(data stored in SCRATCH zone)

SWISSPROT: C6WF92_ACTMD

ID   C6WF92_ACTMD            Unreviewed;       257 AA.
AC   C6WF92;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942};
DE            EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942};
GN   Name=nth {ECO:0000256|HAMAP-Rule:MF_00942};
GN   OrderedLocusNames=Amir_0255 {ECO:0000313|EMBL:ACU34224.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34224.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34224.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase
CC       activity and AP-lyase activity. The DNA N-glycosylase activity
CC       releases various damaged pyrimidines from DNA by cleaving the N-
CC       glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The
CC       AP-lyase activity cleaves the phosphodiester bond 3' to the AP
CC       site by a beta-elimination, leaving a 3'-terminal unsaturated
CC       sugar and a product with a terminal 5'-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00942}.
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|HAMAP-Rule:MF_00942}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00942};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942};
CC   -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000256|HAMAP-
CC       Rule:MF_00942}.
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DR   EMBL; CP001630; ACU34224.1; -; Genomic_DNA.
DR   STRING; 446462.Amir_0255; -.
DR   EnsemblBacteria; ACU34224; ACU34224; Amir_0255.
DR   KEGG; ami:Amir_0255; -.
DR   eggNOG; ENOG4105CSM; Bacteria.
DR   eggNOG; COG0177; LUCA.
DR   HOGENOM; HOG000252208; -.
DR   KO; K10773; -.
DR   OMA; KAKNPLC; -.
DR   OrthoDB; POG091H021U; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; -; 1.
DR   HAMAP; MF_00942; Nth; 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR004036; Endonuclease-III-like_CS2.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR023170; HTH_base_excis_C.
DR   InterPro; IPR005759; Nth.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; SSF48150; 1.
DR   TIGRFAMs; TIGR01083; nth; 1.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WF92.
DR   SWISS-2DPAGE; C6WF92.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00942};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00942};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Endonuclease {ECO:0000313|EMBL:ACU34224.1};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:ACU34224.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942};
KW   Nuclease {ECO:0000313|EMBL:ACU34224.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   DOMAIN       53    200       ENDO3c. {ECO:0000259|SMART:SM00478}.
FT   METAL       202    202       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       209    209       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       212    212       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
FT   METAL       218    218       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00942}.
SQ   SEQUENCE   257 AA;  27839 MW;  96B075A7DCFA0A7F CRC64;
     MVGGARGGAR PETRLGLVRR ARRTVRVLGV GYPDAHCELD FTTPLELLVA VVLSAQCTDK
     RVNQVTPALF ARYRSAEEYA AADRTELEEL VRPTGFYRNK AAAISGLAAE IVERHDGEVP
     GTQAELVKLP GVGRKTANVV LGDAFGVPGI TVDTHFGRLV RRWGWTTEED PVKVEHAVGA
     LVERKDWTLL SHRTIFHGRR VCHARTPACG ACLLAPQCPS FGTGPTDPVR AAKLVKGDEA
     EHLIGLAERV RAGERLG
//

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