ID A0A134ACC5_9FIRM Unreviewed; 705 AA.
AC A0A134ACC5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=HMPREF1863_01465 {ECO:0000313|EMBL:KXB65369.1};
OS Peptoniphilus coxii.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=755172 {ECO:0000313|EMBL:KXB65369.1, ECO:0000313|Proteomes:UP000070442};
RN [1] {ECO:0000313|Proteomes:UP000070442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00729 {ECO:0000313|Proteomes:UP000070442};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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:KXB65369.1}.
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DR EMBL; LSDG01000043; KXB65369.1; -; Genomic_DNA.
DR RefSeq; WP_068368954.1; NZ_KQ960181.1.
DR AlphaFoldDB; A0A134ACC5; -.
DR STRING; 755172.HMPREF1863_01465; -.
DR PATRIC; fig|755172.3.peg.1426; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000070442; 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; 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:UP000070442};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 619..698
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 705 AA; 80493 MW; 0D1D0B50DE4C75A6 CRC64;
MTIRERVLET IEKKGPLSER TLFKALQVNG NLQKEMKALL RDMVKEGSLY RDEESRYHSS
EQEGLMVGRL QGNEKGFGFF VADDEDQDDL YIHRTKINSA MHNDRVLVKG IESKDPSKGD
EGRVVTVLDR SNERVVGVYD DAGKFGFVMP DEKKISDDIF IPSRWKNGAK SGQKVVVDIE
RFPSDDKKAE GKIVEILGYP DEKGVDILSI AYAMGLDLEF PKEVLDEAHR VPQEVPKEAI
EKREDFRSAP TFTIDGADSK DFDDALSVEK LPNGHYRIGI HIADVAEYVK AGSALDKEAY
HRGNSVYLIN KVLPMLPEEL SNGICSLNEG VDRLCLSVIV ELDDKGKVYN HTITETVINS
DRRLIYSNVS DFLEGLRTDD SLKDLTEELT ILNTIAKNRK KMRDRRGNID FSFKEPSIEL
DDKGHPINIT VSDQREANQL IEEFMLLANE LVSETYSKKK LPFLYRVHEE PTAEKLELLN
SVIRPFGYRI DLTKDITPKD IQKLTEQVEG KDEESLIQTM VLRSMQKARY SDERYMHFGL
AAEYYSHFTS PIRRYADLTI HRVIKEDLHH ELNQRLIDEY KSTFGDIADH ISATEKAAQE
AERKVVDVKM AQYMYDHIGE HYDAKVSGIT SFGIFCELDN TVEGLVGYAS MDEFYRFDEE
NYVAIGEKTQ NTIHMGDPVR IVVVGADPIL GRIDFQMEGE DHRKK
//
