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Database: UniProt
Entry: A0A402A6S4_9CHLR
LinkDB: A0A402A6S4_9CHLR
Original site: A0A402A6S4_9CHLR 
ID   A0A402A6S4_9CHLR        Unreviewed;       809 AA.
AC   A0A402A6S4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JUN-2023, entry version 10.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=KTT_47020 {ECO:0000313|EMBL:GCE14843.1};
OS   Tengunoibacter tsumagoiensis.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Tengunoibacter.
OX   NCBI_TaxID=2014871 {ECO:0000313|EMBL:GCE14843.1, ECO:0000313|Proteomes:UP000287352};
RN   [1] {ECO:0000313|Proteomes:UP000287352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uno3 {ECO:0000313|Proteomes:UP000287352};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-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:GCE14843.1}.
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DR   EMBL; BIFR01000002; GCE14843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402A6S4; -.
DR   OrthoDB; 9758662at2; -.
DR   Proteomes; UP000287352; Unassembled WGS sequence.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 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; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS51172; CBM3; 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:UP000287352}.
FT   DOMAIN          502..655
FT                   /note="CBM3"
FT                   /evidence="ECO:0000259|PROSITE:PS51172"
FT   DOMAIN          699..809
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          652..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..697
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        469
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   809 AA;  87539 MW;  67DD344F9B2D99EB CRC64;
     MSLRSLFGTT WHRRVLSSLL ATGLMLSALA FSFAPSYLTH VKAAPAFNYG EALQKSIYFY
     EEQSSGHKPD WNRVPWVGDS ALNDGSDVGL NLTGGWYDAG DHVKFGLPMA YSATMLAWGV
     IANRDAYTSD GQLTNIMNNL HFVNDYFIKA HPAPNVLYGQ VGNGSDDHAF WGPAEVMQMN
     RPAYKIDASC PGSDLAGETA AAMAASSIVF SSTDATYAST LLDHAKQLYS FADNYRGKYD
     SCITAASGYY TSYSGYNDEL VWGAIWLYQA TNDPSYLTKA ENYYANLGTE PQSTTHSYKW
     TIGWDDVSYG TYVLLAQITG QQQYKDDAQR WLDYWTVGVN GQKITYSPGG EAFLDQWGSL
     RYAADTAFVA LIYADYLGAG NALYSRYHDF AVGQINYILG ANPRNCSYMV GFGSCYPQTP
     HHRESHDSWT NNIGNPTYQR HILYGALVGG PSSANDSFTD NRQDYATNEP ADDYNAALTG
     ALARLYKEYG GSPVASMPDK AKDDDEIYSE AAINASGSNF TEIKAEFINK SGWPARITSN
     LSLRYYFTLD AGVTPNMLTL NTNYSECGSN FLSGPTQYAG NIYYVTASCA GTPIYPGGQS
     AFQKQVQFRI TSSGAWDPSN DWSFQGVAPN GSNPVKVTNL PVFDGNTQVW GQLPDGSGLP
     TPTPTPVTTP TPTPVTTPTP TPVTTPTPTP TATPTPTPTP ITGSACSVSY VIQNQWPGGF
     TANMTITNTG SSTINGWTLA FTFPNGQQIT QIWNGALNQQ GSQVAIQNLS YNNVIAPGGT
     VNPGFNGSWT TSNSAPTSFT LNGTTCSMS
//
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