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Database: UniProt
Entry: A0A1F6VF70_9BACT
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ID   A0A1F6VF70_9BACT        Unreviewed;       676 AA.
AC   A0A1F6VF70;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=A2738_02405 {ECO:0000313|EMBL:OGI68287.1};
OS   Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_01_FULL_42_15.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1801742 {ECO:0000313|EMBL:OGI68287.1, ECO:0000313|Proteomes:UP000178235};
RN   [1] {ECO:0000313|EMBL:OGI68287.1, ECO:0000313|Proteomes:UP000178235}
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:OGI68287.1}.
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DR   EMBL; MFTS01000004; OGI68287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6VF70; -.
DR   Proteomes; UP000178235; 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; 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   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          595..676
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          29..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  76037 MW;  5E09FC8DDADDD010 CRC64;
     MKNSKNNPSN RLEGIISITS KGTGYVAVGD LPAGRQGKNN NQDPEIDSKH LNTALHGDTV
     EIVLHPKGKN RQTAEVSKII SRAKIGFAGV LELQGSMFFL KPDDTKMYTD ILIPENMLNG
     AKAGQKVFAE IVSWTDPRKA PEGKVTKILG TPGDNDAEMH AIAIEKGFDS KLPEKVYREA
     EEIKKGGIKE SDYAGRRDFR KILTFTIDPA DAKDFDDAIS FRRITSPQPS PGEERGKAPS
     PFQGKAGDEV FEIGIHIADV SHYVKVGSAL DKEARERGTS VYLVDRTIPM LPEELSNDLC
     SLVPNKDRLT MSAVFVIDKN AKVKSEWYGR TVIHSQKRFT YEEAEESLGH RPATGEAIKK
     TGDPLHKELA ILNNLAKLLT TERFKNGAIS LEQEEVKFVL DPTGVPIKVI TKERGDSNRL
     VEEFMLLANK KVAEILSKNL SLYRIHDLPS KEKMADLAYF LRSLGHKISL VNGIISSHEI
     NKLLKKLEGK NEEGTVNRAV IRSMAKAIYS TKNIGHYGLA FEYYTHFTSP IRRYPDIIVH
     RLLTDYLSGK KVSKEHLLEY EKTARISSEQ EKRASDAERA SIKYKQVEYM SKRTGESFEG
     VISGITEWGI YVEETETKCE GLVRVRDMKD DFYIFNEKKL ELVGQKRKKK YKLGDKVKIK
     VKGVDLERKT IDYILL
//
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