ID A0A091KNP0_COLST Unreviewed; 1539 AA.
AC A0A091KNP0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0000313|EMBL:KFP29429.1};
DE Flags: Fragment;
GN ORFNames=N325_11853 {ECO:0000313|EMBL:KFP29429.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP29429.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP29429.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP29429.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR EMBL; KK536064; KFP29429.1; -; Genomic_DNA.
DR Proteomes; UP000053615; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR013136; WSTF_Acf1_Cbp146.
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; PF10537; WAC_Acf1_DNA_bd; 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; PS51136; WAC; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000053615};
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 1..92
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 387..460
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1126..1176
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1129..1174
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1431..1501
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 111..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..359
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 745..772
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 657..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP29429.1"
FT NON_TER 1539
FT /evidence="ECO:0000313|EMBL:KFP29429.1"
SQ SEQUENCE 1539 AA; 176421 MW; 52967DBE2D33BFCF CRC64;
FSDFFERTIL CNSLVWSCAV TGKPGLTYQE ALESEKKARH NLQSFPEALI IPILYLATLT
HRSRLHEICD EIFAYVKDRY FVGETVEVAR NNGARLQCKI LEVIAPSHHN GMANGHTSST
DGDTIIISDS DDSETHNSSA QNGEKKAIID PSLFKYKVQP IKKDLYETVI VKASQLSRRK
HLFSRDRLKL FLKQHCEPHD GVIKTKATSV AKYNLAEQNF SYFFPDDPPT FIFSPASRRR
GRPPKRPYTS LEDEIITKQN TQGKKRKVAR EKTKFQKQKE EMQAMAFEKA KLKQEKANAI
EAKKKEKEDK EKKREELKKI VEEERMKKKE EKERLKIEKE KEREKLREEK RKYVEYLKQW
SKPREDMECD DLKELPIPMP VKTRLPPEIF GDALMVLEFL YAFGELFDLQ DEFPEGVTLG
KLLFLSQEVL EEALVGNDTE GPLCELLFFF LTAIFQAMAE EEEEVAKDQI ADAETKDLTE
ALDEDADPTK SALSAVATLA AAWPQLHQGC NLKNLDLDSC TLSEILRLHI LASGADVTSA
NAKYRYQKRG GFDATDDACM ELRLSNPGLL KKLSSTSVYD LLPGEKMKIL HALCGKLLTL
VSTRDFIEDS VDVLRQAKQE FRELKAEQHR KEREAAAARI RKRKEERLKE QELKMKEKQE
KLKEEEQRNP AVEVSVGEEE REDLDTSTES KEIERKEQDM DTVTEDEEDL GPNKKRGRGR
RGQNEYKEFT RQEEATCEKS EPLTAEDEEA LKQEQQKKEK ELLEKIQNAT ACTNITPLGR
DRLYRRYWIF PSVPGLFIEE DYSGLTEDML LPRTSSFENS IQSCTNEPQV FSKTGESLKS
SESTSNIDQD SHTSVVVEVP RPVRKPNRWC FYSSREQLDQ LLEALNSRGH RESALKETLL
QEKSRIYEQL RDFPVEKFHI PDKPQSDIRP PSGRGRMQNA HDGSYVPAEK QLEVRLRDFL
LDIEDRIYQG TLGAIKVTDR QSWRAALEHG RYEFLNDENK ENGIIKTVNE EPEEMEIDDQ
DNKLIVKDRL VGLKTEAPSA ASTSTSTPQP VNNVVHCLAS ALLQIEQGIE RRFLKAPLDP
SDGGRSYKTV LDRWRESLLS STSLSQVFLH LSTLDRSVIW SKSILNARCK VCRKKGDAES
MVLCDGCDRG YHTYCIRPKL KVIPEGDWFC PECRPKQRSR RLSSRQRPSV ESDEETADQL
GEGEEEANYD ETGQTEEQRY EEEQDEEDES QEEEEISTSK QGRPQVKFPL KMRAAKLNNP
FSSQNSQRQA RYASQSQQNT PKQTESSPKV TRRGLRNIRS APPSVTKPSL RLHSRTTRQS
QSSLQADVFV ELLGPRRRRR GRKSTDSPLE NSPSNSLGFR IVDTADPNEQ LRKYPVSASN
LSLPATEPKR RGRKRQSTES SPQTSLNRRS SGRQGGVHEL SAFEQLVVEL VRHDDSWPFM
KLVSKIQVPD YYDIIKKPIA LNIIREKVNK CEYKLASEFI EDVELMFSNC FEYNPRNTSE
AKAGTRLQAF FHIQAQKLGL PVAPGHVEHA APVAKKSRI
//
