ID   LYSM4_ARTBC             Reviewed;         519 AA.
AC   D4B4Q2;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 2.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=LysM domain-containing protein ARB_03442 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_03442;
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=EFE30100.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ABSU01000034; EFE30100.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003010740.1; XM_003010694.1.
DR   AlphaFoldDB; D4B4Q2; -.
DR   SMR; D4B4Q2; -.
DR   EnsemblFungi; EFE30100; EFE30100; ARB_03442.
DR   GeneID; 9524853; -.
DR   KEGG; abe:ARB_03442; -.
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; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Chitin-binding; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..519
FT                   /note="LysM domain-containing protein ARB_03442"
FT                   /id="PRO_5003053765"
FT   DOMAIN          312..358
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          467..510
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   REGION          314..358
FT                   /note="LysM domain"
FT                   /evidence="ECO:0000305"
FT   REGION          407..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        470..485
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        476..491
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        484..498
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        503..508
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   519 AA;  55652 MW;  AD22BBA350B312FD CRC64;
     MGQLKQLAGI LALASPAIAA FSVYALHDPD ALKASLGVTS ECLSALNYTV ECDGPSAVRA
     TKNSDNDPWS MDDLTTLCTD GCSKSLSTWF DAVEQKCEGE EVTINGLVVD PKAFPMKYIS
     GYDLACLRDS NDNWCFYEAQ DWDSGVFTSW DKKQPDACSG ENPPADCDKK GSEEDVDTLY
     VTNSYDKELY CSECFMLLWR QRIESPVFPQ GNLLDHFTKQ FSKLEAACST KLPLTTPAPT
     VVLGAKDTLP PATGYHTDGS TVFRYSSPPA PTITTEEPIA KRTAAPRAMK TFYTPATPDR
     TPQLGAMAPC GKYYNVVAGD TCASISSEFE VTMDELLTYN PELHPNCENL WANFAICVAP
     VSPNPMTVDG SCGENNAGAT CDGSPFGSCC NNEGRCVPCG PEATAAPDAP DAQGQTVHDD
     EPPEEPHIEE PPKDIPAGDD DDRKKAKLPL PSGKYPLPSN STMISKDGSC NEYISCVGSP
     FGVCCSTSGW CGYGKPWCGV GNCVSGYCDT EDKASGKPQ