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Entry version 81 (29 Sep 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Toxin A

Gene

tcdA

Organism
Clostridium novyi
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

Precursor of a cytotoxin, which enters into host cells and mediates autoprocessing to release the active toxin (N-acetylglucosaminyltransferase TcdA) into the host cytosol (By similarity).

Once entered into host cells, acidification in the endosome promotes the membrane insertion of the translocation region and formation of a pore, leading to translocation of the GT44 and peptidase C80 domains across the endosomal membrane (By similarity).

This activates the peptidase C80 domain and autocatalytic processing, releasing the N-terminal part (N-acetylglucosaminyltransferase TcdA), which constitutes the active part of the toxin, in the cytosol (PubMed:17334356).

By similarity1 Publication

Active form of the toxin, which is released into the host cytosol following autoprocessing and inactivates small GTPases (PubMed:8810274, PubMed:16157585).

Acts by mediating monoglycosylation of small GTPases of the Rho family (Rac1, RhoA, RhoG and Cdc42) in host cells at the conserved threonine residue located in the switch I region ('Thr-37/35'), using UDP-N-acetyl-alpha-D-glucosamine as the sugar donor (PubMed:8810274, PubMed:16157585).

Monoglycosylation of host small GTPases completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption and cell death (PubMed:8810274).

2 Publications

<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

<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

N-acetylglucosaminyltransferase TcdA:
Mn2+By similarity, Mg2+By similarityNote: Has higher activity with Mn2+, but most likely uses Mg2+ in host cells. Required for glucosyltransferase activity.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Protease activity is activated upon binding to 1D-myo-inositol hexakisphosphate (InsP6), which induces conformational reorganization.By similarity

<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 282 hour(-1) with UDP-alpha-D-glucose as substrate (PubMed:16157585). kcat is 2800 hour(-1) with UDP-N-acetyl-alpha-D-glucosamine as substrate (PubMed:16157585).1 Publication
  1. KM=307 µM for UDP-alpha-D-glucose1 Publication
  2. KM=17 µM for UDP-N-acetyl-alpha-D-glucosamine1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei141UDP-N-acetyl-alpha-D-glucosamineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi284Magnesium or manganeseBy similarity1
Metal bindingi286Magnesium or manganeseBy similarity1
Metal bindingi520Magnesium or manganeseBy similarity1
Binding sitei5571D-myo-inositol hexakisphosphateBy similarity1
Binding sitei6071D-myo-inositol hexakisphosphateBy similarity1
Binding sitei6511D-myo-inositol hexakisphosphateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei657For protease activityPROSITE-ProRule annotation1
Active sitei707Nucleophile; for protease activityPROSITE-ProRule annotation1
Binding sitei7821D-myo-inositol hexakisphosphateBy similarity1

<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 functionEnterotoxin, Glycosyltransferase, Hydrolase, Protease, Thiol protease, Toxin, Transferase
Biological processVirulence
LigandLipid-binding, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.B62, 1497

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT44, Glycosyltransferase Family 44

Transport Classification Database

More...
TCDBi
1.C.57.1.4, the clostridial cytotoxin (cct) family

<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:
Toxin A1 Publication (EC:3.4.22.-1 Publication)
Cleaved into the following chain:
N-acetylglucosaminyltransferase TcdACurated (EC:2.4.1.-2 Publications)
<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:tcdA
Synonyms:toxA1 Publication
<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>OrganismiClostridium novyi
<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 identifieri1542 [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 lineageiBacteriaFirmicutesClostridiaEubacterialesClostridiaceaeClostridium

<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

Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Membrane, 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>Mutagenesisi385 – 387SNA → INQ: Changes substrate preference and promotes glucosyltransferase activity instead of N-acetylglucosaminyltransferase activity. 1 Publication3

<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 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_00004511921 – 2178Toxin AAdd BLAST2178
ChainiPRO_00004511931 – 548N-acetylglucosaminyltransferase TcdABy similarityAdd BLAST548

<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

Undergoes autocatalytic cleavage to release the N-terminal part (N-acetylglucosaminyltransferase TcdA), which constitutes the active part of the toxin, in the host cytosol (PubMed:17334356). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and promotes autoprocessing (PubMed:17334356).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>Sitei548 – 549Cleavage; by autolysisBy similarity2

