIVAGTVGTTHRFGGVGSAGGLNPETPDSPTEADVTAKEVVASLDASVKELLLKSISLNSTAFEGEIDGVKSFVGSKTETALLEFAKEHLAMGPIAEERANAKILHLIPFDSGRKCMGVVVALDNGKARLYVKGASEIMLEKCTQILRDPSNGITAGPLTQENRETVLKLIETYARNSLRTIGIIYRDFAHWPPAKARRTGEDKEEIVFEDICSQMTFVGMVGIKDPLRPGVPEAVQLCQKAGVVVRMVTGDNKITAEAIAKDCGILQPNSLVMEGPEFRNLSKAKQEEIIPRLHVLARSSPEDKRILVKRLKDMGEIVAVTGDGTNDAPALKMADVGFSMGIAGTEVAKEASAIILMDDNFNSIVKALKWGRAVNDAVKRFLQFQLTVNVTAVILTFISAVSNKEQDSVLTAVQLLWVNLIMDTLAALALATDPPADSVLDRKPERRGSGIISTTMWKMIIGQAIYQLAITLLIYFGKQGVLPNYDDNVTDDQIQTLVFNTFVWMQIFNQWNNRRLDNNFNIFEGLTKNLFFLGISAIMMGGQVLIVFVGGQAFSIAKEKQTGAMWAYALILGFISIPVGMIIRLIPDSLFERMVPEYIKRRANKTPDLTVSDDERFEYYPPAFAEVRDELAFLKQFKGGRINNLKFAMKHPRETFMPKRSASHSRSNSKSNSINVPMTPIRKDSTGGAPSIAPPTPDSRRRSRSTRSRSNSALGASMVMTGIIAGSVAAGWAPSPVERRPDSDFGLFPPKSSPHAESSQSEVQPSQRSLTPSINEEQETPDIVPSIVEQTVPILSVPKPPGQKSA
Protein: Uroporphyrinogen decarboxylase (UPD) (URO-D) (EC 4.1.1.37) (Q9USJ5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uroporphyrinogen-III synthase
- Protoporphyrinogen oxidase
- Probable oxygen-dependent coproporphyrinogen-III oxidase
- Ferrochelatase, mitochondrial
- Porphobilinogen deaminase
- Probable uroporphyrinogen-III C-methyltransferase
- Delta-aminolevulinic acid dehydratase
- 5-aminolevulinate synthase, mitochondrial
- Putative holocytochrome-c synthase
- Biotin synthase
Sequence:
MYPKMKNDLILRAAKGEEVERPPVWIMRQAGRYLPEYHKLRAKQSFFEMCQTPETACELTLQPVTRFKGLLDAAIIFSDILVIPQALGMQVVMLEQKGPHFPKPLVVPEDIDLLEKTPNISAKLGYVMDAISLTREKLDGQVPLMGFSGAPWTIMAYMIEGGGSKTFAKAKSWLFRYPEASHKLLKIITDATVSYLIQQVYAGAQLLQIFDSWAGELSPEDFTEYAYPYLVRICQEVKQHLKKKKRDEVPMIVFAKGAWYAIDQLCDSGYDVIGLDWTVSPKEAVRIRGNRRVTFQGNLDPNILYGTREIIEARTKEMIQDFGGGKQGYIINLGHGITPGVNPDDVRFFLEKCHQYGSA
Protein: Kazachoc, isoform F (A0A0B4LHE0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MPDRFQVTKADEDTALDYNQDESASGKLLGDIHDETLDSGDIHRAEENQKSSIDPNLYLYDDDLETRPHISTFISSIANYENTIPAATDPDAKPAAPSARMGTLIGVFLPCIQNIFGVILFIRLTWVVGTAGAVCGFLIVLTCCCVTMLTAISMSAIATNGVVPAGGSYFMISRSLGPEFGGAVGMLFYTGTTLAAAMYIVGAVEIVLTYMAPWASIFGDFTKDADAMYNNFRVYGTLLLIFMGLIVFLGVKFVNKFATVALACVILSIIAVYVGIFDNIHGNEKLYMCVLGKRLLKDIPLENCTKEDSFLRDIYCPDGKCEEYYLANNVTKVKGIKGLASGVFYDNIFPSFLEKGQFISYGKSAIDIENTSGESYNQIMADITTSFTLLIGIFFPSVTGIMAGSNRSGDLADAQKSIPIGTICAILTTSTVYLSSVMFFAGTVDNLLLRDKFGQSIGGKLVVANIAWPNQWVILIGSFLSTLGAGLQSLTGAPRLLQAIARDEIIPFLAPFAKSSKRGEPTRALLLTIVICQCGILLGNVDLLAPLLSMFFLMCYGFVNLACAVQTLLRTPNWRPRFKFYHWSLSLIGLTLCISVMIMTSWYFALIAMGMAIIIYKYIEYRGAEKEWGDGIRGMALTAARYSLLRLEEGPPHTKNWRPQILVLSKLNDNLLPKYRKIFSFATQLKAGKGLTICVSVIKGDHTKITNKAVDAKATLRKYMTDEKVKGFCDVLVAQQIGEGLSSVIQTIGLGGMKPNTVIIGWPYSWRQEGRNSWKTFIQTVRTVAACHMALMVPKGINFYPESNHKIGGNIDIWWIVHDGGLLMLLPFLLKQHRTWRNCKLRIFTVAQIEDNSIQMKKDLKTFLYHLRIEADVEVVEMNNSDISAYTYERTLMMEQRNQMLRALGLNKKENSKVVQTIVDHHYDATKTASKVRFADPTIEETQHHDSQNDEKRNSIDLDGPENADTPETTSNKDESTEKADGDFKSSVKPDEFNVRRMHTAIKLNEVIVEKSQDAQLVIMNLPGPPREVRAERERNYMEFLEVLTEGLEKVLMVRGGGREVITIYS
