ID G5C7I6_HETGA Unreviewed; 2108 AA.
AC G5C7I6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=GW7_13174 {ECO:0000313|EMBL:EHB17497.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB17497.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB17497.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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 -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; JH173684; EHB17497.1; -; Genomic_DNA.
DR STRING; 10181.G5C7I6; -.
DR eggNOG; KOG2747; Eukaryota.
DR InParanoid; G5C7I6; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15618; PHD1_MOZ_MORF; 1.
DR CDD; cd15527; PHD2_KAT6A_6B; 1.
DR Gene3D; 3.40.630.30; -; 2.
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; 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:SF73; HISTONE ACETYLTRANSFERASE KAT6B; 1.
DR Pfam; PF01853; MOZ_SAS; 2.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF21524; SAMD1_WH; 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); 2.
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; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHB17497.1};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 103..176
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 215..274
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 271..322
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 716..1040
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 72..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1045..1072
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 473..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1153
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1187
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1415
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1469
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 942
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 2108 AA; 235660 MW; F915FF9D3F1CCB00 CRC64;
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSASH GLDKKTVSEQ LELSVQDGSV
LRVTNKGLAS YKDPDNPGRF SAVKPGTFPK SAKGSRGSCN DLRNVDWNKL LRRAIEGLEE
PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGGLD
GKAKAAPQYP SAFPSSLPPV SLLPHEKDQP RADPIPICSF CLGTKESNRE KKPEELLSCA
DCGSSGHPSC LKFCPELTTN VKALRWQCIE CKTCSACRIQ GKNADNMLFC DSCDRGFHME
CCDPPLSRMP KGMWICQVCR PKKKGRKLLH EKAAQIKRRY AKPIGRPKNK LKQRLLSVTS
DEGSMNAFTG RGSPGRGQKT KVCTTPSSGH AASGKDSSSR LAVTDPTRPG ATTKITTTST
YISASTLKVN KKTKGLIDGL TKFFTPSPDG RRSRGEIIDF SKHYRPRKKV SQKQSCTSHV
LATGTTQKLK PPPSSLPPPN PISGQSPSSQ KSNTSTSSTS PQSSSSQSSV PSFSSLTNNS
QLKALFDGLS HIYTTQGQSR KKGHPSYAPP KRMRRKTDLS STAKSKAHFF GKRDIRSRFI
SHSSSSWGMS RGSIFKAIAH FKRTTFLKKH RMLGRLKYKV TPQMGTPSPG KGSLADGRIK
PDQDDDTEIK ISIKQENTDV NMIGNKDVVT EEDLDVFKQA QELSWEKIEC ESGVEDCGRY
PSVIEFGKYE IQTWYSSPYP QEYARLPKLY LCEFCLKYMK SKNILLRHSK KCGWFHPPAN
EIYRRKDLSV FEVDGNMSKI YCQNLCLLAK LFLDHKTLYY DVEPFLFYVL TKNDEKGCHL
VGYFSKEKLC QQKYNVSCIM IMPQHQRQGF GRFLIDFSKP LDEVCGPIYH HPHLTVPAEE
EASLCWIAIA DVGLWATQFF MSRPLFTSYL LSRREGQAGS PEKPLSDLGR LSYLAYWKSV
ILEYLCHHHE RHISIKAISR ATGMCPHDIA TTLQHLHMID KRDGRFVIIR REKMILDHME
KLKTCSRVNE LDPECLRWTP ILISNVAVSE EEREAEKEAE RLMEQASCWE KEEQEILSSR
ANSRQSPAKV QSKNKYLHSP ESRPGAGERG QLMEMAKESS EEEEEEEDEE EEDDEEEEEE
EEEEEEEEEE EENIQSSPPR LTKPQSVAIK RKRPFVLKKK RGRKRRRINS SVTTETISET
TEVLNEPFDH SDEERPMPQL EPTCELELEV EEESRKPVLR RAYQHQPGKK RQTELEEGKD
NHCFKNAGPC RNNTDDDANN LKEGSKDNPE PLKCKQAWPK GTKRGVSKWR QNKERKTGFK
LNLYTPPETP MEPDEQVTVE EQKEISEDRS SPALMEMEQE VRETTEAPLP RDGNRREDSC
VPGSPHKSPS EKPADLIKPE EEEEEEEEEE EGTVEKDPDD ARSQEKEEPE ISMSKEDHVH
QDDHEEEEEE DEEPSHNEDH DADDEDDSHM ESTGVEKEEL PREAFKEVLE NQEAFLDLSV
QPSYSNPEVL MDCSVGTTAS CHSEPKELSG DTETAPESDE EPPEEQAKKQ DQKDSEEVES
EFKEGNMATM EIDSETVQAV QSLTQENREQ DDTFQDCAET QEACRSLQNY THADQSPQIA
ATLDDCQQSD HSSPVSSVHS HPGQSVHSVN SPSVPTLENS YAQISPDQSA ISVPSLQNME
TSPMMDVPSV SDHSQQVVDS GFSDLGSIES TTENYENPSS YDSTMGGSIC GNSSSQNSCS
YSNLTSSNLT QSSCAVTQQM SNMSGSCSML QQTTISSPPT CSVKSPQGCV GERPPSSSQQ
LAQCSMAANF SPPMQLADIP ETGNANIGLY ERMGQSDFGA GHYPQPSATF SLAKLQQLTN
TLIDHSLPYS HSAAVTSYAN SASLSTPLSN TGLVQLSQSP HSVPGGPQAQ ATMTPPPNLT
PPPMNLPPPL LQRNMAASNI GISHSQRLQT QIASKGHISM RTKSASLSPA AATHQSQIYG
RSQTVAMQGP ARTLTMQRGM NMSVNLMPAP AYNVNSVNMN MNTLNAMNGY SMSQPMMNSG
YHSNHGYMNQ TPQYPMQMQM GMMGTQPYAQ QPMQTPPHSN MMYTAPGHHG YMNTGMSKQS
LNGSYMRR
//
