ID A0A0M3KFY2_ANISI Unreviewed; 306 AA.
AC A0A0M3KFY2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Doublesex- and mab-3-related transcription factor 3 (inferred by orthology to a human protein) {ECO:0000313|WBParaSite:ASIM_0001989301-mRNA-1};
GN ORFNames=ASIM_LOCUS19280 {ECO:0000313|EMBL:VDK68580.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001989301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001989301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK68580.1, ECO:0000313|Proteomes:UP000267096}
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; UYRR01036962; VDK68580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3KFY2; -.
DR WBParaSite; ASIM_0001989301-mRNA-1; ASIM_0001989301-mRNA-1; ASIM_0001989301.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; 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; IPR005173; DMA.
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 Pfam; PF03474; DMA; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000267096};
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 20..67
FT /note="DM"
FT /evidence="ECO:0000259|PROSITE:PS50809"
FT DNA_BIND 20..67
FT /note="DM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00070"
FT REGION 94..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 220..247
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 97..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 35319 MW; 5D700C408C2D72D8 CRC64;
MSFDFTPSIR CEQRERKPKC ARCRNHGLVS WLKGHKQRCA FKKCVCEKCN LIAERQRVMA
AQVALKRKQA AEDALALGLR VVAGECTSFD LPQGPLWPFD NNTTPSEQQN ESRSESPIPE
ETTVTNDKPP SLSKEMMLAE QDQQKENRLE RLKPLELLSM LFEEQERRVL ELVLEGCNGQ
LLKAIEYFVC IRQSQRLKHP ETRDFREPEE KCIAESHSEL QCSHQDLSET RQESQQLEQQ
KHYMLRQEPS FGDELAPIRR DESRVDFSMS SLLARNVHDT TTASLSSYPN AFTKWTPQMI
SQSTTT
//
