ID A0A1G2D7X7_9BACT Unreviewed; 721 AA.
AC A0A1G2D7X7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=A3D65_06950 {ECO:0000313|EMBL:OGZ09582.1};
OS Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_02_FULL_50_13.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798661 {ECO:0000313|EMBL:OGZ09582.1, ECO:0000313|Proteomes:UP000177996};
RN [1] {ECO:0000313|EMBL:OGZ09582.1, ECO:0000313|Proteomes:UP000177996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGZ09582.1}.
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DR EMBL; MHLL01000018; OGZ09582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2D7X7; -.
DR STRING; 1798661.A3D65_06950; -.
DR Proteomes; UP000177996; 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; 2.
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; 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 639..720
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 40..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 82445 MW; D450EACDA3D03611 CRC64;
MPACTFKRTR HRYPQITISL YRREQSGVKH QMKYLKKQYR PKGEWQKDRA RRRVKQEAKK
HISTHRTETA TNGNDSREDG HPRFPTNHEV EGTIRVSSKG VGYVEVEGMK EDVEIDPAFL
GTALDQNRVR IVLHGKITGS RQTGEVTAIL FRSKTKFTGV LDREGGSFFL IPDDHRMYKN
ILIPAQNLHG AQKGEKVFVE MKDWKDARKE PLGEVLRVLG VPDTHEVEMQ AIVLERGFDT
TFDPDVLLAA EEIPLAIPED EAAKRRDFRE TLTFTIDPHD AKDFDDALSW KKLPEGKIEV
GVHIADVSHY VTPGIRIDKE ALERGTSVYL VDRTIPMLPE RLSNGICSLV EGEDRLTFSA
VFTMDPRGKL LGEWFGRTII HSAKRFSYEE AQAVIDTGKG PHCEALLSLN AIAKILRNKR
IEAGAIAFEA EEVKFELDKN GKPLRVYKKV LQDTNKLIEE FMLLANKRVA ELIATKDKRA
ESVFVYRVHD QPNEERMQDL RDFLHGIGYN LKLDKNGQIS SHNINKMLED VRGRAEEAMI
QMATVRSMAK AVYATKNIGH FGLGFEYYTH FTSPIRRYPD LMVHRLLESY LKGHPVPKKK
LEEQEHLARY SSQMEVAAAE AERASIKYKQ CEYFAERIGL EIAGTISGVT EWGIYVEDPE
TKAEGMVHVR DIPNDYYFFE QKNYRIIGKS KGKSYRLGDK VRVKIATVDL KKKLIGMKLV
S
//