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UniProtKB - P07984 (GUNA_CELFI)

Entry version 116 (25 May 2022)
Sequence version 1 (01 Aug 1988)
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Protein

Endoglucanase A

Gene

cenA

Organism
Cellulomonas fimi
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

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 sitei247PROSITE-ProRule annotation1
Active sitei283Proton donorPROSITE-ProRule annotation1
Active sitei423NucleophilePROSITE-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

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P07984

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		CBM2, Carbohydrate-Binding Module Family 2
GH6, Glycoside Hydrolase Family 6

<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 A (EC:3.2.1.4)
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A
<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:cenA
<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>OrganismiCellulomonas fimi
<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 identifieri1708 [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 › Actinobacteria › Micrococcales › Cellulomonadaceae › Cellulomonas

<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 – 31Tat-type signalPROSITE-ProRule annotationAdd BLAST31
<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_000000790332 – 449Endoglucanase AAdd BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi35 ↔ 1341 Publication
Disulfide bondi248 ↔ 2911 Publication
Disulfide bondi390 ↔ 4261 Publication

<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

The linker region (also termed 'hinge') may be a potential site for proteolysis.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P07984

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P07984

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

More...SMRi		P07984

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>Domaini32 – 137CBM2PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni127 – 170DisorderedSequence analysisAdd BLAST44
Regioni139 – 168Linker ('hinge') (Pro-Thr box)Add BLAST30
Regioni438 – 449CatalyticAdd BLAST12

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi127 – 141Polar residuesSequence analysisAdd BLAST15
Compositional biasi142 – 167Pro residuesSequence analysisAdd BLAST26

<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 6 (cellulase B) family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.290, 1 hit
3.20.20.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR016288, Beta_cellobiohydrolase
IPR036434, Beta_cellobiohydrolase_sf
IPR001919, CBD2
IPR008965, CBM2/CBM3_carb-bd_dom_sf
IPR012291, CBM2_carb-bd_dom_sf
IPR018366, CBM2_CS
IPR001524, Glyco_hydro_6_CS
IPR006311, TAT_signal

The PANTHER Classification System

More...PANTHERi		PTHR34876, PTHR34876, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00553, CBM_2, 1 hit
PF01341, Glyco_hydro_6, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001100, Beta_cellobiohydrolase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00733, GLHYDRLASE6

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00637, CBD_II, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49384, SSF49384, 1 hit
SSF51989, SSF51989, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51173, CBM2, 1 hit
PS00561, CBM2_A, 1 hit
PS00655, GLYCOSYL_HYDROL_F6_1, 1 hit
PS00656, GLYCOSYL_HYDROL_F6_2, 1 hit
PS51318, TAT, 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.

P07984-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTRRTAAAL LAAAAVAVGG LTALTTTAAQ AAPGCRVDYA VTNQWPGGFG 
        60         70         80         90        100
ANVTITNLGD PVSSWKLDWT YTAGQRIQQL WNGTASTNGG QVSVTSLPWN 
       110        120        130        140        150
GSIPTGGTAS FGFNGSWAGS NPTPASFSLN GTTCTGTVPT TSPTPTPTPT 
       160        170        180        190        200
TPTPTPTPTP TPTPTVTPQP TSGFYVDPTT QGYRAWQAAS GTDKALLEKI 
       210        220        230        240        250
ALTPQAYWVG NWADASHAQA EVADYTGRAV AAGKTPMLVV YAIPGRDCGS 
       260        270        280        290        300
HSGGGVSESE YARWVDTVAQ GIKGNPIVIL EPDALAQLGD CSGQGDRVGF 
       310        320        330        340        350
LKYAAKSLTL KGARVYIDAG HAKWLSVDTP VNRLNQVGFE YAVGFALNTS 
       360        370        380        390        400
NYQTTADSKA YGQQISQRLG GKKFVIDTSR NGNGSNGEWC NPRGRALGER 
       410        420        430        440 
PVAVNDGSGL DALLWVKLPG ESDGACNGGP AAGQWWQEIA LEMARNARW
Length:449
Mass (Da):46,731
Last modified:August 1, 1988 - v1
<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:i67FF887814B3348D
GO

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
M15823 Genomic DNA Translation: AAA23084.1

Protein sequence database of the Protein Information Resource

More...PIRi		A24993

<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
M15823 Genomic DNA Translation: AAA23084.1
PIRiA24993

3D structure databases

AlphaFoldDBiP07984
SMRiP07984
ModBaseiSearch...

Protein family/group databases

CAZyiCBM2, Carbohydrate-Binding Module Family 2
GH6, Glycoside Hydrolase Family 6

Proteomic databases

PRIDEiP07984

Enzyme and pathway databases

SABIO-RKiP07984

Family and domain databases

Gene3Di2.60.40.290, 1 hit
3.20.20.40, 1 hit
InterProiView protein in InterPro
IPR016288, Beta_cellobiohydrolase
IPR036434, Beta_cellobiohydrolase_sf
IPR001919, CBD2
IPR008965, CBM2/CBM3_carb-bd_dom_sf
IPR012291, CBM2_carb-bd_dom_sf
IPR018366, CBM2_CS
IPR001524, Glyco_hydro_6_CS
IPR006311, TAT_signal
PANTHERiPTHR34876, PTHR34876, 1 hit
PfamiView protein in Pfam
PF00553, CBM_2, 1 hit
PF01341, Glyco_hydro_6, 1 hit
PIRSFiPIRSF001100, Beta_cellobiohydrolase, 1 hit
PRINTSiPR00733, GLHYDRLASE6
SMARTiView protein in SMART
SM00637, CBD_II, 1 hit
SUPFAMiSSF49384, SSF49384, 1 hit
SSF51989, SSF51989, 1 hit
PROSITEiView protein in PROSITE
PS51173, CBM2, 1 hit
PS00561, CBM2_A, 1 hit
PS00655, GLYCOSYL_HYDROL_F6_1, 1 hit
PS00656, GLYCOSYL_HYDROL_F6_2, 1 hit
PS51318, TAT, 1 hit

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 nameiGUNA_CELFI
<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: P07984
<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: August 1, 1988
Last sequence update: August 1, 1988
Last modified: May 25, 2022
This is version 116 of the entry and version 1 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

Documents

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