ID T0IWC6_9SPHN Unreviewed; 770 AA.
AC T0IWC6;
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=M529_06125 {ECO:0000313|EMBL:EQB33105.1};
OS Sphingobium ummariense RL-3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB33105.1, ECO:0000313|Proteomes:UP000015523};
RN [1] {ECO:0000313|EMBL:EQB33105.1, ECO:0000313|Proteomes:UP000015523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL-3 {ECO:0000313|EMBL:EQB33105.1,
RC ECO:0000313|Proteomes:UP000015523};
RX PubMed=24233594;
RA Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a
RT Hexachlorocyclohexane-Degrading Bacterium.";
RL Genome Announc. 1:e00956-13(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:EQB33105.1}.
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DR EMBL; AUWY01000048; EQB33105.1; -; Genomic_DNA.
DR RefSeq; WP_021317142.1; NZ_AUWY01000048.1.
DR AlphaFoldDB; T0IWC6; -.
DR STRING; 1346791.M529_06125; -.
DR PATRIC; fig|1346791.3.peg.1170; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000015523; 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 Reference proteome {ECO:0000313|Proteomes:UP000015523};
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 727..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; 84697 MW; 2A8B8CF90B350363 CRC64;
MASTQKNKTS AKVRPAGFPT RQQVIDFIAE SDQPAGKREI AKAFGLKGQE KIALKALLKD
MADEGLIDIG PARAFHKMGG VPKVTVLRIV DVDDTTLIAT PERWEAEGQP APRLRVVERG
KPKTRQSALT IGDRILARTE EAGRGWVAHP MKKLAKASEE LLGVVEEGEG GKLWLRPVDK
RIRKDTPISD AGTAKRGDLV LAEPVGRPPR ISARVTDILG DPFAPRSFSL IAIHKHGIPH
VFPERAEEEA VVASALALHE DKREDLRHLP IVAIDPVDAR DHDDAVWAAP DEDAANPGGY
KAIVAIADVS YYVRPGSALD KEARKRGNSV YFPDLVVPML PHQLSSDMCS LRAGQDRAAM
ACHLTINAQG KVTGWRFTRA VIRVAAVLAY EDAQAAINGQ KDHDLLEPAL KPLWACWALL
QKARKARDPL ALDLPERRVV LDERGKIVSV AVRERLDAHM LIEDYMIAAN VAAAKALEAK
KAPVMYRVHE PPSREKLVAL KDYLATFDID FALGQVVKPS TFNRLIDRIG EAEEKPQIME
QILRSQTQAY YSPQNMGHFG LALGSYAHFT SPIRRYADLL VHRALVGAHG LELPAPKGGM
PPERTSLSGE DQENMGRVGE MISQHERRAM EAERETVDRY VAAFLAAHVG DLVEARITGV
QNFGFFATVE GLGGDGLVPV STLGEERFYY DEAARALEGV ESGDRYTVGQ RLPLRLAEAD
PINGSLRFEL PDLPAPRGGP LKRDRMRPGT KRGRPANIRH IGSKRGKHRR
//
