ID A0A4W5NJZ8_9TELE Unreviewed; 1339 AA.
AC A0A4W5NJZ8;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Bromodomain and PHD finger containing, 1 {ECO:0000313|Ensembl:ENSHHUP00000051257.1};
GN Name=BRPF1 {ECO:0000313|Ensembl:ENSHHUP00000051257.1};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000051257.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000051257.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 62062.ENSHHUP00000051257; -.
DR Ensembl; ENSHHUT00000053070.1; ENSHHUP00000051257.1; ENSHHUG00000030705.1.
DR GeneTree; ENSGT00940000157794; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15701; ePHD_BRPF1; 1.
DR CDD; cd15676; PHD_BRPF1; 1.
DR CDD; cd20156; PWWP_BRPF1; 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; IPR042008; BRPF1_PHD.
DR InterPro; IPR049583; BRPF1_PWWP.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR042061; Peregrin_ePHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
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:SF85; PEREGRIN; 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 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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000314982};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 21..52
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 314..364
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 368..489
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 754..824
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1210..1293
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 46..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1339 AA; 149661 MW; DA9FEBA1EB71B951 CRC64;
MGLDFDVKTF CHNLRATKPP YECPVETCRK VYKSYSGIEY HLYHYDHDNP TPAQGMPQKK
RKGRPPRMSL VGDGEGGLGK GGGPGQGGNT PGSPNQSEHS HSPGRETMTY AQAQRMVELE
IHGHIHRISI FENIDVVSED DSGAEDPPSS GGGGGGACNG GDSGGGGSEV GGKDRPDTPA
ANGGKATPKS GKHKSKEKKK EGSSHHHSAS SGPVVKLPEV VYRELDQERP DAPTRHSSYY
RYIDKSVEEL DEEVEYDIDE EDYIWLDIMN DKRRSDGVTP IPQEVFEYLM DRLEKESYFE
SHNKTDPSAL IDEDAVCCIC NDGECQNSNV ILFCDMCNLA VHQECYGVPY IPEGQWLCRR
CLQSPSRAVD CALCPNKGGA FKQTDDARWA HVVCALWIPE VCFANTVFLE PIDSIEHIPP
ARWKLTCYIC KQRGSGACIQ CHKANCYTAF HVTCAQQAGL YMKMEPVRET GANGTSFSVR
KTAYCDIHTP PGLARPLGGV GGASMGSSHS EGELEEDDEP SIGHDDDTKG WSSERAKRAK
AKSRLKMKRA RKILAEKRNA APVVSVPCIP PHRYSLTYSH ILTADTKAYR FRPHILSQSL
QSYHLPCVFL PRLSKITSNL TVPRKSQFMQ RLHSYWTLKR QSRNGVPLLR RLQTHLQSQR
NTEQLQPQPQ APQSQAPQSQ VPTRDSEENN LALKEQLKAW QRLRHDLERA RLLVELIRKR
EKLKRETIKV QQMALEMQLT PFLVLLRNTL EQLQDRDTSN FFTEPVPLAE VPDYLDHIER
PMDFQTMWNL LEAHRYLSFE AFEADFGLIV NNCLKYNAKD TVFYRAALRL REMGGAVIRT
ARRQAERIGL DYDTGMHLPR EPSPDSQRDR ERDRERERER DRDQERERDR DGDRPLSSNE
DDLLLPENRQ RLPLEEQLCF LQARFDEVSS GKHSIGRSRR AKALRKEMTV IKRKLAHQRE
GGLGMGVRDS GGGGDRGPSL PHHPSSTGRH DEGEESSSQE ISGKDLSASS SALAPEVGRR
TSVLFSKKNP KMAGPPKRPG RPPKNRDAGH GGAGVSPSPI GPPQLALLSP PRQRKRPHSS
SSSESDSDID NLLPSLPTNG FGGANQPVTE SFRVYRNERS LPRSSSDSES TTSSSSSAAS
DRTSTTPSKQ GRGKQSFSRS AFQEDSSEET SGTENDSYSV GGSRSVSHLG WGRGRSGCRT
PSDDYSSLDA LDLVWAKCRG YPSYPALIID PKMPSEGVFH RGVPIPVPPL DVLKLGEQMT
QEAREHLFLV LFFDNKRTWQ WLPRSKLVPL GVDRELDKEK MLEGRKSNIR KSVQVAYHRA
MQHRNKVQGD PSSDTSDSD
//
