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Database: UniProt
Entry: M2RT13_COCSN
LinkDB: M2RT13_COCSN
Original site: M2RT13_COCSN 
ID   M2RT13_COCSN            Unreviewed;       384 AA.
AC   M2RT13;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=pectinesterase {ECO:0000256|ARBA:ARBA00013229};
DE            EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229};
GN   ORFNames=COCSADRAFT_195471 {ECO:0000313|EMBL:EMD69699.1};
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:EMD69699.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD69699.1, 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   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}.
CC   -!- SIMILARITY: Belongs to the pectinesterase family.
CC       {ECO:0000256|ARBA:ARBA00008891}.
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DR   EMBL; KB445637; EMD69699.1; -; Genomic_DNA.
DR   RefSeq; XP_007694947.1; XM_007696757.1.
DR   AlphaFoldDB; M2RT13; -.
DR   STRING; 665912.M2RT13; -.
DR   GeneID; 19133937; -.
DR   KEGG; bsc:COCSADRAFT_195471; -.
DR   eggNOG; ENOG502R6WA; Eukaryota.
DR   HOGENOM; CLU_012243_2_0_1; -.
DR   OMA; QHRSIFA; -.
DR   OrthoDB; 561027at2759; -.
DR   UniPathway; UPA00545; UER00823.
DR   Proteomes; UP000016934; Unassembled WGS sequence.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR000070; Pectinesterase_cat.
DR   PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR   PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..384
FT                   /note="pectinesterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011110001"
FT   DOMAIN          157..351
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
SQ   SEQUENCE   384 AA;  42148 MW;  8FEC4FE8020755EE CRC64;
     MRLVMIFAGI LQVCAAIPAV NRKACQYPTQ KPLDGCPKNT LLVGPGSNFS TIQSAVLSLP
     NDKNPYNILI LPGNYTEQVN ITRPGPVYLL GQTAHPETRT KNTVNILWHN ATGAGLSTLD
     NAYTSVLTVA PTFNASLTGT GPTGFPVPPN TPFGNTDFRA YNLNFTNDYL PYSAGPSLAI
     SVSYANTGFY YCAFHSYQDT LYIGKLGNAY IYDSEIAGQT DFLYGFGTAW IQSSLLTLRG
     CGGGITAWKG TNTTFENRYG VYIHDSELRK ENATLAIKGK CALGRPWNAL HRSIFADCEM
     DDSILPAGYI QWNAGDPRIG VNTTMAEYKN YGPGWDEAAR RKSNVSVVMG EREYRAYKRV
     ETVFQYPFSG EFGNTAWIDR NPGQ
//
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