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AF9_NEUCR
ID   AF9_NEUCR               Reviewed;         309 AA.
AC   Q7RZK7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Protein AF-9 homolog;
GN   Name=yaf9; ORFNames=NCU00359;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Component of the SWR1 complex which mediates the ATP-
CC       dependent exchange of histone H2A for the H2A variant H2A.Z 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 histones H4 and H2A. The NuA4 complex is
CC       also involved in DNA repair. Yaf9 may also be required for viability in
CC       conditions in which the structural integrity of the spindle is
CC       compromised (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: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00376}.
CC   -!- DOMAIN: The coiled-coil domain is required for assembly into the NuA4
CC       complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the YAF9 family. {ECO:0000305}.
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DR   EMBL; CM002238; EAA28594.1; -; Genomic_DNA.
DR   RefSeq; XP_957830.1; XM_952737.3.
DR   AlphaFoldDB; Q7RZK7; -.
DR   SMR; Q7RZK7; -.
DR   STRING; 5141.EFNCRP00000000220; -.
DR   EnsemblFungi; EAA28594; EAA28594; NCU00359.
DR   GeneID; 3873857; -.
DR   KEGG; ncr:NCU00359; -.
DR   VEuPathDB; FungiDB:NCU00359; -.
DR   HOGENOM; CLU_051385_2_0_1; -.
DR   InParanoid; Q7RZK7; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.60.40.1970; -; 1.
DR   InterPro; IPR037989; Yaf9.
DR   InterPro; IPR038704; YEAST_sf.
DR   InterPro; IPR005033; YEATS.
DR   PANTHER; PTHR23195; PTHR23195; 1.
DR   PANTHER; PTHR23195:SF15; PTHR23195:SF15; 1.
DR   Pfam; PF03366; YEATS; 1.
DR   PROSITE; PS51037; YEATS; 1.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; Coiled coil; Cytoplasm; DNA damage;
KW   DNA repair; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..309
FT                   /note="Protein AF-9 homolog"
FT                   /id="PRO_0000215930"
FT   DOMAIN          8..167
FT                   /note="YEATS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT   REGION          175..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          265..309
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        187..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   309 AA;  34667 MW;  79FFB073B131CEFD CRC64;
     MAPPTGKRVK GVQIFRPFVY GTTARPFDEK TNPKPPGIPD DHTHSWTVFI KGIDDVDITY
     WLRRVQFKLH ESIPNHVRMV EGVKGQPFQI HETGWGEFEI TMKLYYVPES SEKPQTLYHH
     LRLHPFGRTE EEKEAMRLNG GEVISWVYEE QIFNEPYEPF YDILISGALP PSASTLKDGG
     GGGGSGAATP TSANTPGASS SKGGNKKGHE RSHSRASVST NKDGKNNNES KEEPFVIQKS
     EGGVLERSAM IPLVNRPGQP FSRETEQLEI QKLKEAKLKV DEMKKQMMEE LEKKQKRLEA
     LRAESAKAP
 
 
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