UniProt: A0A0J8BTE0

Database: UniProt
Entry: A0A0J8BTE0_STRVR

LinkDB:  A0A0J8BTE0_STRVR 
Original site:  A0A0J8BTE0_STRVR

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (2)   
   SMART (2)   
All databases (21)   

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ID   A0A0J8BTE0_STRVR        Unreviewed;       543 AA.
AC   A0A0J8BTE0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN   ORFNames=ACM01_37320 {ECO:0000313|EMBL:KMS68850.1};
OS   Streptomyces viridochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS68850.1, ECO:0000313|Proteomes:UP000037432};
RN   [1] {ECO:0000313|EMBL:KMS68850.1, ECO:0000313|Proteomes:UP000037432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS68850.1,
RC   ECO:0000313|Proteomes:UP000037432};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUN-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:KMS68850.1}.
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DR   EMBL; LFNT01000069; KMS68850.1; -; Genomic_DNA.
DR   RefSeq; WP_048585873.1; NZ_LFNT01000069.1.
DR   AlphaFoldDB; A0A0J8BTE0; -.
DR   PATRIC; fig|1938.3.peg.8186; -.
DR   OrthoDB; 9801198at2; -.
DR   Proteomes; UP000037432; 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};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..543
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005295076"
FT   DOMAIN          345..434
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          433..543
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          334..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  56583 MW;  F59ABD391D796EDF CRC64;
     MRSRTRTTPR VAAVVAALLG LLVPLLSFAT PAQAAATGLH IQNGRLLEAS GNDFVMRGVN
     HAHTWYPGET QSLADVKALG ANTVRVVLSD GHRWTRNSAA DVAAVITQCK ANRLICVLEV
     HDTTGYGEEA AAGTLDHAAD YWIGLKDVLT GQENYVIINI GNEPWGNTNP AGWTEPTTAA
     VKKLRNAGFA HTIMVDAPNW GQDWQGVMRA NAQAVYDADP TGNLIFSIHM YSVYDTAQEI
     TDYLNAFVNA GLPLLIGEFG GPPDQYGDPD EDTMMAVAQQ LRLGYLAWSW SGNTDPILDL
     AIGFDPARLS SWGERVFHGA NGIAATSEEA DIYASSGGDT TPPTAPGTPT ASAVTSSSVT
     LKWAAATDAN GVTGYDVVRV GSGTETAATT TTGTSATVTG LAPETSYTFA VYARDAAGNR
     SPRSGTVAVT TSSGGSSATC GVAYRVTNEW PGGFQGEVVI RNTGSSAING WTLRWTFPDS
     QRVSNLWGGT ATQSGAQVSV ASASYTATIA PAGSVTLGFT ATKGGTNPNP SAFTLNDSAC
     SPV
//

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