ID I4Z8A5_9BACT Unreviewed; 762 AA.
AC I4Z8A5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=PrebiDRAFT_0708 {ECO:0000313|EMBL:EIM32447.1};
OS Prevotella bivia DSM 20514.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM32447.1, ECO:0000313|Proteomes:UP000002786};
RN [1] {ECO:0000313|EMBL:EIM32447.1, ECO:0000313|Proteomes:UP000002786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM32447.1,
RC ECO:0000313|Proteomes:UP000002786};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Improved High-Quality Draft genome of Prevotella bivia DSM 20514.";
RL Submitted (FEB-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|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
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DR EMBL; JH660660; EIM32447.1; -; Genomic_DNA.
DR RefSeq; WP_004336731.1; NZ_JH660660.1.
DR AlphaFoldDB; I4Z8A5; -.
DR GeneID; 78530712; -.
DR HOGENOM; CLU_002333_7_3_10; -.
DR Proteomes; UP000002786; 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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
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:UP000002786};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 649..730
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 736..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 87499 MW; D50E1A3ABFA66BC2 CRC64;
MGKEKKSGKR LTKKQLFEVL ASFFQANPDD TFSFKEIFKA LKLTTHPAKM LAIDVMEEMA
WDDFLAKSGE NAYRLNTKGQ VQEGTFVRKA NGKNTFQPDD GGTPVFVSER NSMAALMGDR
VKVQFMARRQ HHIKEAMVIE ILQRKKDTFV GKLRVEKDIA FLVTQDNLFV HDILIPKKRL
KGGQTGDIAV VKVIAWPDPE HKNILGEVVD ILGEAGNNDV EMNSILAEYG LPYKYPKRVE
DAANKISAEI TKQDYAERED FREVWTCTID PRDAKDFDDA LSIRQLDKNT WEVGVHIADV
SHYVKENDII DREAQQRATS IYLVDRTIPM LPERLCNLIC SLRPDEEKLA YSVIFNLDAE
ANVKKYRIVH TVIKSNRRFV YEEAQQLLED NGVIDGKGMP APAPGKEGYK GEYAEQIILL
DRFAKLLREK RFKNGSVNFD REEMRFEIDE HGKPLQCYFK RSKDANKLVE EFMLLANKTV
AESVGKVAKG KNPKTLPYRV HDNPDPIKFE SLREFSAKFG YKLKSTSTKG ATARALNKLM
AEVEGTKEEK VIQTIALRSM MKAKYTIHNI GHFGLAFDYY THFTSPIRRY PDTMVHRLLT
RYQQGGRSGN KDHYEELCEH SSDMELVAQQ AERDSIKYKM VEFMSDHIGE CYDAHITGIQ
SYGLYAEIDE NHCEGMIPMR DLGDDYYDFD EKNYCLVGRR RHHIYQLGDP IRIQVAKANL
EKKQLDFTLE GNEANTYSGN IAQGKPAKQS HKKDSKKRRR RS
//
