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Protein

Aprataxin-like protein

Gene

hnt3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species (PubMed:24362567, PubMed:21984208). Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined (PubMed:24362567, PubMed:21984210). Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (PubMed:26007660).Curated3 Publications

Catalytic activityi

(DNA)-3'-diphospho-5'-guanosine + H2O = (DNA)-3'-phosphate + GMP.1 Publication
Adenosine-5'-diphospho-5'-(DNA) + H2O = AMP + phospho-5'-(DNA).2 Publications
Adenosine-5'-diphospho-5'-(ribonucleotide)-(DNA) + H2O = AMP + 5'-phospho-(ribonucleotide)-(DNA).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei147Nucleophile2 Publications1
Metal bindingi200ZincCombined sources2 Publications1
Metal bindingi203ZincCombined sources2 Publications1
Metal bindingi217Zinc; via tele nitrogenCombined sources2 Publications1
Metal bindingi221ZincCombined sources2 Publications1

GO - Molecular functioni

  • DNA 5'-adenosine monophosphate hydrolase activity Source: PomBase
  • mismatched DNA binding Source: PomBase
  • single-strand break-containing DNA binding Source: PomBase
  • single-stranded DNA binding Source: PomBase
  • zinc ion binding Source: PomBase

GO - Biological processi

  • DNA repair Source: PomBase

Keywordsi

Molecular functionDNA-binding, Hydrolase
Biological processDNA damage, DNA repair
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Aprataxin-like protein (EC:3.1.11.72 Publications, EC:3.1.12.21 Publication)
Alternative name(s):
Hit family protein 3
Gene namesi
Name:hnt3
ORF Names:SPCC18.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC18.09c.
PomBaseiSPCC18.09c. hnt3.

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi34F → A: Decreased affinity for DNA. 1 Publication1
Mutagenesisi41Y → A: Mildly decreased DNAppG decapping activity. 1 Publication1
Mutagenesisi63D → A: Strongly decreased DNAppG decapping activity. 1 Publication1
Mutagenesisi65F → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi67K → E: Loss of enzyme activity. Strongly reduced affinity for DNA. 1 Publication1
Mutagenesisi130C → A: Decreased affinity for DNA. 1 Publication1
Mutagenesisi138H → A: Decreased enzyme activity. Mildly decreases affinity for DNA. 2 Publications1
Mutagenesisi142S → A or E: Nearly abolishes enzyme activity. Mildly decreases affinity for DNA. 2 Publications1
Mutagenesisi147H → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi147H → N: Loss of enzyme activity. 1 Publication1
Mutagenesisi149H → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi161K → A: Strongly decreases abolishes enzyme activity. Decreased affinity for DNA. 2 Publications1
Mutagenesisi161K → E: Nearly abolishes enzyme activity. Strongly reduced affinity for DNA. 1 Publication1
Mutagenesisi165H → A: Slightly decreased enzyme activity. 1 Publication1
Mutagenesisi165H → E: Nearly abolishes enzyme activity. Strongly reduced affinity for DNA. 1 Publication1
Mutagenesisi168S → A: Decreased enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003146501 – 232Aprataxin-like proteinAdd BLAST232

Proteomic databases

MaxQBiO74859.
PRIDEiO74859.

Interactioni

Subunit structurei

Monomer.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei41Interaction with DNA2 Publications1

Protein-protein interaction databases

BioGridi275769. 3 interactors.
MINTiMINT-4681359.
STRINGi4896.SPCC18.09c.1.

Structurei

Secondary structure

1232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi34 – 38Combined sources5
Helixi39 – 43Combined sources5
Helixi45 – 47Combined sources3
Beta strandi51 – 54Combined sources4
Beta strandi56 – 62Combined sources7
Beta strandi67 – 76Combined sources10
Turni79 – 83Combined sources5
Helixi86 – 92Combined sources7
Helixi94 – 105Combined sources12
Turni106 – 108Combined sources3
Helixi109 – 119Combined sources11
Helixi126 – 130Combined sources5
Beta strandi133 – 140Combined sources8
Beta strandi142 – 145Combined sources4
Beta strandi148 – 153Combined sources6
Helixi163 – 169Combined sources7
Beta strandi174 – 176Combined sources3
Helixi181 – 183Combined sources3
Helixi190 – 192Combined sources3
Helixi193 – 195Combined sources3
Turni201 – 203Combined sources3
Beta strandi206 – 208Combined sources3
Helixi211 – 229Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SP4X-ray1.80A/B33-232[»]
3SPDX-ray1.91A/B/C/D33-232[»]
3SPLX-ray2.10A/B/C/D33-232[»]
3SZQX-ray2.35A31-232[»]
4XBAX-ray1.50A/B33-232[»]
4YKLX-ray2.25B33-232[»]
ProteinModelPortaliO74859.
SMRiO74859.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 160HITAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 67Interaction with DNA3 Publications5
Regioni138 – 149Interaction with DNA3 PublicationsAdd BLAST12
Regioni161 – 165Interaction with DNA3 Publications5
Regioni209 – 212Interaction with DNA3 Publications4

Phylogenomic databases

HOGENOMiHOG000167639.
InParanoidiO74859.
KOiK10863.
OMAiIHAHPSM.
OrthoDBiEOG092C3DRA.
PhylomeDBiO74859.

Family and domain databases

Gene3Di3.30.428.10. 1 hit.
InterProiView protein in InterPro
IPR026963. Aprataxin.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
IPR032566. Znf-C2HE.
PANTHERiPTHR12486:SF7. PTHR12486:SF7. 1 hit.
PfamiView protein in Pfam
PF01230. HIT. 1 hit.
PF16278. zf-C2HE. 1 hit.
SUPFAMiSSF54197. SSF54197. 1 hit.

Sequencei

Sequence statusi: Complete.

O74859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVHKTNDAF KVLMNSAKEP IVEDIPKKYR KQSFRDNLKV YIESPESYKN
60 70 80 90 100
VIYYDDDVVL VRDMFPKSKM HLLLMTRDPH LTHVHPLEIM MKHRSLVEKL
110 120 130 140 150
VSYVQGDLSG LIFDEARNCL SQQLTNEALC NYIKVGFHAG PSMNNLHLHI
160 170 180 190 200
MTLDHVSPSL KNSAHYISFT SPFFVKIDTP TSNLPTRGTL TSLFQEDLKC
210 220 230
WRCGETFGRH FTKLKAHLQE EYDDWLDKSV SM
Length:232
Mass (Da):26,922
Last modified:November 1, 1998 - v1
Checksum:i7B448C953ED13CFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21423.1.
PIRiT41152.
RefSeqiNP_588388.1. NM_001023379.2.

Genome annotation databases

EnsemblFungiiSPCC18.09c.1; SPCC18.09c.1:pep; SPCC18.09c.
GeneIDi2539198.
KEGGispo:SPCC18.09c.

Similar proteinsi

Entry informationi

Entry nameiAPTX_SCHPO
AccessioniPrimary (citable) accession number: O74859
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 1, 1998
Last modified: August 30, 2017
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names