wanglab/gogpt-training-data huggingface dataset:
Protein: Protein OBERON 3 (Protein TITANIA 1) (Protein WUS ENHANCER 9) (Q94B71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that functions redundantly with OBE4 in specification of the hypophysis and establishment of the embryonic root. Involved in the activation of ARF5/MP-dependent gene expression during embryonic root meristem initiation. Involved in shoot meristem homeostasis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9S736}.
Interaction partners:
- Mucin-like protein
- Uncharacterized protein At3g24150
- Histone acetyltransferase
Sequence:
MIGEKDLAGDGECSRTKTSKPRFSNLNNQTHQDDKTGQYHQKGVDFLNVRSNNLDGGFSSKSSPRSGNELTLSYLCENSGKLAESLGQKGKEVVTFSENSSYDDKWVERDFFNLREMNPNSSKRKAHEEEEEAEEEEDKKSNKIETLNLSLALPDVSLSLTASNAVKRPRVVTSERTTTSFSNDFTATAPSMSYSYSHPFSHNISCSMTRNSTDFDCSVGKDDHIWCAGEGTNGSVHSRFRPIGDGGVALANNPVSGKPSSSADYSFFPSELPARPGNEVTISGDSRKKVANLEDNDAVRSERVLYDIVSKSISSVALIIQGMADETLESAKEYLRNLIDSPEKKEKLVNLQNQIDKRSDLSKETLSKCVKDQLDILVAVRTGLKYFLSGKIRIPMNELVEIFLFLRCRNVNCKSLLPVDDCECKICSNNKGFCSSCMCPVCLRFDSASNTCSWVGCDVCSHWCHAACGIQKNLIKPGHSLKGQRGTTEMMFHCIGCAHKSEMFGFVKDVFVCCAKNWGLETLIKELDCVRKVFRGSDDAKGKALHLKANEMVKKLESKQISPLDASNFIIQFFNYAESIPEIPDPPRELTVAAETSYRKDEASVTPSTSKDQKKKSFALTDAMMNSFDSLESMVRIKEAETRMFQKKADEARIEAESFKRMIEMKTEKMEEEYTEKLARLCLQETEERRRNKLEELKKLENSHCDYRNMKLRMEAEIAGLLKRMEVTRQQLV
Protein: Uncharacterized protein, isoform A (Q9VGJ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEPKLQTEKLPVMKPIKSSPHAKLSKQQRQQVNDMVRETEDIAIEPIPAWLDQQKFEPILERDFPDLKKIKSFRLEPTAGKGENYTTLLLRANFELELNDGSEQSISYMAKILPNSGNRENVASWKVFYKERNTYGQYIPEFEQMYKDAGKKISFGPRYYESQIELDDELIVLEDLGKRGFRNVDRQNGLDIQHTEATLEKLAQFHAASAVRFELKGSYPEEYNQNLCSVVDSLKELRENQLKAYIDAFPLYDASHLTNDVQAYGSQADDMFQSFAPKIEGEFRVLNHGDAWCNNIMYQYDEAGKLAEVNFVDLQMSRFSSPAQDLLYLILSSTELDIKIAKFDYLIKFYHEKLIESLKLLKYPKPLPSLRSLHQSIFIYGDWILPIVSILLPLVLIDGGDDANMDSLMDGEGAGDKIRNNMFKNHRVIKHQKEILPWAHRRGAFEITK
Protein: RING/U-box superfamily protein (Q9FK45)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSDESPAFALHSGSSRQRKSLEFRFQQSPRWAPYSSASDGNEQKTSLVNNSLTRPNSSNPQCLNEENGFDRDSTAISTSFRSLLSLSESSVPWETPTNNQSSSLTHCSYPRVFCNPVSVCENPEPDHTQEDSSTNPGSSIMMSTRNHQGSPVEEEVSPNSSSNDMLLDVERSNDTEVANPRSEQGSMTHQRCGICKKLLSQKSPWSSYKILRSRDMPATGVFPCHHVYHVECLDKATPTAQTRDPSCPVCSNTIGVMEQPLIAPETLQMALRSLRRSRTALELETVRVPSNDNQRRHNTRRSHKWDKLSCCLNISFSSSS
Protein: Small ribosomal subunit protein cS23z (30S ribosomal protein 3-1, chloroplastic) (Plastid-specific 30S ribosomal protein 3-1) (PSRP-3 1) (Q9SX22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably a ribosomal protein or a ribosome-associated protein.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:P82412}.
