GenomeNet

Database: UniProt
Entry: Q6P2A1
LinkDB: Q6P2A1
Original site: Q6P2A1 
ID   PRDM9_DANRE             Reviewed;         853 AA.
AC   Q6P2A1; A5XCD9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 123.
DE   RecName: Full=Histone-lysine N-methyltransferase PRDM9;
DE            EC=2.1.1.43;
DE   AltName: Full=PR domain zinc finger protein 9;
DE   AltName: Full=PR domain-containing protein 9;
GN   Name=prdm9; ORFNames=zgc:63970;
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 MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 763-853.
RX   PubMed=18231586; DOI=10.1371/journal.pone.0001499;
RA   Sun X.-J., Xu P.-F., Zhou T., Hu M., Fu C.-T., Zhang Y., Jin Y.,
RA   Chen Y., Chen S.-J., Huang Q.-H., Liu T.X., Chen Z.;
RT   "Genome-wide survey and developmental expression mapping of zebrafish
RT   SET domain-containing genes.";
RL   PLoS ONE 3:E1499-E1499(2008).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-4' of histone H3 during meiotic prophase and is
CC       essential for proper meiotic progression. Does not have the
CC       ability to mono- and dimethylate 'Lys-4' of histone H3. H3 'Lys-4'
CC       methylation represents a specific tag for epigenetic
CC       transcriptional activation. Plays a central role in the
CC       transcriptional activation of genes during early meiotic prophase
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; BC064665; AAH64665.1; -; mRNA.
DR   EMBL; DQ851831; ABI34500.1; -; mRNA.
DR   RefSeq; NP_957196.1; NM_200902.1.
DR   UniGene; Dr.80491; -.
DR   ProteinModelPortal; Q6P2A1; -.
DR   SMR; Q6P2A1; -.
DR   STRING; 7955.ENSDARP00000026323; -.
DR   PaxDb; Q6P2A1; -.
DR   PRIDE; Q6P2A1; -.
DR   Ensembl; ENSDART00000027321; ENSDARP00000026323; ENSDARG00000005382.
DR   Ensembl; ENSDART00000180739; ENSDARP00000148547; ENSDARG00000110150.
DR   GeneID; 393876; -.
DR   KEGG; dre:393876; -.
DR   CTD; 56979; -.
DR   ZFIN; ZDB-GENE-040426-1319; prdm9.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000167583; -.
DR   HOGENOM; HOG000205053; -.
DR   InParanoid; Q6P2A1; -.
DR   KO; K20796; -.
DR   OMA; KSFSRPQ; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q6P2A1; -.
DR   TreeFam; TF315885; -.
DR   Reactome; R-DRE-912446; Meiotic recombination.
DR   PRO; PR:Q6P2A1; -.
DR   Proteomes; UP000000437; Chromosome 12.
DR   Bgee; ENSDARG00000005382; Expressed in 31 organ(s), highest expression level in blastula.
DR   ExpressionAtlas; Q6P2A1; baseline.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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; 7.
DR   SMART; SM00355; ZnF_C2H2; 13.
DR   SUPFAM; SSF57667; SSF57667; 6.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE   2: Evidence at transcript level;
KW   Activator; Chromatin regulator; Chromosome; Complete proteome;
KW   Meiosis; Metal-binding; Methyltransferase; Nucleus;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    853       Histone-lysine N-methyltransferase PRDM9.
FT                                /FTId=PRO_0000363962.
FT   DOMAIN       83    197       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     230    253       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     337    360       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     366    388       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     405    428       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     508    528       C2H2-type 5; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     547    569       C2H2-type 6; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     575    598       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     604    626       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     644    666       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     689    711       C2H2-type 10; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     717    739       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     745    767       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     773    795       C2H2-type 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     801    823       C2H2-type 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     829    852       C2H2-type 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
SQ   SEQUENCE   853 AA;  97136 MW;  44A40327A3F0BAC4 CRC64;
     MSLSPDLPPS EEQNLEIQGS ATNCYSVVII EEQDDTFNDQ PFYCEMCQQH FIDQCETHGP
     PSFTCDSPAA LGTPQRALLT LPQGLVIGRS SISHAGLGVF NQGQTVPLGM HFGPFDGEEI
     SEEKALDSAN SWVICRGNNQ YSYIDAEKDT HSNWMKFVVC SRSETEQNLV AFQQNGRILF
     RCCRPISPGQ EFRVWYAEEY AQGLGAIWDK IWDNKCISQG STEEQATQNC PCPFCHYSFP
     TLVYLHAHVK RTHPNEYAQF TQTHPLESEA HTPITEVEQC LVASDEALST QTQPVTESPQ
     EQISTQNGQP IHQTENSDEP DASDIYTAAG EISDEIHACV DCGRSFLRSC HLKRHQRTIH
     SKEKPYCCSQ CKKCFSQATG LKRHQHTHQE QEKNIESPDR PSDIYPCTKC TLSFVAKINL
     HQHLKRHHHG EYLRLVESGS LTAETEEDHT EVCFDKQDPN YEPPSRGRKS TKNSLKGRGC
     PKKVAVGRPR GRPPKNKNLE VEVQKISPIC TNCEQSFSDL ETLKTHQCPR RDDEGDNVEH
     PQEASQYICG ECIRAFSNLD LLKAHECIQQ GEGSYCCPHC DLYFNRMCNL RRHERTIHSK
     EKPYCCTVCL KSFTQSSGLK RHQQSHLRRK SHRQSSALFT AAIFPCAYCP FSFTDERYLY
     KHIRRHHPEM SLKYLSFQEG GVLSVEKPHS CSQCCKSFST IKGFKNHSCF KQGEKVYLCP
     DCGKAFSWFN SLKQHQRIHT GEKPYTCSQC GKSFVHSGQL NVHLRTHTGE KPFLCSQCGE
     SFRQSGDLRR HEQKHSGVRP CQCPDCGKSF SRPQSLKAHQ QLHVGTKLFP CTQCGKSFTR
     RYHLTRHHQK MHS
//
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