ID B0S130_FINM2 Unreviewed; 701 AA.
AC B0S130;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 OrderedLocusNames=FMG_0652 {ECO:0000313|EMBL:BAG08070.1};
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG08070.1, ECO:0000313|Proteomes:UP000001319};
RN [1] {ECO:0000313|EMBL:BAG08070.1, ECO:0000313|Proteomes:UP000001319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508
RC {ECO:0000313|Proteomes:UP000001319};
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
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}.
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DR EMBL; AP008971; BAG08070.1; -; Genomic_DNA.
DR RefSeq; WP_012290546.1; NC_010376.1.
DR AlphaFoldDB; B0S130; -.
DR STRING; 334413.FMG_0652; -.
DR KEGG; fma:FMG_0652; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_4_1_9; -.
DR Proteomes; UP000001319; Chromosome.
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 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:UP000001319};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 620..700
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT COILED 585..612
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 701 AA; 81267 MW; FB5AEA07CB71A34B CRC64;
MKIKQKVLNI VNSNDYIPLT FDELSSRLNI EKKDKKIFHK IINELQKDKK ILLDKNSNII
PITEQKAYPG TIQGSGSDFC YFIPDDENVD DIFIAKKDLN GAIHKDKVLV TITVEKKPNR
SPEGKVLQIL SRETKKLVGT FDEAKGYGFV ILDDKKYGFD VFVQSGNKNG AKNNDKVVVK
LIKTPSKNHK NPEGVIVEVL GGKDDPGIDI YSIAKTFKLP YEFPKKVKQQ AKEIEQHVDE
SEKKSRMDFR DLLTVSIDGS DAKDFDDAIS ITKKGENFVL YVHIADVSHY VKKNTALDKE
AFRRGTSVYM LDRVIPMLPV ELSNGICSLN PNEDRLCLTI KMEISPTGKT LDYKFYESVI
NSDYRLIYKN VSDFLEDIDN PYEDEKLTDN LLLMKELYEI LSARRKKRGS IDFDFPETKI
ILDENSKVID VTKDERRIGN KLIEEFMLIT NETVASHFGY LDRPFLYRVH EEPDEEKVNT
FKRILSNFGY HLKGKNLYSK DYQRILNELD GKPEKPLLAS LLLRSMQKAE YSENPSIHFG
LASMFYTHFT SPIRRYPDLF IHRIVKNFIN HKPDTNNEKE FMKYIKDIAK QCSATERRAE
EAEREAIDMK SAEYMQQHID EEFEGIISSL TKFGIFVQLD NTIEGLVQFQ SMIDDYYVFD
EKNYTVYGER TKKSYHIGQK VRVKVINSDK DKRQIDFEFV N
//