Keywords - PTMi

Autocatalytic cleavage

<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

12178
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

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SMRi
Q46149

Database of comparative protein structure models

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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
Q46149

<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>Domaini98 – 474GT44Sequence analysisAdd BLAST377
Domaini574 – 787Peptidase C80PROSITE-ProRule annotationAdd BLAST214
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1799 – 1818Cell wall-binding 1PROSITE-ProRule annotationAdd BLAST20
Repeati1820 – 1839Cell wall-binding 2PROSITE-ProRule annotationAdd BLAST20
Repeati1870 – 1889Cell wall-binding 3PROSITE-ProRule annotationAdd BLAST20
Repeati1890 – 1909Cell wall-binding 4PROSITE-ProRule annotationAdd BLAST20
Repeati1910 – 1929Cell wall-binding 5PROSITE-ProRule annotationAdd BLAST20
Repeati1931 – 1950Cell wall-binding 6PROSITE-ProRule annotationAdd BLAST20
Repeati1951 – 1970Cell wall-binding 7PROSITE-ProRule annotationAdd BLAST20
Repeati2004 – 2023Cell wall-binding 8PROSITE-ProRule annotationAdd BLAST20
Repeati2024 – 2043Cell wall-binding 9PROSITE-ProRule annotationAdd BLAST20
Repeati2045 – 2060Cell wall-binding 10PROSITE-ProRule annotationAdd BLAST16
Repeati2064 – 2083Cell wall-binding 11PROSITE-ProRule annotationAdd BLAST20
Repeati2114 – 2133Cell wall-binding 12PROSITE-ProRule annotationAdd BLAST20
Repeati2134 – 2153Cell wall-binding 13PROSITE-ProRule annotationAdd BLAST20
Repeati2155 – 2174Cell wall-binding 14PROSITE-ProRule annotationAdd BLAST20

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>Regioni1 – 93Four-helical bundleBy similarityAdd BLAST93
Regioni98 – 474Glucosyltransferase regionBy similarityAdd BLAST377
Regioni98 – 474N-acetylglucosaminyltransferase regionBy similarityAdd BLAST377
Regioni103 – 105UDP-N-acetyl-alpha-D-glucosamine bindingBy similarity3
Regioni267 – 271UDP-N-acetyl-alpha-D-glucosamine bindingBy similarity5
Regioni284 – 286UDP-N-acetyl-alpha-D-glucosamine bindingBy similarity3
Regioni523 – 525UDP-N-acetyl-alpha-D-glucosamine bindingBy similarity3
Regioni549 – 806Autoprocessing regionBy similarityAdd BLAST258
Regioni758 – 7591D-myo-inositol hexakisphosphate bindingBy similarity2
Regioni807 – 1485Translocation regionBy similarityAdd BLAST679

<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

Consists of 4 functional domains: (1) the N-terminal GT44 domain (glycosyltransferase, also named GTD), which mediates glucosylation of host small GTPases, (2) an autoprocessing region that catalyzes autoprocessing to release the N-terminal GT44 domain in the host cytosol, (3) the translocation region that forms a pore to promote translocation of the GT44 and peptidase C80 domains across the endosomal membrane and (4) the receptor-binding (CROPS) region that mediates binding to host cells and contribute to entry into cells.1 Publication
The receptor-binding (CROPS) region is dynamic and can have open and closed conformations depending of the pH: has an open conformation at endosomal pH and a closed conformation at neutral pH.By similarity
The cell wall-binding repeats bind carbohydrates, probably contributing to entry into cells.By similarity
The four-helical bundle region mediates binding to phospholipids, such as phosphatidylserine and phosphatidic acid (By similarity). This promotes localization to the inner face of the cell membrane close to small GTPases (By similarity).By similarity

<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

Repeat

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.11050, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018337, Cell_wall/Cho-bd_repeat
IPR020974, CPD_dom
IPR038383, CPD_dom_sf
IPR029044, Nucleotide-diphossugar_trans
IPR024770, TcdA/TcdB_cat
IPR024772, TcdA/TcdB_N
IPR024769, TcdA/TcdB_pore_forming

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF19127, Choline_bind_3, 1 hit
PF11713, Peptidase_C80, 1 hit
PF12919, TcdA_TcdB, 1 hit
PF12920, TcdA_TcdB_pore, 1 hit
PF12918, TcdB_N, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53448, SSF53448, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51771, CGT_MARTX_CPD, 1 hit
PS51170, CW, 14 hits

<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>. 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_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.

