ID A0A2I0QV40_9BACI Unreviewed; 715 AA.
AC A0A2I0QV40;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 18-JUN-2025, entry version 27.
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:PKR78188.1};
GN ORFNames=CEY16_08970 {ECO:0000313|EMBL:PKR78188.1};
OS Halalkalibacillus sediminis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Halalkalibacillus.
OX NCBI_TaxID=2018042 {ECO:0000313|EMBL:PKR78188.1, ECO:0000313|Proteomes:UP000243524};
RN [1] {ECO:0000313|EMBL:PKR78188.1, ECO:0000313|Proteomes:UP000243524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3227 {ECO:0000313|EMBL:PKR78188.1,
RC ECO:0000313|Proteomes:UP000243524};
RA He R.-H., Du Z.-J.;
RT "the draft geome sequence of Illustriluteabacillus marina B3227.";
RL Submitted (JUN-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:PKR78188.1}.
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DR EMBL; PJNH01000002; PKR78188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0QV40; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000243524; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:TreeGrafter.
DR CDD; cd04471; S1_RNase_R; 1.
DR FunFam; 2.40.50.140:FF:000213; Ribonuclease R; 1.
DR FunFam; 2.40.50.140:FF:000273; Ribonuclease 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; IPR050180; RNR_Ribonuclease.
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|ARBA:ARBA00022490, 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:UP000243524};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01895}.
FT DOMAIN 624..704
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT COILED 27..54
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 715 AA; 81795 MW; 62732B10908D5979 CRC64;
MKKRLMQFFE HEANKPHGVE ELQETLDFKE SEELQNLMKA LNELEQEGKL VLTRKDRYGL
PEKMNLIKGR VQMHAKGFAF LIPDDEDRDD IYIHQSDLMS AMNGDIVLVR VEADSKDGNR
PEGTVVRIVE RNDQPIVGTY QDNGSFGFVL VDDKRFPSDI FIKKSQANGA AEGHKVIVKI
TEYPKERKSA EGEVVEILGH INDPGIDILT IIHKHGIKAK FDEETLNHAN EVPEQISEDE
IKNRRDLRDE RIVTIDGADA KDLDDAVRVE KLENGNYLLG VYIADVSYYV TEGSPIDKEA
FERGTSTYLT DRVVPMIPHR LSNGICSLNP QVDRLTLGCE MEIDSSGDVV HHEIFQAVIK
TTERMTYSAV NEILNDGDTD TIERYGSLVP MFKHMEELAQ VLRNKRMHRG AIDFDFKEAG
IEVDEAGKPT DVVLRERGVA EKLIEEFMLA ANETVSEHFH WMDVPFIHRI HEEPDAGKLQ
NFFEFVANLG YTIKGTPDDI HPKALQKALD EIRGSKEDLV VSKLMLRSMQ QAKYSPENVG
HFGLATKFYT HFTSPIRRYP DLIVHRLIRT YLIEGDLSSK TTDKWKENLP EIARHTSEME
RHAVDAERET NDLKMAEYMS ERIGEEYDGI ISSITNFGLF VELPNTIEGL VHVSQLTDDY
YHYDEKHHAM IGERTANIFR IGDEVNVRVV STNIEDRVID FEIVGMKPNR KSKKR
//
