ID U1GH17_9ACTN Unreviewed; 145 AA.
AC U1GH17;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Ribonuclease P protein component {ECO:0000313|EMBL:ERF57435.1};
GN ORFNames=H641_03113 {ECO:0000313|EMBL:ERF57435.1};
OS Cutibacterium granulosum DSM 20700.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF57435.1, ECO:0000313|Proteomes:UP000016307};
RN [1] {ECO:0000313|EMBL:ERF57435.1, ECO:0000313|Proteomes:UP000016307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF57435.1,
RC ECO:0000313|Proteomes:UP000016307};
RX PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA Brinkmann V., Meyer T.F., Bruggemann H.;
RT "Comparative genomics reveals distinct host-interacting traits of three
RT major human-associated propionibacteria.";
RL BMC Genomics 14:640-640(2013).
CC -!- FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from
CC pre-tRNA to produce the mature 5'-terminus. It can also cleave other
CC RNA substrates such as 4.5S RNA. The protein component plays an
CC auxiliary but essential role in vivo by binding to the 5'-leader
CC sequence and broadening the substrate specificity of the ribozyme.
CC {ECO:0000256|ARBA:ARBA00002663}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERF57435.1}.
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DR EMBL; AOSS01000098; ERF57435.1; -; Genomic_DNA.
DR AlphaFoldDB; U1GH17; -.
DR PATRIC; fig|1160719.4.peg.597; -.
DR Proteomes; UP000016307; Unassembled WGS sequence.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR000100; RNase_P.
DR InterPro; IPR020539; RNase_P_CS.
DR NCBIfam; TIGR00188; rnpA; 1.
DR PANTHER; PTHR33992; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR PANTHER; PTHR33992:SF1; RIBONUCLEASE P PROTEIN COMPONENT; 1.
DR Pfam; PF00825; Ribonuclease_P; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00648; RIBONUCLEASE_P; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000016307};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT REGION 87..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 145 AA; 15163 MW; 129F4E3676389222 CRC64;
MSTLADATTC SDPGAAPRVG FVVSKAVGNA VTRHRVARQL RHLARPLAEQ LPLGCLIVVR
ALPAAARHPQ QLPSDLSSAW TKALDKLQRH TAAQSSTDSA CDNCPQTNGR TPDDTGAHID
TADAGAKGPA AADELPTMSP VRREV
//
