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UniProtKB - P30573 (CHS3_CANAX)

Entry version 99 (29 Sep 2021)
Sequence version 1 (01 Apr 1993)
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Protein

Chitin synthase 3

Gene

CHS3

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score:

Annotation score:4 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>-Protein inferred from homologyi <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

Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.

Curated

<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>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
Biological processCell wall biogenesis/degradation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.1.16, 1096

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GT2, Glycosyltransferase Family 2

<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:
Chitin synthase 3 (EC:2.4.1.16)
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase 3
Class-IV chitin synthase 3
<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:CHS3
<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>OrganismiCandida albicans (Yeast)
<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 identifieri5476 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Candida/Lodderomyces clade › Candida

Organism-specific databases

Candida Genome Database

More...CGDi		CAL0000195982, CHS3

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:C1_13110C_A
FungiDB:CAWG_00138

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 168CytoplasmicCuratedAdd BLAST168
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei169 – 189HelicalSequence analysisAdd BLAST21
Topological domaini190 – 200ExtracellularCuratedAdd BLAST11
Transmembranei201 – 221HelicalSequence analysisAdd BLAST21
Topological domaini222 – 450CytoplasmicCuratedAdd BLAST229
Transmembranei451 – 471HelicalSequence analysisAdd BLAST21
Topological domaini472 – 1016ExtracellularCuratedAdd BLAST545
Transmembranei1017 – 1037HelicalSequence analysisAdd BLAST21
Topological domaini1038 – 1039CytoplasmicCurated2
Transmembranei1040 – 1060HelicalSequence analysisAdd BLAST21
Topological domaini1061 – 1065ExtracellularCurated5
Transmembranei1066 – 1086HelicalSequence analysisAdd BLAST21
Topological domaini1087 – 1213CytoplasmicCuratedAdd BLAST127

Keywords - Cellular componenti

Cell membrane, Membrane

<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

Miscellaneous databases

Pathogen-Host Interaction database

More...PHI-basei		PHI:31
PHI:7234

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2366568

<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_00001936881 – 1213Chitin synthase 3Add BLAST1213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi588N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi1008N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

Keywords - PTMi

Glycoprotein

<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

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P30573

<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

<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

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 – 97DisorderedSequence analysisAdd BLAST97
Regioni1161 – 1213DisorderedSequence analysisAdd BLAST53

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi11 – 45Basic and acidic residuesSequence analysisAdd BLAST35
Compositional biasi47 – 88Polar residuesSequence analysisAdd BLAST42
Compositional biasi1169 – 1189Polar residuesSequence analysisAdd BLAST21
Compositional biasi1198 – 1213Polar residuesSequence analysisAdd BLAST16

<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 chitin synthase family. Class IV subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

Database for complete collections of gene phylogenies

More...PhylomeDBi		P30573

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.550.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004835, Chitin_synth
IPR029044, Nucleotide-diphossugar_trans

The PANTHER Classification System

More...PANTHERi		PTHR22914, PTHR22914, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53448, SSF53448, 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.

