ID D8S600_SELML Unreviewed; 666 AA.
AC D8S600;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=SELMODRAFT_109529 {ECO:0000313|EMBL:EFJ20261.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ20261.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(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 -!- 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; GL377603; EFJ20261.1; -; Genomic_DNA.
DR RefSeq; XP_002978814.1; XM_002978768.1.
DR AlphaFoldDB; D8S600; -.
DR STRING; 88036.D8S600; -.
DR EnsemblPlants; EFJ20261; EFJ20261; SELMODRAFT_109529.
DR Gramene; EFJ20261; EFJ20261; SELMODRAFT_109529.
DR KEGG; smo:SELMODRAFT_109529; -.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; D8S600; -.
DR OMA; WNDKGRT; -.
DR Proteomes; UP000001514; 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: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:SF19; ENDOGLUCANASE 19-RELATED; 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 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:UP000001514};
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..666
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5018379153"
FT DOMAIN 541..644
FT /note="Carbohydrate binding"
FT /evidence="ECO:0000259|SMART:SM01063"
FT REGION 593..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ SEQUENCE 666 AA; 73679 MW; 7406A1C5DB36CDA8 CRC64;
MSRRNASICA CLGAVLVAAL LESALAFDYS DALGKTFLYY EAQRSGRLPP SQRASWRGDS
ALDDGKSQGV DLVGGYYDAG DNVKFGLPMA FTITMLSWSA IEYGKQIDGA GQMGFAKEAI
KWGTDYFLKA HTAPFELWGQ VGDGLNDHGC WQRPEDMTTS RRAYKIDTSN PGSDLAGETA
AAMAAASIAL RSSDPTYSDL LVEHSKQLFE FADKYRGKYD SSIRLAQNFY TSKSGYADEL
LWASLWLYEA TGDEQYLDYA VDNGGALGGT IWGLMEFSWD VKYPGVQVLA SKILMQGRAS
PRHIPTLELF QSKAQFFLCA ALQKNNGFHL PRTPGGLMYV RSWNNMQYVV TASFLLTVYS
DYLASSRQQL QCPRLSSDSS ELLALAKSQV DYILGDNPRA TSYLIGFGQN YPRQVHHRAS
SIVSIKVDNA FVSCRGGYSS WYLRKMSDPN VLIGALVGGP DLYDNFADER YNFEQTEPAT
YNTGPLIGIL ARLLQDHRYQ QSGRNLSLFL TARVSECSRT YVFSLVSQSS RPQRRGVKSV
LSIRQRLVGS WTLEGQVQYK YEVTVKNTSR RRTVKAIVLQ INRLQEGQYW GLTRTSSSGS
STSRSTSSTS SSSSSDAGDG SFTFPHWRSS LNPLESFVFV YINAASGERA KIRVASYRTT
APGSSV
//
