ID   VAPC1_AQUAE             Reviewed;         144 AA.
AC   O66399;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ribonuclease VapC1 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            Short=RNase VapC1 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE   AltName: Full=Toxin VapC1 {ECO:0000255|HAMAP-Rule:MF_00265};
GN   Name=vapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=aq_aa03;
OS   Aquifex aeolicus (strain VF5).
OG   Plasmid ece1.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2]
RP   POSSIBLE FUNCTION.
RC   STRAIN=VF5;
RX   PubMed=15718296; DOI=10.1093/nar/gki201;
RA   Pandey D.P., Gerdes K.;
RT   "Toxin-antitoxin loci are highly abundant in free-living but lost from
RT   host-associated prokaryotes.";
RL   Nucleic Acids Res. 33:966-976(2005).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An
CC       RNase. {ECO:0000255|HAMAP-Rule:MF_00265}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC   -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR   EMBL; AE000667; AAC07951.1; -; Genomic_DNA.
DR   RefSeq; NP_046399.1; NC_001880.1.
DR   RefSeq; WP_010890545.1; NC_001880.1.
DR   AlphaFoldDB; O66399; -.
DR   SMR; O66399; -.
DR   STRING; 224324.aq_aa03; -.
DR   EnsemblBacteria; AAC07951; AAC07951; aq_aa03.
DR   KEGG; aae:aq_aa03; -.
DR   eggNOG; COG2402; Bacteria.
DR   HOGENOM; CLU_124456_2_0_0; -.
DR   OrthoDB; 2034229at2; -.
DR   Proteomes; UP000000798; Plasmid ece1.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   HAMAP; MF_00265; VapC_Nob1; 1.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR002716; PIN_dom.
DR   InterPro; IPR022907; VapC_family.
DR   Pfam; PF01850; PIN; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Plasmid; Reference proteome;
KW   Toxin-antitoxin system.
FT   CHAIN           1..144
FT                   /note="Ribonuclease VapC1"
FT                   /id="PRO_0000186980"
FT   DOMAIN          6..132
FT                   /note="PINc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ   SEQUENCE   144 AA;  16600 MW;  A58DD8DC538E98F1 CRC64;
     MNSEKVFVDG NVIVDIFDER RVNHKYSVQA IRILLANKFD LLTSSDLITT VYYVLSKIDK
     KKALSDIKEV VNILEIIPFG KAEVEKAIEL MEGDKNFKDL EDTLQYVLAK KEGCKLILSN
     DKSFYSPDIE VLTTEEFCER WNTL