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Database: UniProt
Entry: Q3YRH2_EHRCJ
LinkDB: Q3YRH2_EHRCJ
Original site: Q3YRH2_EHRCJ 
ID   Q3YRH2_EHRCJ            Unreviewed;       230 AA.
AC   Q3YRH2;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=DNA repair protein RadC {ECO:0000313|EMBL:AAZ68683.1};
GN   OrderedLocusNames=Ecaj_0649 {ECO:0000313|EMBL:AAZ68683.1};
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484 {ECO:0000313|EMBL:AAZ68683.1, ECO:0000313|Proteomes:UP000000435};
RN   [1] {ECO:0000313|Proteomes:UP000000435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake {ECO:0000313|Proteomes:UP000000435};
RX   PubMed=16707693; DOI=10.1128/JB.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
CC   -!- SIMILARITY: Belongs to the UPF0758 family.
CC       {ECO:0000256|RuleBase:RU003797}.
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DR   EMBL; CP000107; AAZ68683.1; -; Genomic_DNA.
DR   RefSeq; WP_011304760.1; NC_007354.1.
DR   AlphaFoldDB; Q3YRH2; -.
DR   STRING; 269484.Ecaj_0649; -.
DR   KEGG; ecn:Ecaj_0649; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_0_5; -.
DR   InParanoid; Q3YRH2; -.
DR   Proteomes; UP000000435; Chromosome.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR025657; RadC_JAB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
DR   InterPro; IPR046778; UPF0758_N.
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   Pfam; PF20582; UPF0758_N; 1.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          108..230
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
SQ   SEQUENCE   230 AA;  26122 MW;  15112B17A5FB34DE CRC64;
     MNTKDEHKKQ QIGHRKRLRQ KLLSGGNKGL LDYEILELIL CSSHIRKDVK PIAKRLIKHF
     GSFSKVFFAD FNQLTEVHGI GEASVSAILC IRETLNRILR EDIDHGVIIN QWQKLIEYLR
     IKIGNGNIEN FHILYLNTKY KLLADETQDV GTVNQTPLYI REVIKKSLSL GATSIIIAHN
     HPSGDARPSK ADIEITNQLA ITCNNIGITL IDHVIVTSND HYSFKTHNLL
//
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