ID W3WRD7_PESFW Unreviewed; 387 AA.
AC W3WRD7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=LysM domain-containing protein {ECO:0000259|PROSITE:PS51782};
GN ORFNames=PFICI_11817 {ECO:0000313|EMBL:ETS76430.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS76430.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- FUNCTION: Might have a role in sequestration of chitin oligosaccharides
CC (breakdown products of fungal cell walls that are released during
CC invasion and act as triggers of host immunity) to dampen host defense.
CC {ECO:0000256|ARBA:ARBA00037375}.
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DR EMBL; KI912117; ETS76430.1; -; Genomic_DNA.
DR RefSeq; XP_007838589.1; XM_007840398.1.
DR AlphaFoldDB; W3WRD7; -.
DR GeneID; 19276830; -.
DR KEGG; pfy:PFICI_11817; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_010591_8_0_1; -.
DR InParanoid; W3WRD7; -.
DR OMA; KIGRECT; -.
DR OrthoDB; 1364532at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; LysM domain; 5.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR34997; AM15; 1.
DR PANTHER; PTHR34997:SF2; LYSM DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00257; LysM; 4.
DR SUPFAM; SSF54106; LysM domain; 2.
DR PROSITE; PS51782; LYSM; 4.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..387
FT /note="LysM domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004834978"
FT DOMAIN 37..82
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 127..173
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 216..262
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 340..385
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 91..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 39680 MW; DB53031F9C3D8A18 CRC64;
MFFQTFLASI VLVGATWGYT VDPPTAASSD TIQDCTLWMI ASTGDTCQGI SNTYGLELSQ
LFTYNPSLAS ACAIVVGQSY CVEQNWGVPP ETPTTSKTTT TAAPTTTGNG VSTPTPTMGG
LTSNCNKFYF VPKGSSCKAV LDTNGITIAQ LYAWNTDVLA DCTGLWAEVY VCVGIIGETT
TPNPTTSATT TTTTTPGNGV TTPTPTQPGM VSNCQKFYFV SPGTSCSAVL AANSITLADL
YAYNSGVGAD CSGMWASVYV CVGVIGGGQV TTTSTTTSIP PTTTTTPGNG VSTPTPTQPG
MVSNCDKFFF VQPGTSCSAV LSSTGLTLAQ LYALNSGVGA DCSVVSGDTC SVVSTKTGVS
TANIIAWNPQ AGSTCNIWLG YYICVGI
//
