GenomeNet

Database: UniProt
Entry: A0A1H6EM78_9ACTN
LinkDB: A0A1H6EM78_9ACTN
Original site: A0A1H6EM78_9ACTN 
ID   A0A1H6EM78_9ACTN        Unreviewed;       837 AA.
AC   A0A1H6EM78;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=SAMN05444920_111234 {ECO:0000313|EMBL:SEG98201.1};
OS   Nonomuraea solani.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEG98201.1, ECO:0000313|Proteomes:UP000236732};
RN   [1] {ECO:0000313|EMBL:SEG98201.1, ECO:0000313|Proteomes:UP000236732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEG98201.1,
RC   ECO:0000313|Proteomes:UP000236732};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNVT01000011; SEG98201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6EM78; -.
DR   OrthoDB; 9808897at2; -.
DR   Proteomes; UP000236732; 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; 2.60.120.260; 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; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_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; 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; PF02018; CBM_4_9; 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; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS51173; CBM2; 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:UP000236732};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           26..837
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5009029651"
FT   DOMAIN          723..837
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   ACT_SITE        658
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        706
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        715
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   837 AA;  90923 MW;  FF176D542F709EFC CRC64;
     MTRCRAALLA LFTMVALFPA TAAQAADEGP EQIVNGTFDT GTAPWWGTAN VTLAVTDGRL
     CADIPGGTTN PWDVIIGQDN IPLVEGDTYA YRFFAAATPA KVGRALIQLP VDPWTQYLSA
     APEMSVSGNS YSYTFTAPVS LPNAQVAFQL GGSAEPWRFC MDDVSLKGGA EPEVYEPDTG
     PRVRVNMVGY LPAGPKKATV VTTATEAVDW ELKNAAKETV ASGRTTPRGV DASSGQNVHT
     LDFGSYRKAG KEYTLTADGE TSRPFDIAAD LYDQLPVDAL KFYYTQRSGI EILDGLRPGY
     GRPAGHVGVA PNQGDVSVPC QPGVCDYSLN VKGGWYDAGD HGKYVVNGGI SVFQLMATYE
     RDKATFKDRQ LNIPESGNGT PDILDEARWE QEFLLSMQVP DGKPYAGMAH HKIHDQNWTG
     LPLLPHLDPQ LRELHPTSTA ATLNLAATAA QAARLYAPYD GKFALRNLEA ARKAWTAAKA
     NPERYADPTD GTGGGAYNDP DVSDEFYWAA AELYITTGEK EFRDFVLTSP HHTGDIWRER
     GFDWGNTAQL GRLDLATVPN ALPDRARVRQ SVIEGAEKYL GIQRAHPYGL SYNPPDFDWG
     SNNLVLNNLV VMATAYDLTG QEKYRAGVRE GMDYILGRNA LNQSYVTGYG EVASKNQHSR
     WYARQLDPAL PNPPRGTLAG GPNSGLQDPL AQRLLRGCKP QFCYIDHIES WATNELTINW
     NSPLAWVSAF LADRGERSDC RVRYSAHGAG SFAAQVAIEN TGRHTVDAWA LRWSFLGGQR
     VRQGWGAALS QAGPVVTAKG QGRIKPGRTV TFGFTATNPG GPNPAPEVFW LNGARCK
//
DBGET integrated database retrieval system