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Database: UniProt
Entry: V4AJQ2_LOTGI
LinkDB: V4AJQ2_LOTGI
Original site: V4AJQ2_LOTGI 
ID   V4AJQ2_LOTGI            Unreviewed;      1433 AA.
AC   V4AJQ2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE   Flags: Fragment;
GN   ORFNames=LOTGIDRAFT_136183 {ECO:0000313|EMBL:ESP04399.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP04399.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESP04399.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
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DR   EMBL; KB199753; ESP04399.1; -; Genomic_DNA.
DR   RefSeq; XP_009044885.1; XM_009046637.1.
DR   STRING; 225164.V4AJQ2; -.
DR   EnsemblMetazoa; LotgiT136183; LotgiP136183; LotgiG136183.
DR   GeneID; 20233775; -.
DR   KEGG; lgi:LOTGIDRAFT_136183; -.
DR   CTD; 20233775; -.
DR   HOGENOM; CLU_000162_4_0_1; -.
DR   OMA; DSARCTT; -.
DR   OrthoDB; 5490807at2759; -.
DR   Proteomes; UP000030746; Unassembled WGS sequence.
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:0003712; F:transcription coregulator 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   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; 2.
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; 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; PF02172; KIX; 1.
DR   Pfam; PF06001; RING_CBP-p300; 1.
DR   Pfam; PF02135; zf-TAZ; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM01250; KAT11; 1.
DR   SMART; SM00551; ZnF_TAZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF57933; TAZ domain; 2.
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; PS50134; ZF_TAZ; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
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:UP000030746};
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:PRU00228}.
FT   DOMAIN          1..86
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   DOMAIN          204..283
FT                   /note="KIX"
FT                   /evidence="ECO:0000259|PROSITE:PS50952"
FT   DOMAIN          665..737
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          884..1260
FT                   /note="CBP/p300-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51727"
FT   DOMAIN          1262..1310
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          1323..1404
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50134"
FT   ZN_FING         1..86
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT   ZN_FING         1323..1404
FT                   /note="TAZ-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT   REGION          285..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1117..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..308
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1117..1131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ESP04399.1"
FT   NON_TER         1433
FT                   /evidence="ECO:0000313|EMBL:ESP04399.1"
SQ   SEQUENCE   1433 AA;  160885 MW;  BCF96F1CA92B192F CRC64;
     DPDKSKLIQQ QLVLLLHAHK CQRRENANGE QACALPYCRT MKNVLTHMTS CTAGKTCQIA
     HCASSRQIIT HWKNCHRNDC PVCLPLKHAS DNRRNPAGKY LTSISVVGGG NMAPNTNMTA
     PSTLNAVPQG SGNVSETTFK RAVDALGLSN RPQPPVPPSA TTTLNQQNQN NALQAIIGPG
     GMAQPPTMTA ASSEALQNIA MTSQMTKDWH QDVTQDLRNH LVHKLVQAIF PTPDPTALKD
     TRMKNLVAYA RKVEGDMYET ANSREEYYHL LAEKIYKIQK ELDEKRQQRI RSGQPGPPGP
     PGVPQPRANA PQNGPLSGFN AAESLGLTNL VPGLNNLFNH QQQQQLLQGS QVNPMAPRMP
     GNQQLMSPPL SQQLQNNSQS QQLMQQTGQG GQPPSSVSQI HQSLSKILTP QNQTPTSTVQ
     SNSLNQASAQ SATGLPQQQS QQQQQSGSGK QQNQSLGGLM GPGSVPNGTQ LGQGGPTSVG
     KTLPVATSPA PVVSTASSSI NHVSLAYYLL YVNSMEVKKE IKTEPTSNSL SSLLSSPSKD
     MSSTTNADPP SSVSNGTGVK TEIKNEPGVV KTEPSEAMDT TSAPPSVTPK PEGGSEGTTV
     AEADTKPDTE DSSQGAPSTP VPTAPKSKKN TVESRLLKIF NSVFSVFKPD ELRQALMPTL
     EKLYRQDPES LPFRQPVDPV QLQIPDYYDI VTKPIDLSTI KRKLDTGQYN DPWEYVDDVW
     LMFENAWVYN RKTSRVYKFC SKLAEVFESE IDSVMQSLGY CCGHKYTFSP QVLCCYGKQL
     CTIPRDSMYR SYQNRYVFCE RCFQEIQGDE VELSDDPTQV ATRIKKDQFT LQKNDQMDYE
     QFVNCIECGR KHHVICALWF EPIWPTYTCD NCLKAKGMKR KENRFSAKKL PTTKMGNFLE
     NRVNNYLKKK DVGAGDVSIR VLSSSDKIVE VKPGMKSKFP DEVPDSFPYR SKAMFAFEEI
     DGVDVCFFGM HVQEYGSECQ MPNTRRVYIS YLDSVHFFQP RHLRTAVYHE ILIGYLEYAK
     NMGYTVAHIW ACPPSEGDDY IFHCHPPEQK IPKPKRLQDW YKKMLDKAII ERVCTDYKDI
     LKDAIENNFQ SATEMAYFEG DFWPNVVEES IKELNQEEEE KKKREEAQAA AAEAEAADCN
     DEAEGSNKGR NKKAYKSKNN QRKVAKKSNV PQGSNDLTNK LYQTMEKHKE VFFVIRLHPQ
     QNPPGMPQIR DLDPLCSCEL MDGRDSFLTL AREKHYEFSS FRRAKYSTLA MLYELHNQGK
     DAFCYTCNEC KNHVETRYHC SVCEDFDLCV NCYKKVTHPH RMDKLGFDLD DGSYSGEKQE
     NPQESRRQSI QRCIQSLVHA CQCRDANCRL PSCTKMKRIV HHTKTCKRKT NGGCPICKQL
     IALCCYHAKH CNEGKCQVPF CTHLKHKLRH QQLQQRLQQA QLLRRRMAIM TAT
//
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