ID A0A0Q7K9S5_9ACTN Unreviewed; 142 AA.
AC A0A0Q7K9S5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=ASD06_01900 {ECO:0000313|EMBL:KQX69801.1};
OS Angustibacter sp. Root456.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae.
OX NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX69801.1, ECO:0000313|Proteomes:UP000051170};
RN [1] {ECO:0000313|EMBL:KQX69801.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX69801.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX69801.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX69801.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KQX69801.1}.
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DR EMBL; LMER01000001; KQX69801.1; -; Genomic_DNA.
DR RefSeq; WP_056672352.1; NZ_LMER01000001.1.
DR AlphaFoldDB; A0A0Q7K9S5; -.
DR STRING; 1736539.ASD06_01900; -.
DR OrthoDB; 9804823at2; -.
DR Proteomes; UP000051170; 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; cd18746; PIN_VapC4-5_FitB-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:UP000051170};
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 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
SQ SEQUENCE 142 AA; 15468 MW; 8801F96B932DFDA2 CRC64;
MRYLLDTNVV SALRVRGRNC SVEEWAASVP LGDHFVSAFT IAEIERGVIA KERADAEQGE
VLRRWFEDNV LPAFAGRVLG FDLSAARILA AYRVPEHTPL DDALIAAVAE SAGLTVATRN
TKHFEPLGVA CVNPWDGPTA HD
//