wanglab/gogpt-training-data huggingface dataset:
Protein: Xanthone prenyltransferase A (EC 2.5.1.-) (Q5AY46)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone. Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB. XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring. Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC.
Interaction partners:
Sequence:
MLKHSSAATKENDSPKLKVLDIVSKLEPSLDHSHTHWWKLTSPQLALMLEAADYSIEKQFETLLFHYHWVVPYLGPKPDADGNFKWRSLVSDVGIPLEYSWKWDTATSGPDVRLTIEPINELSGTRVDPLNQAPSLELLHRLAEILPRLDVSWASHFLSTFYDHDKLKYIKESESETGMPLRSTMLVCFEFGRNGITTKTYMSPRKLGQQGFAPLSDYHSAIAALGPSCALDAVTEFLNNSPEGPHLSPFMLAVDNIIPCSSRLKLYFATPRTSYNSIREVLTLGGRLSTVTLESKLRAIHELVKAIMPFPPDLPDDADIPFPEQVLSPTVQDLAESSDMANQRPAFVAGYQYYFDIAPGASLPDIKFYIPIRKAQMNDQAVATGLTNWMRAQGRGAFCNAYTRVLEGLAGGRDLSKCHGLHTHICVMLKGNGEFDVTSYLAPGCK
Protein: Intermembrane phospholipid transport system ATP-binding protein MlaF (EC 7.6.2.-) (P63386)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19383799}; Peripheral membrane protein {ECO:0000305|PubMed:19383799}; Cytoplasmic side {ECO:0000305|PubMed:19383799}.
Interaction partners:
- Intermembrane phospholipid transport system permease protein MlaE
- Intermembrane phospholipid transport system binding protein MlaB
- Intermembrane phospholipid transport system binding protein MlaD
- Intermembrane phospholipid transport system binding protein MlaC
- Intermembrane phospholipid transport system lipoprotein MlaA
- Putrescine export system ATP-binding protein SapD
- Nickel import ATP-binding protein NikD
- Probable D,D-dipeptide transport ATP-binding protein DdpD
- Oligopeptide transport ATP-binding protein OppD
- Dipeptide transport ATP-binding protein DppD
Sequence:
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRVRQFLDGIADGPVPFRYPAGDYHADLLPGS
Protein: phosphoribosylglycinamide formyltransferase 1 (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (A0A1D8PGS7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Bifunctional aminoimidazole ribotide synthase/glycinamide ribotide synthase
- Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase
- Phosphoribosylformylglycinamidine synthase
- Amidophosphoribosyltransferase
- Adenylosuccinate lyase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Methylenetetrahydrofolate dehydrogenase [NAD
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase
- Mis12p
Sequence:
MTLNITVLISGSGTNLQALIDAQKNNQLKGQITQVISSSETAYGLKRAEQACIPTKTHVLKTYYKGTTKDQTDVRKQRREQFNVELANLLINGQIQGSDASYTKPDLIVCAGWMLILSPSVLQPLEKAGITIINLHPALPGAFDGTHAIDRCWKAGQDGEITKGGVMIHRVIAEVDRGTPILVKELDLIKGESLEEYEERVHKVEHVAIVEGTNIILEELSK
Protein: Kelch-like protein 41b (Kelch repeat and BTB domain-containing protein 10b) (F1QEG2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in skeletal muscle development and maintenance.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O60662}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A2AUC9}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60662}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60662}.
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- Cullin 3
- Rho guanine nucleotide exchange factor
- D-arabinitol 2-dehydrogenase [ribulose-forming]
- Mohawk homeobox b.
- Bardet-Biedl syndrome 1.
- Bardet-Biedl syndrome 9.
