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Database: UniProt
Entry: A0A667ZCG1_9TELE
LinkDB: A0A667ZCG1_9TELE
Original site: A0A667ZCG1_9TELE 
ID   A0A667ZCG1_9TELE        Unreviewed;      1249 AA.
AC   A0A667ZCG1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Bromodomain containing 1 {ECO:0000313|Ensembl:ENSMMDP00005038077.1};
GN   Name=BRD1 {ECO:0000313|Ensembl:ENSMMDP00005038077.1};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005038077.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005038077.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A667ZCG1; -.
DR   Ensembl; ENSMMDT00005038878.1; ENSMMDP00005038077.1; ENSMMDG00005017736.1.
DR   GeneTree; ENSGT00940000157236; -.
DR   InParanoid; A0A667ZCG1; -.
DR   OrthoDB; 163389at2759; -.
DR   Proteomes; UP000472263; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   CDD; cd05512; Bromo_brd1_like; 1.
DR   CDD; cd15572; PHD_BRPF; 1.
DR   CDD; cd20157; PWWP_BRPF2; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR000313; PWWP_dom.
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; PTHR13793:SF17; BROMODOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF10513; EPL1; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472263};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          222..272
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          276..398
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          592..662
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1120..1203
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          528..578
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        775..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..820
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..890
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..931
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1038
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1062
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1249 AA;  140449 MW;  E2A0F2B2C222B55B CRC64;
     MRKKARHHRV PVPQRPPSPI KPSPNKQILT YAQAQRMVEM EIDGRIHRLS IYDKLDVISD
     DDPMVQEMME CTSNKENAEK PQQQVLLRSV RLKNNQEKRN AALGITAHGE DGGQHASGNA
     GPKLPEPKFR TVEYNLPAVP KRPATFYKYQ EKTEEELDEE TEYDMDEEDY AWLDLVNEKR
     RSEGVSQVSH NVFEFLVDRF EKESYLESLC QDSEQQVPID EDAVCCICMD GECHNSNAIL
     FCDMCNLAVH QECYGVPYIP EGQWLCRHCL QSPTQPADCI LCPNKGGAVK KTDDDRWGHV
     VCALWVPEVG FSNTTFIEPI DGVSHIPPAR WKLTCYLCKE KGIGACIQCH KANCYTAFHV
     SCAQKAGLFM KMEPVKEVTE TGEPTFSVKK TAYCGAHTPS GCVRRPLTIY DDAKHKNGLC
     KKVDKGKGAG KGKSKGKKKK KSKKPEPEIE EEVATPAIVP NFPPHRLQTI LNQVSVQKKK
     AFVELVLNYW TLKRQSRNGL PLIRRLHTSM QSQKNAQPGL QRQSEEQSRA LKEQLKEWHR
     LRHDLERARL LLELIRKREK LKREEMKLQQ TLLEMQLTPF TILLRALLDQ LQEKDQARIF
     AQPVDISEVP DYLDHIKHPM DFSTMRQRLD AQGYCNLEQF EDDFNLIIAN CMKYNSKDTY
     FHRAAVRLRD QGGALLRKTR RDVERIGFDT ESGMHLTEAP EIKAPPPFSW EDVDRLLVSA
     NREHMSLDQQ LHQLLEKFDL TCAMKSSPSR SKRVKLLKKT ISDVRNEMSL KRVLPSHHHS
     STLSSSSSAS SRSELDKAKE ESVKANGHFP DDEGDKSLPP KLEPSDSIPP LIHSDGDPEP
     PTLKPIDAGP DCNDKSHGKR VKFDGDKFDS LSSPPRLNGH SHTSSQNSLL EGDVSVVATS
     TLAEPTGTVS RRTAVLFHKS KSASPHKSQN GGEEGTGAEE GEIKEAEGEE EEDEDGPQLG
     SKSFLSVVIP RLETLLHSRK RRHSGTRESE EEGAGEEEGE GEGESPVKRL DTGLSNGFVE
     EEEEKELEAS RPLEPRRRCA SESSISSCSS LPGSTSTTLS LPKCGKGKPA LVRRNTVDDK
     SELIACIENG NFAKAARIAA EVGNSNIWMP ASAATVALEP LKLVWAKCSG YPSYPALIID
     PHMPRVGCQH NGVSIPMPPM DVLRIGEQMQ YKAEEKLYLV LFFDNKRSWQ WLPRSKMVPL
     GMDKTIDKIK MMEGRTSSIR KAVQIAFNRA MNHLSIVQDE PVSDLSDVD
//
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