GenomeNet

Database: UniProt
Entry: A2BID7
LinkDB: A2BID7
Original site: A2BID7 
ID   PRD10_DANRE             Reviewed;        1121 AA.
AC   A2BID7; Q1LV64;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   16-JAN-2019, entry version 79.
DE   RecName: Full=PR domain zinc finger protein 10;
DE            EC=2.1.1.-;
DE   AltName: Full=PR domain-containing protein 10;
GN   Name=prdm10; ORFNames=si:ch211-151h10.3, si:dkey-11k4.2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The SET domain is degenerated, suggesting that it has lost
CC       methyltransferase activity.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM13007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; BX908391; CAK04147.1; -; Genomic_DNA.
DR   EMBL; BX908399; CAM13007.1; ALT_SEQ; Genomic_DNA.
DR   SMR; A2BID7; -.
DR   PRIDE; A2BID7; -.
DR   ZFIN; ZDB-GENE-050419-74; prdm10.
DR   HOVERGEN; HBG053664; -.
DR   InParanoid; A2BID7; -.
DR   PhylomeDB; A2BID7; -.
DR   PRO; PR:A2BID7; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   3: Inferred from homology;
KW   Complete proteome; DNA-binding; Metal-binding; Methyltransferase;
KW   Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1121       PR domain zinc finger protein 10.
FT                                /FTId=PRO_0000363965.
FT   DOMAIN      173    290       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     319    341       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     500    522       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     529    551       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     557    579       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     585    608       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     613    635       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     641    664       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     696    719       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     741    764       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     803    826       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS    888   1011       Gln-rich.
FT   COMPBIAS   1105   1108       Poly-Thr.
FT   CONFLICT    401    401       E -> D (in Ref. 1; CAK04147).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1121 AA;  126179 MW;  13D642EEA8FD6C2B CRC64;
     MEAKQESSTV WSTASNNDTG NTPQVHFEAG AVAQIVYSGD QSDRTQQQVV YAADGSSYTS
     VESAEHTLVY IHPADGTQSQ LAVTNAALPT LTEASSSPLG ATDSTVDSED EEEDNDSEDS
     EMDDWEPRAL QPFTPQNLWC EDCNNANPAA CIKHGPLHPI LNRPVMSKAR ASLPLVLYID
     RFLGGVFTKR RIPKRTQFGP LEGPLVRQSE LLDTHIHLKL YMLDPEKEGE RAQDLWFDLS
     DEERCNWMMF VRPAQNHLEQ NLVAYQYGSD IFYTSIKNIQ PKQELKVWYA ASYAEFVNQK
     VHDVTEEERK VLREQEKNWP CYECNRRFMS SEQLQQHLNM HDDKLNLIQR PKSRGRGRGR
     KRFGGARRPG RRTKFLCPQT PVESADKTQE LLASVDKLQF EERTDGALNG LKVVEMAAES
     METETEDALD PPPIHTESLQ DEEDSVTPPP VTEIPESAKD DLSHTSPIDP HLTPQDMRRA
     RRIRNAALKH LFIRKSFRPF KCPQCGKAFR DKEKLEQHMR FHGRDGCRHV CHQCGKGFLS
     STSLEDHLVL HSDQRNYSCL FCAESYDRLE LLKVHVGIHM VNGCFLCPSC KKSFTDFIQV
     KKHVRSFHSE KVFQCSECDK AFCRPDKLRL HMLRHSDRKD FLCSTCGKQF KRKDKLREHM
     QRMHNPEREA KKADRIHRTK ALKQKEPTTD FESFMFKCRL CMMGFRRRGM LVNHLSKRHP
     EMRLEEVPEL TLPIIKPNRD YYCQYCDKVY KSASKRKAHI LKNHPGAELP PSIRKLRPAG
     PGEPDPMLST HTQLTGTIAT APVCCPHCAK QYSSKTKMVQ HIRKKHPEYQ YNSSSNIQAP
     LAATVISSTP AVITTDGTTA EAVVTTDLLT QAMTELSQTL TTDYRTAQGD FQRIQYIPVS
     QAGGGLSQPQ HIQLQVVQVA PASSPHSQHS TVDVSQLHDP HSYSQHSIQV QHIQVAEPTA
     AVQANAQVSG QPLSPSSQQA AQELSTAQLT PVTLAQQTLQ TSSNQTQGAT QHAYLPSNWN
     YRSYPSEIQM MALPHTQYVI AEASTPVTAA VNSSQVKTTH YVISDGQTEL DGKQVSVPST
     ATQGHPDPLE QPAGGQQATT QYIITTTTNG AGASEVHITK P
//
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