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SWC4_GIBZE
ID   SWC4_GIBZE              Reviewed;         624 AA.
AC   Q4HY90; A0A0E0RVY3; I1S052; V6RRV9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=SWR1-complex protein 4;
GN   Name=SWC4; ORFNames=FGRRES_10068, FGSG_10068;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
CC   -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC       dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC       transcriptional regulation of selected genes by chromatin remodeling.
CC       Component of the NuA4 histone acetyltransferase complex which is
CC       involved in transcriptional activation of selected genes principally by
CC       acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also
CC       involved in DNA repair (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex and of the
CC       NuA4 histone acetyltransferase complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SWC4 family. {ECO:0000305}.
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DR   EMBL; DS231669; ESU16737.1; -; Genomic_DNA.
DR   EMBL; HG970332; CEF75408.1; -; Genomic_DNA.
DR   RefSeq; XP_011318999.1; XM_011320697.1.
DR   AlphaFoldDB; Q4HY90; -.
DR   SMR; Q4HY90; -.
DR   STRING; 5518.FGSG_10068P0; -.
DR   EnsemblFungi; ESU16737; ESU16737; FGSG_10068.
DR   GeneID; 23556990; -.
DR   KEGG; fgr:FGSG_10068; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G07207; -.
DR   eggNOG; KOG2656; Eukaryota.
DR   HOGENOM; CLU_018539_3_1_1; -.
DR   InParanoid; Q4HY90; -.
DR   PHI-base; PHI:1525; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043968; P:histone H2A acetylation; IEA:InterPro.
DR   GO; GO:0043967; P:histone H4 acetylation; IEA:InterPro.
DR   InterPro; IPR032563; DAMP1_SANT-like.
DR   InterPro; IPR027109; Swc4/Dmap1.
DR   PANTHER; PTHR12855; PTHR12855; 1.
DR   Pfam; PF16282; SANT_DAMP1_like; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..624
FT                   /note="SWR1-complex protein 4"
FT                   /id="PRO_0000076341"
FT   DOMAIN          146..221
FT                   /note="SANT"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  69444 MW;  49C39529554AEF51 CRC64;
     MTSSDVRDVL NLGDGTVGPR SSKKQKLAAP RPNLKGLARE VQNLGGDNPI AIVPEVTHFK
     KRRFTSRKPT AKWEMRPFKN SARSDSNFTL RHWRRKDEKQ EGIDESQEQI SQGDQPQPQK
     NELEDSAFAK YNVQVSVPQY SEGQYQQSLQ HVDWTKEETD YLLELAQDFD LRWPLIWDRY
     EWNPPATNGE ADDDGDESKA IVPATRSRTL EDLKARYYEV ASKMMAAQKP VQYMTQPEFS
     LHELMAHFNP QQEKLRKEFA LNALTRSREE AREEESLLLE IKRILARSER FNDERRELYN
     RLDYPRSDTD INAFKSSAGL QNLLQNLVTA DKTKKRKSLM PGDVNSPAGT VPPQTAAAAS
     AAATAAAVAQ EAGRRESTAA STGPRESTGP APTPAAANNK KGQQQQQERR KLTTQEELLY
     GVTHHDRLGS GPTFRTEKIN KLFSHKSNQQ QMRITNVLNE LDVPNKLIMP TAATTHQYEQ
     LLAAVNSLLD ARKVSDKLDQ EIKTEQAKKA ERQKAMAPPE AESTAENGQT GQEKKDGDDG
     EACAAAVTAD TSKEETNGDA TSAAGDATKD GLETAVLTSE APDAPPKETE QNIDERPGSS
     GAPHKRSASV LSNVSDKSNK RQKK
 
 
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