ID C4MLH8_MOUSE Unreviewed; 875 AA.
AC C4MLH8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=PRDM9 isoform Hst1f {ECO:0000313|EMBL:ACI23392.1};
GN Name=Prdm9 {ECO:0000313|EMBL:ACI23392.1};
OS Mus musculus domesticus (western European 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=10092 {ECO:0000313|EMBL:ACI23392.1};
RN [1] {ECO:0000313|EMBL:ACI23392.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C3H/HeJ {ECO:0000313|EMBL:ACI23392.1};
RX PubMed=19074312; DOI=10.1126/science.1163601;
RA Mihola O., Trachtulec Z., Vlcek C., Schimenti J.C., Forejt J.;
RT "A mouse speciation gene encodes a meiotic histone H3 methyltransferase.";
RL Science 323:373-375(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000256|ARBA:ARBA00006991}.
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DR EMBL; EU719625; ACI23392.1; -; Genomic_DNA.
DR AlphaFoldDB; C4MLH8; -.
DR BRENDA; 2.1.1.354; 3474.
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; 14.
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; PTHR24394; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24394:SF45; ZINC FINGER PROTEIN 771; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF21549; PRDM2_PR; 1.
DR Pfam; PF09514; SSXRD; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR Pfam; PF21225; zf-C2H2_5; 1.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
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; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 3: Inferred from homology;
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..820
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 821..848
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 849..875
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 875 AA; 100972 MW; E8E6137F22C108B0 CRC64;
MSCTMNTNKL EENSPEEDTG KFEWKPKVKD EFKDISIYFS KEEWAEMGEW EKIRYRNVKR
NYKMLISIGL RAPRPAFMCY QRQAMKPQIN DSEDSDEEWT PKQQVSPPWV PFRVKHSKQQ
KESSRMPFSG ESNVKEGSGI ENLLNTSGSE HVQKPVSSLE EGNTSGQHSG KKLKLRKKNV
EVKMYRLRER KGLAYEEVSE 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 TQNSHLIQHQ RTHTGEKPYV CRECGRGFTQ KSDLIKHQRT HTGEKPYVCR
ECGRGFTQKS DLIKHQRTHT GEKPYVCREC GRGFTQKSVL IKHQRTHTGE KPYVCRECGR
GFTQKSVLIK HQRTHTGEKP YVCRECGRGF TAKSVLIQHQ RTHTGEKPYV CRECGRGFTA
KSNLIQHQRT HTGEKPYVCR ECGRGFTAKS VLIQHQRTHT GEKPYVCREC GRGFTAKSVL
IQHQRTHTGE KPYVCRECGR GFTAKSVLIQ HQRTHTGEKP YVCRECGRGF TQKSNLIKHQ
RTHTGEKPYV CRECGWGFTQ KSDLIQHQRT HTREK
//
