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Protein

Exoglucanase 1

Gene

cbh1

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. 4). 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei229Nucleophile1 Publication1 Publication1
Active sitei234Proton donor/acceptor1 Publication1 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

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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-16499

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.176 6451
3.2.1.91 6451

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM1 Carbohydrate-Binding Module Family 1
GH7 Glycoside Hydrolase Family 7

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

More...
mycoCLAPi
CBH7A_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 1 (EC:3.2.1.911 Publication)
Alternative name(s):
1,4-beta-cellobiohydrolase
Cellobiohydrolase 7A
Short name:
Cel7A
Exocellobiohydrolase I
Short name:
CBHI
Exoglucanase I
<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:cbh1
<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 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 – 172 PublicationsAdd BLAST17
<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_000000792718 – 513Exoglucanase 1Add BLAST496

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 residuei18Pyrrolidone carboxylic acidCombined sources2 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 bondi21 ↔ 893 Publications
Disulfide bondi36 ↔ 423 Publications
<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>Glycosylationi62N-linked (GlcNAc) asparagine1 Publication1
Disulfide bondi67 ↔ 883 Publications
Disulfide bondi78 ↔ 843 Publications
Disulfide bondi155 ↔ 4143 Publications
Disulfide bondi189 ↔ 2273 Publications
Disulfide bondi193 ↔ 2263 Publications
Disulfide bondi247 ↔ 2733 Publications
Disulfide bondi255 ↔ 2603 Publications
Disulfide bondi278 ↔ 3483 Publications
Glycosylationi287N-linked (GlcNAc) asparagine4 Publications1
Glycosylationi401N-linked (GlcNAc) asparagine3 Publications1
Glycosylationi461O-linked (Man) threonine1 Publication1
Glycosylationi462O-linked (Man...) threonine1 Publication1
Glycosylationi463O-linked (Man...) threonine1 Publication1
Glycosylationi464O-linked (Man...) threonine1 Publication1
Glycosylationi469O-linked (Man) threonine1 Publication1
Glycosylationi470O-linked (Man...) threonine1 Publication1
Glycosylationi471O-linked (Man...) threonine1 Publication1
Glycosylationi473O-linked (Man) serine1 Publication1
Glycosylationi474O-linked (Man) serine1 Publication1
Glycosylationi478O-linked (Man) threonine2 Publications1
Glycosylationi480O-linked (Man) serine2 Publications1
Disulfide bondi485 ↔ 5023 Publications
Glycosylationi491O-linked (Man) serine1 Publication1
Disulfide bondi496 ↔ 5123 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

N-glycosylated. The catalytic core domain comprises three N-linked glycans which each consist of a single N-acetylglucosamine residue.1 Publication
O-glycosylated. Within the linker domain, all 8 threonines are variably glycosylated with between at least one, and up to three, mannose residues per site. All serines in this domain are at least partially glycosylated with a single mannose residue (PubMed:9746354). O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose (Probable).1 Publication1 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>Sitei81Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P62694

<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

1513
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
P62694

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

More...
SMRi
P62694

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
P62694

<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>Domaini477 – 513CBM1PROSITE-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>Regioni18 – 453Catalytic1 PublicationAdd BLAST436
Regioni454 – 477LinkerCuratedAdd BLAST24

<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.2 Publications

<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
ENOG410IE3Y Eukaryota
ENOG41101KD LUCA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07999 GH7_CBH_EG, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.70.100.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR013320 ConA-like_dom_sf
IPR001722 Glyco_hydro_7
IPR037019 Glyco_hydro_7_sf

The PANTHER Classification System

More...
PANTHERi
PTHR33753 PTHR33753, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00734 CBM_1, 1 hit
PF00840 Glyco_hydro_7, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00734 GLHYDRLASE7

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
SSF49899 SSF49899, 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

<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.

