ID A0A3A9YV68_9ACTN Unreviewed; 545 AA.
AC A0A3A9YV68;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361153};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361153};
GN ORFNames=D7294_20925 {ECO:0000313|EMBL:RKN39464.1};
OS Streptomyces hoynatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1141874 {ECO:0000313|EMBL:RKN39464.1, ECO:0000313|Proteomes:UP000272474};
RN [1] {ECO:0000313|EMBL:RKN39464.1, ECO:0000313|Proteomes:UP000272474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 29097 {ECO:0000313|EMBL:RKN39464.1,
RC ECO:0000313|Proteomes:UP000272474};
RX PubMed=24243968; DOI=10.1099/ijs.0.055640-0;
RA Veyisoglu A., Sahin N.;
RT "Streptomyces hoynatensis sp. nov., isolated from deep marine sediment.";
RL Int. J. Syst. Evol. Microbiol. 64:819-826(2014).
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:RKN39464.1}.
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DR EMBL; RBAL01000013; RKN39464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9YV68; -.
DR OrthoDB; 9801198at2; -.
DR Proteomes; UP000272474; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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 Reference proteome {ECO:0000313|Proteomes:UP000272474};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..545
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017426714"
FT DOMAIN 348..437
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 435..545
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 545 AA; 57768 MW; 000B95C4780D08EC CRC64;
MKRTRRTLTV LLAGLATLLG LAGPAAARDG DRAEPLATGL HIENGRLLEA NGNDFVMRGV
NHAHTWYQGE TQSFADIKEL GANTVRVVLG SGQRWGPDSP ENVANVIELC KANRMICVLE
VHDTTGYGEQ DGAASLDQAA DYWIGLRDVL VGQEDYVVIN IGNEPWGNTN AAGWTQATID
AVQKLRNAGF EHTLMVDGPN WGQDWQNTMR TTAQQVYDAD PTGNLIFSVH MYAVYESADL
ISAYLHDFVD AGLPIVVGEF SHPADQWGDV NEDAIMATAE ELDLGWLAWS WSGNADPIHD
LTLNFDPAQL TWWGERVFHG PNGIGETAEE ATIFGGGGDP DDTQAPTAPG TPTASEVTAT
SAVLTWPAAT DNVGVTGYDI VRVQGTTETR VGSSATNRVT LTGLTADTTY TLAAYARDAA
GNRSARSATV TVTTSRTPVA ACAVGYRVVN EWNNGFQGEI VIRNTGTAPL TNWTLGFTFS
GGQTITNLWG GTPTQNGGTV TVTPADYTRT IAANGTVTLG FIAGKNGANP APTAFTLNGD
ACATA
//
