ID T0J2B0_9SPHN Unreviewed; 770 AA.
AC T0J2B0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=RLDS_03155 {ECO:0000313|EMBL:EQB18260.1};
OS Sphingobium lactosutens DS20.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1331060 {ECO:0000313|EMBL:EQB18260.1, ECO:0000313|Proteomes:UP000015531};
RN [1] {ECO:0000313|EMBL:EQB18260.1, ECO:0000313|Proteomes:UP000015531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS20 {ECO:0000313|EMBL:EQB18260.1,
RC ECO:0000313|Proteomes:UP000015531};
RX PubMed=24051323;
RA Kumar R., Dwivedi V., Negi V., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium lactosutens Strain DS20T, Isolated
RT from a Hexachlorocyclohexane Dumpsite.";
RL Genome Announc. 1:e00753-13(2013).
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|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:EQB18260.1}.
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DR EMBL; ATDP01000056; EQB18260.1; -; Genomic_DNA.
DR RefSeq; WP_021224589.1; NZ_ATDP01000056.1.
DR AlphaFoldDB; T0J2B0; -.
DR PATRIC; fig|1331060.3.peg.576; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000015531; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
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 650..731
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 725..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..770
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 84621 MW; 955181A929D0EF41 CRC64;
MAFNQKQKKP AKVRAAGLPT RQQVMDFIAE ADTPAGKREI AKAFGLKGQE KIALKALLKD
MADEGLIDIG PARAFHKMGG VPKVTVLRIV DVDDTTLIGT PEKWEAEGQP APRLRIVERG
KSKTRQSALT IGDRVLARTE EAGRGWIAHP MKKLAKASEE LLGVVEEMAD GKLWLRPVDK
RIRKDTPISD AGNARPGDLV LAEPHGRPPR ISARVTDILG DPFAPRSFSL IAIHKHGIPH
IFPDRVEDDA LTVAALPLHE DKREDLRHLP IVAIDPVDAR DHDDAVWAAP DEDEGNPGGY
KAIVAIADVS YYVRPGSALD KEARKRGNSV YFPDLVVPML PHQLSSDMCS LRAGEDRAAM
ACHLTINAQG KVTAWRFTRA VIRVAAVLAY EDAQAAIDGT RDNALLEPAL KPLWACWALL
QKARKARDPL ALDLPERRVV LDEAGKIVSV AVRERLDAHM LIEDYMIAAN VAAAKALEQK
KAPVMYRVHE PPSRDKLVAL KDYLATFDIG FALGQVVKPS TFNQLIAKIG EAEEKPQIME
MILRSQTQAY YAPQNMGHFG LALGSYAHFT SPIRRYADLL VHRALVGAYG LDLPVPKGKD
VPDRSSLSQD DYENMGRVGE MISGHERRAM EAERETIDRY VAAYLSAHVG EVMPARITGV
QNFGFFATVE GLGGDGLVPV STMGAEHFFY DEAGRALQGV ESGDRYTVGQ RLELRLADAD
PINGSLRFEL PDSPAPRGAP MKRDRTRPGI KRGRPANIRH IGGKRGKHRK
//
