PRDM9_DANRE
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 03-AUG-2022, entry version 139.
DE RecName: Full=Histone-lysine N-methyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=PR domain zinc finger protein 9;
DE AltName: Full=PR domain-containing protein 9;
DE AltName: Full=Protein-lysine N-methyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H3]-lysine36 N-trimethyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.359 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H3]-lysine4 N-trimethyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H3]-lysine9 N-trimethyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.355 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.362 {ECO:0000250|UniProtKB:Q96EQ9};
DE AltName: Full=[histone H4]-lysine20 N-methyltransferase PRDM9 {ECO:0000250|UniProtKB:Q96EQ9};
DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q96EQ9};
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 Danionidae; Danioninae; 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., Chen Y.,
RA Chen S.-J., Huang Q.-H., Liu T.X., Chen Z.;
RT "Genome-wide survey and developmental expression mapping of zebrafish SET
RT domain-containing genes.";
RL PLoS ONE 3:E1499-E1499(2008).
CC -!- FUNCTION: Histone methyltransferase that sequentially mono-, di-, and
CC tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3
CC to produce respectively trimethylated 'Lys-4' (H3K4me3) and
CC trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in
CC meiotic prophase by determining hotspot localization thereby promoting
CC meiotic recombination. Can also methylate all four core histones with
CC H3 being the best substrate and the most highly modified. Is also able,
CC on one hand, to mono and di-methylate H4K20 and on other hand to
CC trimethylate H3K9 with the di-methylated H3K9 as the best substrate.
CC During meiotic prophase, binds specific DNA sequences through its zinc
CC finger domains thereby determining hotspot localization where it
CC promotes local H3K4me3 and H3K36me3 enrichment on the same nucleosomes
CC through its histone methyltransferase activity. Thereby promotes
CC double-stranded breaks (DSB) formation, at this subset of PRDM9-binding
CC sites, that initiates meiotic recombination for the proper meiotic
CC progression. During meiotic progression hotspot-bound PRDM9 interacts
CC with several complexes; in early leptonema binds CDYL and EHMT2
CC followed by EWSR1 and CXXC1 by the end of leptonema. EWSR1 joins PRDM9
CC with the chromosomal axis through REC8. In this way, controls the DSB
CC repair pathway, pairing of homologous chromosomes and sex body
CC formation. Moreover plays a central role in the transcriptional
CC activation of genes during early meiotic prophase thanks to H3K4me3 and
CC H3K36me3 enrichment that represents a specific tag for epigenetic
CC transcriptional activation. In addition performs automethylation.
CC Acetylation and phosphorylation of histone H3 attenuate or prevent
CC histone H3 methylation. {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+)
CC + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54197;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:Q9NQV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60261;
CC Evidence={ECO:0000250|UniProtKB:Q9NQV7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000250|UniProtKB:Q9NQV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60325;
CC Evidence={ECO:0000250|UniProtKB:Q9NQV7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60277;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60345;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000250|UniProtKB:Q96EQ9};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96EQ9}.
CC Chromosome {ECO:0000250|UniProtKB:Q96EQ9}. Note=Localizes in nuclei of
CC pre-leptotene, leptotene, and early to mid-zygotene spermatocytes.
CC {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- DOMAIN: The C2H2-type zinc fingers determines the hotspot localization
CC through its binding to specific DNA sequences. Variations in their
CC sequence affects affinity towards DNA-binding motif.
CC {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- PTM: Mono-methylated; automethylated. Tri-methylated; automethylated.
CC {ECO:0000250|UniProtKB:Q96EQ9}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; BC064665; AAH64665.1; -; mRNA.
DR EMBL; DQ851831; ABI34500.1; -; mRNA.
DR RefSeq; NP_957196.1; NM_200902.1.
DR AlphaFoldDB; Q6P2A1; -.
DR SMR; Q6P2A1; -.
DR STRING; 7955.ENSDARP00000026323; -.
DR PaxDb; 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; KOG2461; Eukaryota.
DR GeneTree; ENSGT00940000167583; -.
DR HOGENOM; CLU_002678_32_1_1; -.
DR InParanoid; Q6P2A1; -.
DR OMA; FYCEECL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6P2A1; -.
DR TreeFam; TF315885; -.
DR PRO; PR:Q6P2A1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000005382; Expressed in blastula and 22 other tissues.
DR ExpressionAtlas; Q6P2A1; baseline.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0010844; F:recombination hotspot binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; ISS:UniProtKB.
DR GO; GO:0007292; P:female gamete generation; ISS:UniProtKB.
DR GO; GO:0097676; P:histone H3-K36 dimethylation; ISS:UniProtKB.
DR GO; GO:0097198; P:histone H3-K36 trimethylation; ISS:UniProtKB.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; ISS:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; ISS:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0051567; P:histone H3-K9 methylation; ISS:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; ISS:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB.
DR GO; GO:0048232; P:male gamete generation; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1905516; P:positive regulation of fertilization; ISS:UniProtKB.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; ISS:UniProtKB.
DR GO; GO:1905437; P:positive regulation of histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd19193; PR-SET_PRDM7_9; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044417; PRDM7_9_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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; DNA-binding; Meiosis;
KW Metal-binding; Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..853
FT /note="Histone-lysine N-methyltransferase PRDM9"
FT /id="PRO_0000363962"
FT DOMAIN 83..197
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 230..253
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..360
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..428
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 508..528
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 547..569
FT /note="C2H2-type 6; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 575..598
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 604..626
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 644..666
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 689..711
FT /note="C2H2-type 10; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 717..739
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 745..767
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 773..795
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 801..823
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 829..852
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 291..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..845
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT COMPBIAS 291..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127..133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 275..277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 341..342
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96EQ9"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 747
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 750
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 763
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 775
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 778
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 795
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 803
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 806
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 831
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 834
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
FT BINDING 847
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q9NQV7"
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
