ID E1LAT5_9FIRM Unreviewed; 779 AA.
AC E1LAT5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:EFL58305.1};
GN ORFNames=HMPREF9684_0272 {ECO:0000313|EMBL:EFL58305.1};
OS Veillonella atypica ACS-134-V-Col7a.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=866778 {ECO:0000313|EMBL:EFL58305.1, ECO:0000313|Proteomes:UP000005942};
RN [1] {ECO:0000313|EMBL:EFL58305.1, ECO:0000313|Proteomes:UP000005942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-134-V-Col7a {ECO:0000313|EMBL:EFL58305.1,
RC ECO:0000313|Proteomes:UP000005942};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFL58305.1}.
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DR EMBL; AEDS01000027; EFL58305.1; -; Genomic_DNA.
DR RefSeq; WP_005379918.1; NZ_AEDS01000027.1.
DR AlphaFoldDB; E1LAT5; -.
DR GeneID; 57773714; -.
DR Proteomes; UP000005942; 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; 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; 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 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 618..698
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 721..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..746
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..779
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 89284 MW; 1D1F4848A07ED3E8 CRC64;
MKEKVLAFYK SIYPHTYHID DAAMDCHIKG GRELDAFMDA ARELLKEGRL SFIRKDVYAY
NNDTEFIEGI YKGYRKSFGF VITAPDEEDV YIAEQNKGTA MHNDKVRVRI ITSRDSRHKR
EGVITEVIER ANETVVGTYD RQHSFGFVIP DDERLGTDIY VDLHNTLDAR SGAKVLVKII
KWPEGDKKPE GVITEVLGYK GDVGLDINCI MANYDLPFSF PEDVVKASQH INTTITDDPK
RWDLRDVPMