ID A0A0J7Y2H2_9SPHN Unreviewed; 785 AA.
AC A0A0J7Y2H2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=V473_06885 {ECO:0000313|EMBL:KMS57912.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS57912.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS57912.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS57912.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(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|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:KMS57912.1}.
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DR EMBL; JACT01000001; KMS57912.1; -; Genomic_DNA.
DR RefSeq; WP_066605229.1; NZ_KQ130434.1.
DR AlphaFoldDB; A0A0J7Y2H2; -.
DR STRING; 1420583.V473_06885; -.
DR PATRIC; fig|1420583.3.peg.1384; -.
DR Proteomes; UP000052232; 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:UP000052232};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 665..746
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..785
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 86077 MW; D47D5FC6437C27BB CRC64;
MASTPKNKAS APPRAPVRTK VRPAGFPTRD AVMDFITSSD QPAGKREIAK AFGLKGQEKI
ALKALLKDMA DEGLIDLGPA RAFHKMGGVP KVTVLRIVDV DDTTLIATPE RWEAEGQPAP
RLRVLERGKR GALTIGDRIL ARTEEAGRGY VAHVMKKLAK ASEELLGVVE VMADGKLWLR
PVDKRVRKDT PISDVGNAKP GDLVLAEPHG RPPRIAARVT DILGDPFAPR SFSLIAIHKH
GIPHVFPERV EEEAITASAL PLHEDKREDL RHLPIVAIDP SDARDHDDAV WAIPDDDDAN
AGGYKAIVAI ADVSYYVRPG SALDKEARKR GNSVYFPDQV VPMLPHDLSS DMCSLRAGQD
RAAMACHLTI NANGKVTAWR FTRAVIRVAA VLAYEDAQAA IDGAEDDATP TPSRKQADAL
LDVALQPLWA CWSLLRKARD ARDPLALDLP ERRVVLDEHG KIVSVAVRER LDAHMLIEDY
MIAANVAAAK ALEAKKAPVM YRVHEAPGRE KLVALKDYLA TFDMDFALGQ VIRPSTFNAL
IRKIAESEEK EQIMVQILRS QTQAYYSPQN MGHFGLALGS YAHFTSPIRR YADLLVHRAL
VGAYSLELPA QKGGTIPDRT ALSQDDYENM GRVGELISGH ERRAMEAERE TVDRYVAAFL
SAHVGEIVKA RITGVQNFGF FATVDGLGGD GLVPVSTMGA EHFFYDEAGK ALQGVESGDR
YTVGQRLELR LAEADPINGS LRFELPDNPA PRSGPMKRDR TRPGAHRGRP INIRHQGAKR
GKHKR
//
