ID D1VT23_9FIRM Unreviewed; 704 AA.
AC D1VT23;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:EFA90305.1};
GN ORFNames=HMPREF0628_1561 {ECO:0000313|EMBL:EFA90305.1};
OS Peptoniphilus lacrimalis 315-B.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=596330 {ECO:0000313|EMBL:EFA90305.1, ECO:0000313|Proteomes:UP000005711};
RN [1] {ECO:0000313|EMBL:EFA90305.1, ECO:0000313|Proteomes:UP000005711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=315-B {ECO:0000313|EMBL:EFA90305.1,
RC ECO:0000313|Proteomes:UP000005711};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Peptoniphilus lacrimalis 315-B.";
RL Submitted (DEC-2009) 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:EFA90305.1}.
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DR EMBL; ADDO01000031; EFA90305.1; -; Genomic_DNA.
DR RefSeq; WP_004824396.1; NZ_ADDO01000031.1.
DR AlphaFoldDB; D1VT23; -.
DR eggNOG; COG0557; Bacteria.
DR Proteomes; UP000005711; 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 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000005711};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 616..695
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT COILED 581..608
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 704 AA; 80693 MW; B6B923EAE39AE8AE CRC64;
MIKEKILEVI KNSKPQTKED LAKVFNIKKR DRENFYFLLE NLQRQGLVFE DKKAKLIFVD
NKTYFFGKIQ TSKKGFGFLI TENLDEDIYI SEENLNFALN GDDVIVKKYK DSSGSKPEGK
VVFIVERVNQ KVVGIFQATK NFGFVVADDA KFATDIYIPK KRMNGAKNGQ KVLVKIDKWP
SPGKKPEGRV LEILGYPDEP HVDILSVAKS LDIPMEFSKT VKREAKSLET SVQAEEIKSR
LDLRDKLTFT IDGADSKDFD DAVSLEILEN GNYLLGVHIA DVAHYVKEDS PIDEEAFLRG
NSVYLLNKVI PMLPFELSNG ICSLNEGVDR LTLSCIMEVD KKGQVINKKI CESVINSKKR
LVYDYVSDYL EDGVSDDSLI GLEETLKNMY ELSKILQEKR REMGSIDFEV PEALIKVTED
GWPTEILRRE RRSANKLIED FMLLANTTVA EYFFKFEIPF LYRIHEKPRE EKIQELNSYL
RPLGYMANFG SEIKSRDIQK LLKKVQGKKE ELFISTMALR AMAKARYSPK NDIHFGLCFQ
YYTHFTSPIR RYADLTVHRI IKDFLRGDLS KNKVKKLNDD LQGISEHISA TERVAQEAER
QVESIKMAEY MSDRIGKKYN GIISGITNFG IFVELENLIE GLVSYKTMKG FYEFDPVNYR
AVDVDTKNSF GIGDLVTIKV VNVNLTLGKI DFELESDDNE KEEG
//
