ID H3AME8_LATCH Unreviewed; 1506 AA.
AC H3AME8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
GN Name=KAT6A {ECO:0000313|Ensembl:ENSLACP00000010819.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000010819.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000010819.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU361211};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}.
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DR EMBL; AFYH01135616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01135617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01135618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01135619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000010819; -.
DR Ensembl; ENSLACT00000010899.1; ENSLACP00000010819.1; ENSLACG00000009523.1.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000156962; -.
DR HOGENOM; CLU_001232_0_1_1; -.
DR InParanoid; H3AME8; -.
DR OMA; ECIIEPI; -.
DR TreeFam; TF106483; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000009523; Expressed in post-anal tail muscle and 2 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0010172; P:embryonic body morphogenesis; IEA:Ensembl.
DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0014036; P:neural crest cell fate specification; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 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 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 PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF26; HISTONE ACETYLTRANSFERASE KAT6A; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Nucleus {ECO:0000256|RuleBase:RU361211};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 65..339
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..687
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 241
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1506 AA; 169052 MW; 7F99B5DD10EBDA9E CRC64;
MRKKGRKSST SEWLTDNQEI WDGKRENEDK PPGSEDVVTE KDEELFRDIQ ELALQKVGVT
GPPDPQVRSS SVIEFGKYEI QTWYSSPYPQ EYTRLPKLYL CEFCLKYMKS KTILQQHMKK
CGWFHPPANE IYRKDNLSVF EVDGNISTIY CQNLCLLAKL FLDHKTLYYD VEPFLFYVLT
LNDSKGCHLI GYFSKEKHCQ QKYNVSCIMI LPQYQRKGYG RFLIDFSYLL SKREGQAGSP
EKPLSDLGRL SYMAYWKSVI LECLYYNQEK QISIKKLSKL TGICPQDITS TLHHLGMLDF
RGDRFAIIRR EKLIHDQMAK LQANPRPIEV DQECLRWTPV IVSNSVVSEE EEDDDDEEEG
KGTPESDCKE LVKPITSWNK GDEGFSSIQN GNRFETQVPG NTLGKIRQVL PLKNLPANGE
PSRRGRWGRK GKRRRGRFHD KEEPSLLEER GRLPKQWHSD GMEIQKKHPR KEGSLKRRFS
RSCERLRGRL SVGINTLSRR FSESSEEEMD GARPNSPPVL TKPTLGLGLK GKKPVIHRKR
RERKRKLHNS SVVTETISET TEVLDEPFED SDSERPMPRL EPTFEKEEEE ELGKRETFSR
GYFRCLPPRA TLKQRSTSKK KCREADAESD DANGTPILKP ISPVNKSEIK DSGDATDVAV
PVKKKKGWPK GKRRKPIHWK KRPGRKPGFK LNRDIMPKPA VENGITSACN VAKPGRKPRS
QIRTSSVKDQ KEDILLVEEK KEDRPIEADE EEEEDASICK GQGSLQVDPG IPLSEPKVVK
LFGDNEEDGD EDEKEEKPRS PGEQRQTDDE REELEDNDHE EEEETKVATV ALTARNQNED
HDADDEDDSN LDSTEKNEVE NQPTKDEVKE EPPPPESFLE TRNQSDDKEE EETKNEGEPD
SEEEQVSHET SLDSVHIPGS EEDPAEEQED TKESLIQEFK EEEDIPHTEL DLETVQAVQS
LTQEESNEHD AAYQDCDETL AACQTLQSYN QSEEDPHISM VEDCQASEHN SPISSVQSHP
SQSVRSVSSP SVPTLESSYT QISPEQGSLS APSMQNMETS PMMDVPSVSD HSQQVVDSGF
SDLGSIESTT ENYENPSSYD STMGGSICGN NSSQSSCSYS GLSSSSSLTQ NSCAVTQQMT
NSSCSLMQQS SVPPPANCNI KSPQSCVVER PPSSNQPQPQ QPQSQQQQQP PPQQPPPPPP
AQQQQAPPPL SQCSMTNNFS TPMIMEIPES GNSNNMSLYE RMGQGDFGAG GYPQPSATFS
LAKLQQLTNT IMDPHAMPYS HSPAVTSYAT SVSLSNTGLA QLAPSPHPLS GTPQAQTTMT
PPPTMNLTSS LLQCNMPATN IGIPHTQRLQ GQMPVKSHIA IRSKSAPLPA AAPAHQQQIY
GRSTPAVSMQ AGPRALAVQR GMNMGVNLMP TPPYNVNSMN MNTLNAMNSY RMTQPMMNSS
YHSNPAYMNQ TAQYQMQMGM MGGQAYTQQP MQPNPHGNMM YTGPSHHSYM NAGVPKQSLN
GPYMRR
//
