UDGA_SACS2
ID UDGA_SACS2 Reviewed; 216 AA.
AC Q97WF1;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000305};
DE EC=3.2.2.27 {ECO:0000269|PubMed:15588253};
DE AltName: Full=UDG1 {ECO:0000303|PubMed:15588253};
GN Name=udg1 {ECO:0000303|PubMed:15588253};
GN OrderedLocusNames=SSO2275 {ECO:0000312|EMBL:AAK42437.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INTERACTION WITH PCNA3.
RX PubMed=15588253; DOI=10.1042/bj20041661;
RA Dionne I., Bell S.D.;
RT "Characterization of an archaeal family 4 uracil DNA glycosylase and its
RT interaction with PCNA and chromatin proteins.";
RL Biochem. J. 387:859-863(2005).
CC -!- FUNCTION: Removes uracil bases that are present in DNA as a result of
CC either deamination of cytosine or misincorporation of dUMP instead of
CC dTMP. Can remove uracil from double-stranded DNA containing either a
CC U/G or U/A base pair as well as from single-stranded DNA.
CC {ECO:0000269|PubMed:15588253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC Evidence={ECO:0000269|PubMed:15588253};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:15588253};
CC -!- SUBUNIT: Interacts with the sliding clamp PCNA3 subunit.
CC {ECO:0000269|PubMed:15588253}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC Type 4 (UDGa) family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42437.1; -; Genomic_DNA.
DR PIR; F90397; F90397.
DR RefSeq; WP_009991844.1; NC_002754.1.
DR AlphaFoldDB; Q97WF1; -.
DR SMR; Q97WF1; -.
DR STRING; 273057.SSO2275; -.
DR EnsemblBacteria; AAK42437; AAK42437; SSO2275.
DR GeneID; 44128006; -.
DR KEGG; sso:SSO2275; -.
DR PATRIC; fig|273057.12.peg.2367; -.
DR eggNOG; arCOG00905; Archaea.
DR HOGENOM; CLU_044815_1_3_2; -.
DR InParanoid; Q97WF1; -.
DR OMA; RPWLIAE; -.
DR PhylomeDB; Q97WF1; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR Gene3D; 3.40.470.10; -; 1.
DR InterPro; IPR005273; Ura-DNA_glyco_family4.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR TIGRFAMs; TIGR00758; UDG_fam4; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; DNA damage; DNA repair; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome.
FT CHAIN 1..216
FT /note="Type-4 uracil-DNA glycosylase"
FT /id="PRO_0000439185"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 41..43
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 55
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 82
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
FT BINDING 164
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q5SKC5"
SQ SEQUENCE 216 AA; 24498 MW; 10C6122573C245DB CRC64;
MDNLDLIADE VRKCQKCKLW KFRKNAVPGE GNSKAEIMFI GEAPGENEDI EGKPFVGVAG
KLLTRLINEI LGLSREDVFI TNLVKCRPPN NRDPEEDEIL ACSPYLTRQI ESIRPHIIIT
LGRHSTSYLF KKMNMKMESI GKVRGKFYTW NIYGYKILVF PTYHPAAALY NPPIRKVLEE
DFRKVKEALS SKPITLDNFL YGSGDKGEKG NSNSGK
