Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8YP80

- FPG_NOSS1

UniProt

Q8YP80 - FPG_NOSS1

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.UniRule annotation

Catalytic activityi

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.UniRule annotation
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNAUniRule annotation
Active sitei3 – 31Proton donorUniRule annotation
Active sitei60 – 601Proton donor; for beta-elimination activityUniRule annotation
Binding sitei100 – 1001DNAUniRule annotation
Binding sitei119 – 1191DNAUniRule annotation
Binding sitei164 – 1641DNAUniRule annotation
Active sitei273 – 2731Proton donor; for delta-elimination activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri249 – 28335FPG-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. oxidized purine nucleobase lesion DNA N-glycosylase activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. base-excision repair Source: InterPro
  2. nucleotide-excision repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Formamidopyrimidine-DNA glycosylaseUniRule annotation (EC:3.2.2.23UniRule annotation)
Short name:
Fapy-DNA glycosylaseUniRule annotation
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutMUniRule annotation (EC:4.2.99.18UniRule annotation)
Short name:
AP lyase MutMUniRule annotation
Gene namesi
Name:mutMUniRule annotation
Synonyms:fpgUniRule annotation
Ordered Locus Names:alr4320
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
ProteomesiUP000002483: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 283282Formamidopyrimidine-DNA glycosylasePRO_0000170806Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi103690.alr4320.

Structurei

3D structure databases

ProteinModelPortaliQ8YP80.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation
Contains 1 FPG-type zinc finger.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri249 – 28335FPG-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000020884.
KOiK10563.
OMAiHTRIRFF.
OrthoDBiEOG6QP131.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsiTIGR00577. fpg. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8YP80-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPELPEVETV RRGLNQLTLN RKITGGDVLL HRTIAHPFSV GDFLNGITGS
60 70 80 90 100
TISTWHRRGK YLLAELSASP STTSIPWLGV HLRMTGQLLW LNQDEPLHKH
110 120 130 140 150
TRVRIFFEEE QELRFVDQRT FGQMWWVPPG IAVESVITGL AKLAVDPFSP
160 170 180 190 200
EFTVEYLANK LHNRRRPIKT ALLDQSVVAG LGNIYADEAL FKSGVLPETL
210 220 230 240 250
CTEVQLKQIK LLRTAIIQVL ETSIEAGGTT FSNFLNVKGV NGNYGGVAWV
260 270 280
YNRAGEPCKV CGDVIQRIKL GGRSSHFCRQ CQV
Length:283
Mass (Da):31,617
Last modified:January 23, 2007 - v3
Checksum:iB913C26375DD5CFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000019 Genomic DNA. Translation: BAB76019.1.
PIRiAI2345.
RefSeqiNP_488360.1. NC_003272.1.
WP_010998458.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB76019; BAB76019; BAB76019.
GeneIDi1107922.
KEGGiana:alr4320.
PATRICi22779210. VBINosSp37423_5052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000019 Genomic DNA. Translation: BAB76019.1 .
PIRi AI2345.
RefSeqi NP_488360.1. NC_003272.1.
WP_010998458.1. NC_003272.1.

3D structure databases

ProteinModelPortali Q8YP80.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 103690.alr4320.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB76019 ; BAB76019 ; BAB76019 .
GeneIDi 1107922.
KEGGi ana:alr4320.
PATRICi 22779210. VBINosSp37423_5052.

Phylogenomic databases

eggNOGi COG0266.
HOGENOMi HOG000020884.
KOi K10563.
OMAi HTRIRFF.
OrthoDBi EOG6QP131.

Family and domain databases

HAMAPi MF_00103. Fapy_DNA_glycosyl.
InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view ]
Pfami PF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view ]
SMARTi SM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view ]
SUPFAMi SSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsi TIGR00577. fpg. 1 hit.
PROSITEi PS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576.

Entry informationi

Entry nameiFPG_NOSS1
AccessioniPrimary (citable) accession number: Q8YP80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3