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RNP3_HALMA
ID   RNP3_HALMA              Reviewed;         235 AA.
AC   Q5V2X5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=rrnAC1177;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV46127.1; -; Genomic_DNA.
DR   RefSeq; WP_011223482.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V2X5; -.
DR   SMR; Q5V2X5; -.
DR   STRING; 272569.rrnAC1177; -.
DR   EnsemblBacteria; AAV46127; AAV46127; rrnAC1177.
DR   GeneID; 40152172; -.
DR   KEGG; hma:rrnAC1177; -.
DR   PATRIC; fig|272569.17.peg.1893; -.
DR   eggNOG; arCOG00307; Archaea.
DR   HOGENOM; CLU_074509_1_0_2; -.
DR   OMA; INRAACE; -.
DR   Proteomes; UP000001169; Chromosome I.
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..235
FT                   /note="Ribonuclease P protein component 3"
FT                   /id="PRO_0000140037"
SQ   SEQUENCE   235 AA;  25422 MW;  E0F26D46E6DA2B7E CRC64;
     MYEAVYAHPD GDSTVARHAL TAADSEYDGI VVRNHGDEQA DYDADAISDA YGVDVAAGIE
     VRADDPSRAS GFVGNYRSDR TVVVVHGGDR RINRFAVEQP TVDVLAHPMR DDGDFNHVLA
     NAAADNGVRV EFDFGPVLRA SGGSRVRAIK ELRKLRELVE NAGAPFVVSA SPSTHLQIRA
     PRDIIAVGET IGFDADTVRE GLTEWGQIVE RNRERQSGAV IEPGVRLEDD ADDAE
 
 
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