wanglab/gogpt-training-data huggingface dataset:
Protein: Enoyl-CoA hydratase/isomerase family protein (P71621)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTDDILLIDTDERVRTLTLNRPQSRNALSAALRDRFFAALADAEADDDIDVVILTGADPVFCAGLDLKELAGQTALPDISPRWPAMTKPVIGAINGAAVTGGLELALYCDILIASEHARFADTHARVGLLPTWGLSVRLPQKVGIGLARRMSLTGDYLSATDALRAGLVTEVVAHDQLLPTARRVAASIVGNNQNAVRALLASYHRIDESQTAAGLWLEACAAKQFRTSGDTIAANREAVLQRGRAQVR
Protein: Cystatin-11 (Q9H112)
Organism: Homo sapiens (Human)
Function: Has antibacterial activity against the Gram-negative bacteria E.coli. May play a role in sperm maturation and fertilization.
Subcellular location: Secreted {ECO:0000305|PubMed:12072414}. Note=Probably secreted into the epididymis lumen, where it localizes to the outer surface of sperm. Specifically localizes to the postacrosomal and tail regions of sperm. {ECO:0000269|PubMed:12072414}.
Interaction partners:
- Epididymal-specific lipocalin-8
- Epididymal-specific lipocalin-9
Sequence:
MMAEPWQALQLLLAILLTLMALPYQARKKTFLSVHEVMAVENYAKDSLQWITDQYNKESDDKYHFRIFRVLKVQRQVTDHLEYHLNVEMQWTTCQKPETTNCVPQERELHKQVNCFFSVFAVPWFEQYKILNKSCSSD
Protein: Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 protein kinase) (P39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (TFIIH basal transcription factor complex kinase subunit) (P51952)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P50613}. Cytoplasm {ECO:0000250|UniProtKB:P50613}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P50613}. Note=Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (By similarity). {ECO:0000250|UniProtKB:P50613}.
Interaction partners:
- CDK-activating kinase assembly factor MAT1
- Cyclin-H
- General transcription factor IIH subunit 1
- General transcription and DNA repair factor IIH helicase subunit XPD
- DNA-directed RNA polymerase II subunit RPB4
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 3
- General transcription factor IIF subunit 2
- Mediator of RNA polymerase II transcription subunit 6
- TATA box binding protein
Sequence:
ANRNEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNWAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLQHIFIAAGDDLLELIQGLFLFNPCTRITASQALRTKYFSNRPGPTPGCQLPRPNCPVEALKEQSNPAMATKRKRAEALEQ
Protein: Prelamin-A/C [Cleaved into: Lamin-A/C] (P48679)
Organism: Rattus norvegicus (Rat)
Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (By similarity). Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis.
Subcellular location: Nucleus lamina {ECO:0000250|UniProtKB:P02545}. Nucleus envelope {ECO:0000250|UniProtKB:P02545}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P02545}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C. Also localizes to the micronuclear envelope in response to response to genome instability. {ECO:0000250|UniProtKB:P02545}.
Interaction partners:
- Emerin
- Barrier-to-autointegration factor
- Lamin-B1
- Lamin B2
- Sad1 and UNC84 domain containing 2
- Barrier-to-autointegration factor-like protein
- Caspase-6
- Granzyme B
- Sterol regulatory element-binding protein 1
- Sad1 and UNC84 domain containing 1
Sequence:
METPSQRRPTRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLLAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTLKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQSQGGGSVTKKRKLESSESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLMTYRFPPKFTLKAGQVVTIWASGAGATHSPPTDLVWKAQNTWGCGTSLRTALINATGEEVAMRKLVRSLTMVEDNDDEEEDGDELLHHHRGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKAASGSGAQVGGSISSGSSASSVTVTRSFRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSSQNCSIM
Protein: Immunoglobulin lambda variable 6-57 (Ig lambda chain V-VI region AR) (Ig lambda chain V-VI region EB4) (Ig lambda chain V-VI region NIG-48) (Ig lambda chain V-VI region SUT) (Ig lambda chain V-VI region WLT) (P01721)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAWAPLLLTLLAHCTGSWANFMLTQPHSVSESPGKTVTISCTGSSGSIASNYVQWYQQRPGSAPTTVIYEDNQRPSGVPDRFSGSIDSSSNSASLTISGLKTEDEADYYCQSYDSSN
Protein: Outer membrane protein YfaZ (P76471)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:16522795}.
