ID K2QBC6_9LACT Unreviewed; 812 AA.
AC K2QBC6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=C426_1757 {ECO:0000313|EMBL:EKF50832.1};
OS Lactococcus garvieae DCC43.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1231377 {ECO:0000313|EMBL:EKF50832.1, ECO:0000313|Proteomes:UP000006787};
RN [1] {ECO:0000313|EMBL:EKF50832.1, ECO:0000313|Proteomes:UP000006787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCC43 {ECO:0000313|EMBL:EKF50832.1,
RC ECO:0000313|Proteomes:UP000006787};
RX PubMed=23209230; DOI=10.1128/JB.01864-12;
RA Gabrielsen C., Brede D.A., Hernandez P.E., Nes I.F., Diep D.B.;
RT "Genome Sequence of the Bacteriocin-Producing Strain Lactococcus garvieae
RT DCC43.";
RL J. Bacteriol. 194:6976-6977(2012).
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:EKF50832.1}.
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DR EMBL; AMQS01000031; EKF50832.1; -; Genomic_DNA.
DR RefSeq; WP_003136287.1; NZ_AMQS01000031.1.
DR AlphaFoldDB; K2QBC6; -.
DR PATRIC; fig|1231377.3.peg.1737; -.
DR eggNOG; COG0557; Bacteria.
DR Proteomes; UP000006787; 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; 2.
DR HAMAP; MF_01895; RNase_R; 1.
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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 632..712
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 723..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 91611 MW; 96B68590DBD494BB CRC64;
MKIKEVILGY LKEHPSRAYA VEELAMELDL TKAADFKFFV KTLASLEGEG LLEFTKNGKV
KLSEVKAELV GVFRANANGF GFVTVDSDEP DVFIPKGRTA FALDGDEVKV ELKTNANPLK
GTSAEGVVTE ILKRAVTQLV GTFVKFDEKE RKEFDRIGYV KSRNKKIPYH VFLTDKGLQP
EDKAIVRVDI TAYPDKKNPK SMQGLATEIV GEAGDKGIDV LEVLASLGIR SEFPADVLAQ
ADAVPEEVND KDIMGRVDYR NEITFTIDGA DAKDLDDAVH IKRLGNGNFE LGVHIADVSH
YVTENSPLDR EAFERGTSVY VADRVVPMLP ERLSNGICSL NPRVNRLTQS CVMEINAEGK
VLHSQIGPSI IKTTERMTYD DVNLMLDGDQ EALTKYEAIK ESVEGMSELH EILAAMRRRR
GAIDFETMEA RIIVDENGLP IEIRKRSRGT AERMIESFML VANETVATSF ETRHLPGLYR
IHEHPKEEKM TRFLDFAATF GLQVKGTSTE VSQKALQEFL KKVKGQPGEL VLSTMLLRSM
QQARYSEDNY GHFGLAAENY THFTSPIRRY PDLIVHRLIR EMAQPSPKTI EYWAEKIPEI
AQQSSNRERR AVDAEREVEK MKKAEFMEKH VGEEFEGVIA SVTRFGMFIE LENTIEGLVH
ISTIKGEYMN FHERMMALVG ERTGLVFRIG QPIKIQVTKA DKVTGDIDFE YIKSDLDVVE
SNLKSKKEKD SRRRPKANRS DKKDEPKSSR HGQHRSENSK GKKYSSKNKD EDRESRGKGS
NNSYDKKSKK KKKPFYAAAA KGKFGNSKKK KK
//
