ID A0A401NFX6_SCYTO Unreviewed; 1954 AA.
AC A0A401NFX6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-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};
DE Flags: Fragment;
GN ORFNames=scyTo_0012610 {ECO:0000313|EMBL:GCB59840.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB59840.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB59840.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB59840.1}.
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DR EMBL; BFAA01006140; GCB59840.1; -; Genomic_DNA.
DR STRING; 75743.A0A401NFX6; -.
DR OMA; DSARCTT; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:UniProt.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15646; PHD_p300; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF34; CREB-BINDING PROTEIN; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 1.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50134; ZF_TAZ; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 58..137
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 588..660
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 719..799
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 808..1185
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1187..1235
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1250..1331
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 1250..1331
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 140..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1087
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1847..1878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1895..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GCB59840.1"
SQ SEQUENCE 1954 AA; 216458 MW; 99C5B9AD2139C270 CRC64;
GTNQMNVVGG MGVPTPDQSN LIDSALPPSL GTPNQMMGDG SNVGSIGTLP TAAPSTSAVR
KPWHEHVTQD LRNHLVHKLV QAIFPTPDPA ALKDRRMENL VAYARKVEGD MYESANSRDE
YYHLLAEKIY KIQKELEEKR RSRLQKQQGM LPNQGTLTGP GGQPPGMSPA PGMAQVQPVR
PPNGPLSMPN VPNQIINRMP GSQGMSQFGS MSLGNVQMPQ GPMGPRGTPP MNHTVQMSTM
GSIPTLGMPP SRLPQPQGIL GVHTNNIGQP PSQNQFLNQN QFSAASGGMN VNNVGISQTT
NQPGMNQTQA PGISLPLNNS VSMIGLPNAQ MHCPPVSQPT LRQTPSPASV SAPVVATAAG
NLPSIQHPTL SSMSSPQPTT SQSQASTPAS SSGRASTPTP VRSTTPNQTP PRTQTPTRPP
TPVQSQQSIP TPQPMQQATG PPQPATPLSH SAASADGKVA TPTSVASTDT NSQPLITEAP
LSETKPEVRV EEMESEVPET QTEDKTENDE VSSCPQLKEE SNESLETKQE PMEEEEKPEI
RTEPKEEEEA GANPSSQSSA SPPQSRRKFF KPEELRQALM PTLEALYRQD PESLPFRQPV
DPSLLGIPDY FDIVKNPMDL STIKRKLDTG QYQEPWQYVE DVWLMFNNAW LYNRKTSRVY
KYCTKLAEVF ELEIDPVMQS LGYCCGRKYE FSPQTLCCYG KQLCTIPRDA TYFSYQNRYH
FCEKCFNEIQ GDSVTLGDDP AQPQTTISKD QFEKKKNDTL DPEPFVECKE CGRKMHQICV
LHNETIWPSG FVCDNCLKKT GKTRKENKFS SKRLQTTRLG NHLEDRVNKF LRRQNHPEAG
EVYVRVVSSS DKTVEVKPGM KSRFVDTGEM SETFPYRTKA LFAFEEIDGV DVCFFGMHVQ
EYGSDCPTPN TRRVYISYLD SIHFFRPRCL RTAVYHEILI GYLEYVKKLG FTQGHIWACP
PSEGDDYIFH CHPADQKIPK PKRLQEWYKK MLDKAFAERI IHDYKDIFKQ ATEDRLTSAN
ELPYFEGDFW PNVLEESIKE LEQEEEERKR EENSIPSEAP DGKKGDSKNA KKKNNKKTNK
NKSSISRANK KKPGMPNVAN DLSQKLYATM EKHKEVFFVI HFHAGPVVNT LPSVVDPDSL
LSCDLMDGRD AFLTLARDKH LEFSSLRRAK WSTMCMLVEL HNQGQDRFVY TCNECKHHVE
TRWHCTVCED YDLCVNCHNI KGHEHKMVKW GLGLDDESSN QPDPLSKSPQ ESRRLSIQRC
IQSLVHACQC RNANCSLPSC QKMKRVVQHT KGCKRKTNGG CPVCKQLIAL CCYHAKHCQE
NKCPVPFCLN IKHKLRQQQL QHRLQQAQML RRRMATMQRG NVPQPSLPSP TSTAPVTPTG
QQQPSTPQTP QPQPPPQTPP SNSLPSGFPN PPRTQTPTTV SQGKPTNQVA PLPQAPPAQP
PPAAALEVAR QIELEAQQQQ QLYQMANMNN GLGMARQNMI GQQIGPVNQM PAVGMKVARP
PVGQVIPGMQ PGQWPQGTTL SQSQPLQAGM RSSMQMTSPQ TSAGQRMPGV QQPPRSNIPP
NALQDLLRTL KSPSSPQQQQ QVLNILKSNP QLMAAFIKQR TAKYQANQPG MQPQPGMQPQ
PQPRMQQAGM HTQASMQNPL QNQNLNPMQA GTQRPTLSPQ QQGLGSMNAQ GQTMNMMNPG
HSPTLATINP QFRQLLIRRQ LIQQQQQQQQ QQQQQQQQQQ GTGMAGGMAG HTQFQQPPGA
AYPQTIPQQR IQQHMSMQGV SMGQLTQMGQ INQLSQPGMG ADGTPTIQQA LQQRILQQQQ
MKQQMGSPGQ PNPMSPQQHM LSGQPQSSHL QSQQIATSLS NQVRSPQPVP SPRPQSQPPH
SSPSPRIQPQ PSPHHVSPQT GSPHPGLAGP QANPMDQGHF STPEQSAMLP QLTNPGISAI
HSGTADLGLG ADSSSLSSST ITCDTLEKFV EENL
//
