ID A0A2M8S1N5_9PAST Unreviewed; 787 AA.
AC A0A2M8S1N5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CVP05_08335 {ECO:0000313|EMBL:PJG85024.1};
OS Conservatibacter flavescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Conservatibacter.
OX NCBI_TaxID=28161 {ECO:0000313|EMBL:PJG85024.1, ECO:0000313|Proteomes:UP000229329};
RN [1] {ECO:0000313|EMBL:PJG85024.1, ECO:0000313|Proteomes:UP000229329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_4 {ECO:0000313|EMBL:PJG85024.1,
RC ECO:0000313|Proteomes:UP000229329};
RA Christensen H.;
RT "Reclassification of Bisgaard taxon 7 as Conservatibacter flavescens gen.
RT nov., sp. nov.";
RL Submitted (NOV-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:PJG85024.1}.
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DR EMBL; PHHA01000019; PJG85024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8S1N5; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000229329; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 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:UP000229329};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 648..729
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 730..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..787
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 787 AA; 90350 MW; 5A632A4BB5ED5128 CRC64;
MPKKKTSLDP NFHIEAKKYP NPIPSREFIL SIIREHNAPM TKEEILTALS ISDESEKEGM
RRRLRAMEND GQLVFTKRKR YALPEKLDLL KGMVVGHRDG YGFLQIDGQK EDWFISNVQM
QRAMHGDYVL AQPNGIDRRG RKEVRIVRVL ESRKTQIVGR FFLEAGIGYV VPDDSRISRD
ILIPNEHRKG ARMGQVVVVE LQPRTASFTQ AVGKVVEILG DNMAKGMEVE IAVRNHEIPH
VFPKSVEKYV QRFSEQVPEE AKKGRVDLRH LPLVTIDGED ARDFDDAVYC QKQSNGWKLW
VAIADVSYYV RLNTALDKEA YQRGTSVYFP NRVIPMLPEV LSNGLCSLNP QVDRLCMVCE
LDISNKGKMT GYKFYEAVMN SHARLTYSKV WKILEGDETL RERYCVLVPH LENLYEMFKA
LLNARRQRGA IDFETLETKF IFNAQGRIER IEPVVRNEAH KIIEECMILA NIAAANFMER
HQEAALYRIH ATPSEEKLTA FRGFLRECGL VLEGGLKPTT ADYAKLLEQV RERPDHELIQ
TMLLRSLSQA VYDPDNIGHF GLALAEYAHF TSPIRRYPDL TLHRGIKYLL AKKEGSKRRT
TDGGGYHYTL DEMDILGEHC SMTERRADEA TRDVADWLKC EYMQDHVGEE FNGVISSVTG
FGLFVRLDDL FIDGLVHVSS LDNDYYRFDV ARQVLVGENS GMLYRLGDKV RIRVEAVSLE
QRQVDFSLVS SQRTPRRAGK TNKEKLKKNM RYAESLEKQR KHKGKSEKAK GKKSKLTKKA
AKKSVKR
//
