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Database: UniProt
Entry: A0A365HCP9_9ACTN
LinkDB: A0A365HCP9_9ACTN
Original site: A0A365HCP9_9ACTN 
ID   A0A365HCP9_9ACTN        Unreviewed;       137 AA.
AC   A0A365HCP9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=DPM19_00470 {ECO:0000313|EMBL:RAY16696.1};
OS   Actinomadura craniellae.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2231787 {ECO:0000313|EMBL:RAY16696.1, ECO:0000313|Proteomes:UP000251891};
RN   [1] {ECO:0000313|EMBL:RAY16696.1, ECO:0000313|Proteomes:UP000251891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW63021 {ECO:0000313|EMBL:RAY16696.1,
RC   ECO:0000313|Proteomes:UP000251891};
RA   Li L., Xu Q.H., Lin H.W., Lu Y.H.;
RT   "Actinomadura craniellae sp. nov. isolated from marine sponge Craniella
RT   sp.";
RL   Submitted (JUN-2018) 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|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:RAY16696.1}.
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DR   EMBL; QLYX01000001; RAY16696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365HCP9; -.
DR   OrthoDB; 4377304at2; -.
DR   Proteomes; UP000251891; 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; cd09873; PIN_Pae0151-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; IPR044153; PIN_Pae0151-like.
DR   InterPro; IPR022907; VapC_family.
DR   PANTHER; PTHR35901:SF1; EXONUCLEASE VAPC9; 1.
DR   PANTHER; PTHR35901; 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:UP000251891};
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          4..120
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         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
SQ   SEQUENCE   137 AA;  15352 MW;  3CC74E68D70F96B7 CRC64;
     MSLVVDASIV FRLLANVKGD DLLRQRLARK LHAPAVIDVE IASVVRGHVI TSKPQVRISE
     ARAQIMLERY SQLKIVRHPM QPLQRRVLEL RNNLTAYDGM YVALAELLGV PLLTDDAKFA
     GSTGHRAEIH RYPPPQA
//
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