ID A0A1F5APS4_9BACT Unreviewed; 689 AA.
AC A0A1F5APS4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=A2Y70_04950 {ECO:0000313|EMBL:OGD20137.1};
OS Candidatus Aminicenantes bacterium RBG_13_64_14.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797271 {ECO:0000313|EMBL:OGD20137.1, ECO:0000313|Proteomes:UP000178665};
RN [1] {ECO:0000313|EMBL:OGD20137.1, ECO:0000313|Proteomes:UP000178665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD20137.1}.
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; MEXZ01000119; OGD20137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5APS4; -.
DR STRING; 1797271.A2Y70_04950; -.
DR Proteomes; UP000178665; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
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; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00357; CSP; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 601..681
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 689 AA; 76780 MW; D6EDBE133DAF087E CRC64;
MTALKILALL KRYKEGLPFD EILIELGVKR RDRAKALEEI RKLEARGQVR YLRSRFLLAE
KTDLVRGRFV TARPGFGFVT PEGGGKDIFI PARHAQGALP GDEVTVVVNE RGKFGKPEGK
VERILKKGRT ALLGVYRERG GAPFLQPFDS PSQDDVPLKS RGKLGPAPGM IVEADRATLA
VTRVFGMPED PGVDAHVVIR RYGLRQQFPE EVLGEAAGIP DVLSAGTIEG RRDFRDWPSV
TIDGEKAQDF DDAVSIRRLP AGGWLLGVHI ADVSHYVRPA SPLDGEAFER GTSVYFPDLT
LPMLPEKLSN DLCSLRPREP RLTVSALMDI GDDGRVGRTE FAPSIIRTAH RMTYASVFKI
LEGDAAEAKA YADVVPDLLL MRELARALRE RRLAEGSLDF DLVEPELVYE KGKLLAVAAT
ERNEAHRLIE EFMVTANVAA ATAFSEKKIP AVYRVHPPPD VGDLEKLRDL ILNFGLTLPE
PAKVRSNDLQ RVLKKAEGLP GEKFVGRQVL RAMKLAVYST GNVGHYGLAQ DHYTHFTSPI
RRYPDLVVHR ILKGLLAREE PGRLDLDAIA AKSSERERNA AEAEQALLEW RIFRLLKDRL
GDEFSGMVVD VIKVGLIVEI EEYFVSGLLP FDSLRGDYEP KPAARRLRPR RLRKTFDLGD
EVRVILVSCD PALRRMSFVP AVDPEESRP
//
