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Database: UniProt
Entry: M5C4K3_THACB
LinkDB: M5C4K3_THACB
Original site: M5C4K3_THACB 
ID   M5C4K3_THACB            Unreviewed;       253 AA.
AC   M5C4K3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Carbohydrate esterase family 4 protein {ECO:0000313|EMBL:CCO33970.1};
GN   ORFNames=BN14_08060 {ECO:0000313|EMBL:CCO33970.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO33970.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO33970.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(2013).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
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:CCO33970.1}.
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DR   EMBL; CAOJ01012399; CCO33970.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5C4K3; -.
DR   HOGENOM; CLU_021264_11_2_1; -.
DR   Proteomes; UP000012065; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10951; CE4_ClCDA_like; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR   PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..253
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004063861"
FT   DOMAIN          41..227
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   253 AA;  28124 MW;  ED9F444AA0CA8D4B CRC64;
     MRFSAAQITT LASALFGVAN ASSSLGSRSA DSVVLKCREP NTVAITFDDG PYNWTKELVH
     KLDSYGAKGT FFVNGNNYGC IYSEENVERI QYLVERGHQI ASHTWRHEHL PQLSGDRLDA
     EFRKTNEAIR KITGCSPAFM RPPYGEYNDE VVEKATKNGQ TVVVIWDFDS ADSIGATVEQ
     SKSHYDNILA QHPSSILTLN HETIETTPNQ VIPYALQKIQ EKGLRMVTVA ECLGMPACST
     QTSPATRDWS WTC
//
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