(data stored in SCRATCH zone)

SWISSPROT: Q3IEI2_PSEHT

ID   Q3IEI2_PSEHT            Unreviewed;       258 AA.
AC   Q3IEI2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 94.
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000256|SAAS:SAAS00635501};
DE            EC=3.2.2.- {ECO:0000256|SAAS:SAAS00643393};
DE            EC=3.2.2.23 {ECO:0000256|SAAS:SAAS00635500};
DE            EC=4.2.99.18 {ECO:0000256|SAAS:SAAS00643413};
GN   Name=mutM {ECO:0000313|EMBL:CAI85544.1};
GN   OrderedLocusNames=PSHAa0447 {ECO:0000313|EMBL:CAI85544.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85544.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85544.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC       oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC       recognizes and removes damaged bases. Has a preference for
CC       oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has
CC       AP (apurinic/apyrimidinic) lyase activity and introduces nicks in
CC       the DNA strand. Cleaves the DNA backbone by beta-delta elimination
CC       to generate a single-strand break at the site of the removed base
CC       with both 3'- and 5'-phosphates. {ECO:0000256|SAAS:SAAS00635477}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
CC       methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC       methyl)formamidopyrimidine. {ECO:0000256|SAAS:SAAS00635490}.
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate. {ECO:0000256|SAAS:SAAS00643435}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS00643423};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|SAAS:SAAS00635466}.
CC   -!- SIMILARITY: Belongs to the FPG family.
CC       {ECO:0000256|SAAS:SAAS00643420}.
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DR   EMBL; CR954246; CAI85544.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3IEI2; -.
DR   STRING; 326442.PSHAa0447; -.
DR   EnsemblBacteria; CAI85544; CAI85544; PSHAa0447.
DR   KEGG; pha:PSHAa0447; -.
DR   eggNOG; ENOG4105ERD; Bacteria.
DR   eggNOG; COG0266; LUCA.
DR   HOGENOM; HOG000020881; -.
DR   KO; K10563; -.
DR   OMA; RNSRLRW; -.
DR   OrthoDB; POG091H01RH; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR   InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   SUPFAM; SSF81624; SSF81624; 1.
DR   TIGRFAMs; TIGR00577; fpg; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS01242; ZF_FPG_1; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IEI2.
DR   SWISS-2DPAGE; Q3IEI2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   DNA damage {ECO:0000256|SAAS:SAAS00643418};
KW   DNA repair {ECO:0000256|SAAS:SAAS00643382};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00643405};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00643419,
KW   ECO:0000313|EMBL:CAI85544.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00643430,
KW   ECO:0000313|EMBL:CAI85544.1}; Lyase {ECO:0000256|SAAS:SAAS00643421};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00640292};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS00643397};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Zinc {ECO:0000256|SAAS:SAAS00640325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00391,
KW   ECO:0000256|SAAS:SAAS00640308}.
FT   DOMAIN        1    101       FPG_CAT. {ECO:0000259|PROSITE:PS51068}.
FT   DOMAIN      224    258       FPG-type. {ECO:0000259|PROSITE:PS51066}.
SQ   SEQUENCE   258 AA;  28468 MW;  0219839342BFECD5 CRC64;
     MGITPHVLNQ VVTKVNIHNG SMRWPVPDDV YQLTGLTVTG VERRAKYLLL HCALGSTILH
     LGMSGNLRVV SANEPLKKHD HIEFIFANGK ALRLNDPRRF GCCLWQAPGS VHKLLAKLGP
     EPLTDEFFAK QVYQQSRNKK VPVKQFIMNN AIVVGVGNIY ANESLFKAGI DPRREAGKVS
     LKSFEALIPI IKDTLAAAIT QGGTTLKDFA QSDGKPGYFA QQLLVYGRKG QPCLVCKSEL
     QEVRLGQRST VFCGKCQK
//

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