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UniProtKB - P43379 (CDGT2_NIACI)

Entry version 129 (25 May 2022)
Sequence version 1 (01 Nov 1995)
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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Niallia circulans (Bacillus circulans)
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

<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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+Note: Binds 3 Ca2+ ions per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi54Calcium 11
Metal bindingi56Calcium 1; via carbonyl oxygen1
Metal bindingi59Calcium 11
Metal bindingi60Calcium 11
Metal bindingi78Calcium 1; via carbonyl oxygen1
Metal bindingi80Calcium 11
Metal bindingi166Calcium 21
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei167Substrate1
Metal bindingi217Calcium 2; via carbonyl oxygen1
Metal bindingi226Calcium 21
Binding sitei254Substrate1
<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 sitei256Nucleophile1
Metal bindingi260Calcium 2; via carbonyl oxygen1
Active sitei284Proton donor1
Metal bindingi342Calcium 3; via carbonyl oxygen1
Binding sitei354Substrate1
<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>Sitei355Transition state stabilizerBy similarity1
Binding sitei398Substrate1
Binding sitei402Substrate1
Metal bindingi604Calcium 31

<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 functionGlycosyltransferase, Transferase
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.1.19, 649

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P43379

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		CBM20, Carbohydrate-Binding Module Family 20
GH13, Glycoside Hydrolase Family 13

<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:
Cyclomaltodextrin glucanotransferase (EC:2.4.1.19)
Alternative name(s):
Cyclodextrin-glycosyltransferase
Short name:
CGTase
<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:cgt
<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>OrganismiNiallia circulans (Bacillus circulans)
<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 identifieri1397 [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 › Bacilli › Bacillales › Bacillaceae › Niallia

<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

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi256D → N: Reduces activity 23000-fold. Reduces activity 520000-fold; when associated with N-355. 1 Publication1
Mutagenesisi284E → Q: Reduces activity 4100-fold. 1 Publication1
Mutagenesisi355D → N: Reduces activity 56000-fold. Reduces activity 520000-fold; when associated with N-256. 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 – 271 PublicationAdd BLAST27
<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_000000143128 – 713Cyclomaltodextrin glucanotransferaseAdd BLAST686

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 bondi70 ↔ 771 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P43379

<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.

1 Publication

<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

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P43379

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

More...SMRi		P43379

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P43379

<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>Domaini526 – 607IPT/TIGAdd BLAST82
Domaini608 – 713CBM20PROSITE-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>Regioni28 – 165A1Add BLAST138
Regioni127 – 128Substrate binding2
Regioni166 – 229BAdd BLAST64
Regioni172 – 174Substrate binding3
Regioni220 – 223Substrate binding4
Regioni230 – 433A2Add BLAST204
Regioni259 – 260Substrate binding2
Regioni434 – 522CAdd BLAST89
Regioni523 – 609DAdd BLAST87
Regioni610 – 713EAdd BLAST104

<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

May consist of two protein domains: the one in the N-terminal side cleaves the alpha-1,4-glucosidic bond in starch, and the other in the C-terminal side catalyzes other activities, including the reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the maltooligosaccharide produced.

<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 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 2 hits
2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006048, A-amylase/branching_C
IPR031319, A-amylase_C
IPR006046, Alpha_amylase
IPR013784, Carb-bd-like_fold
IPR002044, CBM_fam20
IPR006047, Glyco_hydro_13_cat_dom
IPR013780, Glyco_hydro_b
IPR017853, Glycoside_hydrolase_SF
IPR013783, Ig-like_fold
IPR014756, Ig_E-set
IPR002909, IPT_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00128, Alpha-amylase, 1 hit
PF02806, Alpha-amylase_C, 1 hit
PF00686, CBM_20, 1 hit
PF01833, TIG, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00110, ALPHAAMYLASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00642, Aamy, 1 hit
SM00632, Aamy_C, 1 hit
SM01065, CBM_2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49452, SSF49452, 1 hit
SSF51445, SSF51445, 1 hit
SSF81296, SSF81296, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51166, CBM20, 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.

