ID E6WR29_PSEUU Unreviewed; 819 AA.
AC E6WR29;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=Psesu_0923 {ECO:0000313|EMBL:ADV26774.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV26774.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV26774.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) 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}.
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DR EMBL; CP002446; ADV26774.1; -; Genomic_DNA.
DR AlphaFoldDB; E6WR29; -.
DR STRING; 743721.Psesu_0923; -.
DR KEGG; psu:Psesu_0923; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000008632; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 712..793
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 89993 MW; DE14696F8D88BEE7 CRC64;
MNKTGSRGSS RKGAGGAGAG KGAGSSVGGK GGKRQAGKLP PWMPEPAPAT RQAGRSGAGN
APSAARPPRR NTAGPAVTDP FAAREAQRYD NPIPSREAIL AVLEEAEGPQ TAEQLAGLLG
LHDPERFDAL GKRLGAMVRD GQLVQNRRGG FAPVEQTNLI PGVVIANPEG FGFLRPDSGG
GDDLFLPPYE MRKVMHGDRA LANVTGIDRR GRREGSIARV LERGVHRLVG RFGSEAGISF
VIPDDRRMQR NLHIPPDATC GAREGQLVVC EIVAPPDTRR PPIGKVVAVL GDSLTPSLVV
ETAIHSHNLP HEFPPEVLDE ATAVPLTVEP SMIGDRVDLR ELPLVTIDGE DAKDFDDAVY
CEPNRQGFRL VVAIADVSHY VRPGTPLDDE AQKRATSVYF PGFVVPMLPE TLSNGICSLN
PKVDRMCFVA DMQVDHDGEV VRSKFYEAVM NSHARLTYTQ VWKAVGEDDA EAKAQIGALM
PQVERLHQLY QVLAAARARR GAIEFESSEV RFVLDNRGEV TQAGMLPRND AHKLIEECMI
AANVEAARYL IRSHIPAPFR IHEKPPESKY ADLLEFLKEF GLALPPWSKV VPGDFTRLLK
KVRDRADATL LESVLLRSQS LAIYSPDNAG HFGLALEAYA HFTSPIRRYP DLLVHRAIKH
ALKRGKPEAY QYSARDMAGL ALQCSERERR ADEAEREVDE RYRAAWMEKH VGGQFDGVVS
GVTSFGLFVE LDQSKVNGLV HVTQLPHDYY QFDPIRKMLS GERRGLEFRL GDRVRIVVLK
ASMEDRKIDF RLVDDPAHDA GLPPLPPRGK PAKRPKKRY
//
