ID A0A452I9D6_9SAUR Unreviewed; 1520 AA.
AC A0A452I9D6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0000256|ARBA:ARBA00068253};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000024263.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000024263.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGAGP00000024263.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00475}.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR Ensembl; ENSGAGT00000027620.1; ENSGAGP00000024263.1; ENSGAGG00000017683.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0008623; C:CHRAC; IEA:TreeGrafter.
DR GO; GO:0000228; C:nuclear chromosome; IEA:TreeGrafter.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:UniProtKB-ARBA.
DR GO; GO:0003677; F:DNA binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:TreeGrafter.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:TreeGrafter.
DR GO; GO:0031445; P:regulation of heterochromatin formation; IEA:TreeGrafter.
DR CDD; cd05504; Bromo_Acf1_like; 1.
DR CDD; cd15627; PHD_BAZ1A; 1.
DR FunFam; 1.20.920.10:FF:000029; Bromodomain adjacent to zinc finger domain protein 1A; 1.
DR FunFam; 3.30.40.10:FF:000300; Bromodomain adjacent to zinc finger domain protein 1A; 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 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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 390..455
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1106..1156
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1412..1482
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 639..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 292..362
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 639..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..681
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..705
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1520 AA; 174524 MW; FCAB4B120C6F90F1 CRC64;
MPLLHRKPFV RKKPPADLRP DERVFYCRVT NEIFRDYDDF FERTILCNSL VWSCAVTGKP
GLTYQEALES EKKARLNLQS FPEALIVPIL YLATLTHRSR LHEICDEIFA YVKDRYFVGE
TVEVVRNNGA RLQCKILEVI APSHHNGVAN GHINSTNEDT IVISDSDDSE THNSSAQNGK
KKALIDPSLF KYKVQPIKKE LYESVTVRAS QISRRKHLFS RDRLKLFLKQ HCEPHDGVIR
TKAMSVAKYK IAEQDFSYFF SDDPPTFIFS PANKRRGRPP KRISISRVTF EKAKLKREKA
HAIEAKKKER EDKEKKREEL KKIVEEERLK KKEEKERLKI EKEKEREKLR EEKRKYLEYL
KQWSKPREDM ECDDLKELPV PTPVKTRLPP EIFGDALMVL EFLHAFGELF DLQDEFPEGL
TLEVLEEALA GNDSEGPLCE LLFFFLTAIF QAMAEEEEEV AKDQIADAET KDLTEALDED
ADPTKSALFA VATLAAAWPQ LHQGCNLKNL DLDSCTLSEI LRLHILASGA DVTSANAKYR
YQKRGGFDAT DDACMELRLS NPGLLKKLSS TSVYDLSPGE KMKILHALCG KLLTLVSTRD
FIEDSVDVLR QAKQEFRELK AEQHRKEREA AAARIRKRKE ERLKEQEQKM KEKQEKLKEE
EQRNPAAEVS VGEEEREDLD TSTESKEIEQ KEQDLDTVTE DEEEPGPNKK GRRGKRGQNG
FKEFTRQDET SCEKSEPLTA EEEEALKREQ QKKEKELIEK IQNATACTNI SPLGRDRMYR
RYWIFPSVPG LFIEEDYSGL TEDMLLPRPS SFQNSIPSHI TNELQVSTKT GESLKSSEST
SNIDQDSYTS VAVEVPRPVY KPNRWCFYNS REQLDQLLEA LNSRGHRESA LKETLLQEKN
RIYEQLNSFP VEKFHIPDKP QSDNKPLSSG RGRIQNAHDT FQMSAEKQLE LRLRDFLLDI
EDRIYQGTLG AIKVTDRQSW RENGIIKTVN EDAEEMETDD QAKFIVKDRL VGLKTEAPST
ASTNTSTPQP VNNVVHYLAS ALLQIEQGIE RRFLKAPLDA SDGGRSYKTV LDRWRESLLS
SGSLSQVFLH LSTLDRSVIW SKSILNARCK MCRKKGDAES MVLCDGCDRG YHIYCIRPKL
KAIPEGDWFC PECRPKQRSR RLSSRQRPSM ESDEEASEQF EEEEEETYYE EVGQSEEEDY
EEEQEEEDES QEEEEMSPSK QGRPQVKLPL KMRAAKLNNP FSNRSSQRQA CGRYASRSQQ
NTPKQTESFS KVTGKGIRKI KSAPPSVTKP SLRLNSRTTR QSQGSLRADV FVELLSPRRR
RRGKKTADST SDNSPSLGFR IVATTDSCER LRRSPPVSTQ KFPLQDSESK RRGRKRQSTD
SSPHTSLNRR SSGRQGGVHE LSAFEQLVVE LVRHDDSWPF MKLVSKVQVP DYYDIIKKPI
ALNIIREKVN KCEYKLASEF IEDIELMFSN CFEYNPRNTS EAKAGIRLQA FFHIQAQKLG
LPVASGNVDH AAPAAKKSRI
//
