ID A0A3Q0HDI2_ALLSI Unreviewed; 1741 AA.
AC A0A3Q0HDI2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=KAT6B {ECO:0000313|RefSeq:XP_025068548.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025068548.1};
RN [1] {ECO:0000313|RefSeq:XP_025068548.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR RefSeq; XP_025068548.1; XM_025212763.1.
DR Proteomes; UP000189705; Unplaced.
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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR CDD; cd15527; PHD2_KAT6A_6B; 1.
DR Gene3D; 3.40.630.30; -; 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; 1.
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; IPR036388; WH-like_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; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1..36
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 431..705
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 77..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 710..737
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 187..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..827
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1097
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 607
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1741 AA; 194945 MW; 0ADC124E8ED999C8 CRC64;
MLFCDSCDRG FHMECCDPPL SRMPKGMWIC QVCRPKKKGR KLLHEKAAQI RRRYAKPIGR
PKNKLKQRML SVTSDEGSMN AFTGRGSPGR GQKTKVCTTP SSGHAASVKD SSSRLPVTDP
TRPGATTKIT TTSTYISAST LKVNKKTKGL IDGLTKFFTP SPDGRRSRGE IIDFSKHYRP
RKKVSQKQSC TSHVLATGTT QKLKPPPSSL LPPTPISGQS PNSQKSSTST SSNSPQSSSS
QSSAPSVGSL PNNSQLKGLF DGLSHIYTTQ GQSRKKGHPS YAPPKRMRRK PELSSASKSN
THFYGKKEVR SRFISHSSAS GWGVSRGRAF KAIAHFKRTT FLKKHKILGR LKYKVTPQMG
TPSPGKGSLA DGRIKPDQDN DTEIKLSIKQ ENTDVFLVGS KDTVTEEDLE VFKQARELSL
EKIGCKNTGE TTGRYPSVIE FGKFEIQTWY SSPYPQEYAR LPKLYLCEFC LKYMKSKNIL
LRHSKKCGWY HPPANEIYRR NDLSVFEVDG NVSKIYCQNL CLLAKLFLDH KTLYYDVEPF
LFYVLTKNDE KGCHLVGYFS KEKLCQQKYN VSCIMIMPQY QRQGFGRFLI DFSYLLSRRE
GQAGSPEKPL SDLGRLSYLA YWKSVILEYL NCHHEKQISI KGMSRATGMC PHDIATTLQQ
HSMIDKREDR FVIIRREKLI LNHMEKLKAN PRVNEVDPES LRWTPLLVSN AAVSEEEREA
EKEAERLMEQ ASCWEKEEQE IFSTRANNRQ SPAKVQSKNK YLRSPESVAV VGDRGQSTEQ
CKESSEDDEG EENHPSSPPR LTKPQSLAMK RKRPFILKKK RGRKRRRINS SVTTETISET
TEVLNEPFDN SDEERPMPQL EPTCEIDGED DELKPVIRKV FQYHPGRQKQ DEEEEQDKED
KESHDCNNAD QCKSNMEDAA VLEESTKDNP EPLRCKQGWP KGVKRGPSKW RQNKDRKPGF
KLNLYTPPET PMEPDYQVTV EEQKEEAEDK LCQVPPVAEE ENKEVVKVTQ PQDELTDPEP
EPPNPPSEPF EKMENEDMKV EEEDKNVEEE EEKVRAKDQK KDQLEETLIQ KEESEQLDDR
EEEEEEEEEP SHNEDHDADD EDDSHMGSTE VEKEELPGEA FKEMLENQES FLDVNVQTSN
SNQEDLMDCG VDLAADCEGN HKELTADPEP VPESDDDHTD NNQDQKDSEK LNSGFKEENT
ETMEIDSETV QAVQSLTQEA SEQEDAFQDC AETQEACRSL QNYTHTDQSP QMTTLDDCQQ
SDHSSPVSSV HSHPSQSVRS VNSPNVAPLE NSYAQISPDQ SAISVPSLQN METSPMMDVP
SVSDHSQQVV DSGFSDLGSI ESTTENYENP SSYDSTMGSS ICGNNSSQNS CSYSNLTSSN
LTQSSCAVTQ QMSNINGSCS MMQQTNISSP PTCNVKSPQG CVVERPPSSN QQLSQCSMAA
NFTPPMQLTE IPETGSANIG LYERMGQSEF GAGHYPQPSA TFSLAKLQQL TNTLMDHSLP
YSHSAAVTSY ANSASLSTPL SNTGLVQLSQ SPHAVPGGPQ AQATMTPPPN LTPPPMNLPP
PLLQRNMAAS NIGISHTQRL QTQMAGKGHV SVRTKSTPLP PAATAHQPQI YGRASQTVAM
QGPARTLTMQ RGMNMSVNLM PAPAYNVNSV NMNMNTLNAM NGYSMSQPMM NSGYHSNHGY
MNQTPQYPMQ MQMGMMGTQP YAQQPMQTTP HSNMMYTPPG HHGYMNTGMS KQSLNGSYMR
R
//
