ID A0A0R2CL10_9LACO Unreviewed; 222 AA.
AC A0A0R2CL10;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=DNA repair protein {ECO:0000313|EMBL:KRM89115.1};
GN ORFNames=FD21_GL000275 {ECO:0000313|EMBL:KRM89115.1};
OS Liquorilactobacillus vini DSM 20605.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1133569 {ECO:0000313|EMBL:KRM89115.1, ECO:0000313|Proteomes:UP000051576};
RN [1] {ECO:0000313|EMBL:KRM89115.1, ECO:0000313|Proteomes:UP000051576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20605 {ECO:0000313|EMBL:KRM89115.1,
RC ECO:0000313|Proteomes:UP000051576};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the UPF0758 family.
CC {ECO:0000256|ARBA:ARBA00010243, ECO:0000256|RuleBase:RU003797}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM89115.1}.
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DR EMBL; AYYX01000012; KRM89115.1; -; Genomic_DNA.
DR RefSeq; WP_010580867.1; NZ_AYYX01000012.1.
DR AlphaFoldDB; A0A0R2CL10; -.
DR STRING; 1133569.FD21_GL000275; -.
DR PATRIC; fig|1133569.4.peg.293; -.
DR eggNOG; COG2003; Bacteria.
DR OrthoDB; 9804482at2; -.
DR Proteomes; UP000051576; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08071; MPN_DUF2466; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR025657; RadC_JAB.
DR InterPro; IPR001405; UPF0758.
DR InterPro; IPR020891; UPF0758_CS.
DR NCBIfam; TIGR00608; radc; 1.
DR PANTHER; PTHR30471; DNA REPAIR PROTEIN RADC; 1.
DR PANTHER; PTHR30471:SF3; UPF0758 PROTEIN YEES-RELATED; 1.
DR Pfam; PF04002; RadC; 1.
DR SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS01302; UPF0758; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051576};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 99..221
FT /note="MPN"
FT /evidence="ECO:0000259|PROSITE:PS50249"
SQ SEQUENCE 222 AA; 25359 MW; 55286BF031A47DC2 CRC64;
MNETTSLPKI LHKAKTFSPA ALTDQELLYL TLNKILNLSI SLQQLNEICD QEFDLRQLKY
FSEHEWKLLF KDQTVTWKGK VLCELASRIE KRPKFTLGRV TSSQCLGQQL IEELGMLQQE
VLLVLVLDTK NQVLGRKVIF RGTLDGATVH PREIFNFALR YSAARLIIVH NHPSGDPTPS
TNDLNLTNRL KKCGDLMGIQ LLDHLIVGSL TYLSFQEERL LD
//
