ID H6QSV8_PUCGT Unreviewed; 317 AA.
AC H6QSV8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=PGTG_21886 {ECO:0000313|EMBL:EHS63847.1};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EHS63847.1, ECO:0000313|Proteomes:UP000008783};
RN [1] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; DS178300; EHS63847.1; -; Genomic_DNA.
DR RefSeq; XP_003889408.1; XM_003889359.1.
DR AlphaFoldDB; H6QSV8; -.
DR STRING; 418459.H6QSV8; -.
DR EnsemblFungi; EHS63847; EHS63847; PGTG_21886.
DR GeneID; 13540624; -.
DR KEGG; pgr:PGTG_21886; -.
DR VEuPathDB; FungiDB:PGTG_21886; -.
DR HOGENOM; CLU_029718_1_1_1; -.
DR InParanoid; H6QSV8; -.
DR OrthoDB; 1638835at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT DOMAIN 54..295
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 317 AA; 34994 MW; 52844D155BBBD6B8 CRC64;
MTIAFVQGVK ALNLFCGPSQ QDIKRWAGVN LAGLEFGMQN TGTMNQDPME PPPISQIQHF
RAENVTAFRI QISWQRMQPK IMGPLDPDSL QLLSKYVNSA LACKASVIID LHNYARRDGK
VIGEAEDLPA SSLVDFWTRI AQKFGEFPEV RFGIMNEPHD VKLDIWIETL QAVVTAIRKT
GATNKIILPA NNWSHLQTFA TSYNAGMSKI HNPDGSCTGL IFEIHQYFDS DGSGTSAGFP
VPHTKELQEV VALLAKDDRQ AMITEFGGGH NPDCPSVLAD FVEEAHKALV SHVVYTDNVA
AAVTKSMTTW LSKPWVL
//
