ID A0A1J7ISY0_9PEZI Unreviewed; 341 AA.
AC A0A1J7ISY0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Putative LysM domain protein {ECO:0000313|EMBL:OIW30767.1};
GN ORFNames=CONLIGDRAFT_700348 {ECO:0000313|EMBL:OIW30767.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW30767.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW30767.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW30767.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; KV875096; OIW30767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7ISY0; -.
DR STRING; 1408157.A0A1J7ISY0; -.
DR InParanoid; A0A1J7ISY0; -.
DR OrthoDB; 1364532at2759; -.
DR Proteomes; UP000182658; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 4.
DR Gene3D; 3.10.350.10; LysM domain; 4.
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; 4.
DR SUPFAM; SSF54106; LysM domain; 3.
DR PROSITE; PS51782; LYSM; 4.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Reference proteome {ECO:0000313|Proteomes:UP000182658};
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..341
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012114278"
FT DOMAIN 31..75
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 131..177
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 212..258
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 293..339
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 79..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 35289 MW; 24317C30047D4ED5 CRC64;
MGLASLLVLG LAPQLIAALA LNVRQSVSCD FSTSANSGDT CASFAADWGL TESDFEALNP
GVSCPNLVAE QSYCVIGTSP NTSSSSTKAQ TTSSSSTKAS TTSSTAKVTT TTTSSSPYQP
TQSGLAANCN NFHLVASGDS CAAIETQYGI SAADFSTWNP SIDSTCDNLW LGYYVCVGVP
GAKTTTKATT TAAPTSTGPS PQMPSITGTC NAYHQVASGD SCVTIEQAAG ISSAQFLAWN
PYVDAACDNL WLGYYVCVGA KGATTTAKPT TTTTATPTGP SPQMPSITSS CHKYYQVKSG
DSCYTIEQTN SITLAQFLSW NKYVDAACDN LWLGYYVCVG V
//