Sequence:
MDPKAIKEELRLFQSTLLQDGLKELLNENKFVDCTLKIGDRCFPCHRLIMAACSPYFRELFFSEDGKEKDIGKEVVLDDVDPNIMDMILQYLYSAEIDLVDDNVQEIFAVANRFQIPSVFTVCVNYLQQKLSMANCLAVFRLGLVLSVPRLAIAARDFIADRFETVSSEEEFLQLAPHELLALIGGDMLNVEKEEVVFESVMKWVRNDKANRVKSLAEAFDCIRFRLLPEKYFREKVETDDIIKGDPELLKKLQLVKDAFKGKLPEKKPKEKKEGEVNGEEEGEEMLPGFLNDNRRLGMYGRDLIVMINDTAAVAYDVVENECFLAAMAEQVPKNHVSLCTKKNQLFIVGGLFVDEESKESPLQCYFYQLDSFSSDWRALPPMPSPRCLFNLGESENLLFAIAGKDLQTNESLDSVMCFDTERMKWSETKKLPLHIHGHSVVSHNNLVYCIGGKTDDNKALSKMFVYNHKQSEWRELASMKTPRAMFGAVVHKGKIIVTGGVNEDGLTALSETYDFDTNKWDTFTEFPQERSSVNLVSSGGNLFSIGGFAIVELEDKNIGPSEITDIWQYEEDKKTWSGMLREMRYASGSSCVGMRLNAARMPKL
Protein: Krueppel-like factor 8 (Basic krueppel-like factor 3) (Zinc finger protein 741) (O95600)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor and activator. Binds to CACCC-boxes promoter elements. Also binds the GT-box of cyclin D1 promoter and mediates cell cycle progression at G(1) phase as a downstream target of focal adhesion kinase (FAK).
Subcellular location: Nucleus {ECO:0000269|PubMed:16617055}.
Interaction partners:
- C-terminal-binding protein 1
- C-terminal-binding protein 2
Sequence:
MVDMDKLINNLEVQLNSEGGSMQVFKQVTASVRNRDPPEIEYRSNMTSPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLIGGDGKNAGSVKVDPTSMSPLEIPSDSEESTIESGSSALQSLQGLQQEPAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM
Protein: 65 kDa invariant surface glycoprotein (Q587F0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- T. brucei spp.-specific protein
- Retrotransposon hot spot
Sequence:
MMKYLLVFAIITTRIPVLLVIGSEDNRVPGDKKLTKEGAAALCKMKHLADKVAEKGAEDLKKKTQNFAGFIEFEQEKVDNWLEKLRNRKQYSDGYAKLSDSDVEKVKEIFDKAKDGITKQLPEAEKEAREAERLYDEVKKAAQDARGQDLDDDTAKSTGLYRVLNWYCITKDNNKDITHNCDDGIKFRDHYLSVNRSAIDCSSTGYKEDYDWSANALQSALNDWENVKPKEVKPESGGNDVCKKDESSESHPCTMTGGWQTHYKDSILKLKELEDAHKRGKAAHDAMLGYANTAHAANTKVEQEKPLAEVITAAKDAGKKGAKIIIPAAAPATSTDSTKSEDSAPAEHVDRGIATNETQVEVGIDADFDSLLEAAEAAEVKSRHQRTAMIILAVLVPAIILAAAVAFFIMVKRRRNSSQDVDTGKAEGGVSSVKVVM
Protein: ComD (Major facilitator superfamily protein) (Q86M88)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Rab GTPase domain-containing protein
Sequence:
