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Database: UniProt
Entry: V9KLA8_CALMI
LinkDB: V9KLA8_CALMI
Original site: V9KLA8_CALMI 
ID   V9KLA8_CALMI            Unreviewed;       603 AA.
AC   V9KLA8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=CXXC-type zinc finger protein 1 {ECO:0000256|ARBA:ARBA00023828};
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO98829.1};
RN   [1] {ECO:0000313|EMBL:AFO98829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Muscle {ECO:0000313|EMBL:AFO98829.1};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JW866312; AFO98829.1; -; mRNA.
DR   AlphaFoldDB; V9KLA8; -.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd15553; PHD_Cfp1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR022056; CpG-bd_C.
DR   InterPro; IPR037869; Spp1/CFP1.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR002857; Znf_CXXC.
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; PTHR46174; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR   PANTHER; PTHR46174:SF1; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR   Pfam; PF12269; CpG_bind_C; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00509}.
FT   DOMAIN          24..74
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          118..167
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51058"
FT   REGION          82..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          379..413
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        179..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   603 AA;  70275 MW;  7D0947BF2BE27876 CRC64;
     MEEGLTLTEQ EEEEDEEEEK ASSPLYCICR RPDINCFMIG CDKCNEWFHG DCIHITEKMA
     KGIRQWYCVQ CRADDPTLEI KYRQKKSKER DGEKEPGEKE KRKEQGDTRL DKRKASANQV
     KRSARMCGDC EPCMRTEDCG LCDFCKDMKK FGGPNKIRQK CRLRQCEIRA RKLLRGRGEE
     LPVTKEEPKS EAESVSDEGE EPRPPTPLAP LYHDYAVAVS GREHGKPWRC QADEMLFLHP
     PLRKRAVRVK HVQRRDKRSE RKGKFAPARL AHGSLSPSSD WEGTELLSVL KEERSRRHRQ
     KQKHKQRSRH CDRPDSREVL AGQCLGPGCV LASRSNSKYC SDDCGIKLAA NRIYEILPQR
     IQQWQQCPCI AEEHGKKLLE KIRREQQQAR LRLQDMERKF HELETIISHA KQQVIREDEE
     VNEGDGEEAD FQIFCVSCGH PINPKTALKH MERCYAKYES QTSFGSMYPT RIEGATRLFC
     DVYNTQSKTY CKRLQVLCPE HSRDPKVPAE EVCGCPMVRD VFELTGDFCR VAKRKCNKHY
     CWEKLRRAEV DLERVRVWYK LDELFEQERN VRVAMANRAG LLALMLHQTI QHDPLSTDLR
     SSR
//
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