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Database: UniProt
Entry: F4CAF5_SPHS2
LinkDB: F4CAF5_SPHS2
Original site: F4CAF5_SPHS2 
ID   F4CAF5_SPHS2            Unreviewed;       139 AA.
AC   F4CAF5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   OrderedLocusNames=Sph21_4405 {ECO:0000313|EMBL:ADZ80925.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ80925.1};
RN   [1] {ECO:0000313|EMBL:ADZ80925.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ80925.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) 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; CP002584; ADZ80925.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CAF5; -.
DR   STRING; 743722.Sph21_4405; -.
DR   KEGG; shg:Sph21_4405; -.
DR   PATRIC; fig|743722.3.peg.4691; -.
DR   eggNOG; COG1487; Bacteria.
DR   HOGENOM; CLU_118482_5_2_10; -.
DR   OrthoDB; 9796690at2; -.
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; cd18743; 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   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..121
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         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00265"
SQ   SEQUENCE   139 AA;  16008 MW;  29A92F42A2491713 CRC64;
     MQYLLDTSIC VFYLRGKLDL ARIIREKGRE NFFISEVTVA ELRYGAENSS NPKKSHKAVD
     DFINGLSIVP IFGAINRYAK EKVRLRKLGT PHHDDFDLLI GVTAIEYGLI LVTDNTKHFN
     KLEDIQLENW YQRTLGTSF
//
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