ID A0A1E4J740_9BURK Unreviewed; 755 AA.
AC A0A1E4J740;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ABS94_05450 {ECO:0000313|EMBL:ODU18372.1};
OS Variovorax sp. SCN 67-85.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1660152 {ECO:0000313|EMBL:ODU18372.1, ECO:0000313|Proteomes:UP000094461};
RN [1] {ECO:0000313|EMBL:ODU18372.1, ECO:0000313|Proteomes:UP000094461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU18372.1}.
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DR EMBL; MEFM01000011; ODU18372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4J740; -.
DR Proteomes; UP000094461; Unassembled WGS sequence.
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; 3.
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 594..675
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 83457 MW; F467DBE0DB3A0891 CRC64;
MLDEFEGTVQ GHRDGHGFVQ RDDGEADIYL PPNEMRAVLH KDRVKARVVR QDRRGRPEGR
VVEIVERSEQ PIIGRLLHEG GIWLVAPEDK RYGQDVLIPK GATGPAKVGQ VVVVQLTEPP
ALFGQPVGRV KEVLGEIDDP GMEIEIAVRK YGVPHEFSAE CLAEAKALPE KVRPADKKGR
VDLTDIPLVT IDGEDARDFD DAVYCEPAKV GRGKGWRLLV AIADVSAYVQ TGSGIDIDAY
DRATSVYFPR RVIPMLPEKL SNGLCSLNPE VERLCMVCDM LVAADGEIYA YQFYPAVMFS
HARFTYTEVA AILGNTRGPE AAKRKDRVKD LLNLADVYKA LLKQRGKRGA VDFETTETQI
ICDDAGRIEK IVPRTRNEAH RLIEEAMLAA NVCSADFIAE GKHPGLFRVH EGPTPEKKEI
LRGYLKAMGV GLSITDDPKP GEFQAIAEAT KERPDAQQIH TMLLRSMQQA IYTPINSGHF
GLAYEAYTHF TSPIRRYPDL LVHRVIKAIL GKTRYQLPML PTPGEAHAKL AKRLASRVKA
PTNKPQKATV APSKEVLAWE AAGLHCSANE RRADEASRDV EAWLKCKYMR EHLGEEYGGV
VTAATTFGIF VTLDAMYVEG LVHITELGGE YFKFDEMRQE LRGERTGIRY AIGTRVRVQV
SRVDLDGRKI DFRLVREGEE LMARAMKDKG AASSGVPVKA SAKRGTRHKA AEAGGGEPRG
ERGTSASAGP QSAMQAFKSA VKKAANKMKG RKPRR
//
