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ARP4_EMENI
ID   ARP4_EMENI              Reviewed;         472 AA.
AC   Q5AW89; C8VBB5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Actin-related protein 4;
DE   AltName: Full=Actin-like protein arp4;
DE            Short=Actin-like protein 4;
GN   Name=arp4; ORFNames=AN7441;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Chromatin interaction component of the NuA4 histone
CC       acetyltransferase complex which is involved in transcriptional
CC       activation of selected genes principally by acetylation of nucleosomal
CC       histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Is
CC       required for NuA4 complex integrity. Component of the SWR1 complex
CC       which mediates the ATP-dependent exchange of histone H2A for the H2A
CC       variant HZT1 leading to transcriptional regulation of selected genes by
CC       chromatin remodeling. Component of the INO80 complex which remodels
CC       chromatin by shifting nucleosomes and is involved in DNA repair (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex, of
CC       the INO80 chromatin remodeling complex, and of the SWR1 chromatin
CC       remodeling complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP4 subfamily. {ECO:0000305}.
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DR   EMBL; AACD01000129; EAA62021.1; -; Genomic_DNA.
DR   EMBL; BN001304; CBF79387.1; -; Genomic_DNA.
DR   RefSeq; XP_680710.1; XM_675618.1.
DR   AlphaFoldDB; Q5AW89; -.
DR   SMR; Q5AW89; -.
DR   STRING; 162425.CADANIAP00000532; -.
DR   EnsemblFungi; CBF79387; CBF79387; ANIA_07441.
DR   EnsemblFungi; EAA62021; EAA62021; AN7441.2.
DR   GeneID; 2869645; -.
DR   KEGG; ani:AN7441.2; -.
DR   VEuPathDB; FungiDB:AN7441; -.
DR   eggNOG; KOG0679; Eukaryota.
DR   HOGENOM; CLU_027965_6_2_1; -.
DR   InParanoid; Q5AW89; -.
DR   OMA; GIVEKRC; -.
DR   OrthoDB; 649708at2759; -.
DR   Proteomes; UP000000560; Chromosome IV.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR   GO; GO:0000812; C:Swr1 complex; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   Activator; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..472
FT                   /note="Actin-related protein 4"
FT                   /id="PRO_0000089096"
SQ   SEQUENCE   472 AA;  51437 MW;  87FD5B0C4BFF8762 CRC64;
     MNASVPPSAA EYGGDEVSAI VLDPGFSTTR AGFAGEDTPK SLVPTYYGKY SFEGQEKLIF
     GDDVFVTPRP SLSVGNPMGR DGVVEDWDMA EKLWEYSFTS RLTGAKPSNP LHNGLNDLVE
     GELPTEMEGV ETNEKPLADS PLLMSECSWN PTKAREKTIE IAMEKWGTPA FYLARNGVLA
     SFAAGKASAL VVDIGASNIS VTPVHDGMVL KRGVQHSPLG GDYISSQIRA LFKTNTPQPI
     TITPHYLISS KTAVEAGQPP QAKYKTFPPE KAPDASYRSL LEERTLTEFK ECVVQVWPGP
     TKLSAPGPNG VPNEEMARST PGRPFEFPDG YNQVFGVDRY RVVESLFDAK ATILDPDSQF
     PAPTPAQTIP ELIKAALNGV DVDLRPHLLA NVVVTGASSL LYGFTDRLNQ ELMQLYPGPR
     VRISAPGNTS ERRFSSWIGG SILASLGTFH QMWISKKEFD EHGPNIVEKR CK
 
 
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