ID B2WS97_9BRAS Unreviewed; 479 AA.
AC B2WS97;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=6J23.18 {ECO:0000313|EMBL:ACC91269.1}, CARUB_v10007690mg
GN {ECO:0000313|EMBL:EOA19034.1};
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:ACC91269.1};
RN [1] {ECO:0000313|EMBL:ACC91269.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18296705; DOI=10.1093/molbev/msn029;
RA Warthmann N., Das S., Lanz C., Weigel D.;
RT "Comparative analysis of the MIR319a microRNA locus in Arabidopsis and
RT related Brassicaceae.";
RL Mol. Biol. Evol. 25:892-902(2008).
RN [2] {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).
RN [3] {ECO:0000313|EMBL:EOA19034.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., Prochnik S., Nordborg M., Weigel D., Rokhsar D., Wright S.;
RT "Genome sequencing of Capsella rubella.";
RL Nat. Genet. 0:0-0(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 -!- 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; EF197847; ACC91269.1; -; Genomic_DNA.
DR EMBL; KB870811; EOA19034.1; -; Genomic_DNA.
DR RefSeq; XP_006286136.1; XM_006286074.1.
DR AlphaFoldDB; B2WS97; -.
DR STRING; 81985.B2WS97; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR GeneID; 17878738; -.
DR KEGG; crb:17878738; -.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR OrthoDB; 1347382at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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 PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF22; ENDOGLUCANASE 18-RELATED; 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 Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
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:UP000029121};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 22..479
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5015019391"
FT DOMAIN 24..469
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 431..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 479 AA; 52615 MW; 47C7FBB1C64C808F CRC64;
MGKLLVLMLV GMFLAFESLE ALNYGDALNK SILFFEGQRS GKLPTNQRVK WRGDSALSDG
ASANVNLVGG YYDAGDNVKF VWPMSFTTTL LSWAAIEYQN EISSVNQLGY LRSTIKWATN
FILRAHTSPT MLYTQVGDGN KDHSCWERPE DMDTPRTLFS ITSSSPGSEA AGEAAAALAA
ASIVFKSVDS TYSSTLLNHA KTLFEFADKY RGSYQASCPF YCSYSGYQDE LLWAAAWLYK
ATGEKSYINY VVSNKDWSRA VNEFSWDNKF AGAQALLASE FYKGNNDLAK FKTDVESFVC
ALMPGSSSQQ IKPTPGGILY IRGSSNLQYV TTATTVLFHY SKTLTKAKIG SIQCGSTQFT
ASQIRNFAKS QVDYILGNNP MKMSYMVGFG KNYPTQPHHR GSSLPSIKSK QEKIDCNGGF
SYYNSDTPNP NVHTGAIVGG PNSSDQYSDK RSDYAHAEPT TYINAAFIGP VAALISSFR
//