Protein: Probable membrane protein (O05589)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Large ribosomal subunit protein uL4
- Signal recognition particle receptor FtsY
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL3
Sequence:
MSISCRVREGFVMRLAIVGTAAAAAIGGTLAVAPLTLSTPERVAGGTCSAGQQCDRLAAVLMPDTATPSGPAAAEHAVPAPFEPVADTIAPGLVPRPGVPAAAAVPRVGPPAVPGLPNIPGAAGPALPPPPALPNLAAPSVPGVGIPGIGIPGIGIPGIGIPGVPDPITGVNTAAAVVNGVLGVGGTAAGVVTASAVAVTYLVLAVNALESSGILPTARGTASTVASLLLPGAQSAAAALPAVGLPALPGVTPASLLAMAAAAGLPGVGFPSLPGVSPTDLMAMAAAAGLPTSLPGLAGMSPAELTALVAGGLPMLAAAGLPAGLAGVDPATLAAALPALAAGGLPPGLPALPGVDPAALAAALPALAAGLPALPAGLPPLPAVPALPAPPPLPGPPPLPALPSRLCTPGFGPIGVCIP
Protein: Regulatory protein RecX (Q5F7W3)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Function: Modulates RecA activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01114}.
Interaction partners:
- Protein RecA
- DNA repair protein RecO
- DNA repair protein RadA
- Recombination-associated protein RdgC
- Recombination protein RecR
- ATP-dependent DNA helicase RecG
- Crossover junction endodeoxyribonuclease RuvC
Sequence:
MKPQKSLRARAMDILSRQEVSRIGLKRKLAPHAESEEELENVLNEFAERNWQSDLRYAEAYIRSKSRKHGSLRLKQALAQQGIDEKTSRNLLPDRSSEKQAAIAVLRKKFKHPAANLKEKQKQARFLAYRGFDADTVQTALKHAWDENWEDSC
Protein: NAD-capped RNA hydrolase NudC (DeNADding enzyme NudC) (EC 3.6.1.-) (NADH pyrophosphatase) (EC 3.6.1.22) (O86062)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
Interaction partners:
- Nicotinate phosphoribosyltransferase 1
- Nicotinate phosphoribosyltransferase 2
- Nudix hydrolase domain-containing protein
- NAD-dependent protein deacylase 1
- Nucleoside triphosphate pyrophosphohydrolase
- 5'-nucleotidase SurE
- NH
- Nudix hydrolase domain-containing protein
- NAD-dependent protein deacylase 2
- Soluble pyridine nucleotide transhydrogenase
Sequence:
MAGEFRWQAGRPATAQVGGWVLAHCQQRFLQDDNGLLFPREWLKRQELPLLAEHGVGHWQGEPVYVLELDEPIELPGMAWAPLRQFMLHGDFDQFCMLGYASQIGIWARHNRFCGNCGTRMQAQDHERVMQCPQCGLHQYPRLSPSMIVLVTRGDEVLLARSPRFVPGVYSTLAGFVEAGESVEQCVVREVREEVGVEVANLEYIGSQNWPFPHSLMLGFHAEYVSGEIVPQEDEIEDAQWFSLDALPPLPAQRSIARHLIDLYLARRSGAAEPVLPG
Protein: Indolethylamine N-methyltransferase (Indolamine N-methyltransferase) (EC 2.1.1.49) (EC 2.1.1.96) (Aromatic alkylamine N-methyltransferase) (Amine N-methyltransferase) (Arylamine N-methyltransferase) (Thioether S-methyltransferase) (TEMT) (O95050)
Organism: Homo sapiens (Human)
Function: Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds (By similarity). Catalyzes the N-methylation of tryptamine and structurally related compounds.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Amine oxidase [flavin-containing] B
- Aromatic-L-amino-acid decarboxylase
