ID A0A0B2VHG9_TOXCA Unreviewed; 1331 AA.
AC A0A0B2VHG9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=cbp-1 {ECO:0000313|EMBL:KHN80854.1};
GN ORFNames=Tcan_06947 {ECO:0000313|EMBL:KHN80854.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN80854.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN80854.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN80854.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KHN80854.1}.
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DR EMBL; JPKZ01001669; KHN80854.1; -; Genomic_DNA.
DR STRING; 6265.A0A0B2VHG9; -.
DR OMA; RRWHRIC; -.
DR Proteomes; UP000031036; 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: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 Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.20.1020.10; 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; 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; 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; 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; PS50134; ZF_TAZ; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Bromodomain {ECO:0000256|PROSITE-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:UP000031036};
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 156..228
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 387..731
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 790..871
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 790..871
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 64..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1331 AA; 148852 MW; 7D4B446B04CEC590 CRC64;
MDINGSQTMR EASVGRDTAA VHVFRAKVVL RALKALPLRN SGSVLTNGQM GGTSVVKNEV
SEGVVPNGAV PSSRPTPSDE SATTSGCSSK PGTSSAADGG KPIQGIAKAP KTSETKAGKV
EPKTEIVLEE KKELPEKIFD GNELRNHLKP ILDKLFNLEE SIPFRIPVDP DILGIPDYFD
IVKNPMDLST INDKLDNGLY KNPWQFCDDM WLMFDNAWLY NRKNSKVYKY CTKLSELFVE
EINPVMRKMG YCCGQKLAFT PLALFCYGQS MCTIARDQPY HVYEATSTQY GVTVSDRYTY
CTKCFEALDE NGISLSENPN DTSNMVPKSK FALMKNDQID PEPFEQCKVC HRRWHRICAL
YSKKVFPEGF TCETCRAEKA LSKPENRFTA KKLPHCALSR FIEDRVNKYL KGNPAGKDCE
VIIRVLCATD KEVEVKPLMK QKYGAMGFPD KFPYRTKAVF AFEVIDGTEV CFFGLHVQEY
GSNCPPPNQR RVYIAYLDSV HFFQPRQLRT DVYHEILLGY LHYAMLLGYT MAHIWACPPS
EGDDYIFHCH PPEQKIPKPK RLQDWYKKML DKGVGEHTVF DYKDIYKQAR DDNLTTPMAL
PYFEGDFWPN VIEDCIREVQ NEEQERKRQE EAQQNADDDD EDDVFHTGDN GKSKKNSKKK
NNLKKANMKS KKKPGTSTGN EDPDPLMPSD LMDGRDTFLT RARDEHWEFS SLRRAKYSSI
CFCHALHNQE KGEGLSYTCN NCQGNAVWHC PSCDDFDLCN KCYESMSHPH KLEKVSALVE
VGGEDKQDAG NSRNESIQRC IQSLVHACQC RDANCRRLSC HKMKRVVQHT KVCKKRQNAN
CPVCKQLIAL CCYHAKHCNG TACQVPFCLN IRQKLQEQRR SQNRRADMMM RRRMDMLSAG
GGAAPGAPPG QVQNPAMQAN GAASGMGLSQ ATTSQHGSSQ LQYQSGVPQM NAPVQQMQMG
QPQGMVPGAQ QQHIGQMQQI QSQQQYQPHG GMQSAGPMQM MAGQQSHQIQ SQMQQQHQNI
RLNMPTQMSG MQRPGISGQP QHAQQTMNPP PYARGGPQQG GYGMPGAGPS APYGTAPSSQ
QPILMNQASM QQNPQSQQML HQQGMRSKLY SGQMVEGGRG ASVQQDPQLQ VIIQRLKNAH
APEEKEQVFS DLKKMPHLFA AFIKMKGNGE VQSGQGMSQQ QMNPIQQQGM MRQPQMMSQQ
GGQWQQGGMG AHSNQQQYYQ AQQQGAPQNA QQQPRGPGGQ YAPMGSHSQL GGSAPGAQPQ
SQWQQQFQRN PQPVSPAMQQ QFNQVRSPPI GRSPSVGGLA PSPMMQPGGA QQLQQMPPQG
AVSGQDQQPY R
//
