RNP4_METJA
ID RNP4_METJA Reviewed; 128 AA.
AC Q58372;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=MJ0962;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=18558617; DOI=10.1093/nar/gkn360;
RA Pulukkunat D.K., Gopalan V.;
RT "Studies on Methanocaldococcus jannaschii RNase P reveal insights into the
RT roles of RNA and protein cofactors in RNase P catalysis.";
RL Nucleic Acids Res. 36:4172-4180(2008).
RN [3]
RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=21683084; DOI=10.1016/j.jmb.2011.05.012;
RA Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.;
RT "Cooperative RNP assembly: complementary rescue of structural defects by
RT protein and RNA subunits of archaeal RNase P.";
RL J. Mol. Biol. 411:368-383(2011).
RN [4]
RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT.
RX PubMed=22298511; DOI=10.1093/nar/gks013;
RA Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P.,
RA Gopalan V.;
RT "Fidelity of tRNA 5'-maturation: a possible basis for the functional
RT dependence of archaeal and eukaryal RNase P on multiple protein
RT cofactors.";
RL Nucleic Acids Res. 40:4666-4680(2012).
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, ECO:0000269|PubMed:18558617,
CC ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}.
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 protein
CC subunits. Forms a subcomplex with Rnp1 which stimulates the catalytic
CC RNA. {ECO:0000269|PubMed:18558617, ECO:0000269|PubMed:21683084,
CC ECO:0000269|PubMed:22298511}.
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; L77117; AAB98964.1; -; Genomic_DNA.
DR PIR; B64420; B64420.
DR RefSeq; WP_010870476.1; NC_000909.1.
DR PDB; 6K0A; EM; 4.60 A; G/H=1-128.
DR PDB; 6K0B; EM; 4.30 A; G/H=1-128.
DR PDBsum; 6K0A; -.
DR PDBsum; 6K0B; -.
DR AlphaFoldDB; Q58372; -.
DR SMR; Q58372; -.
DR STRING; 243232.MJ_0962; -.
DR EnsemblBacteria; AAB98964; AAB98964; MJ_0962.
DR GeneID; 1451860; -.
DR KEGG; mja:MJ_0962; -.
DR eggNOG; arCOG04345; Archaea.
DR HOGENOM; CLU_079140_3_1_2; -.
DR InParanoid; Q58372; -.
DR OMA; HVVITCL; -.
DR OrthoDB; 107253at2157; -.
DR PhylomeDB; Q58372; -.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..128
FT /note="Ribonuclease P protein component 4"
FT /id="PRO_0000153852"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
SQ SEQUENCE 128 AA; 15567 MW; 462D677CE5B159D3 CRC64;
MKKFLEKKLK KIAYERIDIL MSLAEEEAKK GNWDRAKRYV YLARRIAMKM RIRFPKKWKR
RICKKCGTFL LYGRNARVRI KSKRYPHVVI TCLECGAIYR IPMIREKKEK RRKKLEERLK
AKSNSQTS
