ID A0A0H3C4B2_CAUVN Unreviewed; 128 AA.
AC A0A0H3C4B2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ECO:0000313|EMBL:ACL93498.1};
GN OrderedLocusNames=CCNA_00031 {ECO:0000313|EMBL:ACL93498.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL93498.1, ECO:0000313|Proteomes:UP000001364};
RN [1] {ECO:0000313|EMBL:ACL93498.1, ECO:0000313|Proteomes:UP000001364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX PubMed=20472802; DOI=10.1128/JB.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00265};
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000256|ARBA:ARBA00038093, ECO:0000256|HAMAP-Rule:MF_00265}.
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DR EMBL; CP001340; ACL93498.1; -; Genomic_DNA.
DR RefSeq; WP_010917921.1; NC_011916.1.
DR RefSeq; YP_002515406.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3C4B2; -.
DR SMR; A0A0H3C4B2; -.
DR GeneID; 7332121; -.
DR KEGG; ccs:CCNA_00031; -.
DR PATRIC; fig|565050.3.peg.32; -.
DR HOGENOM; CLU_118482_5_3_5; -.
DR OrthoDB; 9796690at2; -.
DR PhylomeDB; A0A0H3C4B2; -.
DR Proteomes; UP000001364; Chromosome.
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; cd18736; PIN_CcVapC1-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; PTHR33653; RIBONUCLEASE VAPC2; 1.
DR PANTHER; PTHR33653:SF1; RIBONUCLEASE VAPC2; 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:UP000001364};
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 3..122
FT /note="PIN"
FT /evidence="ECO:0000259|Pfam:PF01850"
FT BINDING 6
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
SQ SEQUENCE 128 AA; 14130 MW; F651787BDDEF9339 CRC64;
MAYVLDTNVA IHLRDGDPEV TTRVTALNGA ILLSIISRVE LEGGVYREAA QAGLRRSRLD
VMLKVLPVLD FDGAAADEYR RIVESAGYSR RKVVDRMIAA QALAHRATFV TFNADDFRDI
PGLSLLAW
//
