UniProt: F0ZRH6

Database: UniProt
Entry: F0ZRH6_DICPU

LinkDB:  F0ZRH6_DICPU 
Original site:  F0ZRH6_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 (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (14)   

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ID   F0ZRH6_DICPU            Unreviewed;       521 AA.
AC   F0ZRH6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=DICPUDRAFT_36716 {ECO:0000313|EMBL:EGC33455.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC33455.1, 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; GL871141; EGC33455.1; -; Genomic_DNA.
DR   RefSeq; XP_003290026.1; XM_003289978.1.
DR   AlphaFoldDB; F0ZRH6; -.
DR   STRING; 5786.F0ZRH6; -.
DR   EnsemblProtists; EGC33455; EGC33455; DICPUDRAFT_36716.
DR   GeneID; 10504371; -.
DR   KEGG; dpp:DICPUDRAFT_36716; -.
DR   eggNOG; ENOG502QRF6; Eukaryota.
DR   InParanoid; F0ZRH6; -.
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; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298:SF18; CELLULASE-RELATED; 1.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 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..521
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5005128791"
FT   DOMAIN          28..447
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   REGION          454..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        388
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ   SEQUENCE   521 AA;  57238 MW;  1E76F6E72F3B6A2B CRC64;
     MKIISILFII YLICINNSHL VYAQSTNYCE ALKYSLLFYK AQRAGRLPDN DIPWRGNSVL
     KDTYNNKFDS NGDGILSKGY FDAGDAVKFG FPMAYSMTML GWVYVTYKDN IVNCGLDSLY
     KDVLKWGSDY IIACHVEDNV FVGQIADGDL DHSFWVAPEN LTYVRDSFAI DSSKTGTDLA
     MEAAAALSVT SMVFSSSDPT YSSNCLDHSK KLYNFAINNP KNVYQSSISN AGSFYSSGGY
     NDEIAWASVW LYKATNQQNY LDTAKTYFSY NDVQYAKELS WDQKGVPTGL LLLQITNDAS
     YKSRVEEALN SWISGSYVTF TPGGLAYLRQ WGPCRYAMSM ALVAAVYGKS GDDYTKFAKS
     QLNYVLGDNP KKFSFVVGWG TNYPKNPHHR ASHHPTDGIK NPAVNTYVLY GALVGGPKND
     DVYDDNREDY VQSEVALDYN VGLVGTLAAF SAGSEPASKT NPYSGGPITN PGSGSNSGPN
     TGSNPDSNSD SDSDSINASI SIRGYSSLLL IIYLIINVLL L
//

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