ID G2YU90_BOTF4 Unreviewed; 345 AA.
AC G2YU90;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Similar to MOSC domain containing protein {ECO:0000313|EMBL:CCD55188.1};
GN ORFNames=BofuT4P213000006001 {ECO:0000313|EMBL:CCD55188.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD55188.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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DR EMBL; FQ790353; CCD55188.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YU90; -.
DR STRING; 999810.G2YU90; -.
DR eggNOG; KOG2362; Eukaryota.
DR HOGENOM; CLU_028286_1_1_1; -.
DR InParanoid; G2YU90; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR005303; MOCOS_middle.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008177}.
FT DOMAIN 157..333
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
SQ SEQUENCE 345 AA; 39248 MW; 3996C41D558BBDB8 CRC64;
MFYNLNPFSS PSTTTEITDL LIYPIKSCRG ISIKSSHLTT HGLDLDRRWM FVSGDDHKFI
TIRDISSMTL IDTAFATAKY PSESGSEDAE YLVVSIRNTD KKVMVPARPT EQWLKDNTSL
TQVEIWDYKT DGYVYKDEIN SIFNEFFEKE VKLVYKGPTP RILRGNGAPE ILGREESTNF
PDVMPVLIAN EASLQELNQR LAKKGADEIT IERFRPNIIV RGKNERNNED IAPAAWTEDN
WKRVRIINQS NSGLLSTVMG SNGVDIDVQA RCARCQVPNV NPETAEKNKH EPWDTLVSYR
RVDEGIKWKP CFGMLGVPRL DGPIAVGMKF EVLETTENHK YMKGF
//
