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Database: UniProt
Entry: W9X0P0_9EURO
LinkDB: W9X0P0_9EURO
Original site: W9X0P0_9EURO 
ID   W9X0P0_9EURO            Unreviewed;       561 AA.
AC   W9X0P0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=MADS-box transcription factor, other eukaryote {ECO:0000313|EMBL:EXJ74042.1};
GN   ORFNames=A1O5_02336 {ECO:0000313|EMBL:EXJ74042.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ74042.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ74042.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ74042.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MEF2 family.
CC       {ECO:0000256|ARBA:ARBA00025805}.
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:EXJ74042.1}.
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DR   EMBL; AMGX01000003; EXJ74042.1; -; Genomic_DNA.
DR   RefSeq; XP_007741142.1; XM_007742952.1.
DR   AlphaFoldDB; W9X0P0; -.
DR   STRING; 1182543.W9X0P0; -.
DR   GeneID; 19187069; -.
DR   eggNOG; KOG0014; Eukaryota.
DR   HOGENOM; CLU_024080_1_0_1; -.
DR   OrthoDB; 448298at2759; -.
DR   Proteomes; UP000019471; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd00265; MADS_MEF2_like; 1.
DR   Gene3D; 3.40.1810.10; Transcription factor, MADS-box; 1.
DR   InterPro; IPR033896; MADS_MEF2-like.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   PANTHER; PTHR48019:SF93; SERUM RESPONSE FACTOR; 1.
DR   PANTHER; PTHR48019; SERUM RESPONSE FACTOR HOMOLOG; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SRF-like; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019471};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1..61
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50066"
FT   REGION          73..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..237
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..275
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  61284 MW;  D5127CED7CB22F92 CRC64;
     MGRRKIEIRA IKDDRNRSVT FLKRKGGLFK KAYELSVLCS VDVAVIIFGH NKKLYEFSSG
     DINETLRRYQ YYGAPHEHKG PTDFKNKGGE DDDEEEEDED QPAHAREESL PPQHLPPQLQ
     HHNSFAHIQQ PMASVSPPMP NGMFQPRHGT PQPPHMISRP PSQNMIRRTS SNLVPMQHPH
     PTPPPPQNGF AYVPNPPIYN PQATPPVPPQ PSPQPQYQTF PPPQQQQPQP PPPLPQSHQQ
     MQQAHQQYLQ EQRRHSQPPP VSQPTLQPPP QAEARVSPQP ESLNLRPPEQ ATPPQPKHLS
     SKSRSIFTPI DEGGSVLAQH FFGAPDPKPQ VKKEEESPDL KPPPRSTTAS AIPRPSSQTG
     RPQTTVPEFA PPARTNTSGS KSGARPKLNL QIPSEAEDND SATGGSPSQS ANPSANPARG
     GDHIVLPPPS PSASAVMSAG TSGPPNPFAR PPPPTSNANR DAYNDNRNTI ETPISALPSR
     YMNNDLLPSP SNFFSEWDRM SAVLPSPLVF PTPADGRGLG FGSRDAAREA ASEQANGEKR
     KGSVDLPEKE GDVKKVKTGA S
//
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