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Database: UniProt
Entry: C1IG81_9ENTR
LinkDB: C1IG81_9ENTR
Original site: C1IG81_9ENTR 
ID   C1IG81_9ENTR            Unreviewed;       540 AA.
AC   C1IG81;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA repair protein RecN {ECO:0000256|ARBA:ARBA00021315};
DE   AltName: Full=Recombination protein N {ECO:0000256|ARBA:ARBA00033408};
DE   Flags: Fragment;
GN   Name=recN {ECO:0000313|EMBL:ACE74859.1};
OS   Siccibacter turicensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Siccibacter.
OX   NCBI_TaxID=357233 {ECO:0000313|EMBL:ACE74859.1};
RN   [1] {ECO:0000313|EMBL:ACE74859.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Z610 {ECO:0000313|EMBL:ACE74859.1};
RX   PubMed=19321218; DOI=10.1016/j.ijfoodmicro.2009.02.022;
RA   Kuhnert P., Korczak B.M., Stephan R., Joosten H., Iversen C.;
RT   "Phylogeny and prediction of genetic similarity of Cronobacter and related
RT   taxa by multilocus sequence analysis (MLSA).";
RL   Int. J. Food Microbiol. 136:152-158(2009).
CC   -!- FUNCTION: May be involved in recombinational repair of damaged DNA.
CC       {ECO:0000256|ARBA:ARBA00003618}.
CC   -!- SIMILARITY: Belongs to the RecN family.
CC       {ECO:0000256|ARBA:ARBA00009441}.
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DR   EMBL; EU569460; ACE74859.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1IG81; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd03241; ABC_RecN; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR004604; DNA_recomb/repair_RecN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   NCBIfam; TIGR00634; recN; 1.
DR   PANTHER; PTHR11059; DNA REPAIR PROTEIN RECN; 1.
DR   PANTHER; PTHR11059:SF0; DNA REPAIR PROTEIN RECN; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF003128; RecN; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
FT   DOMAIN          3..497
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACE74859.1"
SQ   SEQUENCE   540 AA;  59264 MW;  0B5EFE77773C3DAB CRC64;
     RELEVDFHAG MTAITGETGA GKSIAIDALG LCLGGRADAD MVRPGAGRAD LCARFSLKDT
     PAALRWLEQN QLDDGRECLL RRVISSDGRS RGFINGTAVP LSQLRELGQL LIQIHGQHAH
     QLLLKPDHQK ALLDGYAGEH TLTQQMAAAY REWHQSCRAL AQHQQLSQER AARAELLAYQ
     LKELNEFNPL PGEFEQIDEE YKRLANSGQL LSTSQQALNA LADGEDSNVQ SQLYSVRNLV
     TELVGMDDKL SGVLTMLEEA AIQISEASDE LRHYCERLDL DPNRLYELEQ RLSRQITLAR
     KHHIAPEALP AFHAALLDEQ QQMDNQSDTL EALTQAVSVQ HQQALAIAGQ LHAARVKYAA
     ELSELITDSI HSLSMPHGQL LIQVEFDEHH LTAEGADRID FRVSTNPGQP LQALSKVASG
     GELSRIALAI QVITARKMET PALIFDEVDV GISGPTAAVV GRLLRQLGES TQVMCVTHLP
     QVAGCGHQHF FVSKETDGAM TETHMQPLDK RARLQELARL LGGSEVTRNT LANAKELLAA
//
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