ID A6EL71_9BACT Unreviewed; 741 AA.
AC A6EL71;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
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=SCB49_05927 {ECO:0000313|EMBL:EDM45321.1};
OS unidentified eubacterium SCB49.
OC Bacteria; Bacteroidota; environmental samples.
OX NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM45321.1, ECO:0000313|Proteomes:UP000003659};
RN [1] {ECO:0000313|EMBL:EDM45321.1, ECO:0000313|Proteomes:UP000003659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCB49 {ECO:0000313|EMBL:EDM45321.1,
RC ECO:0000313|Proteomes:UP000003659};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM45321.1}.
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DR EMBL; ABCO01000001; EDM45321.1; -; Genomic_DNA.
DR AlphaFoldDB; A6EL71; -.
DR STRING; 50743.SCB49_05927; -.
DR Proteomes; UP000003659; 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 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000003659};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 656..737
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 741 AA; 84745 MW; FF4862CB6F4286F8 CRC64;
MKRKKKSFGR KRTKTINGLS DKILAILRKD HSKPYNYKQI AAKLNVDDAN SRNQIIKVLK
ELQGAKEITE IDRGKYILAP NQNYYTGRVD IAGRGQGYII VDELEDDILV KNKNLNKALN
GDTVEVYVYK RKRGGKSEGE ITKIIERKKT EFVGTISIQD RFAFVEMNDH KMYTDIFVHK
SNINGAKQGE RVLVEIIDWP EKADSPNGNV IKSLGMPGEH NTEIHSILAQ YGLPYEFPAE
VEDYANKIDT SIHASEIAKR RDMRKDLTFT IDPKDAKDFD DALSFTELEN GNYEIGIHIA
DVSHYLKPGT VLDDEAFERA TSVYLVDRVV PMLPEILSNG ACSLRPHEEK YTFSAVFEMN
KKAEVVNEWF GRTVTYSDAR FAYEEAQLII ENNSHPEPVE GQLNTTITSE ISITDKEYEV
EQPIAKAILE MDRLAKILRK ARMNNGAISF DKVEVKFILD KEANPEGVYF KESKDANKLI
EEFMLLANRS VAAFIGKQNP KKTFVYRVHD EPDDEKIAAL ENLIKQFGYK MDTRDKKSTS
QSLNQLLSDV VGKKEQNLID TLAIRSMSKA VYTTNNIGHY GLAFDYYSHF TSPIRRYPDV
MVHRLLQHYL DGNPSAKEDT FEENCRHCSD MEGLAARAER DSIKYMQIKY MKDHQDEEFV
GVISGVTEWG IYVEIVSNKC EGMVRIQDMQ DDIYEFIKED FAVVGRKNHT KFVLGDEVIV
KVKNADLARK HLDFTMLGPN D
//
