ID A0A2Y9G1C8_TRIMA Unreviewed; 1188 AA.
AC A0A2Y9G1C8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Bromodomain-containing protein 1 isoform X1 {ECO:0000313|RefSeq:XP_012412030.1};
GN Name=LOC101350656 {ECO:0000313|RefSeq:XP_012412030.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_012412030.1};
RN [1] {ECO:0000313|RefSeq:XP_012412030.1}
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_012412030.1; XM_012556576.2.
DR AlphaFoldDB; A0A2Y9G1C8; -.
DR STRING; 127582.A0A2Y9G1C8; -.
DR GeneID; 101350656; -.
DR InParanoid; A0A2Y9G1C8; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000248480; Unplaced.
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:UP000248480};
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 1059..1142
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 71..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 515..565
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 874..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 133132 MW; 9705ADC377F8D048 CRC64;
MRRKGRCHRG PTARHPSSPC GVKHSPTRET LTYAQAQRMV EIEIEGRLHR ISISDPLEII
LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NETPPSAHGT PASAGALPEP
KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLDIIN EKRKGDCVSV
VSQNMFEFLM DRFEKESYCE NQKQGEQQSF IDEDAVCCIC MDGECQNSNV ILFCDLCNLA
VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL
YMKMEPVKEL TGGAATFSVR KTAYCDVHTP PGCTRRPLNI YGDAEMKNGV CRKESSVKAV
RSTSKVRKKA KKARKTPAER CAVLPTVCAP YIPPQRLNKI ANQVAIQRKK QFVERAHSYW
LLKRLSRNGA PLLRRLQSSL QSQRSTQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE
LLRKREKLKR EQVKAEQRAM ELRLTPFTVL LRSVLDQLQE KDPARIFAQP VSLKEVPDYL
DHITHPMDFA TMRKRLEAQG YRTLTEFEED FNLIVDNCMK YNAKDTVFYR AAVRLRDQGG
VVLRQTRRHV DSVGFEEATG MHLPERPPAA PPRPFSWEDV DRLLNPANRV HMALEDQLRE
LLDKLDLTCS MKSSGSRSKR AKLLKKEIAL LRNKLSQQPS QPPRPAESGI GSFEEDGAPL
EQEAGDAGDK SPPKLEPSDA LPLPSDSETN SEPPTLKPVE LNPEQSKLFK RVTFGNEAHS
PCSQSALAHG HPAAPSPASG GAVPAAPALA EPSSDVNRRT SVLFCKSKSV SPPKSAKNTE
TQPTSPQLGT KTFLSVVLPR LETLLQPRKR SRSTCGDSEA EEEAPGKRLD TGLTNGFGGT
RGEQELGSAL GRKAAPRRRC ASESSISSSN SLLCDASFST PKCGRGKPAL VRRHTLEDRS
ELISCIENGN YAKAARIAAE VGQNSMWIST DAAASALEPL KVVWAKCSGY PSYPALIIDP
KMPRVPGHHN GVTIPAPPLD VLKIGEHMQT KSDEKLFLVL FFDNKRSWQW LPKSKMVPLG
IDETIDKLKM MEGRNSSIRK AVRIAFDRAM NHLSRVHGEP VSDLSDID
//
