ID A0A1F7ZR35_9EURO Unreviewed; 428 AA.
AC A0A1F7ZR35;
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=LysM domain protein {ECO:0000313|EMBL:OGM41739.1};
GN ORFNames=ABOM_009461 {ECO:0000313|EMBL:OGM41739.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM41739.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM41739.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(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:OGM41739.1}.
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DR EMBL; LYCR01000104; OGM41739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZR35; -.
DR STRING; 109264.A0A1F7ZR35; -.
DR OrthoDB; 2476752at2759; -.
DR Proteomes; UP000179179; 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; 4.
DR SUPFAM; SSF54106; LysM domain; 4.
DR PROSITE; PS51782; LYSM; 4.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..428
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009534090"
FT DOMAIN 143..190
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 229..275
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 315..363
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 380..426
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 100..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 45251 MW; E21F0ACCD480E2BC CRC64;
MILAQILGLS LFGSVNAATL GKRFSSAGFA TGETDPNVNR GCTYWANSIK STDTCAALER
YYGITTAQLV SWNPSLTATD CTLNEEWSYC VEAPTVPTTT EKTTTTTETP ATTTSTSTGA
GATTTTAVGP SPTQTGLISS CNAFYYVQKD DSCWGIANSY GNFTVEQFYS WNPAVKADCS
GLQPSYYVCV GVAGSTSSTT TSKATTASPT TTSAPHSPQQ SGIISSCNNY YFVEAGDGCV
LIATKHGITL GDFYAWNPAV GSSCSSLQAG YWVCVGVSGG TTTTHATTTK TTTSTTTAGT
GPTPTQSGIT ADCSAYYQAQ EGDDCWSIIN KKYSYLTAAK FYEWNPAIGP SCSNLQQGYY
YCVATKSEGP MPDTISSCAK WHLVASGDSC WSIEQQYSIT STQFDSWNPY VGSSCTTLWL
GYYVCVGV
//
