ID V2YWX6_MONRO Unreviewed; 322 AA.
AC V2YWX6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=BHLH domain-containing protein {ECO:0000259|PROSITE:PS50888};
GN ORFNames=Moror_7184 {ECO:0000313|EMBL:ESK96194.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK96194.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK96194.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK96194.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the MAX family. {ECO:0000256|ARBA:ARBA00007628}.
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:ESK96194.1}.
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DR EMBL; AWSO01000052; ESK96194.1; -; Genomic_DNA.
DR RefSeq; XP_007844438.1; XM_007846247.1.
DR AlphaFoldDB; V2YWX6; -.
DR STRING; 1381753.V2YWX6; -.
DR KEGG; mrr:Moror_7184; -.
DR HOGENOM; CLU_052375_0_0_1; -.
DR OrthoDB; 1465983at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR10328:SF3; PROTEIN MAX; 1.
DR PANTHER; PTHR10328; PROTEIN MAX MYC-ASSOCIATED FACTOR X; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 186..236
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..263
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 36131 MW; 0AB6019D3B3F7261 CRC64;
MEHHQQQQQH QDDQQSIAVT PQYFYSSDQE SQSFISYGSP IQQYQVVHDN PSSRHLSEMQ
QQQGLQYQNM PMMYPNPVYN HSPPHVSLPL SHSPPPPSPE TYDPLSPPIS GSDTSADGIY
NSSGANSPSS SRGNSLVHRH VRYNPTPSPT SSSGRRSRGR SHDSDEDDMG AQAFDNVNLA
HSRKEATRRQ RIEAEQRRRD ELRDGYAKLK DVLPVSNQKS SKVSLLERAT NYIVQLENTN
RDLQARLQLL EQEMQRLRAL NEKISLPSHD TPSPGHFDAD ARPLSPPPDV PMPSHPTAQS
RPQHHSSHQS QVSSPSNSEG GY
//
