ID A0A0W0F6S0_9AGAR Unreviewed; 319 AA.
AC A0A0W0F6S0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=pectinesterase {ECO:0000256|ARBA:ARBA00013229};
DE EC=3.1.1.11 {ECO:0000256|ARBA:ARBA00013229};
GN ORFNames=WG66_15434 {ECO:0000313|EMBL:KTB32005.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB32005.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB32005.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB32005.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KTB32005.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LATX01002272; KTB32005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0F6S0; -.
DR SMR; A0A0W0F6S0; -.
DR eggNOG; ENOG502QSQ4; Eukaryota.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000054988; 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:SF125; PECTINESTERASE A; 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:UP000054988};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..319
FT /note="pectinesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011113034"
FT DOMAIN 35..306
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
SQ SEQUENCE 319 AA; 34295 MW; C8972A5963341A37 CRC64;
MPLLRWILTT ALFSLSWALT SPPSGALVVR QSGTKSGEYS TVSAAVAALG PGTSSKTIFI
YPGTYKEQVY ITYGGPLTIY GYSTNGGSYK DNEVAITNNL NAQDNGGNDP CATVRAHSKF
FKMYNVNIAN TYGPGKQATA LSAKNSNQGY YGCKITGYQD TLLADGPGYQ YYSNCYIEGA
VDYIYGKASA WFGECTLSSN GPGAITANSR ESSSDPGYYV IDSSTITSSA SGLTQKVYLG
RPWRALARVS FQRSTLLDLI NPKGYTTLAD NATPIFMEYQ NTGAGADTSQ RVTFTKQTAL
ITHEQVLGSD YASWIDISF
//