P30573-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNFRDSSSP RRGYSEFDPE SGEGLGRKKS LIRPERSRMD ESHPRFHYTQ 
        60         70         80         90        100
VANQESNHIK VQPSSTGVDP RKSNELSTSR SHLSNYATPP HQEEEEDEGI 
       110        120        130        140        150
PLMDIHNASP NVSSDQNNDL KGGREVYGLN DEINDYGSSP KKNQVISSSR 
       160        170        180        190        200
PMNNEKPAKP KHDIYFWKVY CYAITFWAPA PLLKLFGLPT KDRQFAWREK 
       210        220        230        240        250
IGLISCILYV GAFVAYLTFG FTKTVCSSQV VRTQINHVNG GYLIINGRAY 
       260        270        280        290        300
DLTSSQHPKA AGIQAGSNVL YPPMNAGGKD ASFLFQNVNG NCKGLIKPRD 
       310        320        330        340        350
NCSIPYDGDE LAWYMPCRLF NQDGSTKPNN TFAYYKGWAC HTSETARDAY 
       360        370        380        390        400
YKLKVNGDVY FTWDDVKNSS RNLVVYSGNV LDLDLINWIE TDDVTYPELF 
       410        420        430        440        450
DKLRDDETYR GLDISLVLTN SEERQAARCL TEIIKVGSID TDTIGCIASK 
       460        470        480        490        500
VVLYMSLVFI LSVVVVKFIM ACWFKWVTSR KQGATMYDSK AWAKRNREIE 
       510        520        530        540        550
DWVDHDHGIG AEVKTVPVKA RANYKAAKTN RQSVFHRAQK LSLGPNADLS 
       560        570        580        590        600
QYYDNPNALS KTFKYTTMST QAALLGRNGY GKRGNNANKS VSGGFNGRQS 
       610        620        630        640        650
NLYLTDQGSS TDLLNRPVSS YNPFDSMGDD SIVINGLSPD IIHPDVVPQP 
       660        670        680        690        700
PVEYQPFGYP LAHTINLVTC YSEDEEGIRI TLDSIATTDY PNSHKLILVI 
       710        720        730        740        750
CDGIIKGSGN DETTPDIVLD MMSDLTVPRD EVEAYSYVAV AQGSKRHNMA 
       760        770        780        790        800
KVYAGFYKYN DETVPPEKQQ RIPMITIVKC GTPEEASAPK PGNRGKRDSQ 
       810        820        830        840        850
IILMSFLQKV VFDERMTSLE YEMLQSIWRI TGLMAEFYEI VLMVDADTKV 
       860        870        880        890        900
FPDSLTHMVA EMVKDPTIMG LCGETKISNK AQTWVTAIQV FEYYISHHQA 
       910        920        930        940        950
KAFESIFGGV TCLPGCFCMY RIKAPKGSDG YWVPILANPD IVERYSDNVV 
       960        970        980        990       1000
DTLHRKNLLL LGEDRYLSSL MLRTFPTRKQ VFVPKAACKT VVPDKFKVLL 
      1010       1020       1030       1040       1050
SQRRRWINST VHNLFELVLV KDLCGTFCFS MQFVIFIELI GTLVLPAAIT 
      1060       1070       1080       1090       1100
FTIYVIIVAI VSKPTPVMSL VLLAVIFGLP GCLIVITVSS LSYLVYFVIY 
      1110       1120       1130       1140       1150
LFALPIWNFV LPSYAYWKFD DFSWGETRTV AGGDKGDHSA VEGKFDSSKI 
      1160       1170       1180       1190       1200
AMKRWREWER ERRSTENRKQ QQQQQLTNNS SNNLAVPGAA WDPSNTGGNL 
      1210 
IDDLSQGSSS GSS
Length:1,213
Mass (Da):136,208
Last modified:April 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:iE6D313EEACD10BC6
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
D13454 Genomic DNA Translation: BAA02707.1

Protein sequence database of the Protein Information Resource

More...PIRi		S39951

<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
D13454 Genomic DNA Translation: BAA02707.1
PIRiS39951

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Chemistry databases

BindingDBiP30573
ChEMBLiCHEMBL2366568

Protein family/group databases

CAZyiGT2, Glycosyltransferase Family 2

Organism-specific databases

CGDiCAL0000195982, CHS3
VEuPathDBiFungiDB:C1_13110C_A
FungiDB:CAWG_00138

Phylogenomic databases

PhylomeDBiP30573

Enzyme and pathway databases

BRENDAi2.4.1.16, 1096

Miscellaneous databases

PHI-baseiPHI:31
PHI:7234

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR004835, Chitin_synth
IPR029044, Nucleotide-diphossugar_trans
PANTHERiPTHR22914, PTHR22914, 1 hit
SUPFAMiSSF53448, SSF53448, 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 nameiCHS3_CANAX
<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: P30573
<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: April 1, 1993
Last sequence update: April 1, 1993
Last modified: September 29, 2021
This is version 99 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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