Interaction partners:
- Aldose sugar dehydrogenase YliI
Sequence:
MKKIALAGLAGMLLVSASVNAMSISGQAGKEYTNIGVGFGTETTGLALSGNWTHNDDDGDVAGVGLGLNLPLGPLMATVGGKGVYTNPNYGDEGYAAAVGGGLQWKIGNSFRLFGEYYYSPDSLSSGIQSYEEANAGARYTIMRPVSIEAGYRYLNLSGKDGNRDNAVADGPYVGVNASF
Protein: Large ribosomal subunit protein mL37 (39S ribosomal protein L37, mitochondrial) (L37mt) (MRP-L37) (A4FUC0)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10600119}.
Interaction partners:
- Large ribosomal subunit protein mL65
- Large ribosomal subunit protein uL2m
- Large ribosomal subunit protein mL62
- Small ribosomal subunit protein uS7m
- Translation initiation factor IF-2, mitochondrial
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein mS25
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein uL24m
- Aurora kinase A interacting protein 1.
Sequence:
MALASGPARRVLARPWGLGLEGCGVPRRGAYEWGVRSTRKPEPPPLDRVYEIPGLEPITFAGKMHFMPGLARPVFPPWDPGWTHPKFRRLPPLQEHPLYKDEVCYIFHQRCRLLEGVKQALWLTKTKLIEGLPEKVLSLADNPRNHIENQDERVLNVISHARLWHSTEDIPKRETYCPVIVDSLIQLCKSQILKHPSLARRICAQKNMLSTTWKRESTLIQVHGSSGAQLNAKDPLPPIASREEVEATKNHVLETFSPISPTISLQECHIYDVNDDTGFREGYPYPCPHTLYLLESANLRAHRFQPDQLRAKMILFAFGNALAQARLLYGNDPKVLEQPVVVQSVGTDGRVFQFLVLQLNTTDLASEEGIKNLVWVDSDQLLYQHFWCLPVIKKKVVVEPVGPTGFQPETFRKFLALYLHGAV
Protein: Flagellar motor switch protein FliM (Q9WZE6)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
Subcellular location: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250|UniProtKB:P06974}.
Interaction partners:
- Flagellar motor switch protein FliG
- Motility protein A
- Flagellar protein, putative
- Chemotaxis protein CheY
- Flagellar hook-associated protein 1
- Flagellar M-ring protein
- Flagellar basal-body rod protein FlgB
- Flagellar basal-body rod protein FlgC
- Flagellar biosynthesis protein FliP
- CheY-P phosphatase CheC
Sequence:
MSDVLSQEEINQLIEALMKGELKEEDLLKEEEEKKVKPYDFKRPSKFSKEQLRTFQMIHENFGRALSTYLSGRLRTFVDVEISIDQLTYEEFIRSVMIPSFIVIFTGDVFEGSAIFEMRLDLFYTMLDIIMGGPGENPPNRPPTEIETSIMRKEVTNMLTLLAQAWSDFQYFIPSIENVETNPQFVQIVPPNEIVLLVTASVSWGEFTSFINVCWPFSLLEPLLEKLSDRFWMMGRKPEKVEERMEELRKASQKIPVTVQAVIGETELRLKEILDLEVGDVIRLGTHYKDEIRIDVEGRPKFRGIPGVFKGKYAVKVTGEFTNGGEYE
Protein: Heat shock transcription factor 4 (Q3UG93)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGAGRRPRHRPPHPLEPDGFRKVVSIEQGGLLRPERDHVEFQHPSFVRGREQLLERVRRKVPALRGDDSRWRPEDLSRLLGEVQALRGVQESTEARLQELRQQNEILWREVVTLRQSHSQQHRVIGKLIQCLFGPLQTGPSSTGAKRKLSLMLDEGSACSASAKFNACPVSGALLQDPYFIQSPLPETTLGLSPHRARGPIISDIPEDSPSPEGHRLSPSGGCRRVKGLALLKEEPASPGGDGEAGLALAPNECDFCVTAPPPLPVAVVQAILEGKGSYSPEGPRSVQQPEPRGPREVPDRGTLGLDRGNRSPESLLPPMLLRPAPETLEPVAPVDVLGPSLHGREWTLMDLDMELSLMQPLAPETDEAELTVKELNSSGVGKDHTLGTPLMLDVQADLEGAALSVPGALTLYNVTESNASYLDPGASPSSP
Protein: Uncharacterized protein, isoform E (M9NF21)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGVKVKETTPQQIEELRDRFNRKYASSPPAAPFHPTDIDRIRNDHLWLQRFLEMYDLDMETSFNSLWETCILRQSTGANDIDESELNQEYLKEGSVFVHNTDVDGKPLLVFRVKMHSKSKNLDELIRIVVYWVERTQREQHLTQLTIFFDMSGTSLASMDLEFVKRIVETFKQFYPNSLNYILVYELGWVLNAAFKVIKAVLPPKAVEILKMISKKDINQYINKDNCLAIWGGEDNYEFSFVPEAKKVISKPVAANAGDDDQFADKKLQFILRQTEAAATTAGRS
Protein: E3 ubiquitin-protein ligase RNF216 (Ring finger protein 216) (E7F859)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MADGSSDDDVIHLASFNTHRSRAKRVRTRTSYITISSSSDSDDEPVRFVPNGTVVVKDDEEEEEVSILEPQPSPHRELIRPAAKWGASTFPSLASGSSRHPTSAHAHPPSVVAAHPTLGNQAIGVLTTDQNAVPSTSREHALRRPPLRDKDSLPLQTDPSSSTHSVNQANSAFSPPSTTESGQSDSGHKIEVVVWPRTERTIKRPRTPQETVLVEVRRDEQPLAPGIPAQLPAPADNERPGPSMPREPLIPQDSHRTSLDLLVKGVTDLFPDVQDAYVAELIERGDLKDLNVICNILLENPDYPKKANSVLTQSSVLLETNDSETQESENYFDYFKLKTVGPEVVVQAADMLMGDFRMLSCQDIKWALNCLKGHYAITRKALFEALKKWQENSTDPSGKKKRRREPNERAYIDFKFEQGSFKLERKMYFLEKNRRWSRGNETTLEASLVKELQFYEQKAKEMAEHEDFLLALQVNEEQYQKDGQLIECGCCCGEFAFEEMTQCTDGHLFCKECLVKYAQEAVFGSGRSELSCMDGNCTCSFPNSELEKVLPENILCKYYERQAEEAVAATCADELVRCPFCNFPALLDKDVSLFSCPNPRCRKESCRKCHVVWKEHAGKTCEQVLERDEIRLRVAFEEKMTAARVRKCHKCATGLVKSEGCNRMWCRCGAYMCYLCREPINGYNHFCQHARSPGAPCRHCKKCSLWTDPTQDDERIIQEIQKEGEAELNKKTTQPNQPETTGKRVGPPPEPIPAKRPRVTPPAPNAAPQAVRAPLLIPQVMLPGPQRLFLQPIPAPYVPPLPNLPPVNYQPRNLNFDFNMPMHYGPPHRFFRPL
Protein: Transmembrane E3 ubiquitin-protein ligase 1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TUL1) (P36096)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions and support a role in protein quality control. Mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12 and other proteins containing exposed hydrophilic residues within their transmembrane domains, leading to their sorting into internal vesicles in late endosomes. Targets also the unpalmitoylated endosomal SNARE TLG1 to the MVB pathway.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11788821}; Multi-pass membrane protein {ECO:0000269|PubMed:11788821}.
