ID V9KFL7_CALMI Unreviewed; 827 AA.
AC V9KFL7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Bromodomain-containing protein 1-like protein {ECO:0000313|EMBL:AFO97096.1};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO97096.1};
RN [1] {ECO:0000313|EMBL:AFO97096.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen {ECO:0000313|EMBL:AFO97096.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JW864579; AFO97096.1; -; mRNA.
DR AlphaFoldDB; V9KFL7; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd15670; ePHD_BRPF; 1.
DR CDD; cd15572; PHD_BRPF; 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; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
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; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
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 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 213..263
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 267..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 REGION 759..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 827
FT /evidence="ECO:0000313|EMBL:AFO97096.1"
SQ SEQUENCE 827 AA; 95199 MW; 99D7C6FFBB69FA16 CRC64;
MRRKGRYIRV AARHPTSPCK LKHSPSREML TYAQAQRMVE MEIDGRLHRI SIYDPLEIIS
EDDLTAQEIV ECNSNKENSE RPPVFIKSKR IKNKVKKKEA TVQNTHGAPV QLANTLPEPR
FRIVDYHPPS APRRPSSYYR LIEKSPEELN NEVEYDMDEE DYAWLEMINE KRKSDGFSAI
SQNVFEFLMD KLEKESYFEN YNQGDPQSLI DEDAVCCICM DGECQNSNVI LFCDMCNLAV
HQECYGVPYI PEGQWLCRRC LQSPSRSVDC ILCPNKGGAF KKTDDGQWGH VVCALWVPEV
GFANTVFIEP IDGVKNIPAA RWKLTCYLCK QKGFGACIQC HKANCYTAFH VTCAQQAGLY
MKMEPIKETA PNGAITFNVK KTAFCAAHSP PGCVRRPLNI YEAVEVKNGI CRKDSHNKAS
KTKCKSRQKA KKTRKLLAEK CTAVPVVSVP CIQPDRLNAI ISQVSVPRKK QFIQRLHVYW
TLKRQSRNGV PLLRRLQSHL QSQRNVQQRV DDEQNNALKE QLKYWQRLRH DLERARLLVE
LIRKREKLKR EQVKVHQVSM ELQLTPLTVM LRSVLEQLQE KDAAHIFAQP VNLKEVPDYL
DHIKHPMDFS TMRKRLEDHG YKNLDEFEID VNLIIDNCMK YNAKDTIFYR AAVRLRDQGG
VVLRQARREV DKISYDYETG MHLVDPPKKE VTTPFSWEEV DRLLLPANRE HMALEVQLKE
LLDKLDMTCA AKSCGARSRR AKLLRKEINN IRLRLSQQNA ETEHIRNENG SVEDGTKVEQ
DGEEYRDLKS SVPPILEPSD CLPLLASSET PSEPPTLKPI EPSTDQS
//
