位置:首页 > 蛋白库 > NURA_SACS2
NURA_SACS2
ID   NURA_SACS2              Reviewed;         339 AA.
AC   Q97WH1;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=DNA double-strand break repair nuclease NurA {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000305};
GN   Name=nurA {ECO:0000303|PubMed:22135300};
GN   OrderedLocusNames=SSO2248 {ECO:0000312|EMBL:AAK42416.1};
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   SUBUNIT, AND INTERACTION WITH HERA.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=25447518; DOI=10.1016/j.febslet.2014.10.035;
RA   Byrne R.T., Schuller J.M., Unverdorben P., Foerster F., Hopfner K.P.;
RT   "Molecular architecture of the HerA-NurA DNA double-strand break resection
RT   complex.";
RL   FEBS Lett. 588:4637-4644(2014).
RN   [3] {ECO:0007744|PDB:2YGK}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, ACTIVITY REGULATION,
RP   SUBUNIT, INTERACTION WITH HERA, AND MUTAGENESIS OF LYS-202; ILE-295 AND
RP   PHE-300.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=22135300; DOI=10.1093/nar/gkr1157;
RA   Blackwood J.K., Rzechorzek N.J., Abrams A.S., Maman J.D., Pellegrini L.,
RA   Robinson N.P.;
RT   "Structural and functional insights into DNA-end processing by the archaeal
RT   HerA helicase-NurA nuclease complex.";
RL   Nucleic Acids Res. 40:3183-3196(2012).
CC   -!- FUNCTION: Involved in DNA double-strand break (DSB) repair
CC       (PubMed:22135300). Acts probably with HerA to stimulate resection of
CC       the 5' strand and produce the long 3' single-strand that is required
CC       for RadA loading (By similarity). Processes linear dsDNA probes with 3'
CC       or 5' single-stranded overhangs or blunt ends (PubMed:22135300).
CC       {ECO:0000250|UniProtKB:Q8U1N8, ECO:0000269|PubMed:22135300}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q8U1N8};
CC   -!- ACTIVITY REGULATION: Nuclease activity requires the presence of HerA.
CC       {ECO:0000269|PubMed:22135300}.
CC   -!- SUBUNIT: Homodimer (PubMed:22135300, PubMed:25447518). Forms a complex
CC       with HerA (PubMed:22135300, PubMed:25447518).
CC       {ECO:0000269|PubMed:22135300, ECO:0000269|PubMed:25447518}.
CC   -!- INTERACTION:
CC       Q97WH1; Q97WG8: herA; NbExp=3; IntAct=EBI-10110462, EBI-10110451;
CC   -!- SIMILARITY: Belongs to the NurA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006641; AAK42416.1; -; Genomic_DNA.
DR   PIR; A90395; A90395.
DR   RefSeq; WP_009991544.1; NC_002754.1.
DR   PDB; 2YGK; X-ray; 2.50 A; A/B=1-339.
DR   PDBsum; 2YGK; -.
DR   AlphaFoldDB; Q97WH1; -.
DR   SMR; Q97WH1; -.
DR   IntAct; Q97WH1; 1.
DR   MINT; Q97WH1; -.
DR   STRING; 273057.SSO2248; -.
DR   EnsemblBacteria; AAK42416; AAK42416; SSO2248.
DR   GeneID; 44127982; -.
DR   KEGG; sso:SSO2248; -.
DR   PATRIC; fig|273057.12.peg.2343; -.
DR   eggNOG; arCOG00367; Archaea.
DR   HOGENOM; CLU_835811_0_0_2; -.
DR   InParanoid; Q97WH1; -.
DR   OMA; YILKKSH; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; 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   3D-structure; DNA damage; DNA repair; Hydrolase; Manganese; Metal-binding;
KW   Nuclease; Reference proteome.
FT   CHAIN           1..339
FT                   /note="DNA double-strand break repair nuclease NurA"
FT                   /id="PRO_0000434029"
FT   BINDING         58
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N8"
FT   BINDING         133
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U1N8"
FT   MUTAGEN         202
FT                   /note="K->A: Interacts with HerA but lacks activity."
FT                   /evidence="ECO:0000269|PubMed:22135300"
FT   MUTAGEN         295
FT                   /note="I->E: Does not interact with HerA. Does not affect
FT                   dimerization. Strong decrease in nucleolytic activity."
FT                   /evidence="ECO:0000269|PubMed:22135300"
FT   MUTAGEN         300
FT                   /note="F->E: Decreases interaction with HerA. Does not
FT                   affect dimerization. Decreases nucleolytic activity."
FT                   /evidence="ECO:0000269|PubMed:22135300"
FT   HELIX           3..9
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           17..38
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          54..65
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          70..82
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          85..98
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           104..123
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          127..134
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           136..140
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           151..159
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           162..166
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           171..193
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           194..196
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          197..202
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   TURN            208..210
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           216..223
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          226..230
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          233..236
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           248..251
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          255..264
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   STRAND          270..276
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           280..291
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           300..309
FT                   /evidence="ECO:0007829|PDB:2YGK"
FT   HELIX           313..330
FT                   /evidence="ECO:0007829|PDB:2YGK"
SQ   SEQUENCE   339 AA;  39125 MW;  ACF81EEF43C015A8 CRC64;
     MIRKIYDKLV ESHNEIKNQI YNIANYLKQE IQDKVNEYWN EYVINHEQSE TCKFVAIDGG
     SFGRPMRIGI VYAVGAESVI GDNKGVKTLS EDGQIGIFKP GNDAQERISL LMEALELSLA
     LRDGSKGDYI LMDGSLSKKI GNKVDIQQFS DEELKLIRNV DLNGIISIKD ERKMRDLLML
     LNQFLVSKII EEYDGNVLWI SKVSRGRDLF GTDYPDITVL ELFTEKRGFS KLIIKNIDIE
     KISEIPEIEV LRKMEYTTFY TRLDNGKRVI RVDIVGRVDE KIVKEIMDRL SGVSIKGYPF
     PLLKAHMDVR FSAMDREKII KLVGSKLHKD IEWWPSQFY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025