ID A0A410G5L1_9FLAO Unreviewed; 129 AA.
AC A0A410G5L1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=EI546_12830 {ECO:0000313|EMBL:QAA82549.1};
OS Aequorivita sp. H23M31.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=2494375 {ECO:0000313|EMBL:QAA82549.1, ECO:0000313|Proteomes:UP000285517};
RN [1] {ECO:0000313|EMBL:QAA82549.1, ECO:0000313|Proteomes:UP000285517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H23M31 {ECO:0000313|EMBL:QAA82549.1,
RC ECO:0000313|Proteomes:UP000285517};
RA Bae J.-W.;
RT "Complete genome sequencing of Aequorivita sp. H23M31.";
RL Submitted (JAN-2019) 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}.
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DR EMBL; CP034951; QAA82549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410G5L1; -.
DR KEGG; aev:EI546_12830; -.
DR OrthoDB; 9804823at2; -.
DR Proteomes; UP000285517; 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; cd09881; 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:UP000285517};
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 6..124
FT /note="PIN"
FT /evidence="ECO:0000259|Pfam:PF01850"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
SQ SEQUENCE 129 AA; 14378 MW; A4AC01ECA1180C02 CRC64;
MAGELILIDT SILIDWYRKT DKANSVWIRL IEKEYEFAIS SITKYEVYAG ATPSQVALWD
TILATILVLS FDESCVDTAV TINAALKRNR KQIDLADLFI GATAMTHNIG IATLNVNHFE
RIDGLTLVT
//