- Indoleamine 2,3-dioxygenase 2
- Amine oxidase [flavin-containing] A
- Indoleamine 2,3-dioxygenase 1
- Serotonin N-acetyltransferase
- Diamine oxidase [copper-containing]
Sequence:
MKGGFTGGDEYQKHFLPRDYLATYYSFDGSPSPEAEMLKFNLECLHKTFGPGGLQGDTLIDIGSGPTIYQVLAACDSFQDITLSDFTDRNREELEKWLKKEPGAYDWTPAVKFACELEGNSGRWEEKEEKLRAAVKRVLKCDVHLGNPLAPAVLPLADCVLTLLAMECACCSLDAYRAALCNLASLLKPGGHLVTTVTLRLPSYMVGKREFSCVALEKEEVEQAVLDAGFDIEQLLHSPQSYSVTNAANNGVCFIVARKKPGP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (R4GN33)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSEESDMDKAIKDAPVKLCDFGFAKIDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDSVYIHDHENGAEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDTLQSFSWNGRGFTDKVDRLKLAEIVKQVIEEQTTSHESQ
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q57WF0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Uncharacterized protein
Sequence:
MCSCCCEPPVGQWIDIYGGPVRPRRSGFECPLDALQVIAWSVIVTLATLHFTLHVPMLDSLLVCIISPISGFLTFTTAALKLALSCSRIEDPIVFATDVPRYAQEELVQEAAPPGTEPCVFCRRFVILGSKHCSVCDKCVPGFDHHCRWLNTCVGEGNYVMFCCFMGTAWCSIALVFGVGIYVISNAFIHKQDFSDRLKERFGVSSYVTYMVFLFLTLALSAAGLAALGNLIVFHINLCLTRRTTYEHVLSKRAKRREKLSKQSKPLVATDRSKGPCGCLAIQKRRDFRRYKKNPAGSSGAVPDIGVHNLGDNATDGAYPSRDTSQPGETCEIRETTSDHKGGVRLERETHDNEPIA
Protein: Proline dehydrogenase (EC 1.5.5.2) (F1MAR6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Pyrroline-5-carboxylate reductase 3
- Pyrroline-5-carboxylate reductase 2
- Pyrroline-5-carboxylate reductase
- Prolyl 4-hydroxylase subunit alpha-1
- Prolyl 4-hydroxylase subunit alpha-3
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Prolyl 4-hydroxylase subunit alpha 2
- Ornithine aminotransferase, mitochondrial
- Cytosol aminopeptidase
- Catechol O-methyltransferase
Sequence:
MALKRVFLLRSVAPRVAALSTKPRAQEQPPANPEALRGCGAAEAVRPPVPAVDFTNTQEAYRSRRSWELARNLLVLRLCASPVLLAHHEQLFQVARKLLGQRMFERLMKMTFYGHFVAGEDQESIRPLIRHNKAFGVGFILDYGVEEDLSPEEAERKEMESCTSEAERDGSGANKREKQYQVHPAFGDRRDGVISARTYFYASEAKCDNYMENLLQCIEASGGASDGGFSAIKLTALGRPQFLLQFSDVLTRWRQFFHQMAAEQGQAGRPAVDTKLEVAVLQESIAKMGISSRAEIERWFTPETLGVSGTVDLLDWNSLIDSRTQLSRHLVVPNVQTGQLEPLLSRFTEEEEQQMKRMLQRMDVLAKRAREAGVRLMIDAEQSYFQPAISRLTLEMQRRFNVDKPFIFNTFQCYLKDAYDNVTIDMELSRREGWCFGAKLVRGAYMAQERARAVEIGYEDPINPTYEATNAMYHRCLNYVLEELKHSTKAEVMVASHNEDTVSFTLCRMKELGLHPADGQVCFGQLLGMCDQISFPLGQAGFPVYKYVPYGPVMEVLPYLSRRALENSSIMKGAQRERQLLWQELCRRLRTGSLFHHPA
Protein: Ribosome maturation factor RimP (P0A8A8)
Organism: Escherichia coli (strain K12)
Function: Required for maturation of 30S ribosomal subunits, probably at a late stage of ribosomal protein binding, while Era is associated and after RimM.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- 30S ribosome-binding factor
- Transcription termination/antitermination protein NusA
- Small ribosomal subunit protein uS12
