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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
 
 
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