ID   LYSM1_ARTBC             Reviewed;         458 AA.
AC   D4ALG0;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=LysM domain-containing protein ARB_05157 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=ARB_05157;
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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
RN   [3]
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:0000269|PubMed:21919205}.
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; ABSU01000002; EFE36219.1; -; Genomic_DNA.
DR   RefSeq; XP_003016864.1; XM_003016818.1.
DR   AlphaFoldDB; D4ALG0; -.
DR   SMR; D4ALG0; -.
DR   EnsemblFungi; EFE36219; EFE36219; ARB_05157.
DR   GeneID; 9526341; -.
DR   KEGG; abe:ARB_05157; -.
DR   eggNOG; KOG2806; Eukaryota.
DR   HOGENOM; CLU_010591_8_0_1; -.
DR   OMA; AGMTKSC; -.
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; 4.
DR   Gene3D; 3.10.350.10; -; 4.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   Pfam; PF01476; LysM; 4.
DR   SMART; SM00257; LysM; 4.
DR   SUPFAM; SSF54106; SSF54106; 4.
DR   PROSITE; PS51782; LYSM; 4.
PE   1: Evidence at protein level;
KW   Chitin-binding; Reference proteome; Repeat; Secreted; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..458
FT                   /note="LysM domain-containing protein ARB_05157"
FT                   /id="PRO_0000434925"
FT   DOMAIN          157..203
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          245..291
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          325..371
FT                   /note="LysM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          409..455
FT                   /note="LysM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          210..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  49044 MW;  AA4B2CD6A7F45E49 CRC64;
     MVSLKVCFLL LASSELAFGA APGARSRRRG TAPANPYDKD TTSYCTWWLD YNEELPCDQV
     LQANSITLEK FRRWVSGGQS NTPINQWENH KANHKAKNPS ITGNCEGMTV GKSYCVEAAF
     EPTPTASPTG PSGPTGTPGT IETPLPTQPE IAPNCDAFHL VKQGEDCGTI SATYGITSAQ
     FLAWNPSAGK DCTGLWANAY ACVSIVGHEP PKTTSQAPQP TPTKPSNGIE TPLPTQPKIV
     DNCDKFHLVQ SGEGCAAITS KYGISLAQFT QWNPAAGSNC EGLWANAYAC VSIIGHEPMP
     TPTKPSNGIE TPLPTQPEIV DNCNKFYLVQ SGDTCTTIVS KYGITLSDFT KWNPKAGNTC
     AGLWANAYSC VSIIGYTPKP SPTPTPTKPP NGIQTPTPIQ NGMVTNCNKF HFVENGNTCP
     VIQAKYKVTL ADLVRWNPAI KADCTGLWAK TYLCVGTL