RNP4_ARCFU
ID RNP4_ARCFU Reviewed; 107 AA.
AC O30127;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ribonuclease P protein component 4 {ECO:0000255|HAMAP-Rule:MF_00757};
DE Short=RNase P component 4 {ECO:0000255|HAMAP-Rule:MF_00757};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00757};
DE AltName: Full=Rpp21 {ECO:0000255|HAMAP-Rule:MF_00757};
GN Name=rnp4 {ECO:0000255|HAMAP-Rule:MF_00757}; OrderedLocusNames=AF_0109;
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).
CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-
CC Rule:MF_00757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00757};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00757};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00757};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00757}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00757}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 4 family. {ECO:0000255|HAMAP-Rule:MF_00757}.
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DR EMBL; AE000782; AAB91122.1; -; Genomic_DNA.
DR PIR; E69263; E69263.
DR RefSeq; WP_010877623.1; NC_000917.1.
DR AlphaFoldDB; O30127; -.
DR SMR; O30127; -.
DR STRING; 224325.AF_0109; -.
DR DNASU; 1483321; -.
DR EnsemblBacteria; AAB91122; AAB91122; AF_0109.
DR GeneID; 24793663; -.
DR KEGG; afu:AF_0109; -.
DR eggNOG; arCOG04345; Archaea.
DR HOGENOM; CLU_079140_3_1_2; -.
DR OMA; HVVITCL; -.
DR OrthoDB; 128960at2157; -.
DR PhylomeDB; O30127; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00757; RNase_P_4; 1.
DR InterPro; IPR016432; RNP4.
DR InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR Pfam; PF04032; Rpr2; 1.
DR PIRSF; PIRSF004878; RNase_P_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..107
FT /note="Ribonuclease P protein component 4"
FT /id="PRO_0000153849"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
SQ SEQUENCE 107 AA; 13307 MW; 3E670BA75B0ADB59 CRC64;
MLRRDKKRES RIARERVFYL IKRAEEWKNI DYELARRYVE LARKIAMRYR VRIPRELKAT
YCKKCLYPYK AGKFRVRVRK SRVIITCLNC GFERRIPIRP KRVNRKV
