ID A0A1V6QG17_9EURO Unreviewed; 357 AA.
AC A0A1V6QG17;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=LysM domain-containing protein {ECO:0000259|PROSITE:PS51782};
GN ORFNames=PENANT_c004G11451 {ECO:0000313|EMBL:OQD88154.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD88154.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(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:OQD88154.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDYN01000004; OQD88154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QG17; -.
DR STRING; 416450.A0A1V6QG17; -.
DR OrthoDB; 2476752at2759; -.
DR Proteomes; UP000191672; 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; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672};
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..357
FT /note="LysM domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012573799"
FT DOMAIN 133..180
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 221..267
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 81..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 37673 MW; 93F55439B707F266 CRC64;
MLSSSLYLLA TSLTLSTAFA RPNVVRRDET PQLPYDPNTT PYCTWWAISM ADFVRWNPSV
GSNCAGYVSG KSDCVEAYGE PAPGTGTTTT RVTTTSSATT SSTTTSTTTT SSTTTTGCAL
GPSQSGQVAN CNKWDLVQSG DTCSVYLAKY PGLTLANLVA WNPAIGSQCQ FLWEETYICT
GITGWTPSPT TTKATTTSAT PTNGFTTPQP IQPGMIAECN KFHMVVDGDG CDSIAKANGI
TPAQFYALNP ALGNTCSALW LGYYVCVSRI GTAPTTTKAT TTTTKPTNDI ATPTPIQDGS
LERTSPRSLP RTNTPVIGCR ERAYGTGVAA TDNESSGPKF QRQQRTNIAV LGGSKRT
//