ID A0A2K6GRH6_PROCO Unreviewed; 1360 AA.
AC A0A2K6GRH6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A {ECO:0008006|Google:ProtNLM};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000028861.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000028861.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR Ensembl; ENSPCOT00000039796.1; ENSPCOP00000028861.1; ENSPCOG00000027094.1.
DR GeneTree; ENSGT00940000166431; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR InterPro; IPR047171; BAZ1A.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
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; PF02791; DDT; 1.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR SMART; SM00571; DDT; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS51136; WAC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1049..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1102..1120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..128
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 423..488
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT REGION 660..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 318..395
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 660..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1360 AA; 156401 MW; 29E57BF00432FFFC CRC64;
MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP
GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTNLTHRSR LHEICDDIFA YVKDRYFVEE
TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVSSVDGET IIISDSDDSE TQSCSVQNGK
KKDAIDPLLF KYKVQPTKKK ELYESAIVKA TQISRRKHLF SRDKLKLFLK QHCEPQDGVI
KIKASSLLMY KIAEQDFSYF FPDEPPTFIF SPANRRRGRP PKRISISQEH SVSNKQTIAG
YRNKGIKERD KLLKQEEMKS LAFEKAKLKR EKADALEAKK KEKEDKEKKR EELKKIIEEE
RLKKKEEKER LKVEREKERE KLREEKRKYM EYLKQWSKPR EDMECDDLKE LPEPTPVKTR
LPPEIFGDAL MVLEFLNAFG ELFDLQDEFP EGVTLEVLEE ALVGNDSEGP LCELLFFFLT
AIFQAIAEEE EEVAKEQITD ADTKDLTEAL DEDADPTKSA LSAVASLAAA WPQLHQGCSL
KSLDLDSCTL SEILRLHILA SGADVTSANA KYRYQKRGGF DATDDACMEL RLSNPGLVKK
LSSTSVYDLT PGEKMKILHA LCGKLLTLVS TRDYIEDYVD ILRQAKQEFR ELKAEQHRKE
REEAAAREEE REDFDTSTES KEIEQKELDQ DMVTEDEDDS GSHKRSRRGK RGQNGFKEFT
RQEEINCVTS EPLTVAEEEA LKQEYQRKER ELLEKIQSAI ACTNIFPLGR DRMYRRYWIF
PSIPGLFIEE DYSGLTEDML LPKHSLFQNN VQSQDPQVST KTGESLKSES TSNIDHGPCD
HSVQLPKPVH KPNRWCFYSS CEQLDQLIEA LNSRGYRESA LKETLLQEKS RICAQLACFS
EEKFHFSDKP QTDSKPIYSR GRSSNAYDQS QMSAERQLEL RLRDFLLDIE DRIYQGTLGA
IKVYMRLAAV EQGKQGPSQK VIPSAKEVHR RAACLTACLG IKTETPSTVS TNASTPQSVS
NVVHYLAMAL FQIEQGIERR FLKAPLGKYV FYFKILVMFL TFSALDRSTI WRKDKEKWNQ
FLNYTENLFR THWLNRTRRI ELIIRSLLFC TIIMFSNNIY SASKRGRPQV RFPIKARGRL
SSSFSSRGQR QDSGRYPSRS QQSTPKSPVS SKTIGRSLRK INSAPPTETK SLRIASRSTR
HSHGPLQADV FVELLSPCRK RRSRRSANNT PENSPNFPNF RVIATKSSEQ SRSLSVVSKL
SLHDSESKRR CRKRXXXXXX XXXXXXXXXX XXVAVTEFID DIELMFSNCF EYNPRNTSEA
KAGTRLQAFF HIQAQKLGLH VTPSNVDQVS TPPAVKKSRI
//