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Database: UniProt
Entry: A0A5N3X4Y4_MUNRE
LinkDB: A0A5N3X4Y4_MUNRE
Original site: A0A5N3X4Y4_MUNRE 
ID   A0A5N3X4Y4_MUNRE        Unreviewed;       497 AA.
AC   A0A5N3X4Y4;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=DM domain-containing protein {ECO:0000259|PROSITE:PS50809};
GN   ORFNames=FD755_019748 {ECO:0000313|EMBL:KAB0368714.1};
OS   Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Muntiacinae; Muntiacus.
OX   NCBI_TaxID=9886 {ECO:0000313|EMBL:KAB0368714.1, ECO:0000313|Proteomes:UP000326062};
RN   [1] {ECO:0000313|EMBL:KAB0368714.1, ECO:0000313|Proteomes:UP000326062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCam_UCB_Mr {ECO:0000313|EMBL:KAB0368714.1};
RC   TISSUE=Fibroblast cell line {ECO:0000313|EMBL:KAB0368714.1};
RA   Mudd A.B., Bredeson J.V., Baum R., Hockemeyer D., Rokhsar D.S.;
RT   "Discovery of a novel chromosome fission-fusion reversal in muntjac.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00070}.
CC   -!- SIMILARITY: Belongs to the DMRT family.
CC       {ECO:0000256|ARBA:ARBA00006834}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAB0368714.1}.
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DR   EMBL; VCEB01000017; KAB0368714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N3X4Y4; -.
DR   Proteomes; UP000326062; Chromosome 17.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd14417; CUE_DMA_DMRTA1; 1.
DR   Gene3D; 4.10.1040.10; DM DNA-binding domain; 1.
DR   InterPro; IPR001275; DM_DNA-bd.
DR   InterPro; IPR036407; DM_DNA-bd_sf.
DR   InterPro; IPR005173; DMA.
DR   InterPro; IPR026607; DMRT.
DR   InterPro; IPR046472; DMRT5_1_DMB_dom.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR12322; DOUBLESEX AND MAB-3 RELATED TRANSCRIPTION FACTOR DMRT; 1.
DR   PANTHER; PTHR12322:SF71; DOUBLESEX- AND MAB-3-RELATED TRANSCRIPTION FACTOR A1; 1.
DR   Pfam; PF00751; DM; 1.
DR   Pfam; PF03474; DMA; 1.
DR   Pfam; PF20624; DMRT5_DMB; 1.
DR   SMART; SM00301; DM; 1.
DR   SUPFAM; SSF82927; Cysteine-rich DNA binding domain, (DM domain); 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS40000; DM_1; 1.
DR   PROSITE; PS50809; DM_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00070};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00070};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00070}; Reference proteome {ECO:0000313|Proteomes:UP000326062};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00070}.
FT   DOMAIN          89..136
FT                   /note="DM"
FT                   /evidence="ECO:0000259|PROSITE:PS50809"
FT   DNA_BIND        89..136
FT                   /note="DM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00070"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..38
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  52821 MW;  5E95D2D57439AB30 CRC64;
     MEQSQCGSRD RSRSGPPHLA PGLVVAAPPP PSPALPVPPG IPVPPTFLRP SSLFLRAAST
     AGSGGCLPPA ELESGVGAVA GGYPRTPKCA RCRNHGVVSA LKGHKRFCRW RDCACAKCTL
     IAERQRVMAA QVALRRQQAQ EESEARGLQR LLYPGPLGAG ARSSGGSSRT ETSQTASSGP
     ATVTALGLSA SRKASGLATP VFEIFQPDYI EEKQGQKESK CDSCESGQEE LGSKSHQFTL
     RSSPKSNDVA GKQNIRSSSI SENPNKDDSI QSLHPGEQSG GEESPRSLSS SDLESGNESE
     WAKDFTDSTA SHPTVSSRPR DPLDILTKIF PSYRRSRLEG ILQFCKGDVV QAIEEILNGK
     ERKPDTRELA NSGPLENTAF PRVSNFSLAG IGFGTLGNKS AFSPLHTTSA SYGSDSSLYS
     LNPRLGISPF RLAYSSPGRG LSGFMSPYLT PGLVPALPCR PALDYAFSGV IRDSSYLPIK
     DSVTGSRLYS RPNQSNL
//
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