Interaction partners:
- UBX domain-containing protein 3
- DSC E3 ubiquitin ligase complex subunit 2
- Vacuole localized DSC protein 1
- DSC E3 ubiquitin ligase complex subunit 3
- Golgi/endosome-localized DSC protein 1
- E3 ubiquitin-protein ligase RSP5
- E3 ubiquitin-protein ligase PIB1
- Protein SSH4
- Metal homeostatis protein BSD2
- Protein ORM2
Sequence:
MEIDGNTLVFIIVILFLFFSSPGGDGVSSQYEFNQLQRLKQQFRTEHNTFVNMTYTDSFRNITGLKLSYQDMLNNPLQNATYPLPGKDYDRWFPNQNYMVLPNDVIEAINTEVWNTSNDDASNLFPPNITSTLLGKIDLVSNNKYEKIRMPVPRFYEPATDFSEDIPPEGETYWSEWPSYGELHNVSFQHGEIAIQISHMSNLQDNNNYLRRNFINKKNDRWKLLNLQIDFSDKAEKEKHSIYSKAVYDIQRGRILSISQSSKFHSLFALPHYMSFQNDYNEKIFNDVKELVDEFWNFTDYTDVMTMKDVQDAYNNANFKCEYLIFLQLEPWNQYTRDQIKLIDDELNWPLGRPANLSSLPPINVVSGLLYSPDCGVRLGLHNVKGTRYELKIMSIRKHLLFGIALFAAQIYLLLTQMHHTNTPSMVNKISFYCFSMINLVDGSLATLYFVAASVVPELYLPLVISAFSCFILASIFEIRYLISIYASQVNEQNVGIINLLRGNTGTYDENRPRPAFIPDEGSIGGSLYGRFFFMLIIFTFLILSSTSWPRQLRMVFEYILIFILNSYWIPQIFRNAVKGIPSRRERARSSIGGNRSQNKMPLLWSFVIGTTIIRSLPVVYVFTYSSNVFRHHKDVHFVVFLSLWLLFQISILYSQDVLGSRWFLPKHTIPDGYSYFKPLSNEYISEHGGGTAEHTVDCAICMSDVPIYIEEIPETHKVDQHSYMVTPCNHVFHTSCLENWMNYKLQCPVCRSPLPPL
Protein: Transcription elongation factor S-II, putative (Q586X9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00649}.
Interaction partners:
- Protein artemis
- DNA-directed RNA polymerase II, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-dependent RNA polymerases, putative
- Nitroreductase, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- Transcription initiation protein, putative
- Spt4/RpoE2 zinc finger domain-containing protein
- RNA polymerase-like protein
- TATA box-binding protein-like 1
Sequence:
MLQERVFHINDRVWLKTGANTWWPAKVTSVTGVEGVDGRSSETGTSTVTVLTYPGTQNKATYKNVDSHSSAITFFEPSSEKAVTANEDLLQAIRNAEEDKESNALRFEPTHSKNTAPRGTSQRAFSTSGRAGSLNNATQQTAGGKRSREVSRMRQRSTGSHLSPASDDALVQWKKDIDEATDNCDGALLTSTLLKLASVSVTLRQLLRTKIGVSVSRALSKKDLEEQRSLATCIISAWTAKLPEETVRAIEEYNKYEQEAKKRGGTARSGGARHNKRRGTISSSQTREERDVATPSTSESVGNPITIGGGAQPQFVDRVQKLLLQPGDPHSFSVRSDDLRSVAEKICAEVTRSEDRMYLLEHLSKPGLSEIRRRLAMGELSGKDFLELSRWELMTQEEKEDAERRTTEKLRNLEETERSLLHTTSLFECPECHGRECEWRELQIRSADEPTTKFIKCIKCKHNWSEN
Protein: Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF (EC 1.14.11.-) (Novofumigatoninbiosynthesis cluster protein F) (A0A2I1BSZ6)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: Fe(II)/2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Interaction partners:
- Peroxin-7
Sequence:
MTVSTPSKPHICRFPPGADPDVINQAFREDGVVILEGFLTPAQVDKVNCEMKPHLAKVRGGNMRYGPMDTSLETTLEPERRRIHNLAGLSETFRQDILNHPLMHELSRRVFSEFGDYWQYAGSVIDCAPGTPDQFLHRDQPAQKLFNVGPDAPEGFINFLTALTDFTKTNGATRFVWGSHRDWIDKSDENHPIVVAEVKAGDSLFFSGKIVHGGSFNGTNDTYRSSVALPIVPCIMTPYEANIHIPRSTVETMTPLAQRMIGWRSACLPDPYAIGTWTLNMNELGEQMGLKSKGYLEN
