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Protein

Endoglucanase C

Gene

celC

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei502Proton donorBy similarity1
Active sitei652NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase C (EC:3.2.1.4)
Alternative name(s):
Cellodextrinase C
Cellulase C
Endo-1,4-beta-glucanase C
Short name:
EGC
Gene namesi
Name:celC
Synonyms:cel5A
Ordered Locus Names:CJA_1462
OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri498211 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
Proteomesi
  • UP000001036 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 371 PublicationAdd BLAST37
ChainiPRO_000000786538 – 747Endoglucanase CAdd BLAST710

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi39 ↔ 133By similarity
Disulfide bondi183 ↔ 214By similarity
Disulfide bondi193 ↔ 208By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_1462.

Structurei

3D structure databases

ProteinModelPortaliP27033.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 136CBM2PROSITE-ProRule annotationAdd BLAST99
Domaini182 – 211CBM10PROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni280 – 747CatalyticAdd BLAST468

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi137 – 179Ser-rich (linker)Add BLAST43
Compositional biasi227 – 279Ser-rich (linker)Add BLAST53

Sequence similaritiesi

Contains 1 CBM10 (carbohydrate binding type-10) domain.PROSITE-ProRule annotationCurated
Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107QUA. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000066200.
KOiK01179.
OMAiRTIQQTM.
OrthoDBiPOG091H1DNW.

Family and domain databases

Gene3Di2.30.32.30. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM01064. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF57615. SSF57615. 1 hit.
PROSITEiPS51763. CBM10. 1 hit.
PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27033-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGHVTSPSKR YPASFKRAGS ILGVSIALAA FSNVAAAGCE YVVTNSWGSG
60 70 80 90 100
FTAAIRITNS TSSVINGWNV SWQYNSNRVT NLWNANLSGS NPYSASNLSW
110 120 130 140 150
NGTIQPGQTV EFGFQGVTNS GTVESPTVNG AACTGGTSSS VSSSSVVSSS
160 170 180 190 200
SSSRSSVSSS SVVSSSSSVV SSSSSSVVSG GQCNWYGTLY PLCVSTTSGW
210 220 230 240 250
GYENNRSCIS PSTCSAQPAP YGIVGGSSSP SSISSSSVRS SSSSSVVPPS
260 270 280 290 300
SSSSSSVPSS SSSSVSSSSV VSSSSSSVSV PGTGVFRVNT QGNLTKDGQL
310 320 330 340 350
LPARCGNWFG LEGRHEPSND ADNPSGAPME LYAGNMWWVN NSQGSGRTIQ
360 370 380 390 400
QTMTELKQQG ITMLRLPIAP QTLDANDPQG RSPNLKNHQS IRQSNARQAL
410 420 430 440 450
EDFIKLADQN DIQIFIDIHS CSNYVGWRAG RLDARPPYVD ANRVGYDFTR
460 470 480 490 500
EEYSCSATNN PSSVTRIHAY DKQKWLANLR EIAGLSAKLG VSNLIGIDVF
510 520 530 540 550
NEPYDYTWAE WKGMVEEAYQ AINEVNPNML IIVEGISANA NTQDGTPDTS
560 570 580 590 600
VPVPHGSTDL NPNWGENLYE AGANPPNIPK DRLLFSPHTY GPSVFVQRQF
610 620 630 640 650
MDPAQTECAG LEGDEAAQAR CRIVINPTVL EQGWEEHFGY LRELGYGILI
660 670 680 690 700
GEFGGNMDWP GAKSSQADRN AWSHITTNVD QQWQQAAASY FKRKGINACY
710 720 730 740
WSMNPESADT MGWYLTPWDP VTANDMWGQW TGFDPRKTQL LHNMWGL
Length:747
Mass (Da):80,098
Last modified:April 20, 2010 - v2
Checksum:i2A1D90E2612D361A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti85A → P in CAA43597 (PubMed:1953673).Curated1
Sequence conflicti181G → GG in CAA43597 (PubMed:1953673).Curated1
Sequence conflicti262S → C in CAA43597 (PubMed:1953673).Curated1
Sequence conflicti291Q → K in CAA43597 (PubMed:1953673).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61299 Genomic DNA. Translation: CAA43597.1.
CP000934 Genomic DNA. Translation: ACE82870.1.
PIRiS19652.

Genome annotation databases

EnsemblBacteriaiACE82870; ACE82870; CJA_1462.
KEGGicja:CJA_1462.
PATRICi21326306. VBICelJap122165_1442.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61299 Genomic DNA. Translation: CAA43597.1.
CP000934 Genomic DNA. Translation: ACE82870.1.
PIRiS19652.

3D structure databases

ProteinModelPortaliP27033.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi498211.CJA_1462.

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACE82870; ACE82870; CJA_1462.
KEGGicja:CJA_1462.
PATRICi21326306. VBICelJap122165_1442.

Phylogenomic databases

eggNOGiENOG4107QUA. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000066200.
KOiK01179.
OMAiRTIQQTM.
OrthoDBiPOG091H1DNW.

Family and domain databases

Gene3Di2.30.32.30. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM01064. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF57615. SSF57615. 1 hit.
PROSITEiPS51763. CBM10. 1 hit.
PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUNC_CELJU
AccessioniPrimary (citable) accession number: P27033
Secondary accession number(s): B3PDK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: April 20, 2010
Last modified: November 2, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.