ID   SBCC_DEIRA              Reviewed;         909 AA.
AC   Q9RT44;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Nuclease SbcCD subunit C;
GN   Name=sbcC; OrderedLocusNames=DR_1922;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can
CC       inhibit DNA replication and are intermediates in certain DNA
CC       recombination reactions. The complex acts as a 3'->5' double strand
CC       exonuclease that can open hairpins. It also has a 5' single-strand
CC       endonuclease activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily. {ECO:0000305}.
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DR   EMBL; AE000513; AAF11474.1; -; Genomic_DNA.
DR   PIR; A75337; A75337.
DR   RefSeq; NP_295645.1; NC_001263.1.
DR   RefSeq; WP_010888557.1; NC_001263.1.
DR   STRING; 243230.DR_1922; -.
DR   EnsemblBacteria; AAF11474; AAF11474; DR_1922.
DR   KEGG; dra:DR_1922; -.
DR   PATRIC; fig|243230.17.peg.2140; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_1_2_0; -.
DR   InParanoid; Q9RT44; -.
DR   OMA; ISHVQEM; -.
DR   OrthoDB; 1143316at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; DNA recombination; DNA replication; Endonuclease;
KW   Exonuclease; Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..909
FT                   /note="Nuclease SbcCD subunit C"
FT                   /id="PRO_0000105863"
FT   COILED          204..250
FT                   /evidence="ECO:0000255"
FT   COILED          285..453
FT                   /evidence="ECO:0000255"
FT   COILED          484..549
FT                   /evidence="ECO:0000255"
FT   COILED          576..614
FT                   /evidence="ECO:0000255"
FT   COILED          652..751
FT                   /evidence="ECO:0000255"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   909 AA;  100095 MW;  D90F765906B0B8D3 CRC64;
     MKPLHLTLRG FTAFRQTTDL DFADLELFAL VGPTGSGKSS LLDAMTFALY GETARLGATG
     LDALISQGER TLSVALTFEA GGQTYRVTRT RGRKQADNEV RLDRLDPDGE WTGLSSGSQK
     DIAQRIEDVV GLDFDTFTRC VMLPQGQFAA LLHGKPRQRQ ELLGELTGMG RVQQMQTFAA
     DQVKDFKHQS QSLSSVLASE YAGVSEEAAA AVRAQREQTD ADAERLLQQR EELRTQLQRC
     ANXXSLSSRE DTARRLTVQE SRXEGVRQGA ERARRARQVA GVLPLLDAAE RARIAYDRQT
     RELAGAESAL QSAQAQAARA DAALTQAQAQ EPRIPELEEQ ANALREAEAD AARLKRAGGS
     VQATHANPLP WDEDAFETAR EAAQKLEKLR VERSILESEK AALKAALERY AQEERQQQEE
     TAQLERVKAD GLKAKEQLQV AQQREEEARM EAGLASYRSH LHEGEPCPLC LQTVHEVPEG
     ESVDLDELRG QVNLLQKLVQ ERREHFTDLR GQLKTRQLWL DEKKSEYHDW NERNKQRELD
     ARELERHISG NPQDDLQRLL ASLAGRVRQA GANPAQARRD RLAEIQSIRS RIQEAQAALS
     RAQGDLAAAQ ATAQPRSMGG EREADHLAAA DALTKALASL NLTAEAARTA GLPENEIAAL
     EEGARKHEAE VAQLRAALAD LDRQLGLEAF DPAHLAQVSR DLTASDAALS TAREQAGRLA
     EQERQLRDKL TRKADIETQA AEAGRQLDTW QTLNNALKVN EFQQFMLAEV EAQLLTRAGL
     LLFDISDGRY RLSLDKGEYV VQDLWNAGEV RAVKTLSGGE TFLASLSLAI ALSDYLAGNK
     VLGALFLDEG FGTLDPQALE AVATALENLR TQGRMVGIVT HVESLSERLP SRLLVSKSMA
     GSNVIRVDG