ID A0A0A2HZ38_9BACT Unreviewed; 733 AA.
AC A0A0A2HZ38;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 02-APR-2025, entry version 41.
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 ORFNames=JT06_17190 {ECO:0000313|EMBL:KGO32995.1};
OS Desulfobulbus sp. Tol-SR.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
OC Desulfobulbales; Desulfobulbaceae; Desulfobulbus.
OX NCBI_TaxID=1536652 {ECO:0000313|EMBL:KGO32995.1, ECO:0000313|Proteomes:UP000030148};
RN [1] {ECO:0000313|EMBL:KGO32995.1, ECO:0000313|Proteomes:UP000030148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Abu Laban N., Tan B.-F., Dao A., Foght J.;
RT "Draft genome of Desulfobulbaceae bacterium Tol-SR obtained by stable
RT isotope probing of toluene-degrading sulfate-reducing culture enriched from
RT oil sands tailing of Alberta, Canada.";
RL Submitted (SEP-2014) 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 -!- 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:KGO32995.1}.
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DR EMBL; JROS01000120; KGO32995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2HZ38; -.
DR STRING; 1536652.JT06_17190; -.
DR Proteomes; UP000030148; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:TreeGrafter.
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; 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; IPR050180; RNR_Ribonuclease.
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 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:UP000030148};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 644..725
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 733 AA; 83247 MW; D561187C98D2C10F CRC64;
MNKAGSQRPR LKERRLSPES PVSIENDILA FLYQHGAPAA ITELMAGLAH GQAEKNDLET
AIESLIADKL VKKSGKREYS LCKHAPLYEA VLEQNPRGFG FGAHCTSTVD APALKRDPFI
SASRMRLARQ GDRILIRVHR TRSDERPEAS VIKILARGTK RLAGFFIRDR TGCHIVPEDI
RFPFTVSVDA GKYTDVGDGE VVIVRIDESD QSYGNVRGEI LEILGPADNI DVQMRLVIEK
YKIPYEFSEK TGKETAALTD EITPEPGRED LRDILHMTID GETAQDFDDA IAVIKTKSGF
RLYVSIADVS HFVPAESAID HDAYERGTSI YFPGRVIPML PEKLSNNLCS LVPDQDRLTL
TAILNFDRQG TLKEKRLARS IIRSRQRFTY TTVRKILVDQ DKETRNAFKP FLTPLKWAGE
LARALHQKRR DRGALGFTLP EADIELEEDG RIRSIRRAEH NFAHQVIEEF MLAANEAVAA
TFTEQQRAIL YRIHELPAPD KVEEFSIFAK TLGLQLPKVE NSPHWFARVL DLCSGSPKEY
IVNNLLLRTM QQARYSPDNV GHFGLAATDY THFTSPIRRY PDLMVHREVC RLIKLQHDKG
TSHRKHFNLK EAGDFLSSRE RIAISAEREM TDRLKMIFME KHIGETFDAV ISGVTDSLLF
FELLQLFVNG AVAVEDMEGE HFFHEPRQHR LTGEISRKVY QIGNLVRVIL VDVDRSRKRI
NFKLASDKEE IPG
//
