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Database: UniProt
Entry: A0A162JME1_CORDF
LinkDB: A0A162JME1_CORDF
Original site: A0A162JME1_CORDF 
ID   A0A162JME1_CORDF        Unreviewed;       165 AA.
AC   A0A162JME1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=LysM domain-containing protein {ECO:0000313|EMBL:OAA71052.1};
GN   ORFNames=LEL_09643 {ECO:0000313|EMBL:OAA71052.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA71052.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA71052.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA71052.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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}.
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:OAA71052.1}.
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DR   EMBL; AZHF01000009; OAA71052.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162JME1; -.
DR   STRING; 1081108.A0A162JME1; -.
DR   OrthoDB; 1364532at2759; -.
DR   Proteomes; UP000076881; 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; 2.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   PANTHER; PTHR34997; AM15; 1.
DR   PANTHER; PTHR34997:SF1; LYSM DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF01476; LysM; 2.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF54106; LysM domain; 2.
DR   PROSITE; PS51782; LYSM; 2.
PE   4: Predicted;
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..165
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007836603"
FT   DOMAIN          43..90
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          117..163
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   165 AA;  17823 MW;  09CF54DB6671D130 CRC64;
     MKFSVISAIL LPLAAAAATP AQEAAAAAVP DPVQDGITKN CKTYYKAKPG DSCQKIVNDY
     GVFTFNDFYK WNPAVGKNCE SLLGGYYYCV GVPGTPSRCT ENHPTPTQPG SVCKCGQWYK
     VKKGDNCQAL EKKFKISDKD FHKLNGGLNK DCSNLQADVN VCVKA
//
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