ID A0A026WDN9_OOCBI Unreviewed; 442 AA.
AC A0A026WDN9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Doublesex-and mab-3-related transcription factor A2 {ECO:0000313|EMBL:EZA53129.1};
GN ORFNames=X777_06207 {ECO:0000313|EMBL:EZA53129.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA53129.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA53129.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00070}.
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DR EMBL; KK107293; EZA53129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WDN9; -.
DR STRING; 2015173.A0A026WDN9; -.
DR OMA; SHATCAK; -.
DR Proteomes; UP000053097; 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 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; IPR009060; UBA-like_sf.
DR PANTHER; PTHR12322; DOUBLESEX AND MAB-3 RELATED TRANSCRIPTION FACTOR DMRT; 1.
DR PANTHER; PTHR12322:SF123; DOUBLESEX-MAB RELATED 99B; 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 SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS40000; DM_1; 1.
DR PROSITE; PS50809; DM_2; 1.
PE 4: Predicted;
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:UP000053097};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00070}.
FT DOMAIN 46..93
FT /note="DM"
FT /evidence="ECO:0000259|PROSITE:PS50809"
FT DNA_BIND 46..93
FT /note="DM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00070"
FT REGION 90..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 47999 MW; 60641457DE78CAF2 CRC64;
MSLPRGVGLG VDVGQLMQHQ QQQHHVLPAA FFLRASAERY QRTPKCARCR NHGVVSALKG
HKRYCRWRDC VCAKCTLIAE RQRVMAAQVR SQDTVTRSVS GSKRSRISES TTTTILSTSD
IGNEDDRDSD SGGELRADRS LVVSTSSGIP ESEATLRKRT SSLNDSEEGS PEPGSQSPTH
TPPLTPALTP QREDTPAPEN LSLRKSGSPP QTQQTLQPVD LVQPRPSPPL PPLAAATAVH
FPPYAPLYGP TASSLAYCSP ALYQHQHHHH IPEPREIQMQ MQMQNIQQTC GLQLQQQQQQ
QQQQHRSPVD VLLRVFPGRR RADVEALLHR CKGDVVSAME VLVCEDSLQP KSAFSPLAGA
LASAAAASAA SVSAAAYASR AAYCTTPIPS TRHRFLAAPY TGTGYLPTVI KPPNQSLHAN
GTGDAYRETS PDDASDKTSY SE
//