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Database: UniProt
Entry: A0A167BXJ0_9PEZI
LinkDB: A0A167BXJ0_9PEZI
Original site: A0A167BXJ0_9PEZI 
ID   A0A167BXJ0_9PEZI        Unreviewed;       763 AA.
AC   A0A167BXJ0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Glycosyl hydrolase family 31 {ECO:0000313|EMBL:KZL81862.1};
GN   ORFNames=CI238_01727 {ECO:0000313|EMBL:KZL81862.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL81862.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL81862.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL81862.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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:KZL81862.1}.
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DR   EMBL; LFIW01001556; KZL81862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167BXJ0; -.
DR   STRING; 1573173.A0A167BXJ0; -.
DR   Proteomes; UP000076584; 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:InterPro.
DR   CDD; cd14752; GH31_N; 1.
DR   CDD; cd06593; GH31_xylosidase_YicI; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR   PANTHER; PTHR43053:SF4; RE74917P; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF117125; Putative glucosidase YicI, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:KZL81862.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT   DOMAIN          58..233
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          280..601
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          615..696
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
SQ   SEQUENCE   763 AA;  85383 MW;  F8D41FC811D3985B CRC64;
     MVRLRDGMWL PAEGTATEYA EEVYYTTEIE GGKGLSLLCP TRKIKTRGHT LNASTVTLDI
     KAEFDGVISV EATHWAGALN KGPHFELFPD GRPEVDAQIQ KGDKGTTLSS GSLSATIHPD
     FDIQFHSTDG SQRLTSLGSR SVGLAYNPAP STPMQTGDMR DFKHYMFTQT TLGVGETIHG
     LGERFGAYNK VGQSISLWNA DGGTSSEQAY KNVSFWLSSK GYGVFIDTPG KVELEIGSER
     CNRLQTVVEG QRLKWYIIYG PTPKDILKRY TTLTGKAGKV PSWSFGLWLT TSFTTNYDEQ
     TVNTFLEGMK ARGSPVDVFH YDCFWMKAFT WTDFVFDSER FPDPKAQITR LKESGLCKKV
     CVWINPYIAQ HGEAFKEAAE KGYLVKRKNG DVWQWDLWQA GMGLVDFTNP EACQWYEDKL
     NTLFDQGVDS IKTDFGERVP TLDVEWHDKT VDPVKMHNYY AFIYNKVVYE ALQKRYGRNE
     AVLFARAACA GTQRFPLQWG GDCESTPEAM AESIRGGLGL GLSGFSFWSC DIGGFEGYPP
     PWIYKRWVAM GLLCSHSRLH GSSSYRVPWV IDDDDASDEG CSRTLAKWTA LKSRLMPYIF
     SEAQAAVEQG IPLSLRAMCI EFPEDPTSWY LDRQFMLGPS ILAAPIFEES GEVEFYLPKG
     RWTSFFSGEA RDGPGWFKET HGFGSLPLYV RENTVLVLGS EKAVGAVYDY AQDVEVRLYQ
     VKEGSRATIV DSEGQEIGVL EVGEDGKLKD TTILKGDFNV TEL
//
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