ID F9VD13_LACGL Unreviewed; 811 AA.
AC F9VD13;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=LCGL_0754 {ECO:0000313|EMBL:BAK60214.1};
OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK60214.1, ECO:0000313|Proteomes:UP000008520};
RN [1] {ECO:0000313|EMBL:BAK60214.1, ECO:0000313|Proteomes:UP000008520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK60214.1,
RC ECO:0000313|Proteomes:UP000008520};
RX PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT "Complete genome sequence and comparative analysis of the fish pathogen
RT Lactococcus garvieae.";
RL PLoS ONE 6:E23184-E23184(2011).
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; AP009333; BAK60214.1; -; Genomic_DNA.
DR RefSeq; WP_014024589.1; NC_017490.1.
DR AlphaFoldDB; F9VD13; -.
DR STRING; 420890.LCGL_0754; -.
DR KEGG; lgv:LCGL_0754; -.
DR PATRIC; fig|420890.5.peg.751; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_9; -.
DR Proteomes; UP000008520; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008520};
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..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 91840 MW; A48485BE2C57283D CRC64;
MKIKEVILDE LKKHPKKAYA VEELAMELDL TKASDFKLFV KTLAALEGEG LLEFTNNGKV
TLAEVKAELV GIFRANANGF GFVTVDSDEP DVFIPKGRTA FALEGDEVKV ELKSNANPLK
GTSAEGVVTE VLKRSVTQLV GTFVKFDEKE RQEFERIGYV KSRNKKLPYH VFLTDKGLIP
EDKAVVRVDI TAYPDKKNPK SMQGLAVEIV GQAGDKGIDV LEVLASLGIR SEFPEDVLAQ
AEAIPEEVDE KALMGRVDYR NEITFTIDGA DAKDLDDAVH IKRLDNGNYE LGVHIADVSH
YVTENSPLDR EAFERGTSVY VADRVVPMLP ERLSNGICSL NPRVNRLTQS CVMEITPEGK
VLQSQIGPSI IKTTERMTYD DVNLMLAGNE EALEKYAAIK ESVEIMSELH EALAAMRRRR
GAIDFETMEA RIIVDENGLP IEIRKRSRGT AERMIESFML IANETVASSF ETRHLPGIYR
IHEHPKEEKM TRFIDFAATF GLQVKGTSTE VSQKALQEFL KKVKGQPGEM VLSTMLLRSM
QQARYSEDNY GHFGLAAENY THFTSPIRRY PDLIVHRLIR ELAQPSPKTI EYWAEKIPEI
AQQSSNRERR AVDAEREVEK MKKAEFMEKH VGEQFEGVIA SVTRFGMFIE LENTIEGLVH
ISTIKGEYMN FHERMMALVG EKTGLVFRIG QPIKIQVTKA DKVTGDIDFE YIKSDLDVVE
SNLKSKKEKG PRRRPKANRS ENKDEHKASK REKNFSEKSK NKKYRGKSKD EERERKNDFD
KKPNKKKKKK PFYADAAKGK FGKNTKKKSK K
//
