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Database: UniProt
Entry: R7N1Y6_9FIRM
LinkDB: R7N1Y6_9FIRM
Original site: R7N1Y6_9FIRM 
ID   R7N1Y6_9FIRM            Unreviewed;       712 AA.
AC   R7N1Y6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=BN816_01287 {ECO:0000313|EMBL:CDF06566.1};
OS   Firmicutes bacterium CAG:95.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262988 {ECO:0000313|EMBL:CDF06566.1, ECO:0000313|Proteomes:UP000018182};
RN   [1] {ECO:0000313|EMBL:CDF06566.1, ECO:0000313|Proteomes:UP000018182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:95 {ECO:0000313|Proteomes:UP000018182};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDF06566.1}.
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DR   EMBL; CBKF010000050; CDF06566.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7N1Y6; -.
DR   STRING; 1262988.BN816_01287; -.
DR   Proteomes; UP000018182; 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; 3.
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; 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; 2.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
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:UP000018182};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          630..710
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   712 AA;  81669 MW;  344FCF09CAB655E5 CRC64;
     MKKKTREERK NLIIQLVEDS CYVPMKEKEL AIFMQVEPEE REELKSILQE LLNEGSLQMT
     KRGKYIKGDG QAKQQVGTFI SNSRGFGFVE VEGQEEDLFI PEDYTGGAFH LDTVQVELLK
     DQRGKRKEAR VTGILMHGIE QVVGTYDKCK SFGFVIPDNE KLNTDIFIPV ERSKGAVTGH
     KVVAQITDYG DTKHKPEGKI IEILGHVNDP GVDILSIVKG FALPTEFPER VLNQAERVAK
     EVSEADRAGR KDLRQLMTVT IDGEDAKDLD DAISLSYEDG KYNLGVHIAD VSNYVQENSA
     LDREALERGT SVYLVDRVIP MLPHVLSNGM CSLNMGEDRL ALSCLMTVDQ KGNVIDHEIV
     ESVIHVDERM NYTDVNKILE EHDPVLCRRY EAQVSMFHCM KKLADILREK RKSRGSIDFD
     FPESKIELDK EGNPISIKPY ERRIANKIIE DFMLLANETV AQHFYWMEIP FVYRTHETPD
     PEKIMKLGTF IRNFGYNIKV KTGDNEIHPK EIQKLLGKIE GTPEEALLSR LTLRSMKRAS
     YQTECMGHFG LACPYYCHFT SPIRRYPDLQ IHRIIKEQLR GRMDGKRILH YEEILPEVAK
     HSSRMERRAD EAERETEKLK KAQYMVSRIG EKFEGVISGV TAWGIYVELP NTVEGMVHVS
     RMAGDYYYYD EQAYEMIGRD TGRTFRLGQK VDVIVDDVDL QMKSVDFVLQ KE
//
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