ID   LYSM6_ARTBC             Reviewed;         573 AA.
AC   D4AY86; D4AY87;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=LysM domain-containing protein ARB_01155/01156 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_01155/01156;
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 domain binds chitin and potentially related
CC       carbohydrates, and might be involved in damping host defense.
CC       {ECO:0000305|PubMed:19299132}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE31902.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EFE31903.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000018; EFE31902.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; ABSU01000018; EFE31903.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003012542.1; XM_003012496.1.
DR   RefSeq; XP_003012543.1; XM_003012497.1.
DR   AlphaFoldDB; D4AY86; -.
DR   EnsemblFungi; EFE31902; EFE31902; ARB_01155.
DR   EnsemblFungi; EFE31903; EFE31903; ARB_01156.
DR   GeneID; 9526613; -.
DR   GeneID; 9526614; -.
DR   KEGG; abe:ARB_01155; -.
DR   KEGG; abe:ARB_01156; -.
DR   eggNOG; ENOG502SNDA; Eukaryota.
DR   HOGENOM; CLU_973832_0_0_1; -.
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; 1.
DR   Gene3D; 3.10.350.10; -; 1.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   Pfam; PF01476; LysM; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Chitin-binding; Glycoprotein; Reference proteome; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..573
FT                   /note="LysM domain-containing protein ARB_01155/01156"
FT                   /id="PRO_5003054097"
FT   DOMAIN          373..419
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          375..405
FT                   /note="LysM domain"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   573 AA;  62495 MW;  8BE3FB9AC171C92C CRC64;
     MIPRNLISGL FLLPFVVAEL NIYGYLDLKT LADGFHTTTA CIAALNQTVD CDARTAVAAA
     VADTYYWTLD NVTTLCTSQC QQSLTSWTSA VDAACGNRPI VEDGIVKLAS STPLTYKEGF
     DLVCLKSGDS WCMIESQEWE GSDILKYPTD YCSTGDPEYD GPECFEKGFD QLAIEAGDER
     MTSLYEKDLL CSDCFLKVFR QRLLSPFLLK GGYTSYLVEQ FQDMQSYCST SMPYATSTSE
     VFMGTATRTM PTGSPPPTTT CGGPTIQPTD PPLSCEAITD KYNVTTGDSH SDLHGEFSLA
     SKPRFLKANA IDRQHEPIEK LDHAICYAGT SEPPGGSYES QPPVHQPTGA SEYYTTAIPP
     APTSTGTTPS CGRYYEVVAG DQCNTIALHF GITVDAFLSL NTQIDERCSN LWIAYAYCVA
     PVDIVDQPMT IVDQDIATQG NVLPATELPS PRMGRVVLNI MIGSVVTQLL ENAALSMDIA
     GVRRTSAQQG IVIRVPVIQT LAKRVLTVRA DQALQETKHV PALNLAHVAT WRDIVEMEPT
     TAHPGDAILE RAKGPRIHSI ALYVTVLYLD LWI