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Database: UniProt
Entry: A0A1G1FA10_9BACT
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ID   A0A1G1FA10_9BACT        Unreviewed;       714 AA.
AC   A0A1G1FA10;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=A2X56_01595 {ECO:0000313|EMBL:OGW28517.1};
OS   Nitrospirae bacterium GWC2_57_13.
OC   Bacteria; Nitrospirota.
OX   NCBI_TaxID=1801697 {ECO:0000313|EMBL:OGW28517.1, ECO:0000313|Proteomes:UP000177780};
RN   [1] {ECO:0000313|EMBL:OGW28517.1, ECO:0000313|Proteomes:UP000177780}
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|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:OGW28517.1}.
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DR   EMBL; MHDZ01000044; OGW28517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1FA10; -.
DR   STRING; 1801697.A2X56_01595; -.
DR   Proteomes; UP000177780; 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; 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   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          632..713
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   714 AA;  80333 MW;  0FFE6BE93A637BEC CRC64;
     MPTSDKELIE RIKARISRPM LIRELMRQLR IKPERKRELK RILDDLVMRG EIVRTRGNRF
     GLSEKMDLET GRFQAHPAGY GFVIPEKKGR PDIYIAARSR LDAMDGDTVV VRVSPPSERK
     KAPGKREGVI VRILARAHTK VVGSFELSPS QAGVYGFVTP SNPRIAHDVI IGQKNAGGAS
     DGDLVSAELI SYPMLGRPPE GRIIRIIGKP GQPGIEAEIV IEEHELPVEF HPAALKEAEA
     VPQEVMPSMS RGRRDLRDLP TATIDGETAK DFDDALSIEK IPTGYRLWVH IADVANYVKE
     GSYLDQEAYR RGTSVYLPDR AIPMLPTSLS NGICSLNPGV DRLTLTAEMD FTSQGVLSRY
     DLYESVIRSN ERMTYTAVKE ILVDRDRAQR RRYAALAPQF ELMGELMEIL RKRRMKRGSI
     DFDLPEPQIV LDLQGKISDI TRAERNRAHM IVEEFMLAAN ETVAAHMEER EIPCVYRVHD
     EPKEDAVLAL QEFLSSVGIT LAAGKKLKPL HLQRAVEQAK GTPLEAAVNT VILRAMKQAR
     YATENSGHFG LAAETYTHFT SPIRRYPDLM VHRITKQAIR GLAVKDTATA DDAEAFLSKA
     AAHSSLRERV AMEAERDVVT MLKLQFMKDR IGESHKGVIT GVTAFGFFVQ LNALFVEGLV
     HVSSLTDDYY HYIENQHSLR GEQKKKAYRI GDQVTVRVDR VDRERKRIDF TLAK
//
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