(data stored in ACNUC1104 zone)

SWISSPROT: A1SD17_NOCSJ

ID   A1SD17_NOCSJ            Unreviewed;       288 AA.
AC   A1SD17;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   SubName: Full=DNA-(Apurinic or apyrimidinic site) lyase / Formamidopyrimidine-DNA glycosylase {ECO:0000313|EMBL:ABL79702.1};
DE            EC=3.2.2.23 {ECO:0000313|EMBL:ABL79702.1};
DE            EC=4.2.99.18 {ECO:0000313|EMBL:ABL79702.1};
GN   OrderedLocusNames=Noca_0157 {ECO:0000313|EMBL:ABL79702.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79702.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL79702.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in
CC         DNA is broken by a beta-elimination reaction, leaving a 3'-
CC         terminal unsaturated sugar and a product with a terminal 5'-
CC         phosphate.; EC=4.2.99.18;
CC         Evidence={ECO:0000256|SAAS:SAAS01121890};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|SAAS:SAAS00610166};
CC   -!- SIMILARITY: Belongs to the FPG family.
CC       {ECO:0000256|SAAS:SAAS00557294}.
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DR   EMBL; CP000509; ABL79702.1; -; Genomic_DNA.
DR   RefSeq; WP_011753653.1; NC_008699.1.
DR   STRING; 196162.Noca_0157; -.
DR   EnsemblBacteria; ABL79702; ABL79702; Noca_0157.
DR   KEGG; nca:Noca_0157; -.
DR   eggNOG; ENOG4105EQC; Bacteria.
DR   eggNOG; COG0266; LUCA.
DR   HOGENOM; HOG000020886; -.
DR   KO; K10563; -.
DR   OMA; LQYCPTC; -.
DR   OrthoDB; 1162346at2; -.
DR   BioCyc; NSP196162:GH4V-156-MONOMER; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
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   Gene3D; 3.20.190.10; -; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
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   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SD17.
DR   SWISS-2DPAGE; A1SD17.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   DNA damage {ECO:0000256|SAAS:SAAS01087016};
KW   DNA repair {ECO:0000256|SAAS:SAAS01087019};
KW   DNA-binding {ECO:0000256|SAAS:SAAS01087047};
KW   Glycosidase {ECO:0000256|SAAS:SAAS01087011,
KW   ECO:0000313|EMBL:ABL79702.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01087030,
KW   ECO:0000313|EMBL:ABL79702.1};
KW   Lyase {ECO:0000256|SAAS:SAAS01087025, ECO:0000313|EMBL:ABL79702.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00551678};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS01087023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   Zinc {ECO:0000256|SAAS:SAAS00551670};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00391,
KW   ECO:0000256|SAAS:SAAS00551733}.
FT   DOMAIN        2    120       FPG_CAT. {ECO:0000259|PROSITE:PS51068}.
FT   DOMAIN      239    273       FPG-type. {ECO:0000259|PROSITE:PS51066}.
SQ   SEQUENCE   288 AA;  31083 MW;  1106D459162AC567 CRC64;
     MPELPEVEAL ALDLRGRLDG HAIAKIHVAA FSALKTFDPP LSALEGTLVD DVTRHGKFLD
     IEASGLHLVL HLARAGWVRW RDEVPTIPPK PSTKSTLAVR IVLDDQSGLD VTEAGTRKSL
     AMYVVRDPHD VPGIASLGPD PLTDEFTIDR LREILEREGR KQLKGVLRHQ GTIAGIGNAY
     SDEILHAARM SPFKAAGTLT DDELQVLYDA LRGTLGDAVG RSRGLAASEL KGEKKSHLAV
     HGRAGQACPV CGDTVREVSF ADSSLQYCPT CQTGGKPLAD RRLSKLLK
//

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