ID W0TX95_MUSMC Unreviewed; 819 AA.
AC W0TX95;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Prdm9 protein {ECO:0000313|EMBL:BAO48045.1};
GN Name=Prdm9 {ECO:0000313|EMBL:BAO48045.1, ECO:0000313|MGI:MGI:2384854};
OS Mus musculus castaneus (Southeastern Asian house mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10091 {ECO:0000313|EMBL:BAO48045.1};
RN [1] {ECO:0000313|EMBL:BAO48045.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HMI/Ms {ECO:0000313|EMBL:BAO48045.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAO48045.1};
RX PubMed=24449848; DOI=10.1093/dnares/dst059;
RA Kono H., Tamura M., Osada N., Suzuki H., Abe K., Moriwaki K., Ohta K.,
RA Shiroishi T.;
RT "Prdm9 polymorphism unveils mouse evolutionary tracks.";
RL DNA Res. 21:315-326(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AB844113; BAO48045.1; -; mRNA.
DR AlphaFoldDB; W0TX95; -.
DR AGR; MGI:2384854; -.
DR MGI; MGI:2384854; Prdm9.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd19193; PR-SET_PRDM7_9; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 12.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR003655; aKRAB.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR048414; PDRM9-like_Znf-C2H2.
DR InterPro; IPR044417; PRDM7_9_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019041; SSXRD_motif.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16515:SF52; HISTONE-LYSINE N-METHYLTRANSFERASE PRDM9; 1.
DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF21549; PRDM2_PR; 1.
DR Pfam; PF09514; SSXRD; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR Pfam; PF21225; zf-C2H2_5; 1.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50806; KRAB_RELATED; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 2: Evidence at transcript level;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 27..90
FT /note="KRAB-related"
FT /evidence="ECO:0000259|PROSITE:PS50806"
FT DOMAIN 30..100
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 248..362
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 517..540
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 541..568
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 569..596
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 597..624
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 625..652
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 653..680
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 681..708
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 709..736
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 737..764
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 765..792
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 793..819
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 94586 MW; 70533C13180445D8 CRC64;
MSCTMNTNKL EENSPEEDTG KFEWKPKVKD EFKDISIYFS KEEWAEMGEW EKIRYRNVKR
NYKMLISIGL RAPRPAFMCY QRQAMKPQIN DSEDSDEEWT PKQQVSPPWV PFRVKHSKQQ
KESSRMPFSG ESNVKEGSGI ENLLNTSGSE HVQKPVSSLE EGNTSGQHSG KKLKLRKKNV
EVKMYRLRER KGLAYKEVSE PQDDDYLYCE KCQNFFIDSC PNHGPPLFVK DSMVDRGHPN
HSVLSLPPGL RISPSGIPEA GLGVWNEASD LPVGLHFGPY EGQITEDEEA ANSGYSWLIT
KGRNCYEYVD GQDESQANWM RYVNCARDDE EQNLVAFQYH RKIFYRTCRV IRPGCELLVW
YGDEYGQELG IKWGSKMKKG FTAGRELRTE IHPCLLCSLA FSSQKFLTQH MEWNHRTEIF
PGTSARINPK PGDPCSDQLQ EQHVDSQNKN DKASNEVKRK SKPRQRISTT FPSTLKEQMR
SEESKRTVEE LRTGQTTNTE DTVKSFIASE ISSIERQCGQ YFSDKSNVNE HQKTHTGEKP
YVCRECGRGF TAKSNLIQHQ RTHTGEKPYV CRECGRGFTQ KSVLIQHQRT HTGEKPYVCR
ECGRGFTQKS DLIKHQRTHT GEKPYVCREC GRGFTAKSNL IQHQRTHTGE KPYVCRECGR
GFTEKSSLIK HQRTHTGEKP YVCRECGWGF TAKSNLIQHQ RTHTGEKPYV CRECGRGFTQ
KSSLIKHQRT HTGEKPYVCR ECGRGFTAKS NLIQHQRTHT GEKPYVCREC GWGFTQKSNL
IKHQRTHTGE KPYVCRECGW GFTQKSDLIQ HQRTHTREK
//
