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Database: UniProt
Entry: A0A2U2ZN77_9ACTN
LinkDB: A0A2U2ZN77_9ACTN
Original site: A0A2U2ZN77_9ACTN 
ID   A0A2U2ZN77_9ACTN        Unreviewed;       747 AA.
AC   A0A2U2ZN77;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=DI272_05950 {ECO:0000313|EMBL:PWI13737.1};
OS   Streptomyces sp. Act143.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2200760 {ECO:0000313|EMBL:PWI13737.1, ECO:0000313|Proteomes:UP000245455};
RN   [1] {ECO:0000313|EMBL:PWI13737.1, ECO:0000313|Proteomes:UP000245455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Act143 {ECO:0000313|EMBL:PWI13737.1,
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:PRU10060, 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:PWI13737.1}.
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DR   EMBL; QFRX01000001; PWI13737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2ZN77; -.
DR   OrthoDB; 9808897at2; -.
DR   Proteomes; UP000245455; Unassembled WGS sequence.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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; 2.60.120.260; Galactose-binding domain-like; 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; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_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; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10060};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10060};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10060};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245455};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           30..747
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5015369998"
FT   DOMAIN          33..154
FT                   /note="CBM-cenC"
FT                   /evidence="ECO:0000259|Pfam:PF02018"
FT   DOMAIN          182..265
FT                   /note="Cellulase Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF02927"
FT   DOMAIN          275..737
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        718
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        727
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   747 AA;  80277 MW;  0665F481DCBD85AA CRC64;
     MKRRSTTLLS LTALLGAVLV AAPTSPATAD EVEQLKNGTF DTTTEPWWAT SNVTAGLSGG
     RLCADVPGGT TNRWDAAVGQ NDVTLVKGET YKFAFTADGS PDGHVVRAIV GLQVAPYDTY
     FEVSPQLSVS GNSYSYTFTS PVDATQAQVG FQLGGSADAW KFCMDDVSLL GGVPPEVYEP
     DTGPRVRVNQ VAYLPSGPKN ATLVTDATGK LPWQLKNASG TVVAQGTTVP RGVDASSAQN
     VHSIDFGAYK KAGTGYTLVA DGETSRPFDI GTGAYRQLRL DALKYYYTQR SGIAIRDDLR
     PGYGRAAGHV DVAPNQGDSA VPCQPGVCDY KLDVTGGWYD AGDHGKYVVN GGISTWELLS
     TYERALHART GQPAKLGDNT LAIPESGNKV PDILDETRWE LEFLLKMQVP AGQPLAGMAH
     HKIHDEAWTG LPLLPSDDPQ KRELHPATTE ATLNLAATAA QAARLYKPYD KAFAAKTLAA
     ARTAWTAALA HPDLHADPDD GTGGGAYPDT DATDEFYWAA AELYLTTGEK QFADHVLDSP
     VHTADIFGPL GYDWARTAAA ARLDLATVPS KLPGRDKVRR SVVKGADRYL ATLKSQPYGM
     PYAPTDNLYD WGSNHQILHN GIVIATAYDI TGATKYRDGA LQSVDYLFGR NALNMSYVTG
     YGEVNSHNQH SRWYAHQLDP NLPNPPRGTL AGGPNSSIQD PYAQSKLQGC VGQFCYIDDI
     QSWSTNEHTI NWNSALSRMA SFVADQT
//
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