MSNANNNNYNHNNNKETQSGNNNNNNNNNNNNNNNNKNKNNNNNNIQNENNFNSPNDGENINNNMNNSHNNNHNTSDRISQYSSSEHNIKKEHNRNGSNTSIISASNFNNFMDENSTENNRLSQRPAPAILNIIQSLIKNPTDDVNGSKRNTLEGIVKKYPSFKSLDGSSISLSQSQSSMDSSPLTTSNSKSPNHHPQPSPNVLSRSSCAIDSPSLNSTQLQPNTTTTTTTSSSLNKNNNNKNNNNNNNNNNNNNNNNNNNNNTIDEGGCSNDKSPSSSSYQVNNNNKPKNNISRLELPTSLRSSNNAMDSSAAPSSNTSRPQFSQPQSEVPSSCSPPGNGLLRGAIEEKEESTDNFEKNDNIINDENNNNQSTSVTVNICENQLENNNNNINSPPQQQSPSTVNDGDGGGCAAGDSFDTTESDHSISGRRMTKMFSDAPIKEYQVTTIEDPLYSLTTTTVNNVSINENTPSSPSITPIKLKQPKPDEDEELSIKNKKQASRQTVQLEMGTFDLDGKPNEQIVGSNSSDETFEGVDVVGIDSDKIVGRDRAFSSAMKESEVVIGEQTVNVDLTQEDMDNINFQPPNTDPPPPQPLTSKQILIIFSGLMVSLFLSSLDMTIVATALPAIVADLHGLEQLPWVVTIYLLTSTSVSPLFGKFSDIFGKKILLLSSLIIFLIGSLLCAVATTMNMLILARAIQGIGGGGLMSAVMIVMAEIVPLRDRGKYQGLLGAVYAVSSVVGPLMGGTFTDNITWRWAFWINLPLGAVAFVVVFFALKIPQKVIPWREGIKKVDVLGSLSLVAATISFLLALNWGGIDYPWTSPIIICLFIGTALFVALFIVNEKYWFNVHPIIPLDLFKTRNYVLCSIGSFLLGFVMFGVIYYIPLYFQYVRGATATASGLQLLPTMLGIVLFGAISGLLITRFGHYKSYPIIGMGFMMIGIYLISLWNHQSTQNEFIGYQCFIGVGIGLTMQILVLIVQNSVNVIYISISTATVSFFRTIGGVVSVSVFSAILNQQFSQNLNGLLEKDAFVLGGMSPHNFNMENIKHIENPIHQQQIRDAYQSALSIVFLSAAPFAGLGCILILFVKNQKLRTTMITQKDKDQEILKKNLEKLQKELHNDDSIDINEEYDENENNENNERSDVNINEIENNNNNTNNDIELDIQTPPRKSTIST
Protein: Putative plasmid segregation protein (A0A0A0PKY3)
Organism: Bacillus phage Bp8p-C
Interaction partners:
Sequence:
MITVEHVDIKKQPFGSICDLVLDESGNLSNREVAKGFNVVVDVGARTLNILTVDGLVEQPELSIQTNDGMFTAYKQVGSHLETSLGATIPDGKYPQIIAAREFKGRNIDPLIDAAYATQANNIMNVLDKVLINSWAFVQCIVFTGGGSELLKPYLLPRVPNNVEAVVLDRYANARGLRKYGMRQAKKNIKRADHYGG
Protein: Kolavenyl diphosphate synthase TPS5, chloroplastic (EC 5.5.1.29) (Terpene synthase 5) (VacTPS5) (A0A2K9RG07)
Organism: Vitex agnus-castus (Chaste tree)
Function: Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase that produces kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSLAYSQATSLLLSSTTRGGVPSLMHIPATNSPARINTGATPFWKLPFPARPLRQYKSITRARNQVILTAEKSVDVDTEKNTHHQKATAETTRELVERIRWMLQNMDDGELSVSPYDTAWVALVEDIGGSGRPQFPTSLEWISNNQYPDGSWGDRKFLFYDRILNTLACVVALKTWNMHPDKCEKGLKFIKENIHSLENENEEYMPVGFEVAFPSLIETAKKLGIEIPDDSPGMKDIYAKRHLKLKKIPMDLLHKMPTSLLFSLEGMKGLDWQKLLNLRFEGSFLSSPSSTAYALQHTKDELSLQYLLKAIKKFNGGVPNAYPVDMFEHLWSVDRLQRLGISRYFEPEIEECMKYAYRYWTDKGICWARNTNVQDVDDSSMGFRLLRLHSFPVTIDAFKQFEKGGEFCSIPGQSTHAITGMYNIFRASQVLFPGDHILADARKYSAKFLHQKRVNEAIVDKWIITKDLPGEVGYALDVPFYASLPRLEARFFLEHYGGDDDVWIGKTLYRMLYVNCDTYLELAKLDYNVCQAVHQHEWTNIRRWYKDCSVGEFRLAERSLLRAYYIAASTVFEPERSGERLAWAKTAILLETILSQKLHSEEKHTVVDEFKHGSISISGNGRRHQTRISLAETLIYTVNQLSSDIKQAHGRDIHQQLHHAWQKWLTTWEGRGNLGEAEAELLVRTLHLSSGLDESWFSHPKYQQLLEVTSKVCHQLRLFQNRKMHDPKGCTIDLVTGTTFQIEAGMQELVKLVFTKSSEDLDAHTKQSFFAIARSFYYTAYCDPEAIESHVDKVLFDKVV
Protein: Peptidyl-prolyl cis-trans isomerase FKBP2 (PPIase FKBP2) (EC 5.2.1.8) (13 kDa FK506-binding protein) (13 kDa FKBP) (FKBP-13) (FK506-binding protein 2) (FKBP-2) (Immunophilin FKBP13) (Rotamase) (P26885)
Organism: Homo sapiens (Human)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase B
- Cytochrome c oxidase subunit 8A, mitochondrial
- Ferritin heavy chain
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
- Peptidyl-prolyl cis-trans isomerase A
- Neuroblast differentiation-associated protein AHNAK
- Fos-related antigen 1
- Splicing factor 1
- Glycogen phosphorylase, muscle form
- Mitogen-activated protein kinase kinase kinase 11
Sequence:
MRLSWFRVLTVLSICLSAVATATGAEGKRKLQIGVKKRVDHCPIKSRKGDVLHMHYTGKLEDGTEFDSSLPQNQPFVFSLGTGQVIKGWDQGLLGMCEGEKRKLVIPSELGYGERGAPPKIPGGATLVFEVELLKIERRTEL
Protein: Neuroguidin (A0A8I6ATG6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MIRVTWTGWGRHDPGIALAAPPDSLAETKSVSHCLPQGLSLLEVKDQLLLMYLMDLSHLILDKASGGSLQGHPAVLRLVEIRTVLEKLRPLDQKLKYQIDKLVKTAVTGSLSENDPLRFKPHPSNMMSKLSSEDEEENEAEEDQSEASGKKSVKGASKKYVPPRLVPVHYDETEAEREQKRLEKAKRRALSSSVIRELKEQYSDAPEEIRDVRHPHVTRQSQEDQHRINYEESMMVRLSVSKREKGLRRRASAMSSQLHSLTHFSDISALTGGTAHLDEDQNPVKKRKKMPKKGRKKKGFRRRW
Protein: Myocardin related transcription factor A (A0A0G2K3Y9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
VDFSSVVCLPPSVIAVNGLDGGGAGENDEEPVLLSLSAAPSPQSEAVANELQELSLQPELTLGLHPGRNPNLPPLSERKNVLQLKLQQRRTREELVSQGIMPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERSELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEALIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLESRASDLLPSATSISPTQVLSQLPMAPDPGETLFLAEQPPLPPPPLLPPSLTSGSIVPTAKPAPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDKGAPAMDSSYAKILQQQQLFLQLQILNQQQQQQQQQHYNYQAILPAPPKPSGETPGSSAPTPSRSLSTSSSSSSGTPGPGGLARQNSTALAGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQVSPAPGAPKAPATTSVLSKAGEVVVAFPAALLSTGSALVTAGLAPAEMVVATVTSNGMVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDAFGEMVTSPLTQLTLQASPLQIVKEEGARAASCCLSPGARAELEGLDKDQMLQEKDKQIEELTRMLQQKQQLVELLRLQLEQQKRAQQPAPASSPVKRESSFSSCQLSCQPQGAARAFGPGLVVPTTNHGDAQAPAPESPPVVVKQEAGPPEPDLAPASQLLLGSQGTSFLKKVSPPTLVTDSTGTHLILTVTNKSADGPGLPTGSPQQPLSQPGSPAPGPPAQMDLEHPPQPSFATPTSLLKKEPPGYEETVTQQPKQQENGSSSQHMDDLFDILIQSGEISADFKEPPSLPGKEKSPPAEAYGPPLTPQPSPLSELPQAAPPPGSPTLPGRLEDFLESSTGLPLLTSGHEGPEPLSLIDDLHSQMLSSSAILDHPPSPMDTSELHFAPEPSSGMGLDLAVGHLDSMDWLELSSGGPVLSLAPLSTTAPSLFSMDFLDGHDLQLHWDSCL
Protein: Retrotransposon hot spot (RHS) protein, putative (Q584M5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRANSPAAPQGNNENQQVADNIEAAMRRPRDENVPPPAAAAAQPPQIRQRTEEGPNWTMNSSIEDVLLQRYEGLRDMTLHDFLLKKFFNTYDTENVAMDVFVQSPEDYILDAGILGRIRRLYQFEEYKELYNQFSEMKRKARYLDEKEIYYLSQWEEKGRGEIREFVGPMARGRLDGALEVAKRAEKRAAQTAGGAVELEGVYESIYNAKWSYVMSGYNEEPLGMKVFDGKPQCIWTEAEVDITPDPANVDAEIEERPDGLEIFVLTSEKGWPYNGFALDDAEICLENFKHVYIRREIMRVWYIIQRGLQGRWVEKAEITPRHIVIGTPGIGKSYGVGSFLLHSLLHFNDGMLDVVAYFVGKIAYLIYNKKPGEGGKVEQYEDVKAAVRVIAALVFKKKKGHIIVDICKNAQTPPDGLPVHAWGVTLLTSPDEAHFHHWSKDKRDVGIIINCDDVRDMKAFVAWTKLSVASGYAALDEEAQARIVEELKNEWETIKSRINVVGPVPRCVYNSAGYTKRVSQAKKMITSINGDNKSHYEDIMGKIADWRNDKVTHRLVKIVRVRDAGESVDEYRCRPLSVCIGNAIFFKLLAIDVEKMAIRQVTMSDESAAANVFESRALLSLLFPRVFKVIADNLKYLRRGGEIADRRSILNDMAPQQLKLTGQKALPAAHQRPIDNCEYMVLYRPATGNEPVVDGFFFVEGRLRRAPDGAAPPTTPNIAVLLQVTKSDRHPTTTDKVQKFRENMARYFSDWGAFSRDMVWEMIYINSVNGGTITIRQLCDGDDPAEAADMWRNMAQYQVTLREEMQGQLMRAYRDECWYRDAPLLAMEPAPQPRNEQAGAQGG
Protein: Valosin-containing protein homolog, putative (Q585X7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- MPN domain-containing protein
- Ubiquitin fusion degradation protein, putative
- Ubiquitin thioesterase OTU
- UBX domain-containing protein
- UBX domain-containing protein
- Ubiquitin fusion degradation protein 2, putative
- Guanine nucleotide-binding protein subunit beta-like protein
- Polyubiquitin, putative
Sequence:
MGAKARRPNHREGRRGSNNENNHHDGSGGGAGGDARLKIPNQRGEHMRHNDMKSTTSVLSGAKVADVNCGSEGSKSFVAVSLNVRSDSCLPSNEARLSPHSLKELGIISGAVLCVEGDGSVRAFVEAFCSSSCASQTIMLADEVAAAFSGKQVTVSVAKDICPLIPLSSLVLEITKEARIAVGADGLTSSTDIPFLQVCSAFRRRYQRRLVFRGMRAALHVGTVPYYVDVLECCCKSVAEGCVEGDTDVRQIDLGILIDGSKIRYIGRGTVCETELFDGEPVPVGVEKKQSHLLVLGDTGTGKSYFLRREAHEAATLHSRQVETVSVEVLSQGNMCDISSSTVLREVFVRAKAGAPSTVIIDDLHLVCATGDNGVVESGWAKGLLASTLASELDDIRIRQLDVRVVGSAASVESLPRSLLTYDRFGEQVKLLAPGSAEERREFLQNRLKTFGGQAKVTASFVSLAAESTNGFTQRDLVRLLDVASIEAFKETGKTEITDSSITEAIKIVPPSALRQFQVSIPSVKWSDIGGSEVAKKTLQDCVAWCLGKQQWVFRKFNLSPPKGVLLYGPPGCSKTMLAKALANESKMNFVSVKGPEVFSKWVGDSEKAVRDIFARARAAAPCVVFIDELDGMCGHRGRGGVADRVISQFLTELDGLPAALNEGTDALVFVAATNRPDNIDPAVLRPGRIDRKVYVGLPDINERKMIASIQFRNIPLSPELDADYVAARTEGYTGAEVVAVIKEAAFQCVTAGVKSPYISTENVDAALQKVRPRVSPMDVEWYKRWALGQSVSMK
Protein: Slr2005 protein (P73222)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
Sequence:
MKRRKFIRTAGAGLLAVAGVQIGDRLRPATAQASSGLQVEWLGHSAFLFSANGFRILANPFRAIGCTKGFRLPKVQADLVLISSQLWDEGAAENLPGNPRILFEPGSYDIGGIQFQGISAPHDRLGGRRFGQNVVWRWSQGGIRIVHMGGAASPITEEQKILLGSPDLALIPVGGGPKNYDAAEAKAAMAILNPRMVVPTQYATPAADRGNCDLQTLQPFLDLVEGMNVQRINGNSLSLRANNLPAEGTLIRIFSEQGLLV
Protein: Protein preY, mitochondrial (Q9D1C3)
Organism: Mus musculus (Mouse)
Function: In mitochondria, S-adenosylmethionine-dependent methyltransferase chaperone that supports both coenzyme Q biosynthesis, by stabilizing its components, such as COQ5, and NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1) assembly, by stabilizing complex I assembly factors, such as NDUFAF5.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96I23}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
- GPI alpha-1,6-mannosyltransferase 2
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI ethanolamine phosphate transferase 3, catalytic subunit
Sequence:
MLSATCRRLAPALRRLRALSAVAGRFLQVPGARLCSDQSERAEQPHTFHPALLQFLVCPLSKKPLRYEASTNELVNEELGIAYPIIDGIPNMIPQAARTTRQNEKQEEAEQP
Protein: Protein SMALL AUXIN UP-REGULATED RNA 54 (Q9FXI0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the acidification of the apoplast and the facilitation of solutes and water uptake to drive cell expansion (By similarity). Triggers plant growth probably by promoting cell elongation (By similarity). Regulates branch angles and bending (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FJG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FJG1}.
Interaction partners:
- Protein SPIRAL1-like 3
- Kinesin-like protein KIN-5A
- Jacalin-related lectin 34
- Ethylene-responsive transcription factor ERF025
Sequence:
MAIINRSKLTQTTMIKQILKRCSSLGKKQSSEYNDTHEHDGDSLPLDVPKGHFVVYVGGNRVRYVLPISFLTRPEFQLLLQQAEEEFGFDHNMGLTIPCEEVAFKSLITSMLQPTYI
Protein: LIN-24 (Twenty-four) Like (H2KYP1)
Organism: Caenorhabditis elegans
Interaction partners:
- Flavoprotein domain-containing protein
- DNA/pantothenate metabolism flavoprotein C-terminal domain-containing protein
- Cytidine deaminase
- Cytidine deaminase
- Uncharacterized protein T05G5.5
Sequence:
MFSCISPQKSPAFSPEQEKMLKSNRANEPQSFVKGNDAAKSDLIDLEEVVTNWAKTMFDVTKSKAEGKIKKKYLSYNINWTKLFQECSEPTYTILGAKPNVVDAKQDEKVIFKTTFTNTTQREQEYSFKTERCTRSSSTVIIEKGVCRGAEVSLKLKTPCEVVEANAGFTTEVMLNHIGENTSEEELTWGVDSCVKVPPGAETVAELVIIEDIVTRDFRIENRLSGKVLVTITNLKENNSLVTIIEGNICDIIRGMPDYTAKGFRFDGPAAIYETRGQCIFRFGIEQKVRINEFSLNSSRRY
Protein: Lectin, putative (Q385Z7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Protein transport protein Sec31, putative
- SNARE protein, putative
- ADP-ribosylation factor, putative
- Syntaxin 5
- Protein transport protein SEC23
- Protein transport protein SEC23
- Sec16 Sec23-binding domain-containing protein
- Longin domain-containing protein
- Synaptobrevin-type vesicle transport protein, putative
- Golgi reassembly stacking protein
Sequence:
MSAIVHQGVSYRMNQKESGGKHTASVYRGVFFPLSQLLLLAIFATVVSPAAASASPKLTGSQMHRTIEKVIEHHSFTPPLLRNYYGGEGLEHWFVGGTAVVTDDHVRLTGNYRDQEGYMWNREALDMPSFEIIVGFHLHGTARYPADGFAIWLTSSPQNATGPLMGHPMDFQGVGVVFDTFDNDGAGNNPAVYVLYNAEGSENREYTTSNDFKNEHVGSCEYAFRQTSAKFSTARLQYKNETLRVYLSNSAEEDETLCTSVSVQLKTDSKDYYIGITAATGGYSDNHDIAFVHTMPIEGEKYDHDVYSRTTPVEESANHHEAVTEENVAKNDETNKNQTHEQENATSAESANEGEKPLHEEKVEQHDAEKQEKEHKEEEKQNADKHHEEGKRDEEEHQQAEEREEDKQEGRRQSPNPRRKHRSEDQEEENHKGKRTSESKKRSAESTNDEKEVSGTDEEEAAELRHESNRAKGRRASDRRSRRSRDVDRDREEDEATADEDESEDEYQEGEEEEREDVVRRRKANRQRSASSKRNRKRRSRDRRD
Protein: Adenosylcobinamide-phosphate guanylyltransferase (AdoCbi-P guanylyltransferase) (EC 2.7.7.62) (Q58517)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Guanylyltransferase that catalyzes the synthesis of adenosylcobinamide-GDP (AdoCbi-GDP) from adenosylcobinamide-phosphate (AdoCbi-P) and GTP. Is involved in adenosylcobalamin biosynthesis. Binds one GTP per dimer. Cannot use other NTPs or GDP. Does not display AdoCbi kinase activity. Is also able to catalyze the condensation of 2-phospho-L-lactate (LP) with GTP in vitro to form PPi and (2S)-lactyl-2-diphospho-5'-guanosine (LPPG), but is much less efficient than CofC, the presumed enzyme catalyzing this reaction in vivo.
Interaction partners:
- Adenosylcobinamide-GDP ribazoletransferase
- Uncharacterized protein MJ1118
- Probable cobalamin biosynthesis protein CobD
- Bifunctional protein GlmU
- Uncharacterized HTH-type transcriptional regulator MJ1120
- Diaminopimelate epimerase
- UPF0284 protein MJ1598
- Cobyrinate a,c-diamide synthase
- Cobalt-precorrin-4 C
Sequence:
MDALIMAGGKGTRMGGVEKPLIKLCGRCLIDYVVSPLLKSKVNNIFIATSPNTPKTKEYINSAYKDYKNIVVIDTSGKGYIEDLNECIGYFSEPFLVVSSDLINLKSKIINSIVDYFYCIKAKTPDVEALAVMIPKEKYPNPSIDFNGLVPAGINVVSPKHGYQKEEIMVIDELIFNINTKDDLKLAEMLLKKDGL
Protein: Suppressor of variegation 2-10, isoform N (A0A0B4LEH9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRKTRSQTARTQAENAATSSSPGHQSTSSAPIAVNPFDSTKYKECEQMVQMLRVVELQKILSFLNISFAGRKTDLQSRILSFLRTNLELLAPKVQEVYAQSVQEQNATLQYIDPTRMYSHIQLPPTVQPNPVGLVGSGQGVQVPGGQMNVVGGAPFLHTHSINSQLPIHPDVRLKKLAFYDVLGTLIKPSTLVPRNTQRVQEVPFYFTLTPQQATEIASNRDIRNSSKVEHAIQVQLRFCLVETSCDQEDCFPPNVNVKVNNKLCQLPNVIPTNRPNVEPKRPPRPVNVTSNVKLSPTVTNTITVQWCPDYTRSYCLAVYLVKKLTSTQLLQRMKTKGVKPADYTRGLIKEKLTEDADCEIATTMLKVSLNCPLGKMKMLLPCRASTCSHLQCFDASLYLQMNERKPTWNCPVCDKPAIYDNLVIDGYFQEVLGSSLLKSDDTEIQLHQDGSWSTPGLRSETQILDTPSKPAQKVEVISDDIELISDDAKPVKRDLSPAQDEQPTSTSNSETSAQQVDLTLSDSDDDMPLAKRRPPAKQAVASSTSNGSGGGQRAYTPAQQPQQSAVSAMNTMRKAK
Protein: HER-3 protein (Hairy-related 3) (Q90465)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAASNSAATAKPQNVKKVSKPLMEKKRRARINKCLNQLKSLLESACSNNIRKRKLEKADILELTVKHLRHLQNTKRGLSKACDSAEYHAGYRSCLNTVSHYLRASDTDRDSRSIMLTNLTSGLNHNRVPDFSTVESDPALIFTLPSTLRRPHKVPIRTDVSYSSFQQTAERKVCLMPKRTEIGDSDRMSLDAALRSQESKKAETTHFRPKDLKVIECCIFKQNYWRPW
Protein: O-antigen translocase (G3XD19)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- O-antigen polymerase
- UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-acetyltransferase
- UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase
- Probable glycosyltransferase WbpH
- dTDP-glucose 4,6-dehydratase
- Probable glycosyl transferase WbpJ
- LPS biosynthesis protein WbpG
- UDP-N-acetyl-D-glucosamine 6-dehydrogenase
Sequence:
MSAAFINRVARVLVGTLGAQLITIGVTLLLVRLYSPAEMGAFSVWLSFATIFAVVVTGRYELAIFSTREEGELQAIVKLILQLTLLIFVAVAIAVVIGRHLIESMPVVIGEYWFALAVASLGLGINKLVLSLLTFQQSFNRLGVARVSLAACIAVAQVSAAYLLEGVSGLIYGQLFGVVVATALAALWVGKSLILNCIETPWRMVRQVAVQYINFPKFSLPADLVNTVASQVPVILLAAKFGGDSAGWFALTLKIMGAPISLLAASVLDVFKEQAARDYREFGNCRGIFLKTFRLLAVLALPPFIIFWFIGEWAFGLVFGEAWAESGRYAVLMVPLFYMRFVVSPLSYTIYIAQRQSMDLLWQLALLLLTFICFTLPDSVDSVLWFYSIAYAVMYFVYFWMSFQCAKGDAK