LYSM3_ARTBC
ID LYSM3_ARTBC Reviewed; 408 AA.
AC D4AZ68;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=LysM domain-containing protein ARB_01488 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_01488;
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; ABSU01000020; EFE31588.1; -; Genomic_DNA.
DR RefSeq; XP_003012228.1; XM_003012182.1.
DR AlphaFoldDB; D4AZ68; -.
DR SMR; D4AZ68; -.
DR EnsemblFungi; EFE31588; EFE31588; ARB_01488.
DR GeneID; 9519796; -.
DR KEGG; abe:ARB_01488; -.
DR eggNOG; ENOG502RSIH; Eukaryota.
DR HOGENOM; CLU_058843_0_0_1; -.
DR OMA; MVKYALL; -.
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; 3.
PE 3: Inferred from homology;
KW Chitin-binding; Reference proteome; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..408
FT /note="LysM domain-containing protein ARB_01488"
FT /id="PRO_5003054113"
FT DOMAIN 42..91
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 270..320
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 360..406
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 98..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 44085 MW; 999A99C6A8348A5D CRC64;
MVKYALLPLV AVSLVQAGGP EWHHSRTADF AVDPKVHKGC TSWINVVDAS GKLTCDAFLD
TINVAKRQFI FWNPQLNSDC SNIQSKASYC AFLPSHVSKQ TRGQMDPPPK TKPLPPGLFN
DWGNNHAQKR NDPPPKTKPL PPGLFNDWGN NGARKRDGLS PTGGLGDFHG PKEAPPPDWG
HKGVVEGNHG NTMSTRSPIM GTGLPEQQSE PAFMPPHIPN LPNGMENKMV VHATTLTKKL
RPTGSYVKRD ANAPAPTPGS VGVAIVGCKQ YHTVKAKDTC FNIAQQYPGL LFSDFLRLNP
PPSNLDTVCS NLKANTRVCV KGDTKTNLVP TPSAAVGVHA RDVQGWPSPT KPGTNPGCKS
FELVKKGDSC EGVARKHHIS VAQLKQWNPA VGPTCEKLEI GYYACVRV