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Database: UniProt
Entry: Q9GRU5_HETSC
LinkDB: Q9GRU5_HETSC
Original site: Q9GRU5_HETSC 
ID   Q9GRU5_HETSC            Unreviewed;       365 AA.
AC   Q9GRU5;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   08-NOV-2023, entry version 75.
DE   SubName: Full=Beta-1,4-endoglucanase 2 {ECO:0000313|EMBL:CAC12959.1};
GN   Name=eng2 {ECO:0000313|EMBL:CAC12959.1};
OS   Heterodera schachtii (Sugarbeet cyst nematode) (Tylenchus schachtii).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Heterodera.
OX   NCBI_TaxID=97005 {ECO:0000313|EMBL:CAC12959.1};
RN   [1] {ECO:0000313|EMBL:CAC12959.1}
RP   NUCLEOTIDE SEQUENCE.
RA   De Meutter J.J.J.;
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAC12959.1}
RP   NUCLEOTIDE SEQUENCE.
RA   De Meutter J., Tytgat T., Gheysen G.D.C., Coomans A., Gheysen G.D.R.;
RT   "Biochemical characterisation of pharyngeal secretions from Heterodera
RT   schachtii stage 2 juveniles.";
RL   Eur. J. Biochem. 0:0-0(0).
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; AJ299387; CAC12959.1; -; mRNA.
DR   AlphaFoldDB; Q9GRU5; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..365
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004326542"
FT   DOMAIN          35..277
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          301..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..365
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  38854 MW;  278F393D1B56F47D CRC64;
     MLVLLVLLAI VGITFVDAAA PPYGQLSVSG TKLVGSNGKP VQLIGNSLFW HQWYPQFWNA
     ETVKALKCNW NSNVVRTAMG VEQGGYLSDA NTAYRLTAAV IEAAIAQGIY VIVDWHAHEP
     NADKAIEFFT KIAKAYGSNP HLLYETFNEP LDVSWNDVLV PYHKKVISAI RAIDKKNVII
     LGTPKWSQDV DVAAQNPIKG FSNLMYTLHF YASSHFVDGL GNKLKTAVNK GLPVFVTEYG
     TCEASGNGNL NSGSMSSWWS LLDQLQISYV NWAIADKSEA CAALTGGTSA ANVGTSSRWT
     QSGNMVASQH KKKSTGVNCN GGGGAAAKPA AKPAAKPAAK PAAKPAAKSK GKSSKAKKPN
     AKKSG
//
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