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UniProtKB - P0C956 (GEL4_ASPFU)

Entry version 66 (23 Feb 2022)
Sequence version 1 (05 May 2009)
Previous versions | rss
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Protein

1,3-beta-glucanosyltransferase gel4

Gene

gel4

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis (By similarity).

By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei1061,3-beta-glucan 1; donor substrate; via carbonyl oxygenBy similarity1
Binding sitei1741,3-beta-glucan 1; donor substrateBy 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 sitei175Proton donorBy similarity1
Binding sitei1751,3-beta-glucan 2; acceptor substrateBy similarity1
Binding sitei2171,3-beta-glucan 2; acceptor substrate; via carbonyl oxygenBy similarity1
Binding sitei2221,3-beta-glucan 2; acceptor substrateBy similarity1
Active sitei277NucleophileBy similarity1
Binding sitei3091,3-beta-glucan 1; donor substrateBy 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

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 functionTransferase

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		CBM43, Carbohydrate-Binding Module Family 43
GH72, Glycoside Hydrolase Family 72

<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:
1,3-beta-glucanosyltransferase gel4 (EC:2.4.1.-)
Alternative name(s):
Glucan elongating glucanosyltransferase 4
<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:gel4
ORF Names:AFUA_2G05340
<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>OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
<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 identifieri330879 [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 › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Fumigati ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002530 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

<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

Cell membrane, Membrane

<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 – 25Sequence analysisAdd BLAST25
<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_000024555326 – 5191,3-beta-glucanosyltransferase gel4Add BLAST494
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000245554520 – 548Removed in mature formSequence analysisAdd BLAST29

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>Glycosylationi51N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi69N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi88 ↔ 117By similarity
Glycosylationi181N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi231 ↔ 364By similarity
Disulfide bondi249 ↔ 280By similarity
Disulfide bondi386 ↔ 437By similarity
Disulfide bondi395 ↔ 461By similarity
Disulfide bondi414 ↔ 419By similarity
Glycosylationi425N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi519GPI-like-anchor amidated alanineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

The GPI-like anchor contains a phosphoceramide lipid group.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P0C956

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		746128.CADAFUBP00002184

<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

3D structure databases

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

More...SMRi		P0C956

Database of comparative protein structure models

More...ModBasei		Search...

<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>Regioni133 – 1411,3-beta-glucan 1 binding; donor substrateBy similarity9

<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 72 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QPST, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_021855_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0C956

Identification of Orthologs from Complete Genome Data

More...OMAi		CATQMSA

Database of Orthologous Groups

More...OrthoDBi		728071at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004886, Glucanosyltransferase
IPR017853, Glycoside_hydrolase_SF
IPR012946, X8

The PANTHER Classification System

More...PANTHERi		PTHR31468, PTHR31468, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03198, Glyco_hydro_72, 1 hit
PF07983, X8, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00768, X8, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51445, SSF51445, 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.

P0C956-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKFVYAAAGA SLVGSALATL PVIEAKVLKA CCWTIALDAN SYGNKFFYSN 
        60         70         80         90        100
NGTEFFIRGV AYQQEYQANG TSTENSDYTD PLANVDNCKR DIPYLKQLRT 
       110        120        130        140        150
NVIRTYAVDP TKDHDECMKL LDDAGIYLIT DLSAPSESIN RADPAWNTDL 
       160        170        180        190        200
YKRYTSVIDA FAKYSNVIGF FAGNEVANDN NNTNSIAYVK AAVRDMKSYI 
       210        220        230        240        250
KSKDYRSSLL VGYATDDDAH IRADLADYLV CGDKESSIDM FGYNIYEWCG 
       260        270        280        290        300
DSSFEKSGYK DRTEEFSKYP VPAFFSEYGC IDPKPRKFTD VAALYGPQMN 
       310        320        330        340        350
DVWSGGIVYM YFQEANDYGL VSVSGDNVKT KEDFSYLSVQ MQKVTATGVN 
       360        370        380        390        400
SASYTASNTA VPTCPSVGAK WEASNKLPPS PNSELCDCMV ETLSCTVKDS 
       410        420        430        440        450
VDEKEYGDLF DYLCAAGVCG GINSNSTSGD YGAYSVCSAK QKLSFVMNQY 
       460        470        480        490        500
YKKNNKAATA CDFDGKAQTK KGADASGSCA SLISQAGTAG TGSVTAGATG 
       510        520        530        540 
SSGSGSASET SKGAAGVAAS PMAVKVGNWQ FGAYIATALF AGVGMLVL
Length:548
Mass (Da):58,873
Last modified:May 5, 2009 - 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:i191DA9A1D29778FE
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
AAHF01000008 Genomic DNA Translation: EAL87626.1

NCBI Reference Sequences

More...RefSeqi		XP_749664.1, XM_744571.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		EAL87626; EAL87626; AFUA_2G05340

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3506753

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		afm:AFUA_2G05340

<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
AAHF01000008 Genomic DNA Translation: EAL87626.1
RefSeqiXP_749664.1, XM_744571.1

3D structure databases

SMRiP0C956
ModBaseiSearch...

Protein-protein interaction databases

STRINGi746128.CADAFUBP00002184

Protein family/group databases

CAZyiCBM43, Carbohydrate-Binding Module Family 43
GH72, Glycoside Hydrolase Family 72

Proteomic databases

PRIDEiP0C956

Genome annotation databases

EnsemblFungiiEAL87626; EAL87626; AFUA_2G05340
GeneIDi3506753
KEGGiafm:AFUA_2G05340

Phylogenomic databases

eggNOGiENOG502QPST, Eukaryota
HOGENOMiCLU_021855_2_1_1
InParanoidiP0C956
OMAiCATQMSA
OrthoDBi728071at2759

Family and domain databases

InterProiView protein in InterPro
IPR004886, Glucanosyltransferase
IPR017853, Glycoside_hydrolase_SF
IPR012946, X8
PANTHERiPTHR31468, PTHR31468, 1 hit
PfamiView protein in Pfam
PF03198, Glyco_hydro_72, 1 hit
PF07983, X8, 1 hit
SMARTiView protein in SMART
SM00768, X8, 1 hit
SUPFAMiSSF51445, SSF51445, 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 nameiGEL4_ASPFU
<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: P0C956
Secondary accession number(s): Q4WHH9
<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: May 5, 2009
Last sequence update: May 5, 2009
Last modified: February 23, 2022
This is version 66 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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