RNP3_NATPD
ID RNP3_NATPD Reviewed; 236 AA.
AC Q3IPJ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Ribonuclease P protein component 3 {ECO:0000255|HAMAP-Rule:MF_00756};
DE Short=RNase P component 3 {ECO:0000255|HAMAP-Rule:MF_00756};
DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00756};
DE AltName: Full=Rpp30 {ECO:0000255|HAMAP-Rule:MF_00756};
GN Name=rnp3 {ECO:0000255|HAMAP-Rule:MF_00756}; OrderedLocusNames=NP_3726A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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_00756}.
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_00756};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00756}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00756}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 3 family. {ECO:0000255|HAMAP-Rule:MF_00756}.
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; CR936257; CAI49954.1; -; Genomic_DNA.
DR RefSeq; WP_011323571.1; NC_007426.1.
DR AlphaFoldDB; Q3IPJ7; -.
DR SMR; Q3IPJ7; -.
DR STRING; 348780.NP_3726A; -.
DR EnsemblBacteria; CAI49954; CAI49954; NP_3726A.
DR GeneID; 3703114; -.
DR KEGG; nph:NP_3726A; -.
DR eggNOG; arCOG00307; Archaea.
DR HOGENOM; CLU_074509_1_0_2; -.
DR OMA; INRAACE; -.
DR OrthoDB; 66325at2157; -.
DR Proteomes; UP000002698; 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:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00756; RNase_P_3; 1.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR023539; RNase_P_comp-3_arc.
DR InterPro; IPR002738; RNase_P_p30.
DR Pfam; PF01876; RNase_P_p30; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW tRNA processing.
FT CHAIN 1..236
FT /note="Ribonuclease P protein component 3"
FT /id="PRO_1000046630"
SQ SEQUENCE 236 AA; 25695 MW; CA7EFF4594397539 CRC64;
MYEGVHAHPD GNATVARFAE TAASRGYDGI VVRNHGDAQT DYDADAVAAE YGVEVVSGIE
IRTDDTAQAS GLVGNYRSKR DIVCVHGGEL NRFAVEEPKV DVLAHPMRDG DVNHVLAKAA
AENGVHFEFN FGRVLRADGG KRVQAIQGLR KLRELVDQYD APYVVSADPE SHLELRSSRD
LAAVGETVGF DREAITDGLA AWADIVERNR RRRSAAVVEP GVRIERADGE TDDSRE