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Database: UniProt
Entry: R0IQE7_9BRAS
LinkDB: R0IQE7_9BRAS
Original site: R0IQE7_9BRAS 
ID   R0IQE7_9BRAS            Unreviewed;       626 AA.
AC   R0IQE7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=CARUB_v10012624mg {ECO:0000313|EMBL:EOA39448.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA39448.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; KB870805; EOA39448.1; -; Genomic_DNA.
DR   RefSeq; XP_006306550.1; XM_006306488.1.
DR   AlphaFoldDB; R0IQE7; -.
DR   STRING; 81985.R0IQE7; -.
DR   GeneID; 17897554; -.
DR   KEGG; crb:17897554; -.
DR   eggNOG; ENOG502QRF6; Eukaryota.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; IPR019028; CBM_49.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF41; ENDOGLUCANASE 5; 1.
DR   Pfam; PF09478; CBM49; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM01063; CBM49; 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   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361166};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000029121};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           27..626
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5005145230"
FT   DOMAIN          534..614
FT                   /note="Carbohydrate binding"
FT                   /evidence="ECO:0000259|SMART:SM01063"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ   SEQUENCE   626 AA;  69063 MW;  75AA3A04A5439A6B CRC64;
     MSKFGGSLFG VSLLLTVLLA AATAAAEYYN YGNALDKTFL FFEAQRSGKL PAAQRVKWRS
     HSGLKDGLAQ GVSLEGGYYD AGDHVKFGLP MAFAVTMLSW AAVDHRKELS ASNQMQQTLW
     SIRWGTDYFI KAHPQPNVLW GQVGDGESDH YCWERAEDMT TSRTAYKLDQ YHPGSDLAGE
     TAAALAAASL AFKPFNSSYS ALLLSHAKEL FSFADKYRGL YTDSIPNAKA FYMSSGYSDE
     LLWAAAWLHR ATGDQYYLKY AMDNAGYMGG TGWGMKEFSW DNKYAGVQIL LSKVLLEGKG
     GAYTSTLKQY QMKADYFACA CLKKNGGYNI QTTAGGLMYV REWNNLQYAS AAAYLLAVYS
     DYLSAANAKL NCPDGSVQPQ ALLDFARSQA DYILGKNRQG MSYVVGYGPK YPIRVHHRGS
     SIPSIFAQRS SVKCVQGFDS WYRRSQADPN VIYGALVGGP DQNDYYSDDR SNYEQSEPTL
     SGTAPLVGLF AKLSGNLGSY GGGSYKPYQT TKPPASSYKA TATTYSPKQS GAQIEFLHSI
     TTNWMAGNTR YYRHKVIIKN NSLKPISDLK LKIEDLSGPI WGVNPTGQKN TYQLPQWQKT
     LRAGQAYDFV YVQGGPQAKV LVLSYN
//
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