ID   LYSM5_ARTBC             Reviewed;         542 AA.
AC   D4AVW3;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=LysM domain-containing protein ARB_00327 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_00327;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE32869.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000013; EFE32869.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003013509.1; XM_003013463.1.
DR   AlphaFoldDB; D4AVW3; -.
DR   EnsemblFungi; EFE32869; EFE32869; ARB_00327.
DR   GeneID; 9519626; -.
DR   KEGG; abe:ARB_00327; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   HOGENOM; CLU_1224486_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; 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..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..542
FT                   /note="LysM domain-containing protein ARB_00327"
FT                   /id="PRO_5003054455"
FT   DOMAIN          264..310
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          487..534
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          439..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   542 AA;  59031 MW;  0460405B7390A402 CRC64;
     MLSSVLFPAM RTLLLLKYVF SLISLSAICC QTVSAIPVVS REGLPMTLSD KCAEALISDV
     ACDPNVLDFK PGYYYSPEIL QRACTDTCKS ALDSYLDRVK SSCGTETIVG PFDLEVSALI
     VPGMRKDLFQ KTCLQDNGRY CNNVAATAAV IADPGVSRFN YLSSVPPGTV PPDPCDIQHV
     CLYVDDQSMR NIWATIDYYS YWVLYIINAG CYNMHRLNGT ELCISAPGQK FVPGDATDLP
     GATVTTPVPA PSDAASGSNR YCGRWYGVKK GDYCNLIVLK FGITMDNFIF LNPALNSNCT
     NLYAEESYCV LPVGDINTYS GKPGYVSTPT GSETTATGIR FEDLPDATEN PYPRPPPGPP
     IAEGTRDDCN YYFDGAEFQY NVTNTYWNSN CQIPPPQVYR VDPESFESWN AGLGNISRPE
     CSFKPGFRYC GRYYALSDDS DEPTPTTPIT TSDDPTSTSA TPTTPTTSSK PSPGAPTMTG
     QPSACNKWHT VTNGESCTVI PKTFGITLEQ FLAWNPTVKS DCTENFWAGY AYCVGVKTLG
     PS