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Database: UniProt
Entry: E3QF14_COLGM
LinkDB: E3QF14_COLGM
Original site: E3QF14_COLGM 
ID   E3QF14_COLGM            Unreviewed;       327 AA.
AC   E3QF14;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Glycosyl hydrolase family 43 {ECO:0000313|EMBL:EFQ29452.1};
GN   ORFNames=GLRG_04596 {ECO:0000313|EMBL:EFQ29452.1};
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN   [1] {ECO:0000313|Proteomes:UP000008782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; GG697345; EFQ29452.1; -; Genomic_DNA.
DR   RefSeq; XP_008093472.1; XM_008095281.1.
DR   AlphaFoldDB; E3QF14; -.
DR   STRING; 645133.E3QF14; -.
DR   EnsemblFungi; EFQ29452; EFQ29452; GLRG_04596.
DR   GeneID; 24409961; -.
DR   VEuPathDB; FungiDB:GLRG_04596; -.
DR   eggNOG; ENOG502QTYK; Eukaryota.
DR   HOGENOM; CLU_009397_4_1_1; -.
DR   OrthoDB; 5470935at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
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; cd18619; GH43_CoXyl43_like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT   SITE            134
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   327 AA;  37244 MW;  FE448262B73D6338 CRC64;
     MAPLINHLYT ADPSAHVFNG KIYIYPSHDR ETDIKFNDNG DQYDMADYHV FSTSSLDPLE
     PVVDHGVVLK TEDVPWVSKQ LWAPDAAFKD GKYYMYFPAR DKQDVFRIGV AVSDKPEGPF
     TPDPEPIKGS YSIDPASFVD DDGQAYLYFG GLWGGQLQCY QKGNDAFDTE WLGPKEPTGE
     GAYALGPRVA RLTNDMHQFD GEVQEIQILD PETKRPIAAD DHDRRFFEAA WLHKKDGLYY
     FSYSTGDTHY ICYATSDSPL GPFTYSGRIL EPVLGWTTHH SIVEFKGRWW LFHHDCELSN
     GVDHLRSVKV KEIFYDSDGK ITTEKLQ
//
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