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Database: UniProt
Entry: A0A0C2FE61_9ACTN
LinkDB: A0A0C2FE61_9ACTN
Original site: A0A0C2FE61_9ACTN 
ID   A0A0C2FE61_9ACTN        Unreviewed;       966 AA.
AC   A0A0C2FE61;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 19.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=LP52_18835 {ECO:0000313|EMBL:KIH97489.1};
OS   Streptomonospora alba.
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH97489.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin,
RT   an unusual lasso Peptide from an understudied halophilic
RT   actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC       {ECO:0000256|RuleBase:RU361166}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E)
CC       family. {ECO:0000256|RuleBase:RU361166}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KIH97489.1}.
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DR   EMBL; JROO01000037; KIH97489.1; -; Genomic_DNA.
DR   RefSeq; WP_040275461.1; NZ_JROO01000037.1.
DR   EnsemblBacteria; KIH97489; KIH97489; LP52_18835.
DR   Proteomes; UP000031675; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR008965; Carb-bd_dom.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like.
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   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361166};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031675};
KW   Glycosidase {ECO:0000256|RuleBase:RU361166};
KW   Hydrolase {ECO:0000256|RuleBase:RU361166,
KW   ECO:0000313|EMBL:KIH97489.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031675};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL        1     34       {ECO:0000256|RuleBase:RU361166}.
FT   CHAIN        35    966       Endoglucanase. {ECO:0000256|RuleBase:
FT                                RU361166}.
FT                                /FTId=PRO_5005110920.
FT   DOMAIN      767    858       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   DOMAIN      859    966       CBM2. {ECO:0000259|PROSITE:PS51173}.
SQ   SEQUENCE   966 AA;  101631 MW;  4A555F49584D72EF CRC64;
     MSPSSSRSRF AAGAVTAASA IALSMLAGAP GAHAAELVTN GGFDNGTTGW WNTENAPAEV
     ADGRLCADVE GGTANAWDAI VGQDGIALTS GESYEFTFTA SASEGTTVRA LIQEPTEPYT
     AFLTANPALT SETQTFSHTF TADATLDDAQ LVFQLGGEAE AWTFCLDDVS LQDGAEPPVY
     EPDTGPPVKV NQVGYLPDGP KNATLVTDAT SAQPWTLRDA DGAAVAEGQT SPQGTEQSSG
     QNVHSIDFSD YTEKGSGYTL AVGDDVSHPF DISGSAYKDL RTDSLSLYYP QRSGIEIDDS
     LMPGYGRAAG HVGVEPNQGD LSVPCAPDSG CDYELDVSGG WYDAGDHGKY VVNGGISASQ
     VMSVWERTTY ADSASPDRLG DGTLPVPEQG NDVPDVLDEA RWEMDFLMKM QVPEGEELAG
     MAHHKMHDEE WTGLPLMPAD DPQPRYLQPP STAATLNLAA TGAQCARVFE SYDSEFADRC
     LETAEKAWQA AQENPDVLAD PENGVGGGAY SDDDVSDEFY WAAAELFITT GEQSYEDAVL
     DHELHTEDVF TAGGLAWGAV APLGRMNLAL VPNKLDDRDR VVDSVVAGAD EYLDTLRNHA
     FGLPYAPPDN VFVWGSNSQV LNNMVVMTAA YDLTGDGAYR DGVLEGMDYI LGRNALGQSY
     VTGYGEQFSK NQHSRWYANQ LDADLPNPPE GTVSGGPNSQ TSTWDPVAQD KLEGCAPQFC
     YIDDIESWAT NELTVNWNAP LAIVSSFIAD QTGEGDPPAE DETAPTAPGK PQVSGVTSSQ
     AELTWEASTD EGGSGVEGYD VYAGTGDGAQ KVGSASGPSF TLTGLESETE YTVHVVARDG
     AGNRSEPGPN AAFTTEAGGT GGEAACEVDY STNDWNGGFT ASVSVVNTGD TPIRDWELGF
     EFGAGQEITH GWNAEWSQDG SAVTASGLSW NSDLAPGSSV SAGFNGTAQD GNPAPEEFTV
     NGQTCA
//
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