GenomeNet

Database: UniProt
Entry: R6SDE0_9FIRM
LinkDB: R6SDE0_9FIRM
Original site: R6SDE0_9FIRM 
ID   R6SDE0_9FIRM            Unreviewed;       722 AA.
AC   R6SDE0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=BN586_01677 {ECO:0000313|EMBL:CDC55574.1};
OS   Dorea formicigenerans CAG:28.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1263073 {ECO:0000313|EMBL:CDC55574.1, ECO:0000313|Proteomes:UP000018109};
RN   [1] {ECO:0000313|EMBL:CDC55574.1, ECO:0000313|Proteomes:UP000018109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:28 {ECO:0000313|Proteomes:UP000018109};
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:CDC55574.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CBFN010000088; CDC55574.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6SDE0; -.
DR   Proteomes; UP000018109; 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; 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; 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000018109};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          630..710
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   COILED          588..622
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   722 AA;  82868 MW;  2ECCEC0A185D6F50 CRC64;
     MSNKTFEKRK KIIYDFICDD MYVPMKFKEM AMVLQVNKEQ RDELRQVLES LEEEGKICLS
     KRGKYCKGEA KRLQGTYRAN QRGFGFVIIP EEDQDIFIGE DDAGGALDGD IVEVIITKAS
     DRDGKRREGK IVKIVERSLT TVVGLYQKKG NKSYGFVIPD NQRILQDIFI PEGKSKEAVD
     GHKVVVELTS YGEKGRSPEG RIVEIIGHVN DPGTDIMSIV KGYDLPVEFP EKVLNQAERV
     SKPVSEADMQ GRKDIRDWQM VTIDGEDAKD LDDAVSVVKN GENYILGVHI ADVTNYVQEN
     SALDREALKR GTSVYLADRV IPMLPHTLSN GICSLNAGED RLALSCIMTV DPKGMVIDHE
     IAETVIHVDR RMSYTSVAKI LEDEDLAEMQ EYEELVPMFQ RMLELSKILR ARRKQRGSID
     FDFPETKMIL DENGHPIDIK PYDRNVATKI IEDFMLLANE TVAEDYYWQE MPFVYRVHEA
     PDDEKIRALA TFINNFGFSM HIGANEVRPK EIQKLLGKVE GTPQEALISR LALRSMKQAR
     YTPENSGHFG LAANYYTHFT SPIRRYPDLQ IHRIIKDNLR GRMNGERMEH YRKILEEVTK
     HASETERRAD EAERETVKLK KVEYMSDRIG NVYTGVISGV TKWGMYVELP NTIEGLIHVA
     NMRDDHYNYD ESRYEMVGER TGKVYKLGQE VRVRVADTDR LMRTIDFVIA KERDEENGED
     EW
//
DBGET integrated database retrieval system