ID M5FPF2_DACPD Unreviewed; 150 AA.
AC M5FPF2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=YlMBF1 {ECO:0000313|EMBL:EJT98510.1};
GN ORFNames=DACRYDRAFT_91026 {ECO:0000313|EMBL:EJT98510.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT98510.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJT98510.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT98510.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the MBF1 family.
CC {ECO:0000256|ARBA:ARBA00009802}.
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DR EMBL; JH795873; EJT98510.1; -; Genomic_DNA.
DR AlphaFoldDB; M5FPF2; -.
DR STRING; 1858805.M5FPF2; -.
DR HOGENOM; CLU_112609_0_1_1; -.
DR OMA; NKAHQGT; -.
DR OrthoDB; 120438at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013729; MBF1_N.
DR PANTHER; PTHR10245:SF15; ENDOTHELIAL DIFFERENTIATION-RELATED FACTOR 1; 1.
DR PANTHER; PTHR10245; ENDOTHELIAL DIFFERENTIATION-RELATED FACTOR 1 MULTIPROTEIN BRIDGING FACTOR 1; 1.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF08523; MBF1; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 92..137
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
FT REGION 18..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 150 AA; 16043 MW; D706E1A43DF13AB8 CRC64;
MSDWDAKLVI GSKAKVPKVT RSESELNSAR RSGAVVSSDK KITAGSNKAH AGTDHQRIAK
LDRENEVAPP TKVAPSVGRA IMDARASLTP PLSQKDLAQK INEKPSVIAD YESGRAIPNP
QVLGKMERIL KVKLRGADVG KKLDTPGAKK
//