Q46149-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLITREQLMK IASIPLKRKE PEYNLILDAL ENFNRDIEGT SVKEIYSKLS
60 70 80 90 100
KLNELVDNYQ TKYPSSGRNL ALENFRDSLY SELRELIKNS RTSTIASKNL
110 120 130 140 150
SFIWIGGPIS DQSLEYYNMW KMFNKDYNIR LFYDKNSLLV NTLKTAIIQE
160 170 180 190 200
SSKVIIEQNQ SNILDGTYGH NKFYSDRMKL IYRYKRELKM LYENMKQNNS
210 220 230 240 250
VDDIIINFLS NYFKYDIGKL NNQKENNNNK MIAIGATDIN TENILTNKLK
260 270 280 290 300
SYYYQELIQT NNLAAASDIL RIAILKKYGG VYCDLDFLPG VNLSLFNDIS
310 320 330 340 350
KPNGMDSNYW EAAIFEAIAN EKKLMNNYPY KYMEQVPSEI KERILSFVRN
360 370 380 390 400
HDINDLILPL GDIKISQLEI LLSRLKAATG KKTFSNAFII SNNDSLTLNN
410 420 430 440 450
LISQLENRYE ILNSIIQEKF KICETYDSYI NSVSELVLET TPKNLSMDGS
460 470 480 490 500
SFYQQIIGYL SSGFKPEVNS TVFFSGPNIY SSATCDTYHF IKNTFDMLSS
510 520 530 540 550
QNQEIFEASN NLYFSKTHDE FKSSWLLRSN IAEKEFQKLI KTYIGRTLNY
560 570 580 590 600
EDGLNFNKWK RVTTSELLKV IEEVNSTKIY ENYDLNMILQ IQGDDISYES
610 620 630 640 650
AVNVFGKNPN KSILIQGVDD FANVFYFENG IVQSDNINNI LSRFNDIKKI
660 670 680 690 700
KLTLIGHGEN VFNPKLFGGK TVNDLYTNII KPKLQHLLER EGVILKNKYL
710 720 730 740 750
KINILGCYMF TPKVDINSTF VGKLFNKISR DLQPKGFSKN QLEISANKYA
760 770 780 790 800
IRINREGKRE VLDYFGKWVS NTDLIAEQIS NKYVVYWNEV ENTLSARVEQ
810 820 830 840 850
LNKVAEFAKD INSIIQTTNN QELKQSLVNT YADLITTLYS ELLKEDIPFE
860 870 880 890 900
LDNIQIKERI ILNEISRLHD FSNIILDFYQ KNNISNNMII LFDSIIKEKD
910 920 930 940 950
YYNVKLANKI TGETSVIKTY SDSLWNFTNK YKKIVDDIKG IIVKDINGEF
960 970 980 990 1000
IKKADFEIEQ NPSLLNSAML MQLLIDYKPY TEILTNMNTS LKVQAYAQIF
1010 1020 1030 1040 1050
QLSIGAIQEA TEIVTIISDA LNANFNILSK LKVGSSVASV IIDGINLIAA
1060 1070 1080 1090 1100
LTELKNVKTN FERKLIEAKV GMYSIGFILE SSSLISGLLG ATAVSEILGV
1110 1120 1130 1140 1150
ISVPVAGILV GLPSLVNNIL VLGEKYNQIL DYFSKFYPIV GKNPFSIQDN
1160 1170 1180 1190 1200
IIIPYDDIAI TELNFKYNKF KYGYAKISGL KVGLVTHIGE NIDHYFSAPS
1210 1220 1230 1240 1250
LDHYIELSIY PALKLNDTNL PKGNVVLLPS GLNKVYKPEI SAIAGANSQE
1260 1270 1280 1290 1300
GNGVEVLNLI RNYYVDSNGN TKFPWKYEAP FEYSFSYMRV EYFDTKVNVI
1310 1320 1330 1340 1350
LDNENKTLII PVLTIDEMRN KISYEILGDG GQYNVILPVN QTNINIVSNK
1360 1370 1380 1390 1400
NDIWNFDVSY IVKESKIEDN KFVLDGFINN IFSTLKVSND GFKIGKQFIS
1410 1420 1430 1440 1450
IKNTPRAINL SFKINNNIVI VSIYLNHEKS NSITIISSDL NDIKNNFDNL
1460 1470 1480 1490 1500
LDNINYIGLG SISDNTINCI VRNDEVYMEG KIFLNEKKLV FIQNELELHL
1510 1520 1530 1540 1550
YDSVNKDSQY LINNPINNVV KYKDGYIVEG TFLINSTENK YSLYIENNKI
1560 1570 1580 1590 1600
MLKGLYLESS VFKTIQDKIY SKEKVNDYIL SLIKKFFTVN IQLCPFMIVS
1610 1620 1630 1640 1650
GVDENNRYLE YMLSTNNKWI INGGYWENDF NNYKIVDFEK CNVIVSGSNK
1660 1670 1680 1690 1700
LNSEGDLADT IDVLDKDLEN LYIDSVIIIP KVYTKKIIIH PIPNNPQINI
1710 1720 1730 1740 1750
INTQSIHDKC HLIIDSVLTN NYHWESDGDD LIITNGLDIN IRILQGLSFG
1760 1770 1780 1790 1800
FKYKNIYLKF SNYDELSLND FLLQNYNVKG LYYINGELHY KNIPGDTFEY
1810 1820 1830 1840 1850
GWINIDSRWY FFDSINLIAK KGYQEIEGER YYFNPNTGVQ ESGVFLTPNG
1860 1870 1880 1890 1900
LEYFTNKHAS SKRWGRAINY TGWLTLDGNK YYFQSNSKAV TGLQKISDKY
1910 1920 1930 1940 1950
YYFNDNGQMQ IKWQIINNNK YYFDGNTGEA IIGWFNNNKE RYYFDSEGRL
1960 1970 1980 1990 2000
LTGYQVIGDK SYYFSDNING NWEEGSGVLK SGIFKTPSGF KLFSSEGDKS
2010 2020 2030 2040 2050
AINYKGWLDL NGNKYYFNSD SIAVTGSYNI KGIQYYFNPK TAVLTNGWYT
2060 2070 2080 2090 2100
LDNNNYYVSN GHNVLGYQDI DGKGYYFDPS TGIQKAGVFP TPNGLRYFTM
2110 2120 2130 2140 2150
KPIDGQRWGQ CIDYTGWLHL NGNKYYFGYY NSAVTGWRVL GGKRYFFNIK
2160 2170
TGAATTGLLT LSGKRYYFNE KGEQLTLV
Length:2,178
Mass (Da):250,136
Last modified:November 1, 1996 - 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:i9B0ADCE031C4A75A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z23281 Genomic DNA Translation: CAA80819.1
Z48636 Genomic DNA Translation: CAA88565.1

