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Database: UniProt
Entry: A0A1G2D7X7_9BACT
LinkDB: A0A1G2D7X7_9BACT
Original site: A0A1G2D7X7_9BACT 
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
//
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