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Database: UniProt
Entry: A0A0B0MRT1_GOSAR
LinkDB: A0A0B0MRT1_GOSAR
Original site: A0A0B0MRT1_GOSAR 
ID   A0A0B0MRT1_GOSAR        Unreviewed;       586 AA.
AC   A0A0B0MRT1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=F383_00334 {ECO:0000313|EMBL:KHG02199.1};
OS   Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG02199.1, ECO:0000313|Proteomes:UP000032142};
RN   [1] {ECO:0000313|Proteomes:UP000032142}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA   Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA   Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA   Wilkins T.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KHG02199.1}.
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DR   EMBL; JRRC01247434; KHG02199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B0MRT1; -.
DR   Proteomes; UP000032142; 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: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   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:UP000032142};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          494..576
FT                   /note="Carbohydrate binding"
FT                   /evidence="ECO:0000259|SMART:SM01063"
FT   REGION          460..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        377
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ   SEQUENCE   586 AA;  65020 MW;  85C4D3E2F221B46C CRC64;
     MFLEAQRSGK LPFDQRVKWR GDSGLKDGAL QGVDLVGGYY DAGDHVKFGL PMAFSVTMLA
     WGTIEYRKEI TNLNQMGHTL WAIRWGTDYF IKAHTQPNVL WGQVGDGDSD HYCWERAEDM
     TTPRTAYKLD EAHPGSDLAG ETAAALAAAA IAFKPYNSSY SELLLVHAKQ LFSFADKFRG
     LYDDSIQCAK QFYTSSGYSD ELLWVATWLF RATGDEHYLK YVVDNAVYMG GTGWAVKEFS
     WDNKYAGVQI LLSKVLMEQK GGAYISTLKQ YQAKADYFAC ACLQKNDGYN VHLTPGGLMY
     VHEWNNLQYA SAASFLLAVY SDYLSAANAK LTCPDGQIQP HEVLNFAKSQ ADYILGKNPK
     SMSYLVGYGP KYPTHVHHRG ASIASISVLP SMVSCVQGFE AWYRSPEADP NVIYGALVGG
     PDQNDGFNDD RSSYEQTEPT LAGSAPLVGL FAKLESLSGN KGPYHKRPTT EQPSQNYHHQ
     TSVPSTKSPG VPPVRFLHSI TNTWNVGKTT YYRHKVAIKN TSEKPITDLK LVLEDLSGNL
     WGLSSTPVKN TYELPPWLKV LNPGSDCSFV YIQEGPQAKV SVLSYQ
//
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