ID A0A101SWN0_9ACTN Unreviewed; 551 AA.
AC A0A101SWN0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=AQJ64_22600 {ECO:0000313|EMBL:KUN81441.1};
OS Streptomyces griseoruber.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN81441.1, ECO:0000313|Proteomes:UP000052982};
RN [1] {ECO:0000313|EMBL:KUN81441.1, ECO:0000313|Proteomes:UP000052982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN81441.1,
RC ECO:0000313|Proteomes:UP000052982};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT for the species Streptomyces griseoruber.";
RL Submitted (OCT-2015) 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:RU361153};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|RuleBase:RU361153}.
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:KUN81441.1}.
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DR EMBL; LMWW01000036; KUN81441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101SWN0; -.
DR STRING; 1943.AQJ64_22600; -.
DR Proteomes; UP000052982; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42754:SF1; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42754; ENDOGLUCANASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361153};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361153};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361153}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 354..443
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 441..551
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 551 AA; 56781 MW; D2C6E4DED35B028A CRC64;
MPSSPPRKRS VTTLLTGLAV LLGLVALGVL APAPAQARPD GLAATGLHIA DGRLVEANGN
DFVMRGVNHA HTWYPGRLQS LADIKALGAN TVRVVLADGH RWSANSASDV ANVVAQCKAN
RLICVLEVHD TTGYGEDSAA GTLDQAADYW IGLKDVLAGQ ENYVVINIGN EPWGNTDPAG
WTAPTIAAVK KLRDAGFQHT IMVDAPNWGQ DWQGVMRANA RSVYAADTTG NLIFSIHMYS
VFDTAAEITD YLNAFVNAKL PLLIGEFGGP ADQWGDPDED TMMATAQQLN LGYLAWSWSG
NTDPILDLAT AFDPTRLSSW GQRVFNGVNG IAQTAKEATV YGGGTPADTQ APTTPGTPTA
SAVTATSATL TWTAATDNIG VTGYDVVRVA GGTESAVAAS TTNGVTVTGL SASTAYTFAV
YARDAAGNRS ARSGTVAVTT SSAPATPCSV RYRVVGEWPG GFQGEIVLGN PGTAAINGWK
LAFAFADGQT VTTMWGGTPT QSGAAVTVAP ASYTGTIPVG GSVTVGFIGA KGTTNTAPTA
FTLNGSACTT T
//
