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Entry: M2SQF9_COCSN
LinkDB: M2SQF9_COCSN
Original site: M2SQF9_COCSN 
ID   M2SQF9_COCSN            Unreviewed;       524 AA.
AC   M2SQF9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Glycoside hydrolase family 43 protein {ECO:0000313|EMBL:EMD69478.1};
GN   ORFNames=COCSADRAFT_32182 {ECO:0000313|EMBL:EMD69478.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD69478.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD69478.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; KB445637; EMD69478.1; -; Genomic_DNA.
DR   RefSeq; XP_007694224.1; XM_007696034.1.
DR   AlphaFoldDB; M2SQF9; -.
DR   GeneID; 19136671; -.
DR   KEGG; bsc:COCSADRAFT_32182; -.
DR   eggNOG; ENOG502SHCU; Eukaryota.
DR   HOGENOM; CLU_016508_0_0_1; -.
DR   OMA; GHQINIA; -.
DR   OrthoDB; 1891044at2759; -.
DR   Proteomes; UP000016934; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18617; GH43_XynB-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR   PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016934}.
FT   DOMAIN          361..521
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        17
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            147
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   524 AA;  58307 MW;  812490A80E3FC114 CRC64;
     MSTDSPINPI IPGFAPDPSL ILVDDTYFLV NSTFHLFPGL PIYTSRDLVH WHQIGNAINR
     PSQLSFSKAS TLIHDIGNND HLYATGGLYA STLRHHNGTF YIVCTNVVNH SSDSAQESET
     KNFIISTTDI YASAWSDPVY FDFHGIDPSL FFDPQTGKAY LCGSKSPGPS TKITLFEIDV
     TTDEKLTEEK YLWHGTGGIY PEGPHIYFHD GFYYLMIAEG GTHEGHAVTM ARSKNRLDGP
     WDPSPLNPIL SAGGTDEYVQ CTGHCEAFAV KDGQWWGVCL GIRMREKELY GLGRETFLTR
     GSWSADGWLT FERATVQLSI PGVGVDAEKK LSAVPGVDYV YIHDPVLRDY DFDPTGRNVM
     VRASPHDLTA PNASPSFLGK RQRWIEGKSR ATFVVDSSIH ENARVTAGLA VFKDEHRFFS
     VSYSPAQSSP QLTLRVLNTA KKIDQSHTFD LPIRPESLEF IVEYTEMQYE ISYKLDAVGE
     SSKVASVDAK DLSGKDFVGP IFGVFAIGYK KTEIKFEWFE VDSA
//
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