ID A0A0W0Y489_9GAMM Unreviewed; 726 AA.
AC A0A0W0Y489;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=vacB {ECO:0000313|EMBL:KTD51836.1};
GN Synonyms=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=Lqui_0680 {ECO:0000313|EMBL:KTD51836.1};
OS Legionella quinlivanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD51836.1, ECO:0000313|Proteomes:UP000054618};
RN [1] {ECO:0000313|EMBL:KTD51836.1, ECO:0000313|Proteomes:UP000054618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD51836.1,
RC ECO:0000313|Proteomes:UP000054618};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD51836.1}.
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DR EMBL; LNYS01000006; KTD51836.1; -; Genomic_DNA.
DR RefSeq; WP_058506783.1; NZ_UGOX01000001.1.
DR AlphaFoldDB; A0A0W0Y489; -.
DR STRING; 45073.Lqui_0680; -.
DR PATRIC; fig|45073.5.peg.717; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000054618; 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; 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:UP000054618};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 638..719
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 726 AA; 83068 MW; EDAD562681EE02A0 CRC64;
MSKKSKDPYY KREKEKYEVP IPSREFIMQV LEEYGRPMTR QQLLTRLAVE DENEQEVLGY
RLKAMLRDGQ IMQDRRNRFC LLKRINLQRG TVQGHPDGFG FFIPDDGSDD FVLSATEMRA
VMHGDVVLAF QSGFDRRGRP EGQIHEVIEH GNLSVVGKFF TEHGVGFVIP DNKRLTQDIA
IPLGFSAEAK NGQMVLAEII AFPSKRNQAI GKIVHILGDH MAPGMEIEVA IHAHAIPAEW
PPEVQSEMTR VPQSVTEDQI KGRTDLRDLP FVTIDGEDAR DFDDAVYCYK KPKGGFQLYV
AIADVSHYVK VGSALDQEAS RRGNSVYFPG KVVPMLPEAL SNGICSLNPH QDRLCMVAEM
AISSEGKITR SRFYRAVFHS HARLTYNQVG DWLEQGNADE THQPLWPMLE NLYDLYRVLL
KARKLRGAMD FETTETKIEF DDKRKIKKIV PVVRNDAHRL IEECMLAANV ATARFLEKAE
IPALYRVHEV PEEDKITALR QFLGELGLRL EGGKKPSPKD FQKTLSMIHD KHERHLIETV
MLRSLKQAQY REDNEGHFGL AYPAYTHFTS PIRRYPDLLI HRAIGHLLDK KDSDSFGYSH
DEMNKLGKHC SMTERRADEA TREVVSWLKC EYMQDKLGQT FHGTISAVTG FGIFVELDEI
YVEGLVHVTS LRNDYYSFDA VKHRLVGERT NQTYRLGDKM TVLVARVDLD ERKIDFEPVD
EEKKNG
//
