ID A0A168GL86_CORDF Unreviewed; 399 AA.
AC A0A168GL86;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidoglycan-binding Lysin subgroup {ECO:0000313|EMBL:OAA76629.1};
GN ORFNames=LEL_06313 {ECO:0000313|EMBL:OAA76629.1};
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:OAA76629.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76629.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76629.1,
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:OAA76629.1}.
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DR EMBL; AZHF01000004; OAA76629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168GL86; -.
DR STRING; 1081108.A0A168GL86; -.
DR OrthoDB; 2476752at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 5.
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:SF1; LYSM DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF01476; LysM; 4.
DR SMART; SM00257; LysM; 5.
DR SUPFAM; SSF54106; LysM domain; 4.
DR PROSITE; PS51782; LYSM; 5.
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..399
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007897323"
FT DOMAIN 24..71
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 119..166
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 198..245
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 275..322
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 349..397
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 70..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 42837 MW; 60DAF02F7F332B5B CRC64;
MTRFATTFVA ALAGANLAAA KCTYKWRAHA GDTCDSLSAD WGIAVKDFIS WNPSVGANCA
NGVTPDQEYC VEDDGTGNDP TTAPPTSTTL TTTTSSTPTQ PTGGVPSPTQ DGVTKDCKAW
YKVKSGDTCD AIIKKYGAFS TDDFLKWNPA AGKDCTGLWV DYYVCVGVPG TPTSPTPTGS
DPSKPSPTQA GVTKDCQKWY KVKSGDTCDK IKNQFNTFST ADFLKWNPAA GTDCSGLWVD
YYVCVGVPGT PTSPTGSDPS KPSPTQDGIT SKCTKYYKAQ KGDTCQKIVD NLRTFSLSDF
TSWNPAVGKD CTGIWVDYYY CVAVPGTPTN PAPAVPSPHQ DGITKNCKKY YKVQSGDYCD
KIISKYNKAF NLKQLVSWNP AIGNDCSHLF VDFYICVGV
//
