ID A0A3Q0DRL9_CARSF Unreviewed; 1058 AA.
AC A0A3Q0DRL9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Bromodomain-containing protein 1 {ECO:0000313|RefSeq:XP_021565756.1};
GN Name=BRD1 {ECO:0000313|RefSeq:XP_021565756.1};
OS Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC Carlito.
OX NCBI_TaxID=1868482 {ECO:0000313|Proteomes:UP000189704, ECO:0000313|RefSeq:XP_021565756.1};
RN [1] {ECO:0000313|RefSeq:XP_021565756.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_021565756.1; XM_021710081.1.
DR AlphaFoldDB; A0A3Q0DRL9; -.
DR STRING; 1868482.ENSTSYP00000008412; -.
DR KEGG; csyr:103255314; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000189704; Unplaced.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd15702; ePHD_BRPF2; 1.
DR CDD; cd15677; PHD_BRPF2; 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; IPR042004; BRPF2_ePHD.
DR InterPro; IPR042009; BRPF2_PHD.
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000189704};
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 214..264
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 268..389
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 579..649
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 929..1012
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 515..558
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 792..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 119746 MW; B260D70BAED1763F CRC64;
MRRKGRCHRG SAARHPSSPC SVKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEII
LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NEALPSVHGT PASASALPEP
KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLEIIN EKRKGDCVSA
VSQSMFEFLM DRFEKESYCE NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA
VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL
YMKMEPVKEL TGGSTTFSVR KTAYCDVHTP PGCTRRPLNI YGDVEMKNGV CRKESSVKTV
RSTSKVRKKA KKAKKALAEP CAVLPTVCAP YIPPQRLNRI ANQVAIQRKK QFVERAHSYW
LLKRLSRNGA PLLRRLQSSL QSQRSTQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE
LLRKREKLKR EQVKVEQVAM ELRLTPLTVL LRSVLDQLQE KDPARIFAQP VSLKEVPDYL
DHIKHPMDFA TMRKRLEAQG YKNLHEFEED FDLIVDNCMK YNARDTVFYR AAVRLRDQGG
VVLRQARREV DSIGLEEASG MHLPERPVVA PRRPFSWEDV DRLLDPANRT HMSLEEQLRE
LLDMLDLTCA MKSSGSRSKR AKLLKKEIAL LRNKLSQQHS QPPPAGSGTG SFEEDGAPLG
LEAGEEVLPR LETLLQPRKR SRSTCGDSEV EEESPGKRLD TGLTNGFGGA RSEQEPGGAL
GRKTAPRRRC ASESSISSSN SPLCESSFST PKCGRGKPAL VRRHTLEDRS ELISCIENGN
YAKAARIAAE VGQNSMWIST DAAASVLEPL KVVWAKCSGY PSYPALIIDP KMPRVPGHHN
GVTIPAPPLD VLKIGEHMQT KSDEKLFLVL FFDNKRSWQW LPKSKMVPLG IDETIDKLKM
MEGRNSSIRK AVRIAFDRAM NHLSRVHGEP ASDLSDID
//
