ID G1N8B5_MELGA Unreviewed; 1219 AA.
AC G1N8B5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Bromodomain and PHD finger containing 1 {ECO:0000313|Ensembl:ENSMGAP00000008535.3};
GN Name=BRPF1 {ECO:0000313|Ensembl:ENSMGAP00000008535.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000008535.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000008535.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000008535.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_010716888.1; XM_010718586.1.
DR AlphaFoldDB; G1N8B5; -.
DR Ensembl; ENSMGAT00000009334.3; ENSMGAP00000008535.3; ENSMGAG00000008276.3.
DR GeneID; 100547229; -.
DR KEGG; mgp:100547229; -.
DR CTD; 7862; -.
DR GeneTree; ENSGT00940000157794; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR InParanoid; G1N8B5; -.
DR TreeFam; TF316118; -.
DR Proteomes; UP000001645; Chromosome 14.
DR Bgee; ENSMGAG00000008276; Expressed in thymus and 17 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0010698; F:acetyltransferase activator activity; IEA:Ensembl.
DR GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043995; F:histone H4K5 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043996; F:histone H4K8 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR CDD; cd05512; Bromo_brd1_like; 1.
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 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.
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:UP000001645};
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 281..331
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 335..456
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 651..721
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1090..1173
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 43..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1219 AA; 137888 MW; 92E0D5924037E88A CRC64;
MGVDFDVKTF CHNLRATKPP YECPVGSCRK IYKSYSGIEY HLYHYDHDNP PPPQQPPLRK
HKKKGRQGRA GAADKQSPNP SEASQSPGRE VMTYAQAQRM VEVDLHGRVH RISIFDNLDV
VSEDEEAAEE APENGGNKEN GESQAAAAAA AAPKSAKQKS KEKRKDSNHH HHHHNASAGA
APKLPEVVYR ELEQDTPDAP PRPTSYYRYI EKSAEELDEE VEYDMDEEDY IWLDIMNERR
KTEGVSPIPQ EIFEYLMDRL EKESYFESHN KGDPNALVDE DAVCCICNDG ECQNSNVILF
CDMCNLAVHQ ECYGVPYIPE GQWLCRRCLQ SPSRAVDCAL CPNKGGAFKQ TDDGRWAHVV
CALWIPEVCF ANTVFLEPID SIEHIPPARW KLTCYICKQR GSGACIQCHK ANCYTAFHVT
CAQQAGLYMK MEPVRETGAN GTSFSVRKTA YCDIHTPPGS VRRLPALSHS EGEEEDEEEE
EEGKSWSSEK VKKAKAKSRI KMKKARKILA EKRAAAPVVS VPCIPPHRLS KITNRLTIQR
KSQFMQRLHS YWTLKRQSRN GVPLLRRLQT HLQSQRNCDQ RDTEDKNWAL KEQLKSWQRL
RHDLERARLL VELIRKREKL KRETIKVQQV ALEMQLTPFL ILLRKTLEHL QEKDTGNIFS
EPVPLSEVPD YLDHIKKPMD FQTMKQNLEA YRYLNFDDFE EDFNLIINNC LKYNAKDTIF
YRAAVRLREQ GGVVLRQARR QAEKMGIDFE TGMHFPHCVT VEEAQVQDIE DEDMRLLLSE
NQKHLPLEEQ LKILLERLDE VNAGKQSIGR SRRAKMIKKE ITVLRRKLAH PRDLGRDGLE
RHSSSARGVL QSHNPCEKDL QTDSAAEESS SQETGKGLGP NSSSTPAHEV GRRTSVLFSK
KNPKTAGPPK RPGRPPKNRD SQIAPGHGNS PIGPPQLPIM GSSQRQRKRG RSPRPSSSSD
SDSDKSTEDA PMDLPANGFS SGNQPVKKSF LVYRNDCNLP RSSSDSESSS SSSSSAASDR
TSTTPSKQGR GKPSFSRVNF PEDSSEDTSG TENESYSVGA GRGVGHSMVR KGIGRGAGWL
SEDEDSSLDA LDLVWAKCRG YPSYPALIID PKMPREGMFH HGVPIPVPPL EVLKLGEQMT
QEAREHLYLV LFFDNKRTWQ WLPRTKLVPL GVNQDLDKEK MLEGRKSNIR KSVQIAYHRA
MQHRNKVQGE QSSDSSESD
//