ID A0A3L8S599_CHLGU Unreviewed; 1249 AA.
AC A0A3L8S599;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Bromodomain and PHD finger-containing protein 3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=DV515_00012268 {ECO:0000313|EMBL:RLV96921.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV96921.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV96921.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV96921.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV96921.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV96921.1}.
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DR EMBL; QUSF01000065; RLV96921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8S599; -.
DR STRING; 44316.ENSEGOP00005021804; -.
DR Proteomes; UP000276834; 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; cd15572; PHD_BRPF; 1.
DR CDD; cd20158; PWWP_BRPF3; 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; 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:SF19; BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 3; 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; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 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 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:UP000276834};
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 302..352
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 356..477
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 701..775
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1120..1203
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 163..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 660..687
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 163..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 141114 MW; 68703C33AB23DBD9 CRC64;
MASPDFIRET SSMARLIRSP FHREGLSRGS CISLSLAWLQ QHQDNDKDRD LCMCPGKQLC
PICWAPTHFI VGINVSVRSI NPWQGLWTTG MRKPRRRCRQ HLEGRRSPSP YSLKCSPSRE
TLTYAQAQRI VEVDIDGRLH RISIYDPLKL ITEDELTAQD ITECNSNKEN SEQPLFTSRS
KKTPSKGKKK ESCSKHAPGI SLHLPQPKFR VVDSFSQPDA PPLPAAYYRY IEKPPEDLDV
EVEYDMDEED LAWLEMVNEK RRADGYGTVS ADTFELLVDR LEKESYLESR NNGAQQSLID
EDAFCCVCMD DECHNSNVIL FCDICNLAVH QECYGVPYIP EGQWLCRCCL QSPSRPVDCV
LCPNKGGAFK QTSDGRWAHV VCAIWIPEVC FANTVFLEPI EGISNIPPAR WKLTCCICKQ
KGMGAAIQCH KVNCYTAFHV TCAQRAGLFM KIEPMRETSI NGTTFTVRKT AYCESHSPPG
TVRRGGPAAG DWQEVTVKEE EEEEANSGPP KGSMKKNQVK LKQKIKKEPG DVTKGRSSMP
VVAVAQIPSY RLNKICSGLS LQRKNQFMQR LHNYWLLKRQ ARNGVPLIRR LHSHLQSQRN
GEQVPLLPAQ LPAWPPGGDE LYTCPGRAAR KEQDEKTSAV KEELKYWQKL RHDLERARLL
IELIRKREKL KREQVKVQQA AMELQLTPFN VLLRTTLDLL QEKDAAQIFT EPVNLNEASL
FPRDYLEFIS NPMDFSTMRR KLESHLYRTL DEFEEDFNLI VANCMRYNAK DTIFHRAAVR
LRDLGGAILR HARRQADSIG FDTGVGIHLP ESPKPHDFYR FSWEDVDNVL VPENRAHLSL
EAQLKELLEK LDTVSTMRSS GARTRRIRLL RREINSIRHK LAQQQSKALP NGDTVPREGL
ETTSREGHEE GEKDGAKLPY PPTLEPTGPA PTLSELDSLQ DPPTLKPISE SRSLNQLQRR
TVSDRELFDK KALQQESQAV QRLLSNNGLN GLALPSADSP ASPALSSVGR RTSVLFKKAK
NGVKLQRGVE CSLENGEEHR QGGQHSPSCP DGERQARKRS ALGSGLVLEA CSGLMPPKRS
RGKPALSRVP LLEGVNGDSD FSGSGRPLLM SFESQAELEP LELVWAKCRG YPSYPALIID
PKMPREGLLH NGVPIPVPPM DVLKLGEQRQ TEAGEKLFLV LFFDNKRTWQ WLPRDKVFPL
GVDDTVDKLK MMEGRKTSIR KSVQVAYDRA MIHLSRVQGD NPFLPGTYL
//
