(data stored in ACNUC7421 zone)

SWISSPROT: E6SFF3_INTC7

ID   E6SFF3_INTC7            Unreviewed;       286 AA.
AC   E6SFF3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   16-JAN-2019, entry version 44.
DE   SubName: Full=DNA-(Apurinic or apyrimidinic site) lyase Formamidopyrimidine-DNA glycosylase {ECO:0000313|EMBL:ADU46691.1};
DE            EC=3.2.2.23 {ECO:0000313|EMBL:ADU46691.1};
DE            EC=4.2.99.18 {ECO:0000313|EMBL:ADU46691.1};
GN   OrderedLocusNames=Intca_0130 {ECO:0000313|EMBL:ADU46691.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46691.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU46691.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
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; CP002343; ADU46691.1; -; Genomic_DNA.
DR   RefSeq; WP_013491013.1; NC_014830.1.
DR   STRING; 710696.Intca_0130; -.
DR   EnsemblBacteria; ADU46691; ADU46691; Intca_0130.
DR   KEGG; ica:Intca_0130; -.
DR   eggNOG; ENOG4105EQC; Bacteria.
DR   eggNOG; COG0266; LUCA.
DR   HOGENOM; HOG000020886; -.
DR   KO; K10563; -.
DR   OrthoDB; 1162346at2; -.
DR   BioCyc; ICAL710696:GH9U-134-MONOMER; -.
DR   Proteomes; UP000008914; 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; E6SFF3.
DR   SWISS-2DPAGE; E6SFF3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
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:ADU46691.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01087030,
KW   ECO:0000313|EMBL:ADU46691.1};
KW   Lyase {ECO:0000256|SAAS:SAAS01087025, ECO:0000313|EMBL:ADU46691.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00551678};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS01087023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914};
KW   Zinc {ECO:0000256|SAAS:SAAS00551670};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00391,
KW   ECO:0000256|SAAS:SAAS00551733}.
FT   DOMAIN        2    119       FPG_CAT. {ECO:0000259|PROSITE:PS51068}.
FT   DOMAIN      237    271       FPG-type. {ECO:0000259|PROSITE:PS51066}.
SQ   SEQUENCE   286 AA;  30891 MW;  BC48AECE1D180FD2 CRC64;
     MPELPEVQAL VDFLAERTAG LAVTKVELAS ISALKTFNPP PQSLEGAPID GVHRHGKFLD
     IDCDGTHLVF HLARAGWLRW SDQLPTTVLR PGKSPIALRV RLSDGSGFDL TEAGTKKSLA
     AYIVRDPKEV PGVARLGPDP LADDFTLERF RELLTGRRTQ IKGLLRDQEV IAGVGNAYSD
     EILHVAKVSP FAIAGSLPPD VVDRLYAALR ETLSSAVHAA SGKPAKELKD AKRAGMRVHA
     RTGQACPECG DVVREVSFAD TSLQYCATCQ TGGKPLADRR MSRLLK
//

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