- Ribosome maturation factor RimM
- Translation initiation factor IF-2
- Small ribosomal subunit protein uS10
- Ribosomal RNA small subunit methyltransferase A
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein uS7
Sequence:
MSTLEQKLTEMITAPVEALGFELVGIEFIRGRTSTLRIYIDSEDGINVDDCADVSHQVSAVLDVEDPITVAYNLEVSSPGLDRPLFTAEHYARFVGEEVTLVLRMAVQNRRKWQGVIKAVDGEMITVTVEGKDEVFALSNIQKANLVPHF
Protein: Probable zinc metalloprotease EGY2, chloroplastic (EC 3.4.24.-) (Protein ETHYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN 2) (Q9FFK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable membrane-associated metalloprotease that may be involved in chloroplast development.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Rhodanese-like domain-containing protein 4A, chloroplastic
- RHOMBOID-like protein 1
- Small ribosomal subunit protein uS10z/uS10x
- Small ribosomal subunit protein eS19x
- RHOMBOID-like protein 10, chloroplastic
- Adenine nucleotide alpha hydrolases-like superfamily protein
- Signal peptide peptidase
- Serine carboxypeptidase-like 26
- RHOMBOID-like protein 2
- Alpha/beta-Hydrolases superfamily protein
Sequence:
MNLAVASFRGNFGVLSQCSSCCSLQFQPFVAATSSLNFGQTGTSRRKKDLKLERVFRKRETLVRVTETQTEPEGNDDEDNKEGKESSADDPPTKIPTELNSQSTVVNEAPGNEEENKAQFSSQDGDKLEVSSGSPLPGVNVSIIIHVIYKDDSIMFSGCLSFIKSCCEQPLQLDDSMRLPKETIDILRGQVFGFDTFFVTSQEPYEGGVLFKGNLRGKPATSYEKIKTRMENNFGDQYKLFLLTNPEDDKPVAVVVPRRSLEPETTAVPEWFAAGSFGLVALFTLFLRNVPALQSDLLSAFDNLELLKDGLPGALVTALVLGVHELGHILVANSLGIKLGVPFFVPSWQIGSFGAITRIKNIVAKREDLLKVAAAGPLAGFSLGLILFLIGLFVPPSDGIGVVVDASVFHESFLAGGIAKLLLGDALKEGTSISLNPLVIWAWAGLLINGINSIPAGELDGGKIAFSIWGRKTATRLTGASIALLGLSALFSDVAFYWVVLIFFLQRGPIAPLAEEITVPDDKYVSLGILVLFLSLLVCLPYPFAFTGNEAMMIGL
Protein: Ferrochelatase (EC 4.98.1.1) (F4IMT3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000256|RuleBase:RU000607}.
Interaction partners:
Sequence:
MNCPAMTASPSSSSSSSYSTFRPPPPLLPQLSNDSQRSVVMHCTRLPFEAFAATSSNRLLGKHSLPLRAALVTSNPLNISSSSVISDAISSSSVITDDAKIGVLLLNLGGPETLDDVQPFLFNLFADPDIIRLPPVFQFLQKPLAQFISVARAPKSKEGYASIGGGSPLRHITDAQAEELRKCLWEKNVPAKVYVGMRYWHPFTEEAIEQIKRDGITKLVVLPLYPQFSISTSGSSLRLLERIFREDEYLVNMQHTVIPSWYQREGYIKAMANLIQSELGKFGSPNQTCFKPKYMLQVVIFFSAHGVPLAYVEEAGDPYKAEMEECVDLIMEELDKRKITNAYTLAYQSRVGPVEWLKPYTEEAITELGKKGVENLLAVPISFVSEHIETLEEIDVEYKELALKSGIKNWGRVPALGTEPMFISDLADAVVESLPYVGAMAVSNLEARQSLVPLGSVEELLATYDSQRRELPAPVTMWEWGWTKSAETWNGRAAMLAVLALLVLEVTTGKGFLHQWGILPSL
Protein: Glucan endo-1,3-beta-glucosidase 14 (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase 14) ((1->3)-beta-glucanase 14) (Beta-1,3-endoglucanase 14) (Beta-1,3-glucanase 14) (Q9ZQG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, cell wall {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted, cell wall {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.
