ID F1YX57_9STRE Unreviewed; 774 AA.
AC F1YX57;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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:EGE53492.1};
GN ORFNames=SPB_0061 {ECO:0000313|EMBL:EGE53492.1};
OS Streptococcus parauberis NCFD 2020.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=873447 {ECO:0000313|EMBL:EGE53492.1, ECO:0000313|Proteomes:UP000003732};
RN [1] {ECO:0000313|EMBL:EGE53492.1, ECO:0000313|Proteomes:UP000003732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCFD 2020 {ECO:0000313|EMBL:EGE53492.1,
RC ECO:0000313|Proteomes:UP000003732};
RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA Town C.D.;
RL Submitted (FEB-2011) 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:EGE53492.1}.
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DR EMBL; AEUT02000001; EGE53492.1; -; Genomic_DNA.
DR RefSeq; WP_003103256.1; NZ_AEUT02000001.1.
DR AlphaFoldDB; F1YX57; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_4_1_9; -.
DR Proteomes; UP000003732; 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 628..707
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 715..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..774
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 87516 MW; B06FED687F4E3704 CRC64;
MKELILNYLK EHGKSNINDI AAALDMVGAQ KFPNLIKEIS KMESKRLLRF SNDGTISLRK
PREEKEIITV EGVFRANKAG FGFLFVDENE DDMFIGRNDV GYAIDGDKVA VTIKKPADRI
KGTAAEAKVV KVVEHALTTV VGKFVLDDDK PKYAGYIKSK NQKIQQPIYI KKEPVVLDGS
EIIKVEIEKY PTRGHDYFVG NVRDIVGHQG DVGIDVLEVL ESMDIVSEFP DDVLAEANAI
PDAPSDKDLM GRVDLRKEIT ITIDGADAKD LDDAIHIKKL ENGNFELGVH IADVSYYVTE
GSALNREAAE RGTSVYVTDR VVPMLPERLS NGICSLNPNV DRLTQSAIME IDMQGKVVDY
QICQSVINTT FRMTYSRVND MIAGDEEALD EFAPIVEAVQ DMAVLHKILE TMRVKRGALN
FDTSEARIIV NDKGMPVDIV VRSRGIAERM IESFMLAANE CVAEHFSKAK LPFIYRVHEE
PKSEKLQKFL DYASIFGVQI KGTANKISQE ALQDFMAKVE GQPGAEVLNM MLLRSMQQAR
YSETNHGHYG LAAEYYTHFT SPIRRYPDLL VHRMIRDYSH VTEEKKEHFA QVIPELAASS
SRLERRAIDA ERLVEAMKKA EYMEEHVGEE FDAIVASVVK FGMFIELPNT IEGLIHVTSL
PEFYNYNERN MTLQGEKSGT VFKVGQPIHV KLVKANKETG DIDFEYLPSE FDVKEKVEKP
DRQNNRRRNN DSKKGDRFPK NKSNDQNKEE APKKKGRKPF YKDAAKKNSK KRSR
//