P43379-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKFLKSTAA LALGLSLTFG LFSPAQAAPD TSVSNKQNFS TDVIYQIFTD 
        60         70         80         90        100
RFSDGNPANN PTGAAFDGTC TNLRLYCGGD WQGIINKIND GYLTGMGVTA 
       110        120        130        140        150
IWISQPVENI YSIINYSGVN NTAYHGYWAR DFKKTNPAYG TIADFQNLIA 
       160        170        180        190        200
AAHAKNIKVI IDFAPNHTSP ASSDQPSFAE NGRLYDNGTL LGGYTNDTQN 
       210        220        230        240        250
LFHHNGGTDF STTENGIYKN LYDLADLNHN NSTVDVYLKD AIKMWLDLGI 
       260        270        280        290        300
DGIRMDAVKH MPFGWQKSFM AAVNNYKPVF TFGEWFLGVN EVSPENHKFA 
       310        320        330        340        350
NESGMSLLDF RFAQKVRQVF RDNTDNMYGL KAMLEGSAAD YAQVDDQVTF 
       360        370        380        390        400
IDNHDMERFH ASNANRRKLE QALAFTLTSR GVPAIYYGTE QYMSGGTDPD 
       410        420        430        440        450
NRARIPSFST STTAYQVIQK LAPLRKCNPA IAYGSTQERW INNDVLIYER 
       460        470        480        490        500
KFGSNVAVVA VNRNLNAPAS ISGLVTSLPQ GSYNDVLGGL LNGNTLSVGS 
       510        520        530        540        550
GGAASNFTLA AGGTAVWQYT AATATPTIGH VGPMMAKPGV TITIDGRGFG 
       560        570        580        590        600
SSKGTVYFGT TAVSGADITS WEDTQIKVKI PAVAGGNYNI KVANAAGTAS 
       610        620        630        640        650
NVYDNFEVLS GDQVSVRFVV NNATTALGQN VYLTGSVSEL GNWDPAKAIG 
       660        670        680        690        700
PMYNQVVYQY PNWYYDVSVP AGKTIEFKFL KKQGSTVTWE GGSNHTFTAP 
       710 
SSGTATINVN WQP
Length:713
Mass (Da):77,309
Last modified:November 1, 1995 - 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:i8ABBFB2C633A004B
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
X78145 Genomic DNA Translation: CAA55023.1

Protein sequence database of the Protein Information Resource

More...PIRi		A58800

<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
X78145 Genomic DNA Translation: CAA55023.1
PIRiA58800

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
1CDGX-ray2.00A28-713[»]
1CGVX-ray2.50A28-713[»]
1CGWX-ray2.50A28-713[»]
1CGXX-ray2.50A28-713[»]
1CGYX-ray2.50A28-713[»]
1CXEX-ray2.10A28-713[»]
1CXFX-ray2.10A28-713[»]
1CXHX-ray2.41A28-713[»]
1CXIX-ray2.20A28-713[»]
1CXKX-ray2.09A28-713[»]
1CXLX-ray1.81A28-713[»]
1D3CX-ray1.78A28-713[»]
1DTUX-ray2.40A28-713[»]
1EO5X-ray2.00A28-713[»]
1EO7X-ray2.48A28-713[»]
1KCKX-ray2.43A28-713[»]
1KCLX-ray1.94A28-713[»]
1OT1X-ray2.00A28-713[»]
1OT2X-ray2.10A28-713[»]
1PEZX-ray2.32A28-713[»]
1PJ9X-ray2.00A28-713[»]
1TCMX-ray2.20A/B28-713[»]
2CXGX-ray2.50A28-713[»]
2DIJX-ray2.60A28-713[»]
AlphaFoldDBiP43379
SMRiP43379
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiCBM20, Carbohydrate-Binding Module Family 20
GH13, Glycoside Hydrolase Family 13

Proteomic databases

PRIDEiP43379

Enzyme and pathway databases

BRENDAi2.4.1.19, 649
SABIO-RKiP43379

Miscellaneous databases

EvolutionaryTraceiP43379

Family and domain databases

Gene3Di2.60.40.10, 2 hits
2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006048, A-amylase/branching_C
IPR031319, A-amylase_C
IPR006046, Alpha_amylase
IPR013784, Carb-bd-like_fold
IPR002044, CBM_fam20
IPR006047, Glyco_hydro_13_cat_dom
IPR013780, Glyco_hydro_b
IPR017853, Glycoside_hydrolase_SF
IPR013783, Ig-like_fold
IPR014756, Ig_E-set
IPR002909, IPT_dom
PfamiView protein in Pfam
PF00128, Alpha-amylase, 1 hit
PF02806, Alpha-amylase_C, 1 hit
PF00686, CBM_20, 1 hit
PF01833, TIG, 1 hit
PRINTSiPR00110, ALPHAAMYLASE
SMARTiView protein in SMART
SM00642, Aamy, 1 hit
SM00632, Aamy_C, 1 hit
SM01065, CBM_2, 1 hit
SUPFAMiSSF49452, SSF49452, 1 hit
SSF51445, SSF51445, 1 hit
SSF81296, SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51166, CBM20, 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 nameiCDGT2_NIACI
<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: P43379
<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: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 25, 2022
This is version 129 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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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