ID C6PS99_9CLOT Unreviewed; 722 AA.
AC C6PS99;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 83.
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=CcarbDRAFT_1666 {ECO:0000313|EMBL:EET87896.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET87896.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET87896.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET87896.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-2009) 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|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:EET87896.1}.
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DR EMBL; ACVI01000021; EET87896.1; -; Genomic_DNA.
DR RefSeq; WP_007060551.1; NZ_CP011803.1.
DR AlphaFoldDB; C6PS99; -.
DR STRING; 536227.Ccar_22240; -.
DR KEGG; cck:Ccar_22240; -.
DR PATRIC; fig|536227.13.peg.4600; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000004198; 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 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:UP000004198};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 622..702
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT COILED 587..614
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 722 AA; 83309 MW; F697E5491B79B373 CRC64;
MNIRETLISF MTEQAYKPMN MRELERVFSI KKSERKVFEK VLEEMESDGD VVKTRTEYYG
IPDRMGLVVG KLQGHPKGFG FVITDDDRPD IFIPSSYMNG AMNGDKVVAK ITREENRGKK
CEGEIIRILQ RSNKTVIGVY EDSRNFGFVV PEEKRIYQDV FIPKGSRNGA KTGDIVIADI
TSWPDKRRNP EGTVVEILGK KGEKGIDILT IIKKNNLPEE FPVKVQGYAE GIPDEIPEEE
YERRKDLRDL TIVTIDGEDA KDLDDAVSLE KLPNGNYHLG VHIADVSNYV KDKNPLDKEA
LKRATSVYLI DRVIPMLPKK LSNGICSLNP KVDRLTLSCF MEIDKTGKVV DHNITESIIK
TNERMTYTDV TKILRDTDED VIKRYDYLVD TFKLMEELCG ILYKKRIQRG AIDFDFEECK
IILNELGKPI EIKPYERAIA NRIIEEFMLV CNETIAEHMF WANMPFVYRI HEEPDEEKLM
HFNEFVHNLG YVVRMGQEVH PKALQDIVEK VKGKKEETVV STLLLRSMMK ARYAPECTGH
FGLAARYYCH FTSPIRRYPD LIIHRIIKEF INGQIDDKRN KILTADVEYA SKQSSEMERV
AQDAEREVED LKKAEYMSER IGQEFEGIIS SVTNFGMFVE LPNTIEGLVH ISSLDDDYYV
YDEKHLSLIG ERTKNIYKLG DEAKIKVSKV DMFAHEIYFE LVKPEKDEEE LEVSNEIANN
VD
//