P62694-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV
60 70 80 90 100
IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG
110 120 130 140 150
VTTSGNSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV
160 170 180 190 200
SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI
210 220 230 240 250
NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV
260 270 280 290 300
GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD
310 320 330 340 350
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA
360 370 380 390 400
EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT
410 420 430 440 450
NETSSTPGAV RGSCSTSSGV PAQVESQSPN AKVTFSNIKF GPIGSTGNPS
460 470 480 490 500
GGNPPGGNRG TTTTRRPATT TGSSPGPTQS HYGQCGGIGY SGPTVCASGT
510
TCQVLNPYYS QCL
Length:513
Mass (Da):54,073
Last modified:July 21, 1986 - 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:i9F5C0A8A854F2C12
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 conflicti459R → PP AA sequence (Ref. 2) Curated1

Sequence databases

Protein sequence database of the Protein Information Resource

More...
PIRi
A00902 EUTQI

<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

PIRiA00902 EUTQI

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
1AZ6NMR-A478-513[»]
1AZHNMR-A478-513[»]
1AZJNMR-A478-513[»]
1AZKNMR-A478-513[»]
1CBHNMR-A478-513[»]
1CELX-ray1.80A/B19-451[»]
1DY4X-ray1.90A19-451[»]
1EGNX-ray1.60A18-451[»]
1Q2BX-ray1.60A18-451[»]
1Q2EX-ray1.75A/B19-451[»]
2CBHNMR-A478-513[»]
2CELX-ray2.00A/B19-451[»]
2MWJNMR-A478-513[»]
2MWKNMR-A478-513[»]
2V3IX-ray1.05A19-451[»]
2V3RX-ray1.60A19-451[»]
3CELX-ray2.00A19-451[»]
4C4CX-ray1.45A19-451[»]
4C4DX-ray1.32A19-451[»]
4CELX-ray2.20A/B19-451[»]
4D5IX-ray1.42A19-451[»]
4D5JX-ray1.50A19-451[»]
4D5OX-ray1.52A19-451[»]
4D5PX-ray1.89A19-451[»]
4D5QX-ray1.68A19-451[»]
4D5VX-ray1.62A19-451[»]
4P1HX-ray1.50A19-449[»]
4P1JX-ray2.62A19-451[»]
4UWTX-ray1.20A19-451[»]
4V0ZX-ray1.70A19-451[»]
5CELX-ray1.90A19-451[»]
5OA5X-ray2.10A/B18-451[»]
5X34NMR-A478-513[»]
5X35NMR-A478-513[»]
5X36NMR-A478-513[»]
5X37NMR-A478-513[»]
5X38NMR-A478-513[»]
5X39NMR-A478-513[»]
5X3CNMR-A478-513[»]
6CELX-ray1.70A19-451[»]
6GRNX-ray1.79A18-451[»]
7CELX-ray1.90A19-451[»]
8CELmodel-A18-451[»]
ProteinModelPortaliP62694
SMRiP62694
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1 Carbohydrate-Binding Module Family 1
GH7 Glycoside Hydrolase Family 7
mycoCLAPiCBH7A_TRIRE

Proteomic databases

PRIDEiP62694

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IE3Y Eukaryota
ENOG41101KD LUCA

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16499
BRENDAi3.2.1.176 6451
3.2.1.91 6451

Miscellaneous databases

EvolutionaryTraceiP62694

Family and domain databases

CDDicd07999 GH7_CBH_EG, 1 hit
Gene3Di2.70.100.10, 1 hit
InterProiView protein in InterPro
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR013320 ConA-like_dom_sf
IPR001722 Glyco_hydro_7
IPR037019 Glyco_hydro_7_sf
PANTHERiPTHR33753 PTHR33753, 1 hit
PfamiView protein in Pfam
PF00734 CBM_1, 1 hit
PF00840 Glyco_hydro_7, 1 hit
PRINTSiPR00734 GLHYDRLASE7
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001821 CBD_fun, 1 hit
SMARTiView protein in SMART
SM00236 fCBD, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF57180 SSF57180, 1 hit
PROSITEiView protein in PROSITE
PS00562 CBM1_1, 1 hit
PS51164 CBM1_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 nameiGUX1_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: P62694
Secondary accession number(s): P00725
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: December 5, 2018
This is version 92 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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