NURA_SULTO
ID NURA_SULTO Reviewed; 331 AA.
AC Q96YR4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=DNA double-strand break repair nuclease NurA {ECO:0000305};
DE EC=3.1.-.- {ECO:0000269|PubMed:18194801};
DE AltName: Full=StoNurA {ECO:0000303|PubMed:18194801};
GN Name=nurA {ECO:0000303|PubMed:18194801};
GN OrderedLocusNames=STK_21090 {ECO:0000312|EMBL:BAB67213.1};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SSB.
RX PubMed=18194801; DOI=10.1016/j.bbrc.2007.10.019;
RA Wei T., Zhang S., Zhu S., Sheng D., Ni J., Shen Y.;
RT "Physical and functional interaction between archaeal single-stranded DNA-
RT binding protein and the 5'-3' nuclease NurA.";
RL Biochem. Biophys. Res. Commun. 367:523-529(2008).
RN [3]
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-56; GLU-114; ASP-131; TYR-291 AND
RP HIS-299.
RX PubMed=21197557; DOI=10.1007/s00792-010-0351-2;
RA Wei T., Zhang S., Hou L., Ni J., Sheng D., Shen Y.;
RT "The carboxyl terminal of the archaeal nuclease NurA is involved in the
RT interaction with single-stranded DNA-binding protein and dimer formation.";
RL Extremophiles 15:227-234(2011).
CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair (By
CC similarity). Acts probably with HerA to stimulate resection of the 5'
CC strand and produce the long 3' single-strand that is required for RadA
CC loading (By similarity). Exhibits both single-stranded endonuclease
CC activity and 5'-3' exonuclease activity on single-stranded and double-
CC stranded DNA (PubMed:18194801). {ECO:0000250|UniProtKB:Q8U1N8,
CC ECO:0000269|PubMed:18194801}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8U1N8};
CC -!- ACTIVITY REGULATION: The 5'-3' ssDNA and dsDNA exonuclease and ssDNA
CC endonuclease activities are inhibited by SSB.
CC {ECO:0000269|PubMed:18194801}.
CC -!- SUBUNIT: Homodimer (PubMed:21197557). Interacts with the single-
CC stranded DNA-binding protein (SSB) (PubMed:18194801).
CC {ECO:0000269|PubMed:18194801, ECO:0000269|PubMed:21197557}.
CC -!- DOMAIN: The C-terminus is required for interaction with SSB.
CC {ECO:0000269|PubMed:21197557}.
CC -!- SIMILARITY: Belongs to the NurA family. {ECO:0000305}.
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DR EMBL; BA000023; BAB67213.1; -; Genomic_DNA.
DR RefSeq; WP_010980188.1; NC_003106.2.
DR AlphaFoldDB; Q96YR4; -.
DR SMR; Q96YR4; -.
DR STRING; 273063.STK_21090; -.
DR EnsemblBacteria; BAB67213; BAB67213; STK_21090.
DR GeneID; 1460181; -.
DR KEGG; sto:STK_21090; -.
DR PATRIC; fig|273063.9.peg.2401; -.
DR eggNOG; arCOG00367; Archaea.
DR OMA; YILKKSH; -.
DR OrthoDB; 57919at2157; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR InterPro; IPR018977; NurA_domain.
DR Pfam; PF09376; NurA; 1.
DR SMART; SM00933; NurA; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..331
FT /note="DNA double-strand break repair nuclease NurA"
FT /id="PRO_0000434030"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N8"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8U1N8"
FT MUTAGEN 56
FT /note="D->A: Lack of nuclease activity."
FT /evidence="ECO:0000269|PubMed:21197557"
FT MUTAGEN 114
FT /note="E->A: Lack of nuclease activity."
FT /evidence="ECO:0000269|PubMed:21197557"
FT MUTAGEN 131
FT /note="D->A: Lack of nuclease activity."
FT /evidence="ECO:0000269|PubMed:21197557"
FT MUTAGEN 291
FT /note="Y->A: Strong decrease in nuclease activity. Does not
FT form a stable dimer."
FT /evidence="ECO:0000269|PubMed:21197557"
FT MUTAGEN 299
FT /note="H->A: Lack of nuclease activity."
FT /evidence="ECO:0000269|PubMed:21197557"
SQ SEQUENCE 331 AA; 38016 MW; E0F824C0ED808AE8 CRC64;
MIKDVYELLL SRKNEIEKQI SLLDETSNNL LKEKIKEKWK EYCQTQGKLS TVLAIDGGMW
IKELRSGIVY IVNAEIVKAE GFNVTPIDSK ALIGVLRPGN MAKERVSLLM QLLELKLGLK
HGDKAEYILF DGSIVKKIGK HKFSTKISLL DDIDVMDDKI YSLEENDEEL MHKYLVAENQ
LVMSALISKY KGKLVWISKN SKSTELFQEN ISDVSLLELF TKNCGYTIGI EKKISSENII
SPKASTILSN ASFYSFYTRL KEGEKILKIE MFNNEIENII SILSPISIKG YPYPLLKVHT
DVKVSRQDRE RIKQLLNIKK KDIEWWPSQL F
