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Entry version 146 (16 Oct 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Adenine DNA glycosylase

Gene

myh1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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

Adenine glycosylase active on G-A mispairs. Has glycosylase and nicking activities and is active at A/G and A/GO sites.1 Publication

<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

  • Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site. EC:3.2.2.31

<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

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei69Proton donor/acceptorBy similarity1
<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>Sitei172Transition state stabilizerBy 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 bindingi226Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi233Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi236Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi242Iron-sulfur (4Fe-4S)By 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 functionGlycosidase, Hydrolase
Biological processDNA damage, DNA repair
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SPO-110331 Cleavage of the damaged purine

<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:
Adenine DNA glycosylase (EC:3.2.2.31)
<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:myh1
Synonyms:myh
ORF Names:SPAC26A3.02
<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>OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
<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 identifieri284812 [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 lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000002485 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 I

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:SPAC26A3.02

Schizosaccharomyces pombe database

More...
PomBasei
SPAC26A3.02 myh1

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001022421 – 461Adenine DNA glycosylaseAdd BLAST461

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q10159

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q10159

PRoteomics IDEntifications database

More...
PRIDEi
Q10159

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
279177, 18 interactors

Protein interaction database and analysis system

More...
IntActi
Q10159, 4 interactors

STRING: functional protein association networks

More...
STRINGi
4896.SPAC26A3.02.1

<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
Q10159

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

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>Domaini296 – 437Nudix hydrolaseAdd BLAST142

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi340 – 366Nudix boxAdd BLAST27

<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 Nth/MutY family.Curated

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q10159

KEGG Orthology (KO)

More...
KOi
K03575

Identification of Orthologs from Complete Genome Data

More...
OMAi
KRWPTVQ

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q10159

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03431 DNA_Glycosylase_C, 1 hit
cd00056 ENDO3c, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1670.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011257 DNA_glycosylase
IPR004036 Endonuclease-III-like_CS2
IPR003651 Endonuclease3_FeS-loop_motif
IPR004035 Endouclease-III_FeS-bd_BS
IPR003265 HhH-GPD_domain
IPR000445 HhH_motif
IPR023170 HTH_base_excis_C
IPR029119 MutY_C
IPR015797 NUDIX_hydrolase-like_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10576 EndIII_4Fe-2S, 1 hit
PF00633 HHH, 1 hit
PF00730 HhH-GPD, 1 hit
PF14815 NUDIX_4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00478 ENDO3c, 1 hit
SM00525 FES, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48150 SSF48150, 1 hit
SSF55811 SSF55811, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00764 ENDONUCLEASE_III_1, 1 hit
PS01155 ENDONUCLEASE_III_2, 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_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.

Q10159-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDSNHSLDL HSYTQLEVER FRESLIQFYD KTKRILPWRK KECIPPSEDS
60 70 80 90 100
PLEDWEQPVQ RLYEVLVSEI MLQQTRVETV KRYYTKWMET LPTLKSCAEA
110 120 130 140 150
EYNTQVMPLW SGMGFYTRCK RLHQACQHLA KLHPSEIPRT GDEWAKGIPG
160 170 180 190 200
VGPYTAGAVL SIAWKQPTGI VDGNVIRVLS RALAIHSDCS KGKANALIWK
210 220 230 240 250
LANELVDPVR PGDFNQALME LGAITCTPQS PRCSVCPISE ICKAYQEQNV
260 270 280 290 300
IRDGNTIKYD IEDVPCNICI TDIPSKEDLQ NWVVARYPVH PAKTKQREER
310 320 330 340 350
ALVVIFQKTD PSTKEKFFLI RKRPSAGLLA GLWDFPTIEF GQESWPKDMD
360 370 380 390 400
AEFQKSIAQW ISNDSRSLIK KYQSRGRYLH IFSHIRKTSH VFYAIASPDI
410 420 430 440 450
VTNEDFFWIS QSDLEHVGMC ELGLKNYRAA LEIKKRKVTS LSNFKEPKLT
460
SARRIVTKAE C
Length:461
Mass (Da):52,931
Last modified:October 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:i5908E880202E2242
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti7S → F in AAC36207 (PubMed:9737967).Curated1

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
AF053340 mRNA Translation: AAC36207.1
CU329670 Genomic DNA Translation: CAA93225.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T38390
T43679

NCBI Reference Sequences

More...
RefSeqi
NP_594145.1, NM_001019569.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPAC26A3.02.1; SPAC26A3.02.1:pep; SPAC26A3.02

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2542727

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPAC26A3.02

<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
AF053340 mRNA Translation: AAC36207.1
CU329670 Genomic DNA Translation: CAA93225.1
PIRiT38390
T43679
RefSeqiNP_594145.1, NM_001019569.2

3D structure databases

SMRiQ10159
ModBaseiSearch...

Protein-protein interaction databases

BioGridi279177, 18 interactors
IntActiQ10159, 4 interactors
STRINGi4896.SPAC26A3.02.1

Proteomic databases

MaxQBiQ10159
PaxDbiQ10159
PRIDEiQ10159

Genome annotation databases

EnsemblFungiiSPAC26A3.02.1; SPAC26A3.02.1:pep; SPAC26A3.02
GeneIDi2542727
KEGGispo:SPAC26A3.02

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.02
PomBaseiSPAC26A3.02 myh1

Phylogenomic databases

InParanoidiQ10159
KOiK03575
OMAiKRWPTVQ
PhylomeDBiQ10159

Enzyme and pathway databases

ReactomeiR-SPO-110331 Cleavage of the damaged purine

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q10159

Family and domain databases

CDDicd03431 DNA_Glycosylase_C, 1 hit
cd00056 ENDO3c, 1 hit
Gene3Di1.10.1670.10, 1 hit
InterProiView protein in InterPro
IPR011257 DNA_glycosylase
IPR004036 Endonuclease-III-like_CS2
IPR003651 Endonuclease3_FeS-loop_motif
IPR004035 Endouclease-III_FeS-bd_BS
IPR003265 HhH-GPD_domain
IPR000445 HhH_motif
IPR023170 HTH_base_excis_C
IPR029119 MutY_C
IPR015797 NUDIX_hydrolase-like_dom_sf
PfamiView protein in Pfam
PF10576 EndIII_4Fe-2S, 1 hit
PF00633 HHH, 1 hit
PF00730 HhH-GPD, 1 hit
PF14815 NUDIX_4, 1 hit
SMARTiView protein in SMART
SM00478 ENDO3c, 1 hit
SM00525 FES, 1 hit
SUPFAMiSSF48150 SSF48150, 1 hit
SSF55811 SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS00764 ENDONUCLEASE_III_1, 1 hit
PS01155 ENDONUCLEASE_III_2, 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 nameiMYH1_SCHPO
<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: Q10159
Secondary accession number(s): O74679
<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 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2019
This is version 146 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
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