ID B0KKY5_PSEPG Unreviewed; 857 AA.
AC B0KKY5;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN OrderedLocusNames=PputGB1_4936 {ECO:0000313|EMBL:ABZ00821.1};
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869 {ECO:0000313|EMBL:ABZ00821.1, ECO:0000313|Proteomes:UP000002157};
RN [1] {ECO:0000313|EMBL:ABZ00821.1, ECO:0000313|Proteomes:UP000002157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1 {ECO:0000313|EMBL:ABZ00821.1,
RC ECO:0000313|Proteomes:UP000002157};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000926; ABZ00821.1; -; Genomic_DNA.
DR RefSeq; WP_012274448.1; NC_010322.1.
DR AlphaFoldDB; B0KKY5; -.
DR KEGG; ppg:PputGB1_4936; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000002157; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR013668; RNase_R_HTH_12.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08461; HTH_12; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 665..746
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 754..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..857
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 96548 MW; 686CBEED15D2624C CRC64;
MADWQSLDPE AAREAEKYDN PIPSRELILQ RLADRGEPAA REELAKEFGL YEEDQIEALR
RRLRAMERDG QLIYTRRGTY APVDKLDLIC GRISGHRDGF GFLIPDDGSD DLFLGPSQMR
LAFDGDRALA RVSGTDRRGR REGVIVEVIS RAHESVVGRY FEEGGIGYVT PDNPKIQQEV
LVTAGRNGGA KIGQFVEIKI THWPTPRFQP QGDVVEVIGN YMAPGMEIDV ALRSYDIPHV
WPADVVKEAR KFRSEVEEKD KEKRVDLRHL PFVTIDGEDA RDFDDAVYCE PLGKLRLFSG
GWRLYVAIAD VSSYVRLGSA LDVEAQQRGN SVYFPERVVP MLPEELSNGL CSLNPHVDRL
AMVCEMTMNK AGQMVDYQFY EGVIHSHARL TYNKVSSMLE HARTREGKAL REEYKEVVPD
LKNLYNLYKV LVDARHTRGA IDFETQETRI IFGDQRKIAE IRPTVRNDAH KLIEECMLAA
NVATAEFLQK HGVPALYRVH DGPPPERLEK LRAFLGELGL SLHKGKDPSP KDYQALLASI
AGRPDFHLIQ TVMLRSLSQA VYSTENNGHF GLNYEAYTHF TSPIRRYPDL LVHRAIRSII
RSKVDTPHVK RAGAMSIPKA RIYPYDENTL EQLGEQCSMT ERRADEATRD VVNWLKCEFM
KDRVGETFPG VITAVTGFGL FVELTDIYVE GLVHVSALPG DYYHFDPVHH RLSGERTGRS
FRLGDTIEVK VMRVDLDERK IDFEVSDKTL AAPIGRKQRG AAQATEKAEQ PPVAEAKATP
KPRSRKSEAS EAYFPKDAVQ RNAEVRKSRE MKKALMTDAR SSAGSKSEKG GKPSGKPTKH
RKGPPKSGAP RKSKSKS
//
