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RNP4_AERPE
ID   RNP4_AERPE              Reviewed;         163 AA.
AC   Q9YD20;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 79.
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}; OrderedLocusNames=APE_1092.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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_00757}.
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_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-Rule:MF_00757};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC       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}.
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DR   EMBL; BA000002; BAA80077.2; -; Genomic_DNA.
DR   PIR; E72709; E72709.
DR   AlphaFoldDB; Q9YD20; -.
DR   SMR; Q9YD20; -.
DR   STRING; 272557.APE_1092.1; -.
DR   EnsemblBacteria; BAA80077; BAA80077; APE_1092.1.
DR   KEGG; ape:APE_1092.1; -.
DR   eggNOG; arCOG04345; Archaea.
DR   Proteomes; UP000002518; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00757; RNase_P_4; 1.
DR   InterPro; IPR016432; RNP4.
DR   InterPro; IPR007175; Rpr2/Snm1/Rpp21.
DR   Pfam; PF04032; Rpr2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..163
FT                   /note="Ribonuclease P protein component 4"
FT                   /id="PRO_0000153848"
FT   REGION          110..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00757"
SQ   SEQUENCE   163 AA;  18167 MW;  FA24D0F183ABB5EA CRC64;
     MKSRRSRCRR SFTTLVRREE ERLARWALEL ARRGLTGEAR RVAEQLFQLA ASTRVRPPRR
     VKRLFCKNCR TPLIPGLTAR VRLRSQGGMS YTVVTCLSCG WIHRYPYRKG PRGGAPISPP
     AAEYGSGGRD SGEREDKGPQ GPPRQGGRDN RQGGGHQGGP KGD
 
 
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