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Protein

Exoglucanase 2

Gene

cbh2

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed-Annotation score:

Annotation score:5 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

Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (Ref. 3). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable).Curated1 Publication

Miscellaneous

T.reesei produces two different exocellobiohydrolases. They are unique in that they can hydrolyze crystalline cellulose in the absence of endoglucanases.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.1 Publication EC:3.2.1.91

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.06 sec(-1) with cellotriose as substrate, 4.1 sec(-1) with cellotetraose as substrate, 1.1 sec(-1) with cellopentaose as substrate and 14 sec(-1) with cellopentaose as substrate.1 Publication
  1. KM=17 µM for cellotriose1 Publication
  2. KM=2.6 µM for cellotetraose1 Publication
  3. KM=1.3 µM for cellopentaose1 Publication
  4. KM=14 µM for cellohexaose1 Publication

    pH dependencei

    Optimum pH is 4-6.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei199Transition state stabilizer that also modulates the pKa of Asp-245 and may act as a proton acceptor through a water chain1 Publication1
    <p>This subsection of the ‘Function’ 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 sitei245Proton donor1 Publication1

    <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

    • cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
    • cellulose binding Source: InterPro
    • identical protein binding Source: IntAct

    GO - Biological processi

    <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

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.2.1.91 6451

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    CBM1 Carbohydrate-Binding Module Family 1
    GH6 Glycoside Hydrolase Family 6

    mycoCLAP, a database of fungal genes encoding lignocellulose-active proteins

    More...
    mycoCLAPi
    CBH6B_TRIRE

    <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_and_taxonomy_section">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:
    Exoglucanase 2 (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Cellobiohydrolase 6A
    Short name:
    Cel6A
    Exocellobiohydrolase II
    Short name:
    CBHII
    Exoglucanase II
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:cbh2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHypocrea jecorina (Trichoderma reesei)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri51453 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi199D → A: 20% of wild-type activity. 1 Publication1
    Mutagenesisi245D → A: No measurable activity. 1 Publication1

    <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 – 18Sequence analysisAdd BLAST18
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000044127719 – 241 Publication6
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000791125 – 471Exoglucanase 2Add BLAST447

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei25Pyrrolidone carboxylic acid1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi111O-linked (Man...) threonine2 Publications1
    Glycosylationi121O-linked (Man...) threonine2 Publications1
    Glycosylationi130O-linked (Man...) serine2 Publications1
    Glycosylationi133O-linked (Man...) serine2 Publications1
    Glycosylationi134O-linked (Man...) serine2 Publications1
    Glycosylationi139O-linked (Man...) serine2 Publications1
    Glycosylationi146O-linked (Man...) threonine2 Publications1
    <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 bondi200 ↔ 2592 Publications
    Glycosylationi313N-linked (GlcNAc) asparagine2 Publications1
    Glycosylationi334N-linked (GlcNAc...) (high mannose) asparagine2 Publications1
    Disulfide bondi392 ↔ 4392 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

    Asn-334 contains mainly a high-mannose-type glycan (Hex7-9GlcNAc2) in a 3:1 ration with a single GlcNAc. Asn-313 was primarily unglycosylated with a small fraction (18%) bearing a single GlcNAc at this site.By similarity

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei38Not glycosylatedBy similarity1

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P07987

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P07987

    <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_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-8155616,EBI-8155616

    GO - Molecular functioni

    Protein-protein interaction databases

    Molecular INTeraction database

    More...
    MINTi
    P07987

    <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

    Secondary structure

    1471
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P07987

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

    More...
    SMRi
    P07987

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P07987

    <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_and_domains_section">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>Domaini26 – 62CBM1PROSITE-ProRule annotationAdd BLAST37

    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>Regioni66 – 106LinkerCuratedAdd BLAST41
    Regioni107 – 471Catalytic1 PublicationAdd BLAST365

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.Curated

    <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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IEPE Eukaryota
    COG5297 LUCA

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    KCANAQS

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    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
    IPR035971 CBD_sf
    IPR000254 Cellulose-bd_dom_fun
    IPR001524 Glyco_hydro_6_CS

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR34876 PTHR34876, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00734 CBM_1, 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

