ID L0L0Y6_METHD Unreviewed; 122 AA.
AC L0L0Y6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Ribonuclease P protein component 2 {ECO:0000256|HAMAP-Rule:MF_00755};
DE Short=RNase P component 2 {ECO:0000256|HAMAP-Rule:MF_00755};
DE EC=3.1.26.5 {ECO:0000256|HAMAP-Rule:MF_00755};
DE AltName: Full=Pop5 {ECO:0000256|HAMAP-Rule:MF_00755};
GN Name=rnp2 {ECO:0000256|HAMAP-Rule:MF_00755};
GN OrderedLocusNames=Metho_1881 {ECO:0000313|EMBL:AGB50058.1};
OS Methanomethylovorans hollandica (strain DSM 15978 / NBRC 107637 / DMS1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanomethylovorans.
OX NCBI_TaxID=867904 {ECO:0000313|EMBL:AGB50058.1, ECO:0000313|Proteomes:UP000010866};
RN [1] {ECO:0000313|Proteomes:UP000010866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15978 / NBRC 107637 / DMS1
RC {ECO:0000313|Proteomes:UP000010866};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Methanomethylovorans hollandica DSM
RT 15978.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends. {ECO:0000256|HAMAP-
CC Rule:MF_00755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00755};
CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC subunits. {ECO:0000256|HAMAP-Rule:MF_00755}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00755}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000256|ARBA:ARBA00010800, ECO:0000256|HAMAP-
CC Rule:MF_00755}.
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DR EMBL; CP003362; AGB50058.1; -; Genomic_DNA.
DR RefSeq; WP_015325223.1; NC_019977.1.
DR AlphaFoldDB; L0L0Y6; -.
DR STRING; 867904.Metho_1881; -.
DR GeneID; 14406394; -.
DR KEGG; mhz:Metho_1881; -.
DR HOGENOM; CLU_137733_1_0_2; -.
DR OMA; QRELWYA; -.
DR OrthoDB; 19261at2157; -.
DR Proteomes; UP000010866; 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 Gene3D; 3.30.70.3250; Ribonuclease P, Pop5 subunit; 1.
DR HAMAP; MF_00755; RNase_P_2; 1.
DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR038085; Rnp2-like_sf.
DR InterPro; IPR016434; Rnp2_archaea.
DR PANTHER; PTHR15441; RIBONUCLEASE P PROTEIN SUBUNIT P14; 1.
DR PANTHER; PTHR15441:SF2; RIBONUCLEASE P/MRP PROTEIN SUBUNIT POP5; 1.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR PIRSF; PIRSF004952; RNase_P_2; 1.
DR SUPFAM; SSF160350; Rnp2-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00755};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00755};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00755};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00755};
KW Reference proteome {ECO:0000313|Proteomes:UP000010866};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00755}.
SQ SEQUENCE 122 AA; 13692 MW; E4FD5056E0CF0B65 CRC64;
MKTLPSSLRQ RKRYLAIEII TELEVSREEL LREIFSAMGS LYGDIGSSEC AMRLLDFGNR
KGILRCSHMM EERSRAALAT ITTIGGQRAI VHVLGISGTV KGATQKYISV QQYQNPNILI
YK
//