ID F2SEG4_TRIRC Unreviewed; 308 AA.
AC F2SEG4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=LysM domain-containing protein {ECO:0000259|PROSITE:PS51782};
GN ORFNames=TERG_01015 {ECO:0000313|EMBL:EGD84737.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD84737.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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:0000256|ARBA:ARBA00037375}.
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DR EMBL; GG700648; EGD84737.1; -; Genomic_DNA.
DR RefSeq; XP_003239028.1; XM_003238980.1.
DR AlphaFoldDB; F2SEG4; -.
DR STRING; 559305.F2SEG4; -.
DR GeneID; 10375381; -.
DR VEuPathDB; FungiDB:TERG_01015; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_010591_2_0_1; -.
DR InParanoid; F2SEG4; -.
DR OMA; PNVNSKC; -.
DR OrthoDB; 2476752at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; LysM domain; 3.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR34997; AM15; 1.
DR PANTHER; PTHR34997:SF1; LYSM DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF01476; LysM; 3.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 3.
DR PROSITE; PS51782; LYSM; 3.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Signal {ECO:0000256|SAM:SignalP};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..308
FT /note="LysM domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003286015"
FT DOMAIN 32..76
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 138..185
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 259..305
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 190..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 32777 MW; 43A9EC76D89B7A04 CRC64;
MMVNIQLILG VIILLGTRKA ATAALPPHPC AFAATAANGD TCQSLAAERG IGMDQFLKRN
PGVNCNALVA GKTYCLSADD SAPGPTASLN PSPKVPTTTL RAVQTMSPKA STGTPAITLV
SRSGPIRFMT GMAPDCLFYH PVAPGDTCQS IVDKYKSFTL DQFYAWNPAT GRNCESLWLG
YYTCVGVKGG PNSPSQQPPS QQPPSQQPPS QQPPSQQPPS QQPPSQQPPS QQPPSQQPPS
QQSNTSQQTQ PNVNSKCNKW YQVVPGDYCQ KIADKFNISL QTFYAWNPSV GSTCASLWAG
YNVCVGSA
//
