ID A0A1T4KFS7_9FIRM Unreviewed; 707 AA.
AC A0A1T4KFS7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN02745118_00762 {ECO:0000313|EMBL:SJZ41264.1};
OS Selenihalanaerobacter shriftii.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Selenihalanaerobacter.
OX NCBI_TaxID=142842 {ECO:0000313|EMBL:SJZ41264.1, ECO:0000313|Proteomes:UP000190625};
RN [1] {ECO:0000313|Proteomes:UP000190625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-73 {ECO:0000313|Proteomes:UP000190625};
RA Varghese N., Submissions S.;
RL Submitted (FEB-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}.
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DR EMBL; FUWM01000006; SJZ41264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4KFS7; -.
DR STRING; 142842.SAMN02745118_00762; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000190625; 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:UP000190625};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 625..705
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 707 AA; 81588 MW; 06DA1F674AA9E9BF CRC64;
MGAKDEILNF MHNKAYKPLT AEELLNAFEI SQQEEDMFLK ILDRMEQDGE IVQTRIGRYG
IPEKMNLVVG RLERHSKGFG FLIPDDIEKE DVYISAGDIN GAMNNDRIIV RIKGTENGKR
LSGEIIRILE RTNKTIVGDF EASQNFGFVV ADDSHIHYDI FVPKKETNGA SQGQKVVVEI
TRWPEERRNP EGKIIEILGN RGEPGVDIEA IIRKLDLPKE FPNEVKEHVA AISEEIPQQE
AKRRRDLRDL KMVTIDGDDA KDYDDAVSIE KIGDKNVKLG VHIADVAYYV KESDILDQEA
RRRATSIYLV DRVIPMLPEK LSNNLCSLRS GEDRLAMTVL MNYDLETGEL TDYEILESII
NVNHRLTYNK VKEILVNEDE ELIQQYDDFI DELRLMEELC LKLRENRFIQ GSIDFDFPET
RLVLDDDGKP IDIIKVERSI AEKLIEEFMI KTNEVVAEDM YWREVPFIYR VHDYPDQSDL
EALNEFIHNF GYHIKGIDSE THPKALQMVL ENVKGEPEEK VINTVLLRSM KQAHYADQNI
GHFGLASEYY SHFTSPIRRY PDLMIHRIIK EVINQGKLNQ SRSEKLEELL PEITDHSSIR
ERKASDAEME SKDLKKVEYM QDKEGEVYEG IISGMMSFGF FVELPNSIEG LVHVSNLTDD
YYIYHEDKQA YIGERTGNTY RLGDQVEVAV DRVNLADRQV DLVLTSK
//
