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Database: UniProt
Entry: A0A0F2MAF7_SPOSC
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Original site: A0A0F2MAF7_SPOSC 
ID   A0A0F2MAF7_SPOSC        Unreviewed;       448 AA.
AC   A0A0F2MAF7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Carbohydrate-binding protein family 6 protein {ECO:0000313|EMBL:KJR86059.1};
GN   ORFNames=SPSK_02474 {ECO:0000313|EMBL:KJR86059.1};
OS   Sporothrix schenckii 1099-18.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR86059.1, ECO:0000313|Proteomes:UP000033710};
RN   [1] {ECO:0000313|EMBL:KJR86059.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR86059.1,
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:KJR86059.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR86059.1,
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KJR86059.1}.
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DR   EMBL; AXCR01000006; KJR86059.1; -; Genomic_DNA.
DR   RefSeq; XP_016588735.1; XM_016729343.1.
DR   AlphaFoldDB; A0A0F2MAF7; -.
DR   GeneID; 27664620; -.
DR   KEGG; ssck:SPSK_02474; -.
DR   VEuPathDB; FungiDB:SPSK_02474; -.
DR   OrthoDB; 5470935at2759; -.
DR   Proteomes; UP000033710; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd18618; GH43_Xsa43E-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF6; -; 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51175; CBM6; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..448
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002454929"
FT   DOMAIN          319..445
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   ACT_SITE        44
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            157
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   448 AA;  48247 MW;  EDD99825E56FA139 CRC64;
     MKLFGGQGIR DASCYTVLFL VALLSMVNVS EADNPAIQTI YTADPAPFVY NGRMYLFADH
     DEDGSKTFVM KDWRLFSTTD MANWQDHGVV ASLSTFKWAT GRAWAGQVIN RNNKFYYYLP
     MQKSSGAMAI GVGVADNVTG PYKDALGKPL VDNNNIDPTV WINDDGQAYL YYANTGFGYV
     KLNEDMISIS GGPTSMARPT ALTEGPWVDK RNGVYYLIYA GNGPTEDIRY ATSSGPVGPW
     TYKGVIMTAQ GSSFTNHPGI ADYKNNSYFF YHDGALPGGG GYTRSICVEK FNYNADGTIP
     QIKWTTTGPP QIEDLNPYVR QEAETIAFSS GLKTEMSSAG GIHVTSINNG DYIKVNGVGF
     GNGTGAANFT ASVASAGNGG KIELHLGSKT GTLIGTCTVP GTGGAQTWSS VNCPVSNTTG
     THDLVFLFTG SGSGLLFNFD WWQFTRTS
//
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