Protein: Uncharacterized WD repeat-containing protein C9G1.05 (O14301)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Cofilin
- Actin
- F-actin-capping protein subunit beta
- Actin-depolymerizing factor gmf1
- Fimbrin
- Twinfilin
- Tropomyosin
- Coronin-like protein crn1
- Adenylyl cyclase-associated protein
- F-actin-capping protein subunit alpha
Sequence:
MSSQLKSTWAPVPSTKPSQPCKIGTDFKGERIVYPANKAIIIREIEKQENCFQYNEHTAPTTVARFSPSGYYVASGDNQGNVRIWDCAGEDKILKNQVTAISGRITDLDWDGDSQRIIAVGEGKERYGHAFTADSGNSVGEIFGHSSVVNAVSLRKSRPFRAATASDDNSINFFHGTPYRFNRSLRVHSKFVYDVRYSPNDERFASAGADGKVYVFDGKTGDQVYEIDAHKGSIFSISWSPDSSQFVTSSAGYSCKIWDANTGSLIREWLSSDKKQLVGTVWPTKDLIIVVNSKGNLTYLNPSDCKVIDTIYGHQRSITAATLSPDATHFYTASYDGTVLSWDIGKQKAFPLVGESHTNQVMQMIMADDHVITIGMDDTLRVIDIKQGCFAKDNVFPTGYQPIGVCSVEDCLILVTVSDIQVLRSLTGVSTAKTIYQPSAVASHPLKSEFCVGGEDCCVYIHTLEKGELCEVAQCKDSTAPITCLAYSPDGKYLACGDASGKVVLYDANSREVITSRWAFHTGRILGMSWNAKSTHLATASLDTNIHIYSVERPMKYIAMKNAHSLGATQVEWVSENELLSTGSDAAIKVWSVTF
Protein: Homeobox protein TGIF2 (5'-TG-3'-interacting factor 2) (TGF-beta-induced transcription factor 2) (TGFB-induced factor 2) (Q8C0Y1)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor, which probably repress transcription by binding directly the 5'-CTGTCAA-3' DNA sequence or by interacting with TGF-beta activated SMAD proteins. Probably represses transcription via the recruitment of histone deacetylase proteins (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Note=Excluded from nucleoli. {ECO:0000250}.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Homeobox protein TGIF1
Sequence:
MSDSDLGEDEGLLSLTGKRKRRGNLPKESVKILRDWLYLHRYNAYPSEQEKLSLSGQTNLSVLQICNWFINARRRLLPDMLRKDGKDPNQFTISRRGGKASDVALPRGSSPSLLAVSVPAPTNMLSLSVCSMPLHSGQGEKPAAPFPQVELESPKALVTPASTLTLLTRAEAGSPTGGLFNTPPPTPPEQDKDDFSSFQLLVEVALQRAAEMELQKQQEPAPPLLHTPLPFVSENAK
Protein: Inner membrane protein YghB (P0AA60)
Organism: Escherichia coli (strain K12)
Function: May be a membrane transporter required for proton motive force (PMF)-dependent drug efflux. Required, with YqjA, for the proper export of certain periplasmic amidases and, possibly, other Tat substrates. May play a role in determining membrane lipid composition.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane protein YabI
- TVP38/TMEM64 family inner membrane protein YdjZ
- TVP38/TMEM64 family membrane protein YdjX
- Inner membrane protein YqaA
Sequence:
MAVIQDIIAALWQHDFAALADPHIVSVVYFVMFATLFLENGLLPASFLPGDSLLILAGALIAQGVMDFLPTIAILTAAASLGCWLSYIQGRWLGNTKTVKGWLAQLPAKYHQRATCMFDRHGLLALLAGRFLAFVRTLLPTMAGISGLPNRRFQFFNWLSGLLWVSVVTSFGYALSMIPFVKRHEDQVMTFLMILPIALLTAGLLGTLFVVIKKKYCNA
