ID V6Z2P8_STRAG Unreviewed; 793 AA.
AC V6Z2P8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=SAG0136_04590 {ECO:0000313|EMBL:ESV54536.1};
OS Streptococcus agalactiae LMG 14747.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1154860 {ECO:0000313|EMBL:ESV54536.1, ECO:0000313|Proteomes:UP000018482};
RN [1] {ECO:0000313|EMBL:ESV54536.1, ECO:0000313|Proteomes:UP000018482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 14747 {ECO:0000313|EMBL:ESV54536.1,
RC ECO:0000313|Proteomes:UP000018482};
RA Richards V.P., Durkin S.A.S., Kim M., Pavinski Bitar P.D., Stanhope M.J.,
RA Town C.D., Venter J.C.;
RL Submitted (MAY-2013) 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:ESV54536.1}.
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DR EMBL; ANQC01000073; ESV54536.1; -; Genomic_DNA.
DR AlphaFoldDB; V6Z2P8; -.
DR eggNOG; COG0557; Bacteria.
DR Proteomes; UP000018482; 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 629..708
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 718..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..793
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 89483 MW; 9909F56D015F9A51 CRC64;
MKEKILQYLE EHGKSNINDL AASLDMAGAK KFPLLIKEIS KMESKRELRF NDDGMISLRK
PQEKKEQITV QGVFRANKAG FGFLFVDENE DDMFIGRNDV RHAIDGDTVE VVIKKPADRL
KGTAAEARVV KIVDHALKTV VGKFVLDDAK PKYAGYMTSK NQKIQQKIYI KKEPVLLDGT
EIIKVEIEKY PTRSHDYFVG HVRDIVGHQG DVGIDVLEVL ESMDIVSEFP EDVIAEANAV
PDAPSAKDLV SRVDLRQEIT FTIDGADAKD LDDAVHIKRL ENGNFELGVH IADVSYYVTE
GSALNREAAA RGTSVYVTDR VVPMLPERLS NGICSLNPNV DRLTQSAIME INPQGKVVDY
QICQSVINTT YRMTYSDVNE MLAGNQDVLD QYETIKASVQ DMAALHKILE DMRVRRGALN
FDTSEAKIIV NDKGLPVDIV VRERGIAERM IESFMLAANE CVAEHFARKD LPFIYRIHEE
PKVEKLQKFI DYASVFGVQI QGTASKITQS ALQDFMAKIE GHPGSEVLSM MLLRSMQQAR
YSEHNHGHYG LAAEYYTHFT SPIRRYPDLL VHRMIREYAK GATAERQDHF ASVVPELATS
SSQLERRAID AERVVEAMKK AEYMEEHVGE EFEGVVASVV KFGLFVELSN TIEGLIHVTT
LPEFYHYNER TMSLQGEKSG KVFKVGQPIR IKLTRADKET GDIDFEYLPS DYDVVEKVAK
SDRQERGRSR RFDKDRRELD DKVGKGSYRG EKSKSGNKGS QSNKGSQSNK GKKDKKPFYK
KAAKKSQASK KRK
//
