ID F6R7T5_CIOIN Unreviewed; 1533 AA.
AC F6R7T5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000018331.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000018331.3}
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|ARBA:ARBA00000780};
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DR EMBL; EAAA01001157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EAAA01001158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7719.ENSCINP00000018331; -.
DR Ensembl; ENSCINT00000018331.3; ENSCINP00000018331.3; ENSCING00000009030.3.
DR GeneTree; ENSGT00940000166210; -.
DR HOGENOM; CLU_000162_3_0_1; -.
DR InParanoid; F6R7T5; -.
DR TreeFam; TF101097; -.
DR Proteomes; UP000008144; Chromosome 14.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd15557; PHD_CBP_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; 1.20.1020.10; 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; 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:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF08214; HAT_KAT11; 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; 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.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
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 Reference proteome {ECO:0000313|Proteomes:UP000008144};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00203}.
FT DOMAIN 1..55
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 247..319
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 388..468
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 477..856
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 916..997
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 916..997
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 58..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..762
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1533 AA; 173092 MW; 20E361D972BD77A9 CRC64;
QPQQPNNIPM NSQTVKLHLD SPILNEGFKQ GHICSHEEYY HLLAEKIYKI QKELEEKRQK
KPLGAMNGPT SVSQQQQQQQ QQQQQQQHRL AGGFMNKAPG GPSQLRMVNQ VNNVNYMDQS
QVNPASNINM PTNGVVNNNN PNTPLSGTIR QFALAMKEID SSNANRPPMT SPPLSNSPMT
ITNQGSPLSF VTIPTPTSTK VSPTPFINRK PSTEAGKSMG KSIKPPTVFP PNELLQVLMP
IVEKLFKQDP ESIPFRYPVD PDRLNIPDYY DIVKNPIDLT TIRKKLEVGE YQEPWEFVND
VWLMFHNAWL YNRKTSRVYK YCTRLKEIFE QEIDPVMQEL GYCCGRKLEF MPMTLCCYGK
ALCTIQTGAV YYEYQNSSPK YGLLSDRYDF CEKCFNDIQG DLVSLSDEPG QGSNSVPKRD
FMKKKNDVLD PEPFVQCDEC GRKLHTICVL YNPQIWPEGF VCDNCHRSRG SQRKPNRFMA
SKLPHNKLSE HIEHRVNSYL KRHDTNNEAG YIHIRSVYSG EKTVEVKPGM KSKFVDSKEM
PETFPYKAKA FFAFEEIDGV DICFFGVHVQ EYGSDAPIPN QRRVYLSYLD SVHFFRPRHL
RTAVYHEILI GYFEYCKNLG YEFAHIWACP PSEGDDYVFH CHPPEQKIPK PKRLQEWYKK
MLDKAIVDQV VLEYKDIYKQ AKDDRLQAAR ELPYFEGDFW PNVLEESIKE LEQEEEDRKQ
AEANEQAAAE EVGSWWAPQT RRTIKNRRQR KQPQRKLSQR SAKKKIPQVA NDLTDKLYQI
MEKHKEVFFV IRLQAADTIS KLGSIADPDP LMPCELMDGR DSFLTLAREK HYEFSSLRRT
KWSTMAMLVE LHVQGKFDYT CNNCKNRIEA PYHCTVCEDF DLCSTCWGQI GHEHKMEQIG
LALGVWSPGP GSGNLETGRT RAVQQCINSL VHACQCRNAN CNLPACPRMK KIVTHTKSCK
RKTIGGCPIC KQVIALCVYH AKICQEPKCA VPFCYNLKMR MKRQEKQHRR QESFLMRRRM
AIMSATSAQQ GPHTPGADVN AAPATPKQEQ PATPINNMVG PGTPGSQHGG PGTPNAGGMG
MAKQLPGTHL VSPHGGKGMP QPTMPQQQIR TNGPMGMMNQ MSGGLASPMS MQHQIQMPQX
QMNMISPSHP NAPVQGGFPR AVGQTMTQRP MMNPNTMQGQ WGGQPQATNN FNLRQPSMAN
MANVASTNQQ NIGIPRGVSP GPSMPVMKPG NSDKLRKLIT KNPELAARVI QQTRQNRHQP
HQNVLTVQQG GVGGNMGQNI VHTNAPMGQN IRMPNMNQQT GNMNLQQMPQ QIQGQAVANQ
RMVPGANTTT AMQIRLQQQQ QQQQQQRIVR SQNMGMRMQN NMGQIMQTQM PQSMNSLNQP
TMMGQQGGQP HQVMMQQNVA NQHQQMNMQG MQSGIVHQNV PPSRPPSQPM PQGRLPQMSP
HATGNTRTTP LSGQVQMVNQ PAGMMHGTMG GAPMEQHFNN NQPMMSGFTR TMGGMNNTMG
HNMVFADGSN QLSSGQDMMA SSDGLEKFVT NNE
//
