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Database: UniProt
Entry: A0A2H3HYG4_9EURO
LinkDB: A0A2H3HYG4_9EURO
Original site: A0A2H3HYG4_9EURO 
ID   A0A2H3HYG4_9EURO        Unreviewed;       207 AA.
AC   A0A2H3HYG4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Peptidoglycan-binding Lysin subgroup {ECO:0000313|EMBL:PCG89191.1};
GN   ORFNames=PENO1_106080 {ECO:0000313|EMBL:PCG89191.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG89191.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG89191.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG89191.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCG89191.1}.
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DR   EMBL; NPFK01000647; PCG89191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3HYG4; -.
DR   STRING; 290292.A0A2H3HYG4; -.
DR   Proteomes; UP000218381; 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:UP000218381};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          86..132
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          157..203
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   207 AA;  21653 MW;  BAEBDA5A050F4966 CRC64;
     MNGDYQCEDV ESDLNLTEAE LVAWNPWLAG DCDMALYANL NRSDSRAVCI GVSSTILSTT
     TAATASATTT TSAGPTQTGV VAGCQEFFTV ESGDDCSTIE TEFGVTLAEL YAWNPSIGSS
     CTNLWIGYAY CVKGPATTAT TTSVGPTQTG IAANCDKYHN VVTGDSCAAI EDEYGITFAQ
     LYKWNPAIGS NCETLDVGYA VCVGISS
//
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