ID G1NIM5_MELGA Unreviewed; 1493 AA.
AC G1NIM5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 1A {ECO:0000313|Ensembl:ENSMGAP00000013130.3};
GN Name=BAZ1A {ECO:0000313|Ensembl:ENSMGAP00000013130.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000013130.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000013130.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000013130.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR Ensembl; ENSMGAT00000014032.3; ENSMGAP00000013130.3; ENSMGAG00000012463.3.
DR GeneTree; ENSGT00940000158135; -.
DR HOGENOM; CLU_002479_1_0_1; -.
DR InParanoid; G1NIM5; -.
DR TreeFam; TF316326; -.
DR Proteomes; UP000001645; Chromosome 5.
DR Bgee; ENSMGAG00000012463; Expressed in bursa of Fabricius and 17 other cell types or tissues.
DR GO; GO:0016590; C:ACF complex; IEA:Ensembl.
DR GO; GO:0008623; C:CHRAC; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
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; 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.
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:UP000001645};
KW Signal {ECO:0000256|SAM:SignalP};
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:PRU00146}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1493
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032275118"
FT DOMAIN 1..90
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 357..422
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1082..1132
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1385..1455
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 616..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 282..329
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 616..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1493 AA; 171393 MW; 780DD9683E1CB472 CRC64;
IFHFRTILCN SLVWSCAVTG KPGLTYQEAL ESEKKARHNL QSFPEALIIP VLYLATLTHR
SRLHEICDEI FAYVKDRYFV GETVEVIKNN GERLQCQILE VIPPAHHNGM ANGHVSSADG
ETIVISDSDD SETHNSSAQN GKKKAIIDPS LFKYKVQPIK KELYESVIVK ASQLSRRKHL
FSRDRLKLFL KQHCEPHEGV IKTKATSIAK YNLAEQNFSY FFPDDPPTFV FSPASRRRGR
PPKRASISHV SNDNIFNSCE LPEQLEFKIG KKILFFPLLY RKKKEELKKI VEEERMKRKE
EKERLKIEKE KEREKLREEK RRYVEYLKQW SKPREDMECD DLKELPVPMP VKTRLPPEIF
GDALMVLEFL YAFGELFDLQ DEFPEGVTLE VLEEALVGND TEGPLCELLF FFLTAIFQAM
AEEEEEVAKD QIADAETKDL TEALDEDADP TKSALSAVAT LAAAWPQLHQ GCNLKNLDLD
SCTLSEILRL HILASGADVT SANAKYRYQK RGGFDATDDA CMELRLSNPG LLKKLSSTSV
YDLLPGEKMK ILHALCGKLL TLVSTRDFIE DSVDVLRQAK QEFRELKAEQ HRKEREAAAA
RIRKRKEERL KEQELKMKEK QEKLKEEEQR NPAVEEERED LDTSTESKEN ERKEPEIDTV
TEDEEELGPN KKGRRGRRGQ NGYKELTRQD DTSEKSEPLT AEDEEALKQE QQKKEKELLE
KIQNATACTN ITPLGRDRLY RRYWIFPSVP GLFIEEDYSG LTEDMLLPRT SSFQNSVQSC
TNEPQVFSKT GESLKSSEST SNVDQDSHTS VVVEVPRPVY KPNRWCFYSS REQLDQLLEA
LNSRGHRESA LKETLLQEKN RIYEQLSSFP VEKFHIPDKP QSDIRPPPPV RGRMQNAHDA
SQISAEKQLE MRLRDFLLDI EDRIYQGTLG AIKVADRQSW RAALEHGRYE FLNDENKENG
IIKTVNEESE EMETDDQDKF IVKDRLIGLK TEAPSAASTS TSTPQPVNNV VHCLASALLQ
IEQGIERRFL KAPLDASDGG RSYKTVLDRW RESLLSSTSL SQVFLHLSTL DRSVIWSKSI
LNARCKVCRK KGDAESMVLC DGCDRGYHTY CIRPKLKIIP EGDWFCPECR PKQRSRRLSS
RQRPSVESDE EMAERTEGEE EASYDEMRQS EEEDYEEEHE EEDESQEEEE MSPSKHRRPQ
VKFPLKMRAA KLNNPFSSRN IQRQARYASR SQQNTPKQAG SSRVTRRGLR KVKSAPPSVT
KPTLRLSSRT TRQSQSSLQA DVFVELISPR RRRRGRKNAD NALENSPSDS LGFRIIDSTD
SNERVRKYPV AAPKLSLPVS EPKRRGRKRQ STESSPQTSL NRRSSGRQGG VHELSAFEQL
VVELVRHDDS WPFMKLVSKI QVPDYYDIIK KPIALNIIRE KVNKCEYKLA SEFIEDIELM
FSNCFEYNPR NTSEAKAGTR LQAFFHIQAQ KLGLPITSGN VDHAAPVVKK SRI
//
