NOB1_ARCFU
ID NOB1_ARCFU Reviewed; 166 AA.
AC O29862;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Endoribonuclease Nob1;
DE Short=RNase Nob1;
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Endonuclease VapC8;
DE AltName: Full=Putative toxin VapC8 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=nob1; Synonyms=vapC8; OrderedLocusNames=AF_0385;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP POSSIBLE FUNCTION.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
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.
CC Processes pre-16S-rRNA at its 3' end (the D-site) to yield the mature
CC 3' end (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- DOMAIN: Has 2 structurally independent domains; the N-terminal PINc
CC domain which binds Mn(2+), rRNA substrate and probably has
CC endoribonuclease activity, and the C-terminal zinc ribbon domain which
CC also binds rRNA substrate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB90852.1; -; Genomic_DNA.
DR PIR; A69298; A69298.
DR RefSeq; WP_010877892.1; NC_000917.1.
DR AlphaFoldDB; O29862; -.
DR SMR; O29862; -.
DR STRING; 224325.AF_0385; -.
DR EnsemblBacteria; AAB90852; AAB90852; AF_0385.
DR GeneID; 24793923; -.
DR KEGG; afu:AF_0385; -.
DR eggNOG; arCOG00721; Archaea.
DR HOGENOM; CLU_109674_1_0_2; -.
DR OMA; GCGREFD; -.
DR OrthoDB; 102178at2157; -.
DR PhylomeDB; O29862; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd09876; PIN_Nob1-like; 1.
DR HAMAP; MF_00265; VapC_Nob1; 1.
DR InterPro; IPR039907; NOB1.
DR InterPro; IPR033411; Ribonuclease_PIN.
DR InterPro; IPR022907; VapC_family.
DR PANTHER; PTHR12814; PTHR12814; 2.
DR Pfam; PF17146; PIN_6; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding;
KW Toxin-antitoxin system; Zinc.
FT CHAIN 1..166
FT /note="Endoribonuclease Nob1"
FT /id="PRO_0000156044"
FT DOMAIN 5..106
FT /note="PINc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT REGION 122..127
FT /note="Flexible linker"
FT /evidence="ECO:0000250"
FT REGION 128..159
FT /note="Zinc ribbon"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 166 AA; 18639 MW; 82C43BAF9F3B2962 CRC64;
MKCVEVHVID SSAIFQRKAV YRNMVTVPEV VAEILDEASA LYFSVKNFRV EEASPESVEE
VKEAARKTGD IHKLSDTDIK VLAKALDEIK KGNEVVLVTD DYAIQNVAMS LGIRFDGILH
RQISKEFKWV KVCRGCGRRI ESEICPVCGS EAIIRRVKND KNRNSG