GUN19_ORYSJ
ID GUN19_ORYSJ Reviewed; 523 AA.
AC Q6YXT7; A0A0P0XB73; Q0J8F3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Endoglucanase 19;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 19;
DE Flags: Precursor;
GN OrderedLocusNames=Os08g0114200, LOC_Os08g02220; ORFNames=P0427G12.14;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR EMBL; AP005657; BAD10555.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF22762.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03541.1; -; Genomic_DNA.
DR EMBL; AK106851; BAG97853.1; -; mRNA.
DR RefSeq; XP_015649019.1; XM_015793533.1.
DR AlphaFoldDB; Q6YXT7; -.
DR SMR; Q6YXT7; -.
DR STRING; 4530.OS08T0114200-01; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q6YXT7; -.
DR PRIDE; Q6YXT7; -.
DR EnsemblPlants; Os08t0114200-01; Os08t0114200-01; Os08g0114200.
DR GeneID; 4344508; -.
DR Gramene; Os08t0114200-01; Os08t0114200-01; Os08g0114200.
DR KEGG; osa:4344508; -.
DR eggNOG; ENOG502QPI6; Eukaryota.
DR HOGENOM; CLU_008926_1_2_1; -.
DR InParanoid; Q6YXT7; -.
DR OMA; WGASWIY; -.
DR OrthoDB; 1195424at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6YXT7; OS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Cellulose degradation; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..523
FT /note="Endoglucanase 19"
FT /id="PRO_0000249296"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 523 AA; 56214 MW; F047BC4FC913A022 CRC64;
MCSWSLSSHT LTSPVRQAAM EPKSSSCGGA GIRLRLLVVL HLLLLVPSSA MAFNYADALA
KSIIFFEGQR SGKLPPGNRM PWRADSGLTD GAQYNVDLVG GYYDAGDNVK FGLPMAFSTT
MLAWSVLDFG KFMGAELPNA RAAVRWGADY LLKAATATPG ALYVQVADPN QDHRCWERPE
DMDTPRSVYR VTADKPGSDV AGETAAALAA SSMVFRRADP AYSARLLHAA TQVFDFADRH
RGSYSDSLAS SVCPFYCSYS GYHDELLWGA SWLHRASRNA SFMSYVEANG MQLGAGDDDY
SFSWDDKRVG TKVLLAKGFL RNRLHGLELY KAHSDSYICS LVPGTASFQS RYTPGGLLYR
EGSSNMQYVT TATFLMLAYA KYLRSSGATA SCGDGGGGAR GEVSAAELVA VAKRQVDYIL
GKNPAGMSYM VGFGCRYPRR AHHRGASMPS VRAHPGRISC DAGFGYLHSG EPNPNVLVGA
VVGGPDSRDA FADDRGNFAQ SEPATYINAP LVGALAYFAG TTK