Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P37699 (GUNC_RUMCH)

Entry version 130 (07 Oct 2020)
Sequence version 2 (26 May 2009)
Previous versions | rss
Add a publicationFeedback
Protein

Endoglucanase C

Gene

celCCC

Organism
Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) (Clostridium cellulolyticum)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. EC:3.2.1.4

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei99Proton donorBy similarity1
Active sitei155NucleophilePROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		CCEL394503:G1GUL-746-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00696

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GH8, Glycoside Hydrolase Family 8

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Endoglucanase C (EC:3.2.1.4)
Alternative name(s):
Cellulase C
EGCCC
Endo-1,4-beta-glucanase C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:celCCC
Ordered Locus Names:Ccel_0730
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRuminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) (Clostridium cellulolyticum)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri394503 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Firmicutes › Clostridia › Clostridiales › Hungateiclostridiaceae › Ruminiclostridium ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001349 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 321 PublicationAdd BLAST32
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000793633 – 460Endoglucanase CAdd BLAST428

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

There are two forms of the cellulase. The shorter form lacks probably the C-terminal reiterated domains.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		394503.Ccel_0730

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P37699

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini400 – 460DockerinPROSITE-ProRule annotationAdd BLAST61

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 8 (cellulase D) family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG3405, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_036185_0_0_9

Identification of Orthologs from Complete Genome Data

More...OMAi		EAHGYGM

Database of Orthologous Groups

More...OrthoDBi		636673at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1330.10, 1 hit
1.50.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008928, 6-hairpin_glycosidase_sf
IPR012341, 6hp_glycosidase-like_sf
IPR002105, Dockerin_1_rpt
IPR016134, Dockerin_dom
IPR036439, Dockerin_dom_sf
IPR018247, EF_Hand_1_Ca_BS
IPR002037, Glyco_hydro_8
IPR019834, Glyco_hydro_8_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00404, Dockerin_1, 1 hit
PF01270, Glyco_hydro_8, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00735, GLHYDRLASE8

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48208, SSF48208, 1 hit
SSF63446, SSF63446, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00448, CLOS_CELLULOSOME_RPT, 1 hit
PS51766, DOCKERIN, 1 hit
PS00018, EF_HAND_1, 2 hits
PS00812, GLYCOSYL_HYDROL_F8, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P37699-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIKGSSLKRF KSLVMAAIFS VSIISTAIAS SAADQIPFPY DAKYPNGAYS 
        60         70         80         90        100
CLADSQSIGN NLVRSEWEQW KSAHITSNGA RGYKRVQRDA STNYDTVSEG 
       110        120        130        140        150
LGYGLLLSVY FGEQQLFDDL YRYVKVFLNS NGLMSWRIDS SGNIMGKDSI 
       160        170        180        190        200
GAATDADEDI AVSLVFAHKK WGTSGGFNYQ TEAKNYINNI YNKMVEPGTY 
       210        220        230        240        250
VIKAGDTWGG SNVTNPSYFA PAWYRIFADF TGNSGWINVA NKCYEIADKA 
       260        270        280        290        300
RNSNTGLVPD WCTANGTPAS GQGFDFYYDA IRYQWRAAID YSWYGTAKAK 
       310        320        330        340        350
THCDAISNFF KNIGYANIKD GYTISGSQIS SNHTATFVSC AAAAAMTGTD 
       360        370        380        390        400
TTYAKNIYNE CVKVKDSGNY TYFGNTLRMM VLLYTTGNFP NLYTYNSQPK 
       410        420        430        440        450
PDLKGDVNND GAIDALDIAA LKKAILTQTT SNISLTNADM NNDGNIDAID 
       460
FAQLKVKLLN
Length:460
Mass (Da):50,483
Last modified:May 26, 2009 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2F31E1F6CB41504F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti91S → T in AAA73867 (PubMed:1398087).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M87018 Genomic DNA Translation: AAA73867.1
CP001348 Genomic DNA Translation: ACL75109.1

Protein sequence database of the Protein Information Resource

More...PIRi		JC1299

NCBI Reference Sequences

More...RefSeqi		WP_015924276.1, NC_011898.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		ACL75109; ACL75109; Ccel_0730

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cce:Ccel_0730

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87018 Genomic DNA Translation: AAA73867.1
CP001348 Genomic DNA Translation: ACL75109.1
PIRiJC1299
RefSeqiWP_015924276.1, NC_011898.1

3D structure databases

SMRiP37699
ModBaseiSearch...

Protein-protein interaction databases

STRINGi394503.Ccel_0730

Protein family/group databases

CAZyiGH8, Glycoside Hydrolase Family 8

Genome annotation databases

EnsemblBacteriaiACL75109; ACL75109; Ccel_0730
KEGGicce:Ccel_0730

Phylogenomic databases

eggNOGiCOG3405, Bacteria
HOGENOMiCLU_036185_0_0_9
OMAiEAHGYGM
OrthoDBi636673at2

Enzyme and pathway databases

UniPathwayiUPA00696
BioCyciCCEL394503:G1GUL-746-MONOMER

Family and domain databases

Gene3Di1.10.1330.10, 1 hit
1.50.10.10, 1 hit
InterProiView protein in InterPro
IPR008928, 6-hairpin_glycosidase_sf
IPR012341, 6hp_glycosidase-like_sf
IPR002105, Dockerin_1_rpt
IPR016134, Dockerin_dom
IPR036439, Dockerin_dom_sf
IPR018247, EF_Hand_1_Ca_BS
IPR002037, Glyco_hydro_8
IPR019834, Glyco_hydro_8_CS
PfamiView protein in Pfam
PF00404, Dockerin_1, 1 hit
PF01270, Glyco_hydro_8, 1 hit
PRINTSiPR00735, GLHYDRLASE8
SUPFAMiSSF48208, SSF48208, 1 hit
SSF63446, SSF63446, 1 hit
PROSITEiView protein in PROSITE
PS00448, CLOS_CELLULOSOME_RPT, 1 hit
PS51766, DOCKERIN, 1 hit
PS00018, EF_HAND_1, 2 hits
PS00812, GLYCOSYL_HYDROL_F8, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGUNC_RUMCH
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P37699
Secondary accession number(s): B8I7V2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 26, 2009
Last modified: October 7, 2020
This is version 130 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again