ID K1RAE7_CRAGI Unreviewed; 2037 AA.
AC K1RAE7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=CGI_10025017 {ECO:0000313|EMBL:EKC31016.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC31016.1};
RN [1] {ECO:0000313|EMBL:EKC31016.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC31016.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000780};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; JH818313; EKC31016.1; -; Genomic_DNA.
DR RefSeq; XP_019930512.1; XM_020074953.1.
DR HOGENOM; CLU_233323_0_0_1; -.
DR InParanoid; K1RAE7; -.
DR OMA; QSNYMAV; -.
DR OrthoDB; 118560at2759; -.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR CDD; cd15618; PHD1_MOZ_MORF; 1.
DR CDD; cd15527; PHD2_KAT6A_6B; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 4.10.320.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR048589; SAMD1-like_WH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00538; Linker_histone; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF21524; SAMD1_WH; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF103637; CCHHC domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKC31016.1};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ SEQUENCE 2037 AA; 226116 MW; 71AAA7928A60D1B7 CRC64;
MVKDSEKDRL SDPTYAKWLL DAINKVKHQK QRPNFTRICN AVRQFHQVSQ ESIAEQLELT
VQDGLILKVA SKDGNWTYRD PSGVTPCKNR SLKVTLNMDL TKIIVKTIKE LADPQGSNLK
KIKSYIISTY NLDVEEGVEL GEQLKVSLKK GVASGHLVRD GHCIKVGNKG LDESTASSSN
SGSYDEDSAS DLSFCFEQKT KCAKPVLICC FCLGDENKNR DGVPEDLISC AECGNSGHPS
CLKFSPELTE TVKKLRWQCI DCKTCSFCQK SGREDNMLFC DLCDRGFHME CCDPPLSKAP
KGKWKCNICD PDRGNGKGRH FLEMAAKLAK KQKPNKSHHK DKNDAAKCPT PGCDGTGNVN
SKSAYHRTQL ACPKLTAQQR KICRIQKKYR NNKNGDVSES DEETGNVHKS NSRPTKEHPS
SADGSNDSSD EDVSHTFEPF FNIDKPKGLV DGLSKFFTPT NKRTSRVSLN SYNADLAAIP
KHKKMNDQTK SNSQQAANRL IKRSKYLQAN KARRKCLEPP GSGQLKGLFD GLSHLYTAQG
DRTKSHEQLN QDASKKNSKY DFIPVIDETM FTSVKDKLAE SDDSSISSSS AGSSSETSSE
DEQENSFATP SMSNSNSFLT GKHKGFVKRR GAGRGKKPLS ERQVGVGKVV KRGFGRGPGR
PPWKHLIGSV YLGRERVIDK NGLTNHKFNK GHGLKGGKGF SHGNVSEKNG SIKNFFSPKS
ASTPSPRGRG RGAVSHKNSL ADRSAHTTPK GRGRGAVAGK RPSSVSSHSS DNSDDEEEEE
EEVDLSSGLP PGVSDEDLLL FKQAQEKAQE ALLEDAARQN GEPEVAAATP VPLPAVPGGP
GRFPPCIEFG KYEIQTWYSS PYPQEYAKLP KLYICEYCLK YMKSRNILQR HMEKCDLLRP
PANEIYRKDD LSVFEVDGNA SKIYCQNLCL LAKLFLDHKT LYYDVEPFLF YVLTLNDEYG
SHLVGYFSKE KHCQQKYNVS CIMTMPQYQR KGYGRFLIDF SYMLSRVEGH PGSPEKPLSD
LGKVSYLAYW KSVIIEYLHK YQDSRITIKG MSRATGMCPH DIAHSLEMLN MVAQKDDKIV
IAVNKELVKV HMEKLEAKKH LRIDLDQDCL RWTPLISNYV ISEEERKAET ELREMTQMVN
RIAEDMEWIE TVSPTVSPQK GRLFLDVRSP KLMDALASPT KLAAEAKNST SPFKTEENQV
KTPLKEEMDD SSESEMEENH VKSKKESPKK EEKANHPKRK VGRPPGKRKH LDTDLDPQES
KKKRLEKESQ DNDPVDHSGK ENDEQNEKEV SEVKRDEEVP KAKGRRGWPK GVPRGSPVVS
SPQKKKGRPP KNSYRTLMES KKEASSEKNH AKTNENSDSC DIKDQSSCNE NGLFSKTSNE
QDDSVNSPEG NIDLDDLSKE LASGSRESDS SDSESESDNE NVSREIEEAV QALQDAEQTD
MEDMQSDLND MVKKDDDETE QQRERHTPDD LPIPDPSPAP IAIGGDGISD TNSDVPAPLT
PQVPTPSKDP STPECSLLKS HHQEETPSLG PKTDILLESK SDSKLDGMRV SGSPEDPAHE
TDDDDIPSDD NFPEDEINSP SLCGARNLET CLSSDIQDNF DQITNTSANN SIQSNEQMTP
QSVNNCVENP PSVPSVKHSP LPTTSQHQPT MVQQPHLQNQ TCNNMQSVFT PQPNGMNNLQ
PGSNLGSTYG AVDIDVVTQM DLESPTSISS SELQNPISSG TDTTCVSNVQ QAQTLNSMQN
TAPALIGSFS DCAQQMPQPY QQVNMMQGAR YMDMVNTSST GYNMSPSTNT MPYCSSSASS
YTSVLLQQNT TQRLTHSATP CPIPQVPINR QNSAPAGYAA NSCSLAKLQQ LTNGLSDLSG
MPDNQMTPPP TMTPPPPHMT PSRQNLATPP VPNLQSQAVS GAVSLQQTYK QYQRQRANPR
KSPNISVNPN MTTFTPNVTI RTGSNMIVGN YGNFQDIYRM QQQTFNQSYM NHHGFINSRL
QTPQLPMQMF PNMNMNVNPA QQHFQQHMQP PQSNNMYTYG YINGQLGPSL NNGVMRR
//