Protein sequence database of the Protein Information Resource

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PIRi
S55805

<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
Z23281 Genomic DNA Translation: CAA80819.1
Z48636 Genomic DNA Translation: CAA88565.1
PIRiS55805

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VK9X-ray2.85A1-551[»]
SMRiQ46149
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiGT44, Glycosyltransferase Family 44
TCDBi1.C.57.1.4, the clostridial cytotoxin (cct) family

Enzyme and pathway databases

BRENDAi2.4.1.B62, 1497

Miscellaneous databases

EvolutionaryTraceiQ46149

Family and domain databases

Gene3Di3.40.50.11050, 1 hit
InterProiView protein in InterPro
IPR018337, Cell_wall/Cho-bd_repeat
IPR020974, CPD_dom
IPR038383, CPD_dom_sf
IPR029044, Nucleotide-diphossugar_trans
IPR024770, TcdA/TcdB_cat
IPR024772, TcdA/TcdB_N
IPR024769, TcdA/TcdB_pore_forming
PfamiView protein in Pfam
PF19127, Choline_bind_3, 1 hit
PF11713, Peptidase_C80, 1 hit
PF12919, TcdA_TcdB, 1 hit
PF12920, TcdA_TcdB_pore, 1 hit
PF12918, TcdB_N, 1 hit
SUPFAMiSSF53448, SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS51771, CGT_MARTX_CPD, 1 hit
PS51170, CW, 14 hits

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiTCDA_CLONO
<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: Q46149
Secondary accession number(s): Q46147, Q46148, Q798V1
<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: October 7, 2020
Last sequence update: November 1, 1996
Last modified: September 29, 2021
This is version 81 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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