ID Q7KQF7_GLORO Unreviewed; 470 AA.
AC Q7KQF7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 08-NOV-2023, entry version 73.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
DE Flags: Fragment;
GN Name=GR-eng1 {ECO:0000313|EMBL:AAC48325.1};
OS Globodera rostochiensis (Golden nematode worm) (Heterodera rostochiensis).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=31243 {ECO:0000313|EMBL:AAC48325.1};
RN [1] {ECO:0000313|EMBL:AAC48325.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ro1 {ECO:0000313|EMBL:AAC48325.1};
RX PubMed=9560201; DOI=10.1073/pnas.95.9.4906;
RA Smant G., Stokkermans J.P., Yan Y., de Boer J.M., Baum T.J., Wang X.,
RA Hussey R.S., Gommers F.J., Henrissat B., Davis E.L., Helder J., Schots A.,
RA Bakker J.;
RT "Endogenous cellulases in animals: isolation of beta-1, 4-endoglucanase
RT genes from two species of plant-parasitic cyst nematodes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4906-4911(1998).
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 ECO:0000256|RuleBase:RU361153};
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; AF004523; AAC48325.1; -; mRNA.
DR AlphaFoldDB; Q7KQF7; -.
DR SMR; Q7KQF7; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR019028; CBM_49.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
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; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01063; CBM49; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361153};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..470
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004289524"
FT DOMAIN 367..470
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 305..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC48325.1"
SQ SEQUENCE 470 AA; 49804 MW; 1C0B6470689CBBAF CRC64;
FRVFLLHGLH IVFCNALTAT PPPYGQLSVS GTKLVDSSGQ PVQLIGNSLF WHQFQAQYWN
AETVKALKCN WNANVVRAAV GVDLERGYMS DPTTAYNQAV AVIEAAISQG LYVIVDWHSH
ESHVDKAIEF FTKIAKAYGS YPHVLYETFN EPLQGVSWTD ILVPYHKKVI AAIRALDSKN
VIILGTPTWC QDVDIASQNP IKEYKNLMYT FHFYAATHFV NGLGAKLQTA INNGLPIFVT
EYGTCSADGN GNIDTNSISS WWSLMDNLKI SYLNWAISDK SETCSALKPG TPAANVGVSS
SWTTSGNMVA DHDKKKSTGV SCSGSTSSGS SSSNSGNSAA TTTTKKPPSN SGQTTNQKPS
SSAGSSSSSG SASASVTVVS TNTWNGGGQV NFEVKNTGST TLCGVKFSVT LPAGTTVAGS
WNMNAAGSNE YTLPSYINIK AKEANKDAGM TLNGSGKPTA KVLSTTACSG
//
