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Database: UniProt
Entry: A0A1S3CDA0_CUCME
LinkDB: A0A1S3CDA0_CUCME
Original site: A0A1S3CDA0_CUCME 
ID   A0A1S3CDA0_CUCME        Unreviewed;       496 AA.
AC   A0A1S3CDA0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   Name=LOC103499723 {ECO:0000313|RefSeq:XP_008461017.1};
GN   Synonyms=103499723 {ECO:0000313|EnsemblPlants:MELO3C023353.2.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008461017.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|EnsemblPlants:MELO3C023353.2.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_008461017.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_008461017.1; XM_008462795.2.
DR   EnsemblPlants; MELO3C023353.2.1; MELO3C023353.2.1; MELO3C023353.2.
DR   GeneID; 103499723; -.
DR   Gramene; MELO3C023353.2.1; MELO3C023353.2.1; MELO3C023353.2.
DR   KEGG; cmo:103499723; -.
DR   eggNOG; ENOG502QV58; Eukaryota.
DR   InParanoid; A0A1S3CDA0; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   Proteomes; UP000596662; Unplaced.
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:SF129; ENDOGLUCANASE 24; 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:UP000089565};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           28..496
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5041474475"
FT   DOMAIN          31..487
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        414
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        465
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        474
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   496 AA;  54590 MW;  EF777C07025D7959 CRC64;
     MKNPIFSHRT ILFLILSILL SPDFTFAGHD YTDALSKCIL FFEGQRSGFL PQDQRMTWRA
     NSGLGDGWTY KTDLTGGYYD AGDNVKFGFP MAFTTTLLSW SVIEFGDLMP PAELRNSLVA
     IRWATDYLLK TVSQPNRIFV QVGDPSADHF CWERPEDMDT MRTVYAVDAP GTASDVAGET
     AAALAAASMA FRSSDPGYAE TLLQNGIKAF ELADTYRGAY SDNANIRDGV CPFYCDFDGY
     QDELLWGAAW LRRASKNESY LSYIQDNGKT LGAEDSFNEF GWDNKHAGLN VLVSKEALEG
     NIFTLQSYKA SADNFMCTLI PESSSSHIQY TPGGLIYKPG GSNLQHATSI TFLLLAYAHY
     LERTSSTVNC GNVVVGPASL RRQAKQQVDY ILGDNPKGIS YMVGYGNYFP QRIHHRGSSL
     PSVRDHPQPI ACKEGSTYFN SPDPNPNVLV GALVGGPGED DVYEDDRADF RKSEPTTYIN
     APFVGVLAYF AANPGG
//
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