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Database: UniProt
Entry: E6ZJZ9_SPORE
LinkDB: E6ZJZ9_SPORE
Original site: E6ZJZ9_SPORE 
ID   E6ZJZ9_SPORE            Unreviewed;       884 AA.
AC   E6ZJZ9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Glycosyl hydrolase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=sr11602 {ECO:0000313|EMBL:CBQ67652.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ67652.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ67652.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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DR   EMBL; FQ311430; CBQ67652.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZJZ9; -.
DR   EnsemblFungi; CBQ67652; CBQ67652; sr11602.
DR   VEuPathDB; FungiDB:sr11602; -.
DR   eggNOG; ENOG502QPU8; Eukaryota.
DR   HOGENOM; CLU_009024_0_0_1; -.
DR   OrthoDB; 69117at2759; -.
DR   Proteomes; UP000008867; Chromosome 1.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:1901136; P:carbohydrate derivative catabolic process; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR041036; GH5_C.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31308; -; 1.
DR   PANTHER; PTHR31308:SF5; ERGOSTERYL-BETA-GLUCOSIDASE; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF18564; Glyco_hydro_5_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          82..151
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   DOMAIN          673..734
FT                   /note="Glycoside hydrolase family 5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18564"
FT   REGION          602..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..757
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   884 AA;  97102 MW;  1895E4C2AD355F3C CRC64;
     MARSHSTSPI TGATVPDYYI HASDAFFRDT NGRALLLRGV NLSGQNKSPI GQPSQKLQGF
     WESAESGGES FVGQPLNLKD GSADTHLARL RSWGFNCLRY VFTWEAIEHK GPRQYDTEFI
     DYTVQVLRKV KQYGFRVFMD PHQDLFSRFT GGSGAPYWTL IACGLNPRNF TPTQAAYIQA
     EWPNPQNPNP AEFPDMLWAT NYTRLGAATL SVLFFAGKHF APRCIIDGVN IQDWLQSHFL
     GACRQLLQRI VDAGDLVDGC VIGWDSVNEP NQTYIGLDRI SSIPASWQLK KGPVPTPLQS
     FRLGAGQAQT LENWNFGAMG PKRDGSVTVD PKGTMAWLTE DEDRVQGGNR WGWKRDDAWP
     LGQCLWAAHG VWDPATGDVL NDAYFRFFEG PAGSKPAEFA EDYWLPHYRA YANLIRSKHT
     EAIMFIQPPV FEPPPKSLSQ DDLKQRACLS GHFYDGLTLI TKHWNWFNAD AVGLLRGKYP
     GTLFAIRVGN KAIRQCIRDQ LGYLRQDCLD GLGQYPTLIG EIGIPYDLDK KKSYYGDAKG
     RGIGDYSAQT LALDASLNGC DGKNLLNYTI WTYCPDSSHE WGDDWNGEDL SIWSQDDVKG
     AEAESSSQSS IRRKQSTSST SSLRSKRLTS LTPLSSGLTS SSSLHLPALV PGDDDYHAPN
     LLNGSRAAAA FCRPFPVATV GTPASIDFDI KSSEFAYAVD VTAAELGKPG LATEIYLPFL
     HYGADGVAAA ASGDLGNRRD KNASQRWARK QEKKIRSADS LASSTSSLRT SGSSSIDDAS
     SSSASTVLAD SSDLSRTTST RSTAAPSISA EQLLSIDVQL SAGRWEVQGQ YLRWYMNKAE
     AIAEDADNPA EGVFRHSIKV KRKGGPVKLE MSGSAWDILT CGIL
//
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