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Database: UniProt
Entry: A0A3N2G1Z1_9CELL
LinkDB: A0A3N2G1Z1_9CELL
Original site: A0A3N2G1Z1_9CELL 
ID   A0A3N2G1Z1_9CELL        Unreviewed;       956 AA.
AC   A0A3N2G1Z1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN   ORFNames=EDF34_0245 {ECO:0000313|EMBL:ROS30606.1};
OS   Cellulomonas sp. PhB150.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=2485188 {ECO:0000313|EMBL:ROS30606.1, ECO:0000313|Proteomes:UP000273256};
RN   [1] {ECO:0000313|EMBL:ROS30606.1, ECO:0000313|Proteomes:UP000273256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PhB150 {ECO:0000313|EMBL:ROS30606.1,
RC   ECO:0000313|Proteomes:UP000273256};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC       {ECO:0000256|RuleBase:RU361186}.
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:ROS30606.1}.
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DR   EMBL; RKHX01000001; ROS30606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2G1Z1; -.
DR   Proteomes; UP000273256; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 3.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   InterPro; IPR016288; Beta_cellobiohydrolase.
DR   InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR34876; -; 1.
DR   PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00060; FN3; 4.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361186};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361186};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361186};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361186};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361186};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273256};
KW   Signal {ECO:0000256|RuleBase:RU361186}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|RuleBase:RU361186"
FT   CHAIN           38..956
FT                   /note="Glucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361186"
FT                   /id="PRO_5017849968"
FT   DOMAIN          478..563
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          573..658
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          668..753
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          763..848
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          847..956
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          560..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   956 AA;  96969 MW;  7E47B4670069545E CRC64;
     MSTRKRAMGR RARAAATAAT AMALVAVPLC FTSSASAAEP HVDNPYAGAT QYVNPTWAAS
     VESAATRVDA NLAAKMHTVA KQPTAVWMDR ISAITGNADG SGLKFHLDNA LAQKGSGPIV
     VNLVIYDLPG RDCYALASNG ELPATDAGLA RYKTEYIDAI AALLSDPKYA GLRISATIEP
     DSLPNLVTNI SEPLCQQAAP YYKAGVKYAL DKLHAISNVY TYIDIGHSGW LGWDSNAGPA
     ATLFADVAKS TTAGFASIDG FVSDVANTTP LNEPFLPDST ISVGGTPIRS TSFYEWNFDF
     DEIDFTAHMH KLLVAAGFPS SLGMLVDTSR NGWGGSARPT AVSTSTVANT YVNESRVDKR
     VHRGAWCNPL GAGIGELPQA TPAGYSASFL DAFVWIKPPG ESDGASTDIP NDQGKRFDRM
     CDPTFVSPKL SNQLTGATPN APLAGQWFED QFKTLVANAY PVISGGTTPP ADTTAPTAPT
     AVTAGTTTTT TVPLSWTAST DNVAVTGYNV YQGSTLVGTS TSTSYTVTGL SPATAYSFTV
     KAKDAAGNLS AASSAVSATT KTATTTDTTA PSAPTGLTAG TTTTSTVPLS WTASTDNVAV
     TGYDVYNGAT LVASTTGTSY TVTGLAAGTT YSFTVKAKDA AGNVSSASAA ASATTKTVTV
     PDTTAPSAPT GLTAGTTTTS TVPLSWTAST DNVAVTGYDV YQGSTLVGST TATSYTVTGL
     SSATAYSFTV KAKDAAGNVS SASAAASATT KSTTVPDTTA PSAPTGLTAG TTTSSSVPLS
     WTASTDNVAV TGYDVYQGAT LVGSTTTTSY TVTGLNSATA YSFTVKAKDG AGNVSAASAA
     AAATTKPAGV TSSCSVKYTA SSWNTGFTAS IKVTNTGQTP INGWSLGFAF ANGQTITQGW
     SANWSQSGSA VTGSGLSWNA TLAPGASTDI GFNGSHSGTN TSPTAFTVNG VTCTVA
//
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