ID A0A0N5CQD9_THECL Unreviewed; 405 AA.
AC A0A0N5CQD9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=DM domain-containing protein {ECO:0000313|WBParaSite:TCLT_0000243901-mRNA-1};
GN ORFNames=TCLT_LOCUS2440 {ECO:0000313|EMBL:VDM98393.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000243901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000243901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM98393.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UYYF01000502; VDM98393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N5CQD9; -.
DR STRING; 103827.A0A0N5CQD9; -.
DR WBParaSite; TCLT_0000243901-mRNA-1; TCLT_0000243901-mRNA-1; TCLT_0000243901.
DR OMA; LPYFHNF; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
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 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; IPR026607; DMRT.
DR PANTHER; PTHR12322; DOUBLESEX AND MAB-3 RELATED TRANSCRIPTION FACTOR DMRT; 1.
DR PANTHER; PTHR12322:SF116; DOUBLESEX- AND MAB-3-RELATED TRANSCRIPTION FACTOR 1; 1.
DR Pfam; PF00751; DM; 1.
DR SMART; SM00301; DM; 1.
DR SUPFAM; SSF82927; Cysteine-rich DNA binding domain, (DM domain); 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:UP000276776};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00070}.
FT DOMAIN 48..95
FT /note="DM"
FT /evidence="ECO:0000259|PROSITE:PS50809"
FT DNA_BIND 48..95
FT /note="DM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00070"
FT REGION 179..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 44842 MW; 795F082B0F7C6B60 CRC64;
MGFDLTQLSY YSGNQIQQTA FASLSPIRCE EIMHQADNTP VSKRVPNCQK CGQHGRKSRL
KGHKRVCPYR DCECAKCQVV SERQKLMADQ IKIRRRQRKD TLLNITRENI TATLNAAAAV
AASGPLPYFH NFNALFYKQL QQNMRQPAVA AFLPSNSPPS DRMMEAAAFN STSANLSNYL
TNSAPTSKLG QQTPQHHQQQ PQHQQQQASP SSLPHLQFLL QPQATTPTTT TTSTLADGDM
PLHSLTPPCN QSEDNVLIGN NPPIAVPVPI NPIAVSALAP NLSAQDVLSR TLQHQQHQHH
HHHQQQQQQH QQEHQQHHHQ QRELSTLNVN QSLANGQISA FLENEQLFQT LLNNMRQLER
KISVEAAKVA AATAAIPDSS SGSGSSSRPE TTNHLPGIFV DVCSV
//