Interaction partners:
- ATP-dependent DNA helicase
- RBR-type E3 ubiquitin transferase
- SEC1 family transport protein SLY1
- F-box/kelch-repeat protein At1g74510
- Leucine-rich repeat protein 1
- Zinc knuckle
- 3-ketoacyl-CoA synthase 11
- Actin-related protein 4
Sequence:
MATHSLSFFFRVLLLLFLTLSERIKGQGVGINYGQIANNLPSPARVAVLLRSLNITRVKLYDADPNVLFSFSNSQVDFMIGLGNEYLQNMSTDPTKAQDWLQQRLEPHISKTRITSIVVGNEIFKTNDHVLIQSLLPAMKSVYAALTNLGLEKQVTVTSAHSLDILSTSYPPSSGSFKEEFIQYLQPLLDFHSQIESPFLINAYPFFAYKDSPKEVPLEYVLFQPNQGMVDPNTNLHYDNMLFAQVDALYSAIKTLGHTDIEVRISETGWPSKGDENEIGASPENAALYNGNLLKLIQQRKGTPAKQSVPIDVYVFALFNENLKPGPVSERNYGLFYPDGKPVYNVGMQGYLPDIIYTSRATTIKILNLWRVVMGLAVAWFILDMGDKMRMR
Protein: Flagellar biosynthetic protein FliQ (P35535)
Organism: Bacillus subtilis (strain 168)
Function: Role in flagellar biosynthesis.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- FlaA locus uncharacterized protein YlxG
- Flagellar biosynthetic protein FliP
- Flagellar biosynthesis protein FlhA
- Flagellar basal-body rod protein FlgC
- Flagellum-specific ATP synthase
- Flagellar motor switch protein FliM
- Flagellar biosynthetic protein FlhB
- Flagellar biosynthetic protein FliR
- Flagellar M-ring protein
- Probable flagellar assembly protein FliH
Sequence:
MSSEFVISMAEKAVYVTLMISGPLLAIALLVGLIVSIFQATTQIQEQTLAFIPKIVAVLLALIFFGPWMLSTILSFTTELFSNLNRFAG
Protein: DNA (cytosine-5)-methyltransferase 3-like (Q1LZ50)
Organism: Rattus norvegicus (Rat)
Function: Catalytically inactive regulatory factor of DNA methyltransferases that can either promote or inhibit DNA methylation depending on the context. Essential for the function of DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic domain. Acts by accelerating the binding of DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases (By similarity). Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by recruitment or activation of DNMT3 (By similarity). Plays a key role in embryonic stem cells and germ cells. In germ cells, required for the methylation of imprinted loci together with DNMT3A. In male germ cells, specifically required to methylate retrotransposons, preventing their mobilization. Plays a key role in embryonic stem cells (ESCs) by acting both as an positive and negative regulator of DNA methylation. While it promotes DNA methylation of housekeeping genes together with DNMT3A and DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter of bivalent genes. Interacts with the EZH2 component of the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B with the PRC2/EED-EZH2 complex, leading to maintain low methylation levels at the promoters of bivalent genes. Promotes differentiation of ESCs into primordial germ cells by inhibiting DNA methylation at the promoter of RHOX5, thereby activating its expression (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA
- DNA
- Histone H3.3
- Histone H3
- Histone H3
- Histone H3
- Histone H3
- Histone H3.1
- Histone deacetylase 1
- Similar to H3 histone, family 3B.
Sequence:
MGSRETPSSCSKTHETLNLETPESSSTDPDSPLEEQWPKSAPDLKEEDSMDMVLEDSKEPLTPSSPPTGREVIRYEVNVNQRNIEDICLCCGSLQVYAQHPLFEGGICAPCKDKFLETLFLYDEDGHQSYCTICCSGHTLFICESPDCTRCYCFECVDILVGPGTSERINAMACWVCFLCLPFSRSGLLQRRKKWRHQLKAFHDREGASPVEIYKTVSAWKRQPVRVLSLFGNIDKELKSLGFLESSSGSEGGTLKYVEDVTNVVRREVEKWGPFDLVYGSTQPLGYSCDRCPGWYMFQFHRILQYARPRQDSQQPFFWIFVDNLLLTEDDQETTVRFLQTEAVTLQDVRGRVLQNAMRVWSNIPGLKSKHADLTPKEEQSLQTQVRTRSKLAAQKVDSLVKYCLLPLREYFKYFSQNSLPL