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UniProtKB - P30920 (CDGT1_BACCI)

Entry version 131 (07 Apr 2021)
Sequence version 1 (01 Jul 1993)
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Protein

Cyclomaltodextrin glucanotransferase

Gene
N/A
Organism
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

  • Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond. EC:2.4.1.19

<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 2 calcium 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 bindingi61Calcium 11
Metal bindingi63Calcium 1; via carbonyl oxygen1
Metal bindingi66Calcium 11
Metal bindingi67Calcium 11
Metal bindingi85Calcium 1; via carbonyl oxygen1
Metal bindingi87Calcium 11
Metal bindingi173Calcium 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 sitei174Substrate1
Metal bindingi224Calcium 2; via carbonyl oxygen1
Binding sitei230Substrate1
Metal bindingi233Calcium 21
Binding sitei261SubstrateBy similarity1
<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 sitei263NucleophileBy similarity1
Metal bindingi267Calcium 2; via carbonyl oxygen1
Binding sitei267Substrate1
Active sitei291Proton donorBy similarity1
Binding sitei361Substrate1
<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>Sitei362Transition state stabilizerBy similarity1
Binding sitei405Substrate1
Binding sitei409Substrate1

<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

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 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>OrganismiBacillus 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 › Bacillus

<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

Chemistry databases

Drug and drug target database

More...DrugBanki		DB01789, 1-Amino-2,3-Dihydroxy-5-Hydroxymethyl Cyclohex-5-Ene
DB02469, 4,6-dideoxy-4-amino-beta-D-glucopyranoside
DB01841, 4,6-Dideoxyglucose
DB02670, 4-Deoxy-Alpha-D-Glucose
DB02120, 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol
DB01909, Alpha-Cyclodextrin (Cyclohexa-Amylose)
DB03773, alpha-D-quinovopyranose
DB02379, Beta-D-Glucose
DB03323, Maltose
DB02394, Oxiranpseudoglucose
DB03198, Thio-Maltohexaose
DB01719, Thio-Maltopentaose

<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 – 34Add BLAST34
<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_000000143035 – 718Cyclomaltodextrin glucanotransferaseAdd BLAST684

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 bondi77 ↔ 84

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P30920

<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.

<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

1718
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P30920

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		P30920

<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>Domaini532 – 612IPT/TIGAdd BLAST81
Domaini613 – 718CBM20PROSITE-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>Regioni35 – 172A1Add BLAST138
Regioni134 – 135Substrate binding2
Regioni173 – 236BAdd BLAST64
Regioni227 – 230Substrate bindingBy similarity4
Regioni237 – 440A2Add BLAST204
Regioni266 – 267Substrate binding2
Regioni441 – 528CAdd BLAST88
Regioni529 – 614DAdd BLAST86
Regioni615 – 718EAdd 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
IPR006311, TAT_signal

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
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.

P30920-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFQMAKRAFL STTLTLGLLA GSALPFLPAS AVYADPDTAV TNKQSFSTDV 
        60         70         80         90        100
IYQVFTDRFL DGNPSNNPTG AAYDATCSNL KLYCGGDWQG LINKINDNYF 
       110        120        130        140        150
SDLGVTALWI SQPVENIFAT INYSGVTNTA YHGYWARDFK KTNPYFGTMA 
       160        170        180        190        200
DFQNLITTAH AKGIKIVIDF APNHTSPAME TDTSFAENGR LYDNGTLVGG 
       210        220        230        240        250
YTNDTNGYFH HNGGSDFSSL ENGIYKNLYD LADFNHNNAT IDKYFKDAIK 
       260        270        280        290        300
LWLDMGVDGI RVDAVKHMPL GWQKSWMSSI YAHKPVFTFG EWFLGSAASD 
       310        320        330        340        350
ADNTDFANKS GMSLLDFRFN SAVRNVFRDN TSNMYALDSM INSTATDYNQ 
       360        370        380        390        400
VNDQVTFIDN HDMDRFKTSA VNNRRLEQAL AFTLTSRGVP AIYYGTEQYL 
       410        420        430        440        450
TGNGDPDNRA KMPSFSKSTT AFNVISKLAP LRKSNPAIAY GSTQQRWINN 
       460        470        480        490        500
DVYVYERKFG KSVAVVAVNR NLSTSASITG LSTSLPTGSY TDVLGGVLNG 
       510        520        530        540        550
NNITSTNGSI NNFTLAAGAT AVWQYTTAET TPTIGHVGPV MGKPGNVVTI 
       560        570        580        590        600
DGRGFGSTKG TVYFGTTAVT GAAITSWEDT QIKVTIPSVA AGNYAVKVAA 
       610        620        630        640        650
SGVNSNAYNN FTILTGDQVT VRFVVNNAST TLGQNLYLTG NVAELGNWST 
       660        670        680        690        700
GSTAIGPAFN QVIHQYPTWY YDVSVPAGKQ LEFKFFKKNG STITWESGSN 
       710 
HTFTTPASGT ATVTVNWQ
Length:718
Mass (Da):78,047
Last modified:July 1, 1993 - 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:iE08CF0FE9C98BDA1
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
X68326 Genomic DNA Translation: CAA48401.1

Protein sequence database of the Protein Information Resource

More...PIRi		S23674, ALBSGC

<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
X68326 Genomic DNA Translation: CAA48401.1
PIRiS23674, ALBSGC

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
1CGTX-ray2.00A35-718[»]
1CGUX-ray2.50A35-718[»]
3CGTX-ray2.40A35-718[»]
4CGTX-ray2.60A35-718[»]
5CGTX-ray2.50A35-718[»]
6CGTX-ray2.60A35-718[»]
7CGTX-ray3.00A35-718[»]
8CGTX-ray2.40A35-718[»]
9CGTX-ray2.50A35-718[»]
SMRiP30920
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

DrugBankiDB01789, 1-Amino-2,3-Dihydroxy-5-Hydroxymethyl Cyclohex-5-Ene
DB02469, 4,6-dideoxy-4-amino-beta-D-glucopyranoside
DB01841, 4,6-Dideoxyglucose
DB02670, 4-Deoxy-Alpha-D-Glucose
DB02120, 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol
DB01909, Alpha-Cyclodextrin (Cyclohexa-Amylose)
DB03773, alpha-D-quinovopyranose
DB02379, Beta-D-Glucose
DB03323, Maltose
DB02394, Oxiranpseudoglucose
DB03198, Thio-Maltohexaose
DB01719, Thio-Maltopentaose

Protein family/group databases

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

Proteomic databases

PRIDEiP30920

Enzyme and pathway databases

BRENDAi2.4.1.19, 649

Miscellaneous databases

EvolutionaryTraceiP30920

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
IPR006311, TAT_signal
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
PS51318, TAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDGT1_BACCI
<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: P30920
<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: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 7, 2021
This is version 131 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

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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