Interaction partners:
- Small ribosomal subunit protein uS17c
- Uncharacterized protein At4g24700
- AT2G45990 protein
- Protein trichome birefringence-like 12
- Large ribosomal subunit protein uL24c
- Small ribosomal subunit protein bS18c
- Expressed protein
- Large ribosomal subunit protein uL15c
- Small ribosomal subunit protein bS1c
- Maternal effect embryo arrest 9
Sequence:
MMSSMALSSTSLCSSFISQHPKLSITASPPLFHTQTTKPISVKRKIITLAAPETLTAETVTGIDTSDNTPQQTIKVVKPDEKSRVVLKFVWMEKNIGLGLDQHVPGHGTIPLSPYFFWPRKDAWEELKSTLEAKPWISQKKMIILLNQATDIINLWQQSGGNLTSQ
Protein: Serine protease inhibitor 28Dc (Serpin 28Dc) (Serpin-28D) (Q9VLU4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine protease inhibitor which is required for pupal viability and plays an essential role in regulating the melanization reaction. Inhibits spontaneous melanization and appears to be involved in the melanization immune response to physical wounding in larvae and adults. Acts by negatively regulating the Hayan-phenoloxidase (PPO1) cascade in the hemolymph and possibly the trachea. May function by controlling the initial release of the activated form of PPO1, phenoloxidase (PO) and thus maintains PO availability for processes such as wound response and pigmentation.
Subcellular location: Secreted {ECO:0000305|PubMed:18801354}.
Interaction partners:
- Male accessory gland protein
- MIP05602p
- Serine protease inhibitor 77Ba
- Serine protease inhibitor 27A
- RE27547p
- GH21475p
- Serpin 77Bb
Sequence:
MWRLLLALLLVSSVCCESELFRDDLRTPETMAYINGLMQRRHQMQQEAQQHIQAIPPAVPLQSPGLVNGLGNQNDPALNRISGTSVKPSNLPAAYSNGYVDLATSDRIANSVLNFANILGQHLANGKTQIYSPLSIVHSLALLLLGAKGRSYEELSTVFDIPDTSRLHEQFGLMLQDLQQPTREAISAGRPLTDWRASSAMRSNRRAQRPGAHEVHLANGLFTQTGYTLNPDYRRVIVEVYASDLQIQDFEGSPATARYNINAYVAQHTKNHIENIIASDIPQTTRMILANALYFKAFWETDFIESATRPDNFYPNGEGTEPVMRVQMMATGGAYPYHEDHELGCKIIGLPYRGNLSTMYIIQPFKSSVRELMALQKRLTADKIESMISRMYRRAALVAFPKMHLTESVNLKTVMQRMGLGGIFSAVQNDLSLIATNEATRTNALGGNSLQNLEAQRRAGTGGARSDLVVDDIVHKVDFTVNEQGTEAAASSVTYLKKSGPDVLFRGDTPFMVLVRHDPTKLVLFYGLINEPPAAA
Protein: Two-component response regulator PhoP (Q9I4F9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system PhoP/PhoQ that plays a role in the regulation of resistance towards polymyxin B and cationic antimicrobial peptides in response to limiting concentrations of Mg(2+). Functions as a transcriptional activator by direct binding to a cis-acting sequence upstream of the target gene promoters including oprH and pmrH promoters.