    ProDom; a protein domain database

    More...
    ProDomi
    View protein in ProDom or Entries sharing at least one domain
    PD001821 CBD_fun, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00236 fCBD, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51989 SSF51989, 1 hit
    SSF57180 SSF57180, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00562 CBM1_1, 1 hit
    PS51164 CBM1_2, 1 hit
    PS00655 GLYCOSYL_HYDROL_F6_1, 1 hit
    PS00656 GLYCOSYL_HYDROL_F6_2, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P07987-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIVGILTTLA TLATLAASVP LEERQACSSV WGQCGGQNWS GPTCCASGST
    60 70 80 90 100
    CVYSNDYYSQ CLPGAASSSS STRAASTTSR VSPTTSRSSS ATPPPGSTTT
    110 120 130 140 150
    RVPPVGSGTA TYSGNPFVGV TPWANAYYAS EVSSLAIPSL TGAMATAAAA
    160 170 180 190 200
    VAKVPSFMWL DTLDKTPLME QTLADIRTAN KNGGNYAGQF VVYDLPDRDC
    210 220 230 240 250
    AALASNGEYS IADGGVAKYK NYIDTIRQIV VEYSDIRTLL VIEPDSLANL
    260 270 280 290 300
    VTNLGTPKCA NAQSAYLECI NYAVTQLNLP NVAMYLDAGH AGWLGWPANQ
    310 320 330 340 350
    DPAAQLFANV YKNASSPRAL RGLATNVANY NGWNITSPPS YTQGNAVYNE
    360 370 380 390 400
    KLYIHAIGPL LANHGWSNAF FITDQGRSGK QPTGQQQWGD WCNVIGTGFG
    410 420 430 440 450
    IRPSANTGDS LLDSFVWVKP GGECDGTSDS SAPRFDSHCA LPDALQPAPQ
    460 470
    AGAWFQAYFV QLLTNANPSF L
    Length:471
    Mass (Da):49,653
    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:iC4711BC335B1BD88
    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 conflicti359P → R in AAA72922 (Ref. 2) Curated1
    Sequence conflicti449P → A in AAA72922 (Ref. 2) 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
    M16190 Genomic DNA Translation: AAA34210.1
    M55080 Genomic DNA Translation: AAA72922.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A26160

    <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
    M16190 Genomic DNA Translation: AAA34210.1
    M55080 Genomic DNA Translation: AAA72922.1
    PIRiA26160

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CB2X-ray2.00A/B107-471[»]
    1HGWX-ray2.10A/B107-471[»]
    1HGYX-ray2.20A/B107-471[»]
    1QJWX-ray1.90A/B107-471[»]
    1QK0X-ray2.10A/B109-471[»]
    1QK2X-ray2.00A/B109-471[»]
    3CBHX-ray2.00A107-471[»]
    4AU0X-ray1.70A/B109-471[»]
    4AX6X-ray2.30A/B109-471[»]
    4AX7X-ray1.70A/B/C/D109-471[»]
    4I5RX-ray1.50A158-331[»]
    A425-471[»]
    4I5UX-ray1.22A158-331[»]
    A425-471[»]
    ProteinModelPortaliP07987
    SMRiP07987
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    MINTiP07987

    Protein family/group databases

    CAZyiCBM1 Carbohydrate-Binding Module Family 1
    GH6 Glycoside Hydrolase Family 6
    mycoCLAPiCBH6B_TRIRE

    PTM databases

    iPTMnetiP07987

    Proteomic databases

    PRIDEiP07987

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG410IEPE Eukaryota
    COG5297 LUCA
    OMAiKCANAQS

    Enzyme and pathway databases

    BRENDAi3.2.1.91 6451

    Miscellaneous databases

    EvolutionaryTraceiP07987

    Family and domain databases

    Gene3Di3.20.20.40, 1 hit
    InterProiView protein in InterPro
    IPR016288 Beta_cellobiohydrolase
    IPR036434 Beta_cellobiohydrolase_sf
    IPR035971 CBD_sf
    IPR000254 Cellulose-bd_dom_fun
    IPR001524 Glyco_hydro_6_CS
    PANTHERiPTHR34876 PTHR34876, 1 hit
    PfamiView protein in Pfam
    PF00734 CBM_1, 1 hit
    PF01341 Glyco_hydro_6, 1 hit
    PIRSFiPIRSF001100 Beta_cellobiohydrolase, 1 hit
    PRINTSiPR00733 GLHYDRLASE6
    ProDomiView protein in ProDom or Entries sharing at least one domain
    PD001821 CBD_fun, 1 hit
    SMARTiView protein in SMART
    SM00236 fCBD, 1 hit
    SUPFAMiSSF51989 SSF51989, 1 hit
    SSF57180 SSF57180, 1 hit
    PROSITEiView protein in PROSITE
    PS00562 CBM1_1, 1 hit
    PS51164 CBM1_2, 1 hit
    PS00655 GLYCOSYL_HYDROL_F6_1, 1 hit
    PS00656 GLYCOSYL_HYDROL_F6_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiGUX2_HYPJE
    <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: P07987
    <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_and_isoforms">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: December 5, 2018
    This is version 150 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 programFungal 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

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
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