ID A0A3M0JQD6_HIRRU Unreviewed; 2259 AA.
AC A0A3M0JQD6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=DUI87_20397 {ECO:0000313|EMBL:RMC03203.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC03203.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC03203.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC03203.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC03203.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:RMC03203.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QRBI01000131; RMC03203.1; -; Genomic_DNA.
DR STRING; 333673.A0A3M0JQD6; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003713; F:transcription coactivator 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 GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15646; PHD_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; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking 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; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_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:SF29; HISTONE ACETYLTRANSFERASE P300; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 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; SSF69125; Nuclear receptor coactivator interlocking domain; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 339..429
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 532..611
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 900..972
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1120..1496
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1498..1546
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1561..1642
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 339..429
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1561..1642
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1931..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2030..2259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1398
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1730
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1763
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2051..2155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2156..2187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2207..2259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2259 AA; 248118 MW; F559D6B03886D6D3 CRC64;
MAENVVEPGP PSAKRPKLSS PALSVSASDG TDFGSLFDLE HDLPDELISS TELGLTNGGD
INQLQTSLGL AQDAASKHKQ LSELLRAGSS PNLNMGVGGP GQGMASQTQQ NSPGMGMLNS
MVKSPMAQAG LTSPNMAMGT SGPNQGPSAQ STAAMIPTVN SPVNQPGMGM NTGMNAGMNP
GMLAAGNGQG MMQGQVMNGS IGAGRGRPNM PYPNPGMGSA GNLLAETLQQ GTPQMGGQAG
LRGPQPGAMN KMGMMSNPSP YGQPYSQNTG QQIGASGLGP QMQNKAGLQN SLPQFPMDKK
PVPGSGMPNM GQQQAPQVQQ AGMGPAASQG MGSGAPTADP EKRKLIQQQL VLLLHAHKCQ
RREQANGEVR QCNLPHCRTM KNVLNHMTHC QAGKSCQALL GGAAVGLANT GSVGVGQQTT
PSINTTSQID PSSIERAYAA LGLTYQGNQM QTQPQAQVKN QQQGQSPQGL RPMNPMSANP
MGVNGGVGVQ PPNLLPDSML HSTMNSQNPM MSESASVASL GAMPTAQPSN SGIRKQWHED
ITQDLRNHLV HKLVQAIFPT PDPAALKDRR MENLVAYARK VEGDMYESAN SRAEYYHLLA
EKIYKIQKEL EEKRRTRLQK QNMIPNAPGM PQAPMNQGPN MGQPQPGMSA NGPLPDPTLI
RANMPNQMMN RMQAQPGMNQ FGQMNMQLSP MGPRQTPPLQ HPGQLSQAGA MNQMGFPSRM
QQPGVGQPSG QNQFLQQTQF SASSPGMNTA SMPMTQPGNQ TPVSQLSQTA VSIDGQVSNP
PSTSSTEVNS QQTVPEQQQP PLQEVKMEIK TDEGEPEQTE MQMEEKSEAK AEPVVEECKP
DPMEQEEKKP EVKTEVPEGE ERPTTPATQS SPVAGQSKKK IFKPEELRQA LMPTLEALYR
QDPESLPFRQ PVDPQLLGIP DYFDIVKNPM DLSTIKRKLD TGQYQEPWQY VDDIWLMFNN
AWLYNRKTSR VYKYCSKLAE VFEQEIDPVM QSLGYCCGRK LEFSPQTLCC YGKQLCTIPR
DATYYSYQNR YHFCEKCFNE IQGESVSLGD DPSQPQTTIN KEQFSKRKND TLDPELFVEC
IECGRKMHQI CVLHNEIIWP SGFVCDGCLK KTGRTRKENK FSAKRLPATR LGTFLENRVN
DFLRRQNHPE AGEVTVRVVH ASDKTVEVKP GMKARFVDSG EMAESFPYRT KALFAFEEID
GVDLCFFGMH VQEYGSDCPP PNQRRVYISY LDSVHFFRPK CLRTAVYHEI LIGYLEYVKK
LGYTTGHIWA CPPSEGDDYI FHCHPPDQKI PKPKRLQEWY KKMLDKSVSE RIVHDYKDIF
KQATEDRLTS AKELPYFEGD FWPNVLEESI KELEQEEEER KREENTSNES TDVSKGDSKN
AKKKNNKKTS KNKSSLSRGN KKKPGMPNVS NDLSQKLYAT MEKHKEVFFV IRLIAGPAAN
SLPPIIEPDP LIPCDLMDGR DAFLTLARDK HLEFSSLRRA QWSTMCMLVE LHTQSQDRFV
YTCNECKHHV ETRWHCTVCE DYDLCITCYN TKNHDHKMEK LGLGLDDESN NQQTTTTQSP
GDSRRLSIQR CIQSLVHACQ CRNANCSLPS CQKMKRVVQH TKGCKRKTNG GCPICKQLIA
LCCYHAKHCQ ENKCPVPFCL NIKHKLRQQQ LQHRLQQAQM LRRRMASMQR TGVAGQQQGL
PSPTPATPTT PTGQQPPTPQ TPQPQPLPQP VSQPQPAPPN SMPPYTMPRT QPPSAVSQGK
AGGQVTPPTP PQPPQPPVQG PPPAAVEMAM QIQRAAETQR QMAQVQIFQR PIQHQMPQMP
PMGMNPPQIG RGPGGHIDQG MGPGGIQQQP PWVQGALPQA QLQPGMQRPS MMSVGQPGQP
MNMAPQPGMG QVPGAAQPKQ PPLPQAALQN LLRTLRSPSS PMQQQQVLNI LHSNPQLLAA
FIKQRAAKYA GSQNPQGMAG QPGIPQGQPG LQPQQAMQGQ QGGVHPSPAM QNMNPMQAGV
QRPSMPQQQP QQQPQQAMAG MNPQAQQMNM NHSGMAPQFR DLLMRRHQMM EQQRHQQQQQ
GAGPALGPGM ANHNQFQQPQ GVGYPQQQQR MQHHMQQMQQ GNMGQISQLP QAMSAETGAS
LQQAFQQRLL QQQMGSPAQP NPMSPQQHML PNQSQSPHLQ GQQLPSSLTN QVRSPQPVPS
PRPQSQPPHS SPSPRMQPQP SPHHVSPQTS SPHPGLVAAQ ANPMDQGHFA SPDQSAMLSQ
LASNPGIAGL HGTSATELGL SSENSDLNSN LSQSTLDIH
//