ID   NUCS_CORK4              Reviewed;         253 AA.
AC   C4LJL1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Endonuclease NucS {ECO:0000255|HAMAP-Rule:MF_00722};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00722};
GN   Name=nucS {ECO:0000255|HAMAP-Rule:MF_00722}; OrderedLocusNames=ckrop_1272;
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=645127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
CC   -!- FUNCTION: Cleaves both 3' and 5' ssDNA extremities of branched DNA
CC       structures. {ECO:0000255|HAMAP-Rule:MF_00722}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00722}.
CC   -!- SIMILARITY: Belongs to the NucS endonuclease family.
CC       {ECO:0000255|HAMAP-Rule:MF_00722}.
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DR   EMBL; CP001620; ACR18016.1; -; Genomic_DNA.
DR   RefSeq; WP_012731903.1; NC_012704.1.
DR   AlphaFoldDB; C4LJL1; -.
DR   SMR; C4LJL1; -.
DR   STRING; 645127.ckrop_1272; -.
DR   EnsemblBacteria; ACR18016; ACR18016; ckrop_1272.
DR   KEGG; ckp:ckrop_1272; -.
DR   eggNOG; COG1637; Bacteria.
DR   HOGENOM; CLU_069350_0_0_11; -.
DR   OMA; RCSVDYA; -.
DR   OrthoDB; 1002946at2; -.
DR   Proteomes; UP000001473; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   HAMAP; MF_00722; NucS; 1.
DR   InterPro; IPR002793; Endonuclease_NucS.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   PANTHER; PTHR38814; PTHR38814; 2.
DR   Pfam; PF01939; NucS; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..253
FT                   /note="Endonuclease NucS"
FT                   /id="PRO_1000212714"
FT   REGION          63..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   253 AA;  27841 MW;  1294D32BD04F3B4C CRC64;
     MRLVIATCSV DYVGRLTAHL PKATRLLMVK ADGSVSVHAD DRAYKPLNWM TPPCTLTVHP
     IAIDDPDTDF TDGSSVGNSE EQGTDGSAHT AHEEELWVVE NKKGEQLRIT VHDKISDTTY
     DLGEDPGLTK DGVEAHLQEL LAQHPEALGE GFTLVRREYP TPIGPVDILT RDASGKTVAV
     EVKRRGGIDG VEQLTRYVEL LNRDEILAPV QGLFAAQEIK PQARTLAEDR GFTCVTVDYD
     ELRGTPSQEL RLF