VAPC1_THEAC
ID VAPC1_THEAC Reviewed; 194 AA.
AC P57674;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Putative toxin VapC1 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Ta0041;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP POSSIBLE FUNCTION.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
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; AL445063; CAC11190.1; -; Genomic_DNA.
DR RefSeq; WP_010900469.1; NC_002578.1.
DR AlphaFoldDB; P57674; -.
DR SMR; P57674; -.
DR STRING; 273075.Ta0041; -.
DR EnsemblBacteria; CAC11190; CAC11190; CAC11190.
DR GeneID; 1455708; -.
DR KEGG; tac:Ta0041; -.
DR eggNOG; arCOG00721; Archaea.
DR HOGENOM; CLU_109674_1_0_2; -.
DR OMA; GCGREFD; -.
DR OrthoDB; 102178at2157; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR CDD; cd09876; PIN_Nob1-like; 1.
DR HAMAP; MF_00265; VapC_Nob1; 1.
DR InterPro; IPR039907; NOB1.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR033411; Ribonuclease_PIN.
DR InterPro; IPR022907; VapC_family.
DR PANTHER; PTHR12814; PTHR12814; 2.
DR Pfam; PF17146; PIN_6; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome;
KW Toxin-antitoxin system.
FT CHAIN 1..194
FT /note="Ribonuclease VapC1"
FT /id="PRO_0000156049"
FT DOMAIN 34..134
FT /note="PINc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ SEQUENCE 194 AA; 21855 MW; 6F7CC0D844F9FF4F CRC64;
MPWVGSQFHK GDAQTIMALS NVLYQVLIAL GMIYVIDTSA IISRNLNLLE GDLMFPSSVI
GEIKKGKLRY MIDVLLPMIR VASPDHEYLK IVEETAAKTG DLMNLSQTDK DVLALALQYD
ATIVTDDYSI QNVASYLNLG FLNANIKRID KQIAWIYRCT GCKKVFPGPV KVCDICGHEV
KRHYDKRKSM IRKV
