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Database: UniProt
Entry: A0A0F2MDU1_SPOSC
LinkDB: A0A0F2MDU1_SPOSC
Original site: A0A0F2MDU1_SPOSC 
ID   A0A0F2MDU1_SPOSC        Unreviewed;      1641 AA.
AC   A0A0F2MDU1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=LysM domain protein {ECO:0000313|EMBL:KJR87858.1};
GN   ORFNames=SPSK_06871 {ECO:0000313|EMBL:KJR87858.1};
OS   Sporothrix schenckii 1099-18.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR87858.1, ECO:0000313|Proteomes:UP000033710};
RN   [1] {ECO:0000313|EMBL:KJR87858.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR87858.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA   Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA   Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA   Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA   Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA   Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA   Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA   Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA   Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA   Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT   "Comparative genomics of the major fungal agents of human and animal
RT   Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL   BMC Genomics 15:943-943(2014).
RN   [2] {ECO:0000313|EMBL:KJR87858.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR87858.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25480940;
RA   Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA   Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA   Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA   de Camargo Z.P., Felipe M.S.;
RT   "Asexual propagation of a virulent clone complex in a human and feline
RT   outbreak of sporotrichosis.";
RL   Eukaryot. Cell 14:158-169(2015).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJR87858.1}.
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DR   EMBL; AXCR01000004; KJR87858.1; -; Genomic_DNA.
DR   RefSeq; XP_016590534.1; XM_016733544.1.
DR   GeneID; 27668821; -.
DR   KEGG; ssck:SPSK_06871; -.
DR   VEuPathDB; FungiDB:SPSK_06871; -.
DR   OrthoDB; 1753565at2759; -.
DR   Proteomes; UP000033710; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   CDD; cd11618; ChtBD1_1; 3.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 3.10.350.10; LysM domain; 2.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR039279; QRT3-like.
DR   PANTHER; PTHR33928:SF2; PECTATE LYASE SUPERFAMILY PROTEIN DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33928; POLYGALACTURONASE QRT3; 1.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF12708; Pectate_lyase_3; 2.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF54106; LysM domain; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 2.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 4.
DR   PROSITE; PS51782; LYSM; 2.
PE   4: Predicted;
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW   ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1641
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002455031"
FT   DOMAIN          1174..1220
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          1226..1272
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          1427..1477
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          1481..1531
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          1536..1586
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   DOMAIN          1590..1640
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50941"
FT   REGION          1398..1430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1448..1462
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        1502..1516
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        1557..1571
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT   DISULFID        1611..1625
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   1641 AA;  169883 MW;  A40D2080DF6BE7B0 CRC64;
     MLSLAYALFF CALGPLVSLA AASSHHHAHN KLHHRQEHNL HGARDTAIDD AYALVNASLP
     AIAAANKLKL QQPRFNTYQF PPAGNASSYG RSNTTVPVIG RRGHLMANGS STSTGSVPPF
     AANSNTTSRD YIVSPELAKA ARVVAEGTTN KPAGADYTDR AARLKAEHWG QTSPASGDNA
     TSVSDGVEAR AAAASSSFWM ANMAMNGVAP YAAAANYKVW RNVMDYGAKG DGKTDDTVAI
     NKAITDGGRC GQTCGSSTAT PAVIYFPSGT YLVSDTLIMY YNTQFLGDPT ARPTLLAAAS
     FVGYAVVLTD VYIDGANGAE WYIPQSNFLR SVRNFVIDIT NAPANNYVCG IHWQVAQGTD
     LQNIDFYMKD GTTQQGLYME NGSGGFMTDL YFQGGNFGAY LGNQQFTARN LIFSGCLTSI
     QVFWDWAWLL QGLTIIGDNT KNGPSVGITI VDGAGGSAGS TGQGVGSMII TDCVFYFVDT
     AIKTTLVADN SSSFLLQNSL FVQVPVAVYD TGAAKTLLAG SSTGNVQVAS WGFGNIVSGT
     SGTSVFQNGN AITAPVRPAS LLPVGSGNWF TRSAPTYADA SIPATAIVNV KTKGAAGDGA
     TDDTAALNQA LAAAANASQI VFFPYGVYVV TDTLHIPLGS RIVGQAWSTI AGRGARFQDA
     TNPRAVVQVG RAGDAGTVEI SDMLFSVIGP TAGAVVVEWN VHEDTNSSAK GSAAMWNSHI
     RVGGNVGSSL QAATCPMSTS GTPKPACVAA SLLFHLTPAA SAYIENFWVW TADHDLDIAS
     QDMINVYTGR GVLIESQGPT WLWGSASEHS VLYQYQFSRA SNLFCSMLQT ESPYFQPSPG
     APAPFVPGMF PDDPTFADCA LPIAANSRCA LAWPVRILDS TDIFVYSAGL YSWFQSYAKN
     CEIGNNCQDG AMDIQRSENV WIYNLCTKAI VNMVTPLGTA VTVGRLNQNG FLASILGWLE
     GATTIVGDRF AGWSVFASGS LVGLGLSSAC EAALYQTVKC DDSARNLLAA DAYLGSTGNK
     TLTGLVCEAV CEASIAYVRQ SVAAACAVTP HLPGTNVPFV SVVDRLWSNW NQTCFVDPTT
     GTNCNDVIAA FPAAADIAAL PVADLCSYCY TQKLKLMEAS AYSGAYDNTS FAARYAYVAS
     HCSLTGVGNF NGTASAVTGT TPVDVTAPVC VSGKHYTVAS GDTCDSIAVA NAASSATLFA
     INPVLRDCSK ELTVGAVLCL PQTCDTLWTV QPDDTCQSIG NATGNSMDTL VAYNTMLNRN
     CSNLQPAPAS EPSWGATLCV SSPGGAYAGV AASNTSTDGN GGRGNGYAPP YTQPIKPPTG
     ATVAKGTNAT LCAAWYVYDA TLLCAQICLT NDISIRVLTL ANPSLHVPTC DADLVRGTAY
     CVRPLSEVEL TASSALPSSS TASLTSTSTS ATTSKTPSNT PNPISTDGKC GTASSKNATC
     QGSTFGNCCG PSGTCGSTPA FCSGRLGCQP TFGECKPISK DGTCGAASSV DALCLYSSFG
     DCCGASGKCG TTTAFCNTDE GCQSNYGTCV ARVSTDGKCG NASSVDATCL GSTFGNCCGS
     SGTCGSTPAF CYGRLGCQAK YGNCVPISTD GKCGSASSVG AMCLYSAFGD CCSAAGTCGT
     TSAACYLSNG CQATYGTCLA K
//
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