ID A0A091UDN5_PHORB Unreviewed; 1444 AA.
AC A0A091UDN5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0000313|EMBL:KFQ88631.1};
DE Flags: Fragment;
GN ORFNames=N337_01118 {ECO:0000313|EMBL:KFQ88631.1};
OS Phoenicopterus ruber ruber.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC Phoenicopterus.
OX NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ88631.1, ECO:0000313|Proteomes:UP000053700};
RN [1] {ECO:0000313|EMBL:KFQ88631.1, ECO:0000313|Proteomes:UP000053700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ88631.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK429440; KFQ88631.1; -; Genomic_DNA.
DR Proteomes; UP000053700; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR CDD; cd05504; Bromo_Acf1_like; 1.
DR CDD; cd15627; PHD_BAZ1A; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR037325; Acf1_Bromo.
DR InterPro; IPR047171; BAZ1A.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46510; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR PANTHER; PTHR46510:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 1A; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053700};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 293..366
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1031..1081
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1034..1079
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1336..1406
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 16..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..265
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1139
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ88631.1"
FT NON_TER 1444
FT /evidence="ECO:0000313|EMBL:KFQ88631.1"
SQ SEQUENCE 1444 AA; 165500 MW; 8BC4096E7C7EC66A CRC64;
RLQCKILEVI APAHHNGMAN GHASSTDGDT IVISDSDDSE THNSSSQNGE KKAIIDPSLF
KYKVQPIKKE LYETVIVKAS QLSRRKHLFS RDRLKLFLKQ HCEPHDGVIK TKATSIAKYN
LAEQNFSYFF PDEPPTFIFS PASRRRGRPP KRPSTSLEDE ITAKQNTQGN KSKIAREKTK
FQKQKEDMQA MAFEKAKLKR EKANAIEAKK KEKEDKEKKR EELKKIVEEE RMKKKEEKER
LKIEKEKERE KLREEKRKYV EYLKQWSKPR EDMECDDLKE LPVPMPVKTR LPPEIFGDAL
MVLEFLYAFG ELFDLQDEFP EGVTLGKLSF MWQEVLEEAL VGNDTEGPLC ELLFFFLTAI
FQAMAEEEEE VAKDQIADAE TKDLTEALDE DADPTKSALS AVATLAAAWP QLHQGCNLKN
LDLDSCTLSE ILRLHILASG ADVTSANAKY RYQKRGGFDA TDDACMELRL SNPGLLKKLS
STSVYDLLPG EKMKILHALC GKLLTLVSTR DFIEDSVDVL RQAKQEFREL KAEQHRKERE
AAAARIRKRK EERLKEQELK MKEKQEKLKE EEQRNPAVEV SVGEEEREDL DTSTESKEIE
RKEQDMDTVT EDEEELGPHK KRGRGRRGQN GYKEFTRQEE TTCEKNEPLT AEDEEALKQE
QQRKEKELLE KIQNATACTN ITPLGRDRLY RRYWIFPSVP GLFIEEDYSG LTEDMLLPRT
SSFQNSVQSC TNEPQVFSKT GESLKSSEST SNIDQDSHTS VVVEVPRPVY KPNRWCFYNS
REQLDQLLEA LNSRGHRESA LKETILQEKS RIYEQLSSFP VEKFHIPDKP QSDIRPPLGR
GRMQNAHDGS HISAEKQLEL RLRDFLLDIE DRIYQGTLGA IKVTDRQSWR AALEHGRYEF
LNDENKENGI IKTVNEESEE METDDQDKFI VKDRLVGLKT EAPSAASTST STPQPVNNVV
HYLASALLQI EQGIERRFLK APLDASDGGR SYKTVLDRWR ESLLSSTSLS QVFLHLSTLD
RSVIWSKSIL NARCKVCRKK GDAESMVLCD GCDRGYHTYC IRPKLKVIPE GDWFCPECRP
KQRSRRLSSR QRPSVESDEE TAERLGEGEE EANYDEMGQS EEEHYEEEHD EEDESQEEEE
ISPSKQGRPQ VKFPLKMRAA KLNNPFSSRN SQRQARYASR SQQNTPKQTE PSSKVTRRGL
RKAKSAPPSV TKPSLRLNSR TTRQSQGSLQ ADVFVELLGP RRRRRGRKSA DNTLENSPSN
SLGFRIVDTA DSSERLRKYP VSASKLSLPV PEPKRRGRKR QSTESSPQTS LNRRSSGRQG
GVHELSAFEQ LVVELVRHDD SWPFMKLVSK IQVPDYYDII KKPIALNIIR EKVNKCEYKL
ASEFIEDVEL MFSNCFEYNP RNTSEAKAGT RLQAFFHIQA QKLGLPITSG NVDHAAPAAK
KSRI
//
