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Database: UniProt
Entry: A0A2U2ZLE6_9ACTN
LinkDB: A0A2U2ZLE6_9ACTN
Original site: A0A2U2ZLE6_9ACTN 
ID   A0A2U2ZLE6_9ACTN        Unreviewed;       715 AA.
AC   A0A2U2ZLE6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=DI272_02460 {ECO:0000313|EMBL:PWI13121.1};
OS   Streptomyces sp. Act143.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI13121.1, ECO:0000313|Proteomes:UP000245455};
RN   [1] {ECO:0000313|EMBL:PWI13121.1, ECO:0000313|Proteomes:UP000245455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Act143 {ECO:0000313|EMBL:PWI13121.1,
RC   ECO:0000313|Proteomes:UP000245455};
RA   Valanrebinro G., Kumari S., Rameshkumar N.;
RT   "Actinomycin D producing novel Streptomyces isolated from the rhizosphere
RT   of saline tolerant kaipad rice and its draft genome analysis.";
RL   Submitted (MAY-2018) 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|RuleBase:RU361166};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU10059, 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:PWI13121.1}.
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DR   EMBL; QFRX01000001; PWI13121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2ZLE6; -.
DR   OrthoDB; 9808897at2; -.
DR   Proteomes; UP000245455; 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; cd02850; E_set_Cellulase_N; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_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; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361166};
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:UP000245455};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           36..715
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5015372825"
FT   DOMAIN          607..715
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          530..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        525
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        573
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        582
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   715 AA;  74567 MW;  121153A3493EEED3 CRC64;
     MPAFTLLRRP SRPLTAALLT SSLLLGGFLA VPAAAAGTTA VRVNQVGYLP DGPKRATVVT
     TAAQSLTWQL SNASGTVVAS GSTVPRGADT ASGQSVQVAD FSSYQGTGSG YVLRVDGSSS
     DPFDIRANLY DGLRSDAMAF FYHQRSGIAI DASLVGSAYA RPAGHLGVSP NKGDTSVPCQ
     SGVCDYTQDV RGGWYDAGDQ GKYVVNGGIS TWLVVNSFER AERVGKEAAL GDSTLSVPER
     GNGVPDVLDE ARWELDFLMR MQVPAGKPYA GMAFHKIHDA AWTGIPTRPE QDAQPRELHR
     PSTAATLNLA ATAAQCARVF RPYDAAYADR CLAAARRAWT AAQANPAMYA PDSDSTGGGA
     YGDSQVSDEF YWAAAELYAT TGESAYRDAV TSSSWHTAAN AFTSYGFGWA DTAALGRLTL
     ATVPNGLPAS DLARVRSSVV SAADGHLSTM AGQGYAVPIP SDGYFWGSNS EAADNAVVMA
     VAGELTGDAR YRAGVLEALD YLLGRNALGQ SYVTGYGEKS SRNQHHRFWA HQSDSSLPNP
     PAGSLAGGPN SGLQDPVAQE KLAGCAPAAC YIDDIGSYST NEVAVNWNAP LAWLAAYAAE
     RTTDDGGQQP TGSCAVTYKV DNAWSNGFTA TVTVKNTGST AVDGWQLTWS YPGGQRVTSA
     WNASVTQSGA DVTARNVDWN RTVAPGATVS FGVQGSLSGS NPSPTAFALN GSACD
//
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