(data stored in ACNUC7421 zone)

SWISSPROT: RNP4_SULIK

ID   RNP4_SULIK              Reviewed;         104 AA.
AC   C4KJF8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 36.
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};
GN   OrderedLocusNames=M164_0042;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends.
CC       {ECO:0000255|HAMAP-Rule:MF_00757}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'-
CC       extranucleotides from tRNA precursor. {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-
CC       Rule:MF_00757};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5
CC       protein 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}.
DR   EMBL; CP001402; ACR40678.1; -; Genomic_DNA.
DR   RefSeq; WP_012710221.1; NC_012726.1.
DR   SMR; C4KJF8; -.
DR   EnsemblBacteria; ACR40678; ACR40678; M164_0042.
DR   GeneID; 7795420; -.
DR   KEGG; sid:M164_0042; -.
DR   HOGENOM; HOG000230709; -.
DR   KO; K03540; -.
DR   OMA; IRRGYCR; -.
DR   OrthoDB; POG093Z0K3G; -.
DR   BioCyc; SISL426118:GI01-42-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:InterPro.
DR   HAMAP; MF_00757; RNase_P_4; 1.
DR   InterPro; IPR016432; RNase_P_comp-4.
DR   InterPro; IPR007175; Rpr2.
DR   Pfam; PF04032; Rpr2; 1.
DR   PIRSF; PIRSF004878; RNase_P_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KJF8.
DR   SWISS-2DPAGE; C4KJF8.
KW   Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; tRNA processing; Zinc.
FT   CHAIN         1    104       Ribonuclease P protein component 4.
FT                                /FTId=PRO_1000212863.
FT   METAL        57     57       Zinc. {ECO:0000255|HAMAP-Rule:MF_00757}.
FT   METAL        60     60       Zinc. {ECO:0000255|HAMAP-Rule:MF_00757}.
FT   METAL        83     83       Zinc. {ECO:0000255|HAMAP-Rule:MF_00757}.
FT   METAL        86     86       Zinc. {ECO:0000255|HAMAP-Rule:MF_00757}.
SQ   SEQUENCE   104 AA;  12608 MW;  8ABE13847A57EE08 CRC64;
     MRIKNKIKKR IIELIELAYI TARKGDLELA REYIKLAEMY SRKGRVKIPL KYKRMFCRKC
     YTPLITGVTE RRRIRSKILI RTCLICNWQR RYVLSRNKGS NKEN
//

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