ID A0A0V0WS76_9BILA Unreviewed; 1942 AA.
AC A0A0V0WS76;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=Cyb5d2 {ECO:0000313|EMBL:KRX78382.1};
GN ORFNames=T06_1621 {ECO:0000313|EMBL:KRX78382.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX78382.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX78382.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX78382.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX78382.1}.
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DR EMBL; JYDK01000067; KRX78382.1; -; Genomic_DNA.
DR Proteomes; UP000054673; 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 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 InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
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; 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 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; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
PE 4: Predicted;
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:UP000054673};
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 418..516
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 520..599
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 759..817
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 881..1265
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1346..1427
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 418..516
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1346..1427
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 177..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1169
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1942 AA; 213011 MW; 39161D93B4E683C9 CRC64;
MMADQLALGQ PRVKKLKLGS PNLISNNTNN DFNIDWRSLD VELPDELLEP NAAGACHSDV
GGTLQQQGCA TATNALNGSV AACNGPTAVV GPPPSTSDSS GDSFNMPSAV TGLSETVTTC
SSSYVSNGLP MSTVSGGGGN SLTVAGNASL MNAAGVARSP NIRGGAPNNF QEQQAQGAFS
SSGAYMNSSA GAPMPPQYST LNNQRMPMQA PRPPGSSMLN GHQLNAPGPN AQNGIRMNKN
SGFTNVVQST PGNPPPMVGN IVPPSHMQQM ASPNQMIANQ QVNPSPVRMA PGPMGHVPSS
HYQDQHYISS QMIGNVNSAR NHTPDYTFPQ QQQQQHGVMP PYNAGINYVS QRNQFAGPVP
NSSSPLLASL GDAVTTVAAS VQQQQLTMGL NSNAGGIMTS GNIMPTQGSS NGSNTAQDPE
KRKLIQQQLV LLLHAHKCQQ RERDPSGQRS QCSLPHCQTM KNVLNHMTGC TEGRACQDGF
PDSPVVRGVV SPSYRYAAPM AASQTSPSFG PSFPPLENAS VPKEWHKLVT SDLRQHLVTK
LVKAIFPSPD PAAIHDQRIK DLIQYARKVE KEMFDVAEDR EEYYHLLAEK IYKIQKELQE
KKQKRLEMAR AQTVASSQPS APLTPWDSAN PPNRVAPVDS LRSVSPSNSS HHFSNATSLG
SNATLSVKNE SISVKGEECT TYDSISVGSV KVEAGPHIKN EPADGQTASV TESVKMENVK
MENVKLEKGN LEIMKSNPEK VFTQDELVRA LLPVWERIDR MEEAIPFRVP VDPQLLNIPD
YFDIVKKPMD LLTIKENLLG GEYKKPWDFC DHLSEVFVEE IDPVMRMLGY CCGRKLSFTP
LALVCYGQPM CAIPRDAHYY CYEPKFVVEN GIRFVHCTMI RFIPAGLPHC KLSMHVENRV
NKFLRKSNSC AGEVIIRVLA SSDKEVEVKP LMKTKFCTIG EIPEKFPYRT KAIFAYEVVD
GVEICFFGLH VQEYGSNCPQ PNSRRVYIAY LDSVHFFQPK HIRTAVYHEI LLGYLEYVKV
LGYTMAHIWA CPPSEGDDYI FHCHPAEQRI PKPKRLQEWY KKMLDKGIVE RIVVDYKDIY
KHAQDEHLQS ATELPYFEGD YWPNVLEDCI KELDAEEAER RRELEAQAAA DAAGDDVEDL
IDEVHIHEKK KSMKIQKKKS QKNKNSQSKK SKKIISGTGN ELSDKIYTMM EKHKEVFFVV
RLHSAQAAAV LAPVNDPDAL ITCELMDGRD SFLSIARERH WEFSSLRRAK FSTMALCYEL
HTQGQDKFVY TCNGCKGTNA MWHCTICDVS FSLMCILLGV GIVEAEDFDL CQACYEKSNH
EHKMEQIKSI ISDDNSNSGE SGASSANSRN ESIQRCMQSL VHACQCRDAN CRRLSCHKMK
RVVQHTKVCK KRQVGHCPVC KQLVALCCFH ARTCSEPNCS VPFCQNIRQK LNEQQLQLRK
RAQREMQRRM NMMQHQSMPV ATTGPPIYHH HHQSAAPSQP SPSVPAVGGQ PPSAPPAAVR
AAMEVERIAA SQSYARHPNV QMPRQMVAPG ANAMATRHVM PAPTMGAGSG GCWGDPGVPP
KMVGMRGPPP SQVHRHPATA QQDAAGSFQP SGDGMMNPSM QMAMPPRMPY ADGRVQMLLQ
RLKTSNKAEF ESLTRELNND PQLLATVINM RHQQIGAPQV TPNMVPSPRA QWNVSSQVAG
NYGVSSPGMP PPSGQGQMQQ RPQFYPSTGA SSGGGGPAGP QRMPHPSPAQ LGPPSYVSQQ
QHDQQRRMGP APGQYQSGQQ AAALGRGYVG SEQQSQAAYG SSQLPRYQIP VQGGQQQPQQ
QQQQQQQQQQ QQQQRSPPSQ GMLVRSPLQQ SVMSPATPMA GAHLGSQMMH GPAQPGPLPS
NAGAAMHHHP GLIDSGQMPS GGGAGDPSAL PDQSNNDWPA SGSQARRKWF TFATKYFADV
IPEETHALPG MREVVQLALQ CF
//