Protein: Dpr-interacting protein delta, isoform B (IP09803p1) (Q4QQ69)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVLPSKKYKTDYTENSYRAHMKLTIRNLQYGDFGNYRCISKNSLGETEGSIRVYEIPLPSTPSKQVTHTTVESRENNIIPSSRNDTTKSLQTDVGYAMKNDLYPGSASSSSSGGSSSAASSSSSMQTSALPGGVAGNSLSSMGSKGSLAIGKSTFYTERPPNEYAASSVAGLLLHRALLFGSGIYLTLL
Protein: DEAD-box ATP-dependent RNA helicase rde-12 (EC 3.6.4.13) (RNA interference defective protein 12) (P90897)
Organism: Caenorhabditis elegans
Function: Probable ATP-dependent RNA helicase involved in RNAi-mediated gene silencing. Specifically required in the endogenous siRNA pathway for biogenesis of secondary endogenous small interfering RNA (siRNA) intermediates called 22G-RNAs. May associate with and recruit rde-10 to primary siRNA-targeted mRNA for secondary siRNA synthesis. May be recruited to target mRNAs by rde-1 and/or ergo-1.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:24684931}. Cytoplasmic granule {ECO:0000269|PubMed:24684930, ECO:0000269|PubMed:24684931}. Cytoplasm {ECO:0000269|PubMed:24684931}. Cytoplasm, P-body {ECO:0000269|PubMed:24684930}. Note=Colocalizes with pgl-1 in perinuclear P granules. Colocalizes with rsd-6 in a subset of germline and embryonic foci. {ECO:0000269|PubMed:24684930}.
Interaction partners:
- Piwi domain-containing protein
- Nuclear RNAi defective-3 protein
- Argonaute protein hrde-1
- Splicing factor 3B subunit 1 domain-containing protein
- Pre-RNA processing 21
- Matrin-type domain-containing protein
- Splicing factor 3B subunit 4
- Splicing factor 3A subunit 2
- PHD finger-like domain-containing protein 5A
- PSP proline-rich domain-containing protein
Sequence:
MSSFGNNAGGGGREYHDDRSNRDHRHGNGGSDAGQRRREDHNSSYQSYRRPDGRQDSYGGGHQGNHGNSYGRREDDRSHSRDNHGGSRYGERDDRGNNGRSADNRYSQSNYNYDSNRGGQHYQRDNHGSKDDRGPMNQYNDHGSNHNSNSRNDQYRQGSYQGDGHSGYRRDDDRRRNDNDQARPYQSNRDSDRNSPRDHHNYNSQSSPRSHQGGQDRYSAPKEDNQRRYDNHQGGHDSYRGQNSGGYSGNNSGEYRNDYRSQQDSRDHRSGGNNSSSGFKNDGGFGGNDNRGFGNNGGGSFGNPNNSYRGNSNNIGGFHRSDGSNSEGVNAPVRAPRDWVPVTRDIDELVRETADRLADCDVGQDRAVEIRNAEKDVRLTSWTNSGLHPTILETLKRIKYNNVRTIQGAMIPQVLDGHDVLGQAETSAGKTAAFGLPIIDKILRMDEETRNKARQDDGPLALILAPTRELAAQIHEALRTYCQNTDIIVLLSYGQSDRARSLNEIRNGCDILIGTCGRIMDFTVKSHISLLHLRFLVFDEADRLLQDMKKDPLGHLGAIIKDAGFMESAATRQTIMTSATFNASVMTVANELMKRLPGQDEMIKIVLANGRLSKRVNLEFFECKGLAEKNAKLREILKQNVNGKTLKTIIFVQKKDQCDACAAKLTSGGMLAQTLHGDRSQDMREKLINDFKSNRVNLLVTTDLLSRGIDVSDLDRVINFDLPDGDPDQGADTFIHRAGRTGRTGRKENGLCVSFVDPQSDRDSLLAPKLVELIISQNLPDLKVPDFLDAMAKSSRGKSGTSGFGQRGGYGGRGGGFGGTGRGRGGGVFGGGGRGGDFGGSGNFGGSGGGGSFGGSGGGGGFGGVKPSGFGGSRNNAEPTSSGGGFGAPKAPTGFPSDNNDASEDAPAAGGFGFSTKAAQDAKKAEESATLGSSTFGTANNADEEPTETGADGNDDDEW