Interaction partners:
- Two-component sensor PhoQ
- PhoP/Q and low Mg2+ inducible outer membrane protein H1
- Sensor protein kinase PmrB
- Phosphate regulon sensor protein PhoR
- UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase aminotransferase)
- histidine kinase
- histidine kinase
- Lipid A deacylase PagL
- histidine kinase
- histidine kinase
Sequence:
MKLLVVEDEALLRHHLYTRLGEQGHVVDAVPDAEEALYRVSEYHHDLAVIDLGLPGMSGLDLIRELRSQGKSFPILILTARGNWQDKVEGLAAGADDYVVKPFQFEELEARLNALLRRSSGFVQSTIEAGPLVLDLNRKQALVEEQPVALTAYEYRILEYLMRHHQQVVAKERLMEQLYPDDEERDANVIEVLVGRLRRKLEACGGFKPIDTVRGQGYLFTERCR
Protein: Endoribonuclease YSH1 (EC 3.1.27.-) (Yeast 73 kDa homolog 1) (mRNA 3'-end-processing protein YSH1) (Q06224)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Has endonuclease activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:12819204, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-tRNA-processing protein PTA1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Polyadenylation factor subunit 2
- Protein PTI1
- COMPASS component SWD2
- Protein MPE1
- Poly
- RNA end formation protein 2
- Protein CFT1
- mRNA 3'-end-processing protein RNA15
Sequence:
MERTNTTTFKFFSLGGSNEVGRSCHILQYKGKTVMLDAGIHPAYQGLASLPFYDEFDLSKVDILLISHFHLDHAASLPYVMQRTNFQGRVFMTHPTKAIYRWLLRDFVRVTSIGSSSSSMGTKDEGLFSDEDLVDSFDKIETVDYHSTVDVNGIKFTAFHAGHVLGAAMFQIEIAGLRVLFTGDYSREVDRHLNSAEVPPLSSNVLIVESTFGTATHEPRLNRERKLTQLIHSTVMRGGRVLLPVFALGRAQEIMLILDEYWSQHADELGGGQVPIFYASNLAKKCMSVFQTYVNMMNDDIRKKFRDSQTNPFIFKNISYLRNLEDFQDFGPSVMLASPGMLQSGLSRDLLERWCPEDKNLVLITGYSIEGTMAKFIMLEPDTIPSINNPEITIPRRCQVEEISFAAHVDFQENLEFIEKISAPNIILVHGEANPMGRLKSALLSNFASLKGTDNEVHVFNPRNCVEVDLEFQGVKVAKAVGNIVNEIYKEENVEIKEEIAAKIEPIKEENEDNLDSQAEKGLVDEEEHKDIVVSGILVSDDKNFELDFLSLSDLREHHPDLSTTILRERQSVRVNCKKELIYWHILQMFGEAEVLQDDDRVTNQEPKVKEESKDNLTNTGKLILQIMGDIKLTIVNTLAVVEWTQDLMNDTVADSIIAILMNVDSAPASVKLSSHSCDDHDHNNVQSNAQGKIDEVERVKQISRLFKEQFGDCFTLFLNKDEYASNKEETITGVVTIGKSTAKIDFNNMKILECNSNPLKGRVESLLNIGGNLVTPLC
Protein: Glutathione-independent glyoxalase DJR-1.2 (EC 4.2.1.130) (Protein DJ-1 homolog 2) (O16228)
Organism: Caenorhabditis elegans
Function: Catalyzes the conversion of methylglyoxal (MG) or glyoxal (GO) to D-lactate or glycolic acid respectively in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against glyoxal-induced cell death. Protects dopaminergic neurons from glyoxal-dependent neuronal degeneration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22523093}.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Serine/threonine-protein kinase pink-1, mitochondrial
- Probable cation-transporting ATPase catp-6
- Glyoxalase 1
- Superoxide dismutase
- Leucine-rich repeat serine/threonine-protein kinase 1
- Superoxide dismutase 2, mitochondrial
- Superoxide dismutase 1, mitochondrial
- FMN hydroxy acid dehydrogenase domain-containing protein
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MAAQKSALILLPPEDAEEIEVIVTGDVLVRGGLQVLYAGSSTEPVKCAKGARIVPDVALKDVKNKTFDIIIIPGGPGCSKLAECPVIGELLKTQVKSGGLIGAICAGPTVLLAHGIVAERVTCHYTVKDKMTEGGYKYLDDNVVISDRVITSKGPGTAFEFALKIVETLEGPEKTNSLLKPLCLAK
Protein: Sperm-associated antigen 16 protein (Pf20 protein homolog) (Q8N0X2)
Organism: Homo sapiens (Human)
Function: Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8K450}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q8K450}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q8K450}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8K450}. Note=Detected on the sperm flagellum axoneme. Detected in the central apparatus of the axoneme. Colocalizes with SPAG6 on microtubules (By similarity). {ECO:0000250|UniProtKB:Q8K450}.
Interaction partners:
- Sperm-associated antigen 6
- Meiosis expressed gene 1 protein homolog
Sequence:
MAAQRGMPSSAVRVLEEALGMGLTAAGDARDTADAVAAEGAYYLEQVTITEASEDDYEYEEIPDDNFSIPEGEEDLAKAIQMAQEQATDTEILERKTVLPSKHAVPEVIEDFLCNFLIKMGMTRTLDCFQSEWYELIQKGVTELRTVGNVPDVYTQIMLLENENKNLKKDLKHYKQAADKAREDLLKIQKERDFHRMHHKRIVQEKNKLINDLKGLKLHYASYEPTIRVLHEKHHTLLKEKMLTSLERDKVVGQISGLQETLKKLQRGHSYHGPQIKVDHSREKENAPEGPTQKGLREAREQNKCKTKMKGNTKDSEFPIDMQPNPNLNVSKESLSPAKFDYKLKNIFRLHELPVSCVSMQPHKDILVSCGEDRLWKVLGLPKCNVLLTGFGHTDWLSDCCFHPSGDKLATSSGDTTVKLWDLCKGDCILTFEGHSRAVWSCTWHSCGNFVASSSLDKTSKIWDVNSERCRCTLYGHTDSVNSIEFFPFSNTLLTSSADKTLSIWDARTGICEQSLYGHMHSINDAIFDPRGHMIASCDACGVTKLWDFRKLLPIVSIDIGPSPGNEVNFDSSGRVLAQASGNGVIHLLDLKSGEIHKLMGHENEAHTVVFSHDGEILFSGGSDGTVRTWS
Protein: Tryprostatin B synthase (EC 2.5.1.106) (Brevianamide F prenyltransferase) (Fumitremorgin biosynthesis protein B) (B9WZX3)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: Brevianamide F prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Interaction partners:
Sequence:
MPPAPPDQKPCHQLQPAPYRALSESILFGSVDEERWWHSTAPILSRLLISSNYDVDVQYKYLSLYRHLVLPALGPYPQRDPETGIIATQWRSGMVLTGLPIEFSNNVARALIRIGVDPVTADSGTAQDPFNTTRPKVYLETAARLLPGVDLTRFYEFETELVITKAEEAVLQANPDLFRSPWKSQILTAMDLQKSGTVLVKAYFYPQPKSAVTGRSTEDLLVNAIRKVDREGRFETQLANLQRYIERRRRGLHVPGVTADKPPATAADKAFDACSFFPHFLSTDLVEPGKSRVKFYASERHVNLQMVEDIWTFGGLRRDPDALRGLELLRHFWADIQMREGYYTMPRGFCELGKSSAGFEAPMMFHFHLDGSQSPFPDPQMYVCVFGMNSRKLVEGLTTFYRRVGWEEMASHYQGNFLANYPDEDFEKAAHLCAYVSFAYKNGGAYVTLYNHSFNPVGDVSFPN
Protein: Exocyst complex component EXO84 (Exocyst complex protein of 84 kDa) (U1 SNP1-associating protein 3) (P38261)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis and to the budding site. Also involved in assembly of the spliceosome.
Subcellular location: Cytoplasmic vesicle, secretory vesicle. Bud. Bud neck. Note=Cell periphery, bud and bud neck. The polarization of EXO84 requires actin cables.
Interaction partners:
- Exocyst complex component SEC6
- Exocyst complex component SEC5
- Exocyst complex component SEC10
- Exocyst complex component EXO70
- Exocyst complex component SEC3
- Exocyst complex component SEC8
- Exocyst complex component SEC15
- Ras-related protein SEC4
- Lethal
- Protein transport protein SEC9
Sequence:
MVEFSLKKARNNWKHVKKSASSPAKQKTPPSPAKPKQKTKKNPYSDLKDPATSYTLPTINARERSRVATSMQRRLSIHNTNYAPPTLDYSMPLPDMPNMIVPNDNVDSSHNNSSFTTENESVSSKGPSNSLNLSTADLSLNDSSYNKVPARSAMRNTVNPSGSNDPFNNSTSLRKMLANPHFNAKDFVHDKLGNASAITIDKFTSNLTDLSIQVQEEVKLNINKSYNEIMTVNNDLNVAMLELKRVRANINDLNEVLDQCTKIAEKRLQLQDQIDQERQGNFNNVESHSNSPALLPPLKAGQNGNLMRRDRSSVLILEKFWDTELDQLFKNVEGAQKFINSTKGRHILMNSANWMELNTTTGKPLQMVQIFILNDLVLIADKSRDKQNDFIVSQCYPLKDVTVTQEEFSTKRLLFKFSNSNSSLYECRDADECSRLLDVIRKAKDDLCDIFHVEEENSKRIRESFRYLQSTQQTPGRENNRSPNKNKRRSMGGSITPGRNVTGAMDQYLLQNLTLSMHSRPRSRDMSSTAQRLKFLDEGVEEIDIELARLRFESAVETLLDIESQLEDLSERISDEELMLLNLISLKIEQRREAISSKLSQSILSSNEIVHLKSGTENMIKLGLPEQALDLFLQNRSNFIQDLILQIGSVDNPTNYLTQLAVIRFQTIKKTVEDFQDIFKELGAKISSILVDWCSDEVDNHFKLIDKQLLNDEMLSPGSIKSSRKQIDGLKAVGLDFVYKLDEFIKKNSDKIR
Protein: Pheromone-regulated membrane protein 2 (P40534)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Plasma membrane fusion protein PRM1
- Factor-induced gene 1 protein
- Karyogamy protein KAR4
Sequence:
MNNVHIIKPLSLPQRFFSCIFHPLLLIFFTSVILTIWGSFSVIDITMAKMSHAQVKRNDTVSTFASISTATATATTTATTTATMTAVTTQHAIYSANSYSLNKTFIDNTIDQYFESKLRSIESTVGTDMQEKFKSYTDDILDNKQKLINDQISLETELIKEVLEVNNTIFNELLTKSQLINDTWNEISEDAMTIDKDSISQMASNLLLNYSMFDSIFGNYSRKLKSLQNFNGTITDFSTQLDTSSTLSLNFLRNSTDWLQLKRNFTANLQNEISILSGGSTEVTSSTSIIKRSLKTNSEENSVLSAVKNHVFRKCKRMTIIFTVMYFAFVILLMAIERILFQLENQQVNLVMSQINGLTGQTNFTKYNKVLKSLITTLNLSTLYPIPYQLTKLINQKIFKREPEKIDDKKVKKSKLFYCNWWIISNGAHLWLFGFLMLLIHWQIVTRLTNFEVPSLPTFHKRAGPSLYKREVWTDGNITTTIEGFINDSVSLLCENFQMEVNEKFITANLSLQTDPNLKVQSTDILNLWVNDTNTQFEKYLNESSQNWQGIDLQVEPLLGSDSINEFLGQYFLPTYEVTNTNSSFALDIQKYGIINRGINITNASVAALSSLSKRQIKDKEQKQTYFLHTVYKWGLLAVCLTILFHHMLIFIILKL
Protein: C2H2-type domain-containing protein (Q5B154)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Calmodulin
- pH-response transcription factor pacC/RIM101
- Serine/threonine-protein phosphatase 2B catalytic subunit
Sequence:
MDPQDTLQDLGQAPAAHINRSASPSAHAHQQYNNNHNDLTIDPSVTSNSSYPPSSFANNSAPGSEAFAYSSSYLTPATATDHNFARPSLQIPQSFDQGLSHQPAEENFSNLLNSNTGDFDFSLYQGSSPNNTGSDYPSSGLLDPQQSGNQAVNPVDLVSQIPSPHPSNSSQTSPLDQPPSSAMSPPASSPGTFYTPQHSRHTSLDPASAAYMTNVSHPEWQAVMNNSAFHGHRRAPSEVSEVSSAAHSPYLPQHDSFDVADNNPSPLLAAQNDPSLYDNAALGIESFTLSEHHQPQTQGISPHHSPYISPQLMPQHPTDIIPGGPFISAPATNSAYPTPPTEGYPNGGDIGQASQMAPPSINVEFAPPAKAQVFPPEKSTADMDSLSPPPSLRTSRMRSKSDPYAVSISRPRSPSSPSASLDALAASSPRSLSPFNVGRHPYSNPSSREPSPARSARRLSTSSVDSRNYILGLADPQRPGSNNTDSKRVQKHPATFQCTLCPKRFTRAYNLRSHLRTHTDERPFVCTVCGKAFARQHDRKRHEGLHSGEKKFVCRGDLSRGGQWGCGRRFARADALGRHFRSEAGRICIKPLLDEESQERERTLINQQQQHLQPVNQPLMLPGQGTEAQHTGSFILPAALLAQYPALQTLQWDQIPAGTDDTSDIGGRNSFDASSGGEFGFDDDESGISVSGMSTGYASDQGNIYNVDAQGQMLGVNPGEAGYANPNWGK
Protein: Nonribosomal peptide synthetase fmqC (EC 6.3.2.-) (Fumiquinazoline biosynthesis cluster protein C) (Q4WLW8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts. The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from anthranilic acid (Ant), tryptophan (Trp), and alanine (Ala). The trimodular NRPS fmqA is responsible for FQF formation. Modules 1, 2 and 3 of fmqA are predicted to activate and load Ant, Trp and Ala, respectively, providing for the assembly of an Ant-Trp-Ala-S-enzyme intermediate that would undergo double cyclization for chain release and generation of the tricyclic 6-6-6 product fumiquinazoline F. The presence of an E domain predicted for module 2 of fmqA is consistent with epimerization of L-Trp to D-Trp during assembly to generate the R-stereocenter at C14 of FQF. The FAD-dependent monooxygenase fmqB and the monomodular NRPS fmqC then maturate FQF to FQA. FmqB oxidizes the 2',3'-double bond of the indole side chain of FQF, and fmqC activates L-Ala as the adenylate, installs it as the pantetheinyl thioester on its carrier protein domain, and acylates the oxidized indole for subsequent intramolecular cyclization to create the 6-5-5-imidazolindolone of FQA. The FAD-linked oxidoreductase fmqD introduces a third layer of scaffold complexity by converting FQA to the spirohemiaminal FQC, presumably by catalyzing the formation of a transient imine within the pyrazinone ring. FQC subsequently converts nonenzymatically to the known cyclic aminal FQD.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24612080}.
Interaction partners:
- FAD-dependent monooxygenase fmqB
- FAD-linked oxidoreductase fmqD
- PKS-like enzyme, putative
Sequence:
MPDLIQTKSVVLGYGVKMVLAPAKAARSLLIREEAVWRFSLPRVLSTPTTMLETTEPIAHASELDKPSIVVTNTEVDSEDNTSSVLGRYIPQKCLQNARLAAVNSCVNEIFEARFRERPDAPAVCAWDGSYTYRELNDRSSALAHKLRRRGVQAEVLVALLFEKSKFSVVAMHAVIKAGGAFQLWDPSLPVARLGGMFAESKAHLVLASAANARLAAEISENVMVVDESLVPPWESAPLNPGTQPENALYCVFTSGSTGKPKGFLMDHRAFCTCALGVGELLGLNGASRLIQFSANSFDLATFDHILPFLCGACLCIPSEEERKGDLTRAFNRYRATHAVLTPTVSRLLEPEKLTTLQVLLLAGEAPSREDIRRWASTVGLLNGYSPAEAGCITIVNPSLQESHPSKIGFPVSVVPWVVDPDDCNRLVPAGEVGELVLQGHTLARGYFGRPDQSKAAFIPTPAWVRQFGYETYGRLYRTGDLVRFDAEDESLVYIGRKDSQVKIRGQRLELGEVEHALQQFFPRPQIVVVELLTAEDREPALVGFVYQPGSSQHMPAPPQHQDNSLFLVADDQFCADAQKALASLRDILPPYMIPSDLLRISHLPMVPSGKTDRRLIRMRAVDLAPEERRKYSSVLGQSRDQPVTQLEESLLGLWATCLKLPPSQIGVLDNFFHLGGGSLEAIHLAAEARNMGFAELSSAAVFQCPTIREMAGMLDGVTASVQEQDPRGCTSFQLESSLVAELLRKSQCTLEDLQEGFLPLTPFQEKTAKMKPMHLLLDIPGIDHSRLEAAWALVLEKHISFRSIYVEHQGRVYQAFLRQPDTVSIPIRWCDEPVHECAARFCEQDVDLILDGRPWWSMTRINNKIDSVLVLRLTHAQWDALTLDVLFKDFMAAYESRELSRRDLEFPAYMRFRLRHNASPATVRFWSTFLHGSRLTQPLLLDGAAEVDPGNEAMVFVSQQIPMLTPPHGITLGSVFRAAWAFVLARYTGQEDVVFGEFVEGRSLLVKSVEKVTGCAAAETPMRIVVSPTASVRDLLKHSQEQYVARIPYETCELEDIVPSSTSWPTDTTFNHILVIQHEPVLPPVALDGRPCPHRWAFHGRLEDVYVQMVFGPDTLHVGMSGPEIRLSRTIATQLVEKLASTITQFNDRPEALLSEITV
Protein: CDPK-related kinase 2 (AtCRK2) (EC 2.7.11.1) (Calcium/calmodulin-dependent protein kinase 2) (Q9LJL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
Subcellular location: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Cysteine-rich receptor-like protein kinase 21
- Putative cysteine-rich receptor-like protein kinase 16
- Putative cysteine-rich receptor-like protein kinase 23
- Cysteine-rich receptor-like protein kinase 4
- Cysteine-rich receptor-like protein kinase 41
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Cytochrome P450, family 702, subfamily A, polypeptide 8
- Probable WRKY transcription factor 14
- non-specific serine/threonine protein kinase
Sequence:
MGGCTSKPSSSVKPNPYAPKDAVLQNDDSTPAHPGKSPVRSSPAVKASPFFPFYTPSPARHRRNKSRDGGGGESKSVTSTPLRQLARAFHPPSPARHIRDVLRRRKEKKEAALPAARQQKEEEEREEVGLDKRFGFSKELQSRIELGEEIGRGHFGYTCSAKFKKGELKDQEVAVKVIPKSKMTSAISIEDVRREVKILRALSGHQNLVQFYDAFEDNANVYIVMELCGGGELLDRILARGGKYSEDDAKAVLIQILNVVAFCHLQGVVHRDLKPENFLYTSKEENSMLKVIDFGLSDFVRPDERLNDIVGSAYYVAPEVLHRSYTTEADVWSIGVIAYILLCGSRPFWARTESGIFRAVLKADPSFDEPPWPSLSFEAKDFVKRLLYKDPRKRMTASQALMHPWIAGYKKIDIPFDILIFKQIKAYLRSSSLRKAALMALSKTLTTDELLYLKAQFAHLAPNKNGLITLDSIRLALATNATEAMKESRIPDFLALLNGLQYKGMDFEEFCAASISVHQHESLDCWEQSIRHAYELFEMNGNRVIVIEELASELGVGSSIPVHTILNDWIRHTDGKLSFLGFVKLLHGVSTRQSLAKTR
Protein: Prophenin and tritrpticin precursor (C6) [Cleaved into: Prophenin-1 (PF-1); Tritrpticin] (P51524)
Organism: Sus scrofa (Pig)
Function: Exerts antimicrobial activity. It is more effective against Gram-negative bacteria than Gram-positive bacteria.
Subcellular location: Secreted.
Interaction partners:
Sequence:
LLLLALVVPSASAQALSYREAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDPGTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVKQCVGTVTLDQIKDPLDITCNEGVRRFPWWWPFLRRPRLRRQAFPPPNVPGPRFPPPNFPGPRFPPPNFPGPRFPPPNFPGPRFPPPNFPGPPFPPPIFPGPWFPPPPPFRPPPFGPPRFPGRR
Protein: Metallo-beta-lactamase domain-containing protein (Q385U6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPRQTTLSVVCLSTGRGASMVYEGNCSTAYVLCVGDAPVVLFGIGYGVTRQCLRYFGTIPTNIAVFSNRSHMSAELPVVIAVEGRKGRHPRIVASETVMMRLMQHRLAEMHSRAAFGVPGEGGVCDFVNLQTDESSPTVPYRLPDFPSVSLVAFDAVSSLESSCGFVVLHHGSPVLALTGDCAYDAQRYQEVLRMAPVVIVDGRKKGSPDHASFADITRAVDDCRSNGGGPRRVFIGQYGAPADAPPVVSGATVLPIVEGAVVELSEGVCIGDAEELLVPPAPSAIDMCESTKTVCCDRSEGEEAPSSFVMRMAHTGGGGGQDALHEGSSCRRGRGAGIGDWQCGGKEAVIVPEANLGSIGVSAAFEEYMQRAYCALQRYPTQEGGVSGVVQMRSNNTNAPRGPNEAPPSRAQSAEVPNRPRGEESTKHTTGYTCRFTALKT
Protein: Flagellar radial spoke protein 4 (Q01656)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme. Note=Radial spoke.
Interaction partners:
Sequence:
MAAVDSVAQALAYLQVHSPQDGTSMYDHLVKLVSKVLEDQPKNAVDLLETSLLVKKSTFDPKESSPLVPIPVAPDATQTQAAVSIFGDPELPINPATGEPVPADPPNEFEAENMLGAAAVLDCLGVGLGRELGVNIALAAKRIGEDPKLAVRSVRFFGKFLGLYSDYFVFEVAFKKEAAKEAAPAAPAPERVEGEAASSSAPEVPVEEPGKGANKFTYLVCSSLGGPLTRLPDVTPAQVKASRRIKKLLTGRLTSHVSTYPAFPGNEANYLRALIARISAATVVAPSDLFSLNDETGELERAEDWEPPAGREMAAPTAWVHVRPHLKSQGRCEVHKRELPEDADEDEFYNEDELEEGPDLLAALEEDAQLPGEQAAWTPIYSSASEAVKTQAGGLRSLVWPGAVCGGRGSEWTCVYVGWGVKNAPFVPLPPPPVAQEFAWGEVETQELELKPAPPPPEEEAEADE
Protein: Peroxisomal biogenesis factor 5 (F5H3X7)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
Sequence:
MAMRELVEAECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGAPASEAASKPLGVASEDELVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQQIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFISEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGTATDRWYDEYHPEEDLQHTASDFVAKVDDPKLANSEFLKFVRQIGEGQVSLESGAGSGRAQAEQWAAEFI