ID A0A183KM24_9TREM Unreviewed; 949 AA.
AC A0A183KM24;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=SCUD_LOCUS16092 {ECO:0000313|EMBL:VDP60834.1};
OS Schistosoma curassoni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001609501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SCUD_0001609501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP60834.1, ECO:0000313|Proteomes:UP000279833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dakar {ECO:0000313|EMBL:VDP60834.1}, and Dakar, Senegal
RC {ECO:0000313|Proteomes:UP000279833};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UZAK01038318; VDP60834.1; -; Genomic_DNA.
DR STRING; 6186.A0A183KM24; -.
DR WBParaSite; SCUD_0001609501-mRNA-1; SCUD_0001609501-mRNA-1; SCUD_0001609501.
DR Proteomes; UP000050789; Unplaced.
DR Proteomes; UP000279833; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 1.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR035898; TAZ_dom_sf.
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; PF08214; HAT_KAT11; 1.
DR Pfam; PF02135; zf-TAZ; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00551; ZnF_TAZ; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000279833};
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..182
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 184..232
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 251..332
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 251..332
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..82
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 103147 MW; BE5C2A98E59329FD CRC64;
MSLNFSVKCC NSDLRTDLSE PELEEEEARR RREEAMAQAE AEDDEADCSS STNEGLPGDP
DKRSGKKKAK KRKGNKKGNT STASKRKRLD GPIDGAEELS RKVYDTMEKL KEIFFVIRLH
RHNSAASLPP TTDPDQPVHS ELMDSRDAFL QMARERHLEF SSLRRAKYSS MVLLYELHME
LRQSFMYNCN VCGAQIETRW HCNECEEYDL CSRCYKTENH PHPMVQYGLG IDEDSGTNEE
TGDRPSGTGA TPDRRISIEG CIRSLLHACQ CRDANCRMQT CAQMKRVLCH TRNCTKKATN
SCLLCQQLLS LLWHHARSCE ESKCPVPFCS NIKYRVKQKL LQQRLQQNKL LRRRISTMHR
GALPTSESQP PTQSCPTSVI ASISSTSLNP SSINSVHQTQ SPIHQSLTTN TVRNPQLSTS
SNSVEKPLSN TTPVSFQPQT QVQQQGPVLL STGNPQYSQP PRIPVPTVAS QNNQGANPRP
PVVCSSLMPS GGRVIMQPPI NTGPVQRTNT PVTVSVTSGW RPRPVIATAS QGTVHSSTGQ
QSQAQPTSAT STHSSVSVLN PVNSQKPTIS NKPTQVEIDH VSQVISLIKA TGTSSDEQNR
RFIAWIKRHP EFHAAFFALH SQHKQQAELR AQANQRRVTT SGSMPGTSSL STSSALATSS
ISDASQSLLG SSGVSGNVVI VPSSVSANSN SQNTGLNRTQ NINSLSTPMS SMSVVTGSTS
LGSTPAVMHQ PVQWISIQSP ITTNHHQPLI TGCTAQPIQT VPNTTTLRFR AVPGTATLVQ
SQPQQVQHFY NTTQLGPDSA FSGNESGSNM FVSATGSNIL SVGNQQSQVL SAVPQRLTPA
SSSNMGRQSS TPQAAIVHFR SQQHQPLSGT VNPMQPHIIL TNTTAPASGP THLSHQSQPQ
LVSATSNGRQ VVALMTHQNI PHTNVSDPGA PLRDSGSNNS ANNLGNGIQ
//
