ID A0A2S6NPF0_RHOGL Unreviewed; 133 AA.
AC A0A2S6NPF0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Ribonuclease VapC {ECO:0000256|HAMAP-Rule:MF_00265};
DE Short=RNase VapC {ECO:0000256|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC {ECO:0000256|HAMAP-Rule:MF_00265};
GN Name=vapC {ECO:0000256|HAMAP-Rule:MF_00265};
GN ORFNames=CCS01_00555 {ECO:0000313|EMBL:PPQ40171.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ40171.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ40171.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ40171.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) system. An RNase.
CC {ECO:0000256|HAMAP-Rule:MF_00265}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00265};
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000256|HAMAP-Rule:MF_00265}.
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:PPQ40171.1}.
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DR EMBL; NHRY01000027; PPQ40171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NPF0; -.
DR OrthoDB; 9811788at2; -.
DR Proteomes; UP000239724; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd18760; PIN_MtVapC3-like; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
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 PANTHER; PTHR42740; RIBONUCLEASE VAPC3; 1.
DR PANTHER; PTHR42740:SF1; RIBONUCLEASE VAPC3; 1.
DR Pfam; PF01850; PIN; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00265};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00265};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00265};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00265};
KW Reference proteome {ECO:0000313|Proteomes:UP000239724};
KW Toxin {ECO:0000256|HAMAP-Rule:MF_00265};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649, ECO:0000256|HAMAP-
KW Rule:MF_00265}.
FT DOMAIN 2..122
FT /note="PIN"
FT /evidence="ECO:0000259|Pfam:PF01850"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
SQ SEQUENCE 133 AA; 14527 MW; 6C53A0E14CDA58D1 CRC64;
MIVVDSSAWI ANLRGLATPV VRRLRETVDT ADDQILLGDI ILLEVLQGAR DDAHAARIQR
ALETYPIAPM LDADLAVQAA RNYRRLRALG ITIRKTADII IGTFCIAGGH ALLHDDRDFA
AMEHHLGLSV IAP
//
