RNP3_METAC
ID RNP3_METAC Reviewed; 239 AA.
AC Q8TPX2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=MA_1782;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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}.
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DR EMBL; AE010299; AAM05188.1; -; Genomic_DNA.
DR RefSeq; WP_011021785.1; NC_003552.1.
DR AlphaFoldDB; Q8TPX2; -.
DR SMR; Q8TPX2; -.
DR STRING; 188937.MA_1782; -.
DR PRIDE; Q8TPX2; -.
DR EnsemblBacteria; AAM05188; AAM05188; MA_1782.
DR GeneID; 1473671; -.
DR KEGG; mac:MA_1782; -.
DR HOGENOM; CLU_074509_1_0_2; -.
DR InParanoid; Q8TPX2; -.
DR OMA; INRAACE; -.
DR OrthoDB; 66325at2157; -.
DR PhylomeDB; Q8TPX2; -.
DR Proteomes; UP000002487; 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:0003723; F:RNA binding; IBA:GO_Central.
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 PANTHER; PTHR13031; PTHR13031; 1.
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..239
FT /note="Ribonuclease P protein component 3"
FT /id="PRO_0000140038"
SQ SEQUENCE 239 AA; 26214 MW; A6C8470FCF0E638F CRC64;
MGKPKFYDFC VHAVPDGDST AQEQVSLGRH FGFSGIALAN HSDRLPDRKP ILPFIEGFEV
FRGIELVEEN PSKLHSLIGK FRNSMDVLIV HGGSEAVNRA ALENPRVDIL NHPAFDRSSG
LNQVLAKAAA ENGVAIGIIL RPLLHSRGSR RIRLLSDLKS NLELARKYDV SLVLCSDAMS
CFDLRSPMEM LALAEVCGLE EDEALEAIST VPEKIIAKNR PGPGYIKKGI EVLEGEDLF