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Database: UniProt
Entry: R6NJD7_9FIRM
LinkDB: R6NJD7_9FIRM
Original site: R6NJD7_9FIRM 
ID   R6NJD7_9FIRM            Unreviewed;       705 AA.
AC   R6NJD7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=BN627_02068 {ECO:0000313|EMBL:CDC08449.1};
OS   Lachnospiraceae bacterium CAG:364.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1262983 {ECO:0000313|EMBL:CDC08449.1, ECO:0000313|Proteomes:UP000017986};
RN   [1] {ECO:0000313|EMBL:CDC08449.1, ECO:0000313|Proteomes:UP000017986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:364 {ECO:0000313|Proteomes:UP000017986};
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:CDC08449.1}.
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DR   EMBL; CBER010000078; CDC08449.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6NJD7; -.
DR   Proteomes; UP000017986; 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:UP000017986};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          622..702
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   705 AA;  80667 MW;  23AB6D243B6C39E9 CRC64;
     MRAKELAVLL QIPAGKREEL HKILDMLLEE GKISINKRGR YEAVRSSAAK KEAEKKSVKA
     ERKKGQYYTG TFISHPRGFG FLEIPEAEED IFIPEESIGT ALHGDTVQIV VKKDGKDGKR
     CEGEVVKVLE RGTREVVGTY QQCDGFGFVV TDNQRFLKDV FIPAGKSLTA EDGDKVLAEI
     KDHGNKRRSP EGKIIEILGK PGECGVDVLC VAKSYELPME FPEKVAKQAE RIKETLNEGD
     FYGREDLRDV VMVTIDGEDA KDLDDAVSLT KEEDLYHLGV HIADVSNYVQ YNSALDKEAL
     KRGTSVYLAD RVIPMLPKKL SNEICSLNAG EDRLALSCLM DIDKKGRVVS HRIVESVIHV
     KERMSYTDVK KILLQEDEEL AKCYEELLPM FFQMKELSEL LRNRRKKRGA IDFDFPESKL
     VLDERGKVID IYPYEQNIAT RLIEDFMLAA NETVAEEYCM LGLPFVYRTH ENPDMEKMET
     VLEMVHQAGI KVKKGKETIT PKEVQKILKE LEGMECEPFF ARLILRSMKQ AKYTVEDTGH
     FGLAAKYYCH FTSPIRRYPD LQIHRIIKET LRGKMTEAKI QHYRGILEEV ARQSSAMERR
     AEEVERETIK MKKAEYMKQH IGEAFEGTVS GVTEWGFYVE LDNTVEGLVH VNSLTDDYYT
     FDKDRYCLVG DMTGRAYRMG QRVKVWVENA DENTKTVDFK IERMG
//
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