UniProt: F0ZXQ0

Database: UniProt
Entry: F0ZXQ0_DICPU

LinkDB:  F0ZXQ0_DICPU 
Original site:  F0ZXQ0_DICPU

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   F0ZXQ0_DICPU            Unreviewed;       455 AA.
AC   F0ZXQ0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=DICPUDRAFT_40165 {ECO:0000313|EMBL:EGC31287.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC31287.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(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         ECO:0000256|RuleBase:RU361166};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10059,
CC       ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; GL871264; EGC31287.1; -; Genomic_DNA.
DR   RefSeq; XP_003292196.1; XM_003292148.1.
DR   AlphaFoldDB; F0ZXQ0; -.
DR   STRING; 5786.F0ZXQ0; -.
DR   EnsemblProtists; EGC31287; EGC31287; DICPUDRAFT_40165.
DR   GeneID; 10505944; -.
DR   KEGG; dpp:DICPUDRAFT_40165; -.
DR   eggNOG; ENOG502QRF6; Eukaryota.
DR   InParanoid; F0ZXQ0; -.
DR   OMA; GGFQPFF; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF60; ENDOGLUCANASE; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361166};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           24..455
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5005128790"
FT   DOMAIN          26..445
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        386
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        424
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   455 AA;  50197 MW;  DD5249A4C8347ECE CRC64;
     MVRNIKNVTL FIVLGLLINY SIAQDYCSYL KQGLMFYKAQ RAGRLPDNDI SWRGNSVLTD
     SSPGGKLDSN GDGDLSKGYF DAGDGVKFGL PMCWSMVMLG WSFIESQANI ASCGLTDLYL
     EDLKWGTDYI LASHLSDNEF VAQVGNGELD HSYWEPPEFI NYVRSVYTIN QNKPGTELAM
     EAAAALSAAS IAFKSSNPSY ASTCLNHAKT LYNFGKTYQG VYSDSVPDAQ PFYNSYSGYK
     DELVWGAVWL YKATSDPSYL SDAENFYQTN GIGYNGISNS FDWDQTAAGS TVLLYKITGK
     QLYADIMTQT MKYWLPGGGV TYTPGGLAWI RQWGPARYAM SMAFIGTVYG TSDSLQFAKK
     QLDYVLGSNG QSFVVGMGPK YPINPHHRAA HHSTTNNIKD PVNNKYILYG ALVGGPGSDD
     SYVDDREDYI KNEVALDYNA GYVSTLAYFA LGIYL
//

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