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Database: UniProt
Entry: K7GIB5_PELSI
LinkDB: K7GIB5_PELSI
Original site: K7GIB5_PELSI 
ID   K7GIB5_PELSI            Unreviewed;      1574 AA.
AC   K7GIB5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Bromodomain adjacent to zinc finger domain 1A {ECO:0000313|Ensembl:ENSPSIP00000020026.1};
GN   Name=BAZ1A {ECO:0000313|Ensembl:ENSPSIP00000020026.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000020026.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000020026.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR   EMBL; AGCU01049767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01049768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01049769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01049770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 13735.ENSPSIP00000020026; -.
DR   Ensembl; ENSPSIT00000020120.1; ENSPSIP00000020026.1; ENSPSIG00000017675.1.
DR   eggNOG; KOG1245; Eukaryota.
DR   GeneTree; ENSGT00940000158135; -.
DR   HOGENOM; CLU_002479_1_0_1; -.
DR   OMA; CEATGKD; -.
DR   TreeFam; TF316326; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000007267};
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   DOMAIN          22..128
FT                   /note="WAC"
FT                   /evidence="ECO:0000259|PROSITE:PS51136"
FT   DOMAIN          426..491
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          1161..1211
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1466..1536
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          295..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1215..1451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..708
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1230..1269
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1292..1330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1343..1364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1433..1449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1574 AA;  180903 MW;  16A12EF553E3F020 CRC64;
     MPLLHRKPFV REKPPADLRP DERVFYCRVT NEIFRDYDDF FERTILCNSL VWSCAVTGKP
     GLTYQEALES EKRARLNLQS FPKALIVPVL YLATLTHRSR LHEICDEIFA YVKDRYFVGE
     TVEVVRNNGA RLQCKILEVI APPHHNGMAN GHINSTEEDT IVISDSDDSE THNSSAQNGK
     KKALIDPSLF KYKVQPIKKE LYESVTVKAS QIRHHSRRKH LFSRDRLKLF LKQHCEPHDG
     VIRTKAMSVA KYKIAEQDFS YFFPDDPPTF IFSPANKRRG RPPKRVSISC EDKIANKQNT
     PGNRSKVAQE RARFQKQKEE MQAMASEKAK LKREKAHAME AKKKEREDKE KKREELKKIV
     EEERMKKKEE KERLKMEKEK EREKLREEKR KYLEYLKQWS KPREDMECDD LKELPVPIPV
     KTRLPPEIFG DALMVLEFLH AFGELFDLQD EFPEGVTLEV LEEALAGNDT EGPLCELLFF
     FLTAIFQAMA EEEEEVAKDQ IADAETKDLT EALDEDADPT KSALFAVATL AAAWPQLHQG
     CNLKNLDLDS CTLSEILRLH ILASGADVTS ANAKYRYQKR GGFDATDDAC MELRLSNPGL
     LKKLSSTSVY DLSPGEKMKI LHALCGKLLT LVSTRDFIED SVDILRQAKQ EFRELKAEQH
     RKEREAAAAR IRKRKEDRLK EQEQKMKEKQ EKLKEEEQRN PAAEVSVGEE EREDLDTSTE
     SKETERKEQD LDTVTEDEEE LGPNKKGRRG KKRGQNGFKD FTRQDETSCE KSEPLTAEEE
     EALKREQQKK EKELLEKIQN ATACTNISPL GRDRMYRRYW IFPSVPGLFI EEDYSGLTED
     MLLPRPCSFQ NSIQSHIINE LQVSTKTGES LKSSESTSNI DQDSCASVAV EVPRQVYKPN
     RWCFYNSREQ LDQLLEALNS RGYRESALKE TLLQEKNRLY EQLNNFPVEK FHIPDKPQSD
     NKPPSSGRGR IVNAHDTSQM SAEKQLELRL RDFLLDIEDR IYQGTLGAIK VTDRQSWRAA
     LENGQYELLN EENKENGIIK AVNEDAEEME TDDQAKFIVK DRLVGLKTEA PSTASTNTST
     PQPVNNVVRY LASALLQIEQ GTERRFLKAP LVQDANDGGR SYKTVLDRWR ESLLSSGSLS
     QVFLHLSTLD RSIIWSKSIL NARCKMCRKK GDAESMVLCD GCDRGYHIYC IRPKLKAIPE
     GDWFCPECRP KQRSRRLSSR QRPSMESDEE ASEQFEEEEE ETYYEEAGQS EEEDYEEEQE
     EEDESQEEEE LSLSKQGRPQ VKLPLKMRAA KLNNPFSSQS SQRQTSGRYA SRSQHNTPKQ
     NESSSKVTGR GIRKIKSAPP SVTKPSLRLN SRTTRQSQAS LQADVFVELL SPRRRRRGKN
     TTDSTPENSP SLGFRIVATT DSRERVRRSP FSTQKFSLQD NESKRRGRKR QSTDSSPQTS
     LNRRSSGRQG GVHELSAFEQ LVVELVRHDD SWPFMKLVSK IQVPDYYDII KKPIALNIIR
     EKVNKCEYKL ASEFIEDIEL MFSNCFEYNP RNTSEAKAGI RLQAFFHVQA QKLGLPIASG
     NVDHAAPAAK KSRI
//
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