ID A0A2G0CGP9_9BACT Unreviewed; 764 AA.
AC A0A2G0CGP9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ECO:0000313|EMBL:PHK99097.1};
GN ORFNames=CGL56_06445 {ECO:0000313|EMBL:PHK99097.1};
OS Neolewinella marina.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Neolewinella.
OX NCBI_TaxID=438751 {ECO:0000313|EMBL:PHK99097.1, ECO:0000313|Proteomes:UP000226437};
RN [1] {ECO:0000313|EMBL:PHK99097.1, ECO:0000313|Proteomes:UP000226437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKG-38 {ECO:0000313|EMBL:PHK99097.1,
RC ECO:0000313|Proteomes:UP000226437};
RA Wang K.;
RT "The draft genome sequence of Lewinella marina KCTC 32374.";
RL Submitted (OCT-2017) 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:PHK99097.1}.
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DR EMBL; PDLO01000002; PHK99097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G0CGP9; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000226437; 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; 2.
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; 1.
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 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:UP000226437};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 654..734
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 740..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 86782 MW; C59BB7D3CD449C1C CRC64;
MRTDRPKGVI VLIPYMSKKN TKSGKLKARD LERALYQEFK SNARKQFNPK QLQRKLKVKN
SQESIQAALD KMVKTGKVKE NGDHLYQFNR AAAEKRSSQY AEGRVDMTRS GAAYIIMDGE
ANDIFVSQNR LGNAQDGDKV KVRYWTPSGR RKPEGEVSEV LERSVTHFVG TLKIHEKFAE
VVVDGPGGKS ISVAVHRSEL IGAKSGEKVV VQIVDWEENR FGQISGKITA VLGEPGTSNI
EMQAILINNG FQITFPDAVL AESEALPGEI TPQEINIRRD MREVTTFTID PLTAKDFDDA
LSIQTLEDGQ IEIGVHIADV SHYVKPGSAL DEEAASRTTS VYLVDRVCPM LPERISNELC
SLRPNEDKLT FSAVFKFDPK SFKVTDRWFG RTVIHSDRRF TYEEAQEVLD TGEGDFVDEL
DLMDRISDKL RKRRFKEGSI DFNTNEVRFR LDEEGKPLEV YIKDRIDTNM LIEDFMLLAN
REVATFIKKK EERLKQNIPF VYRVHDEPDM EKVAELANFA AALGYEMDLS SPKKVTESYN
KLLAKADEDP MVKMLAPIAI RTMSKAVYTT QNIGHYGLGF ENYTHFTSPI RRYADVLVHR
LLEKNLEEGS LYKANPEKLE ETCKHISSQE RKAVTAERES IKYKQTEFML GNVGEEFDGV
INGLADFGVF IELIDNFVEG MIPFDKMDEA YDISAGKLSI TGKQSGKKLK MGDVVRVRIE
DVDLDRRRID MSLVKVLKVH GQPERKEDAK PKKSRGKRRK MRNG
//
