LYSM2_ARTBC
ID LYSM2_ARTBC Reviewed; 262 AA.
AC D4B4P8;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=LysM domain-containing protein ARB_03438 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_03438;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP DOMAIN, AND FUNCTION PREDICTION.
RX PubMed=19299132; DOI=10.1016/j.tim.2009.01.002;
RA de Jonge R., Thomma B.P.;
RT "Fungal LysM effectors: extinguishers of host immunity?";
RL Trends Microbiol. 17:151-157(2009).
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:0000305|PubMed:19299132}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: The LysM domains bind chitin and potentially related
CC carbohydrates, and might be involved in damping host defense.
CC {ECO:0000305|PubMed:19299132}.
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DR EMBL; ABSU01000034; EFE30096.1; -; Genomic_DNA.
DR RefSeq; XP_003010736.1; XM_003010690.1.
DR AlphaFoldDB; D4B4P8; -.
DR EnsemblFungi; EFE30096; EFE30096; ARB_03438.
DR GeneID; 9524849; -.
DR KEGG; abe:ARB_03438; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_010591_2_0_1; -.
DR OMA; TGMVKNC; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; -; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; SSF54106; 2.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Chitin-binding; Glycoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..262
FT /note="LysM domain-containing protein ARB_03438"
FT /id="PRO_5003054683"
FT DOMAIN 31..75
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 132..179
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 85..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 262 AA; 27820 MW; 24EF9E0024AFBEF6 CRC64;
MVSIPLILGA IILLGTRKAA TAALPPRPCA FAVTAATDDT CQSLGAQWGI GMAQFLKWNP
GVNCNALVAG KTYCLSAGDS ELGPTASLTP SPQVPTTSRA TQTMTSKAST GTLVSRSGPI
KFLNGMAPDC LFYHPVSPGD TCQSIVDRYK AFTLDQFYTW NPSVGKNCES LWLGYYVCTG
VKGGPNSPSQ QPPSQQPPSQ QSPSQQSPSQ QSPSQQPPSQ QPPSQQPPSQ QSNTSQQTQP
NVNSKCKFHI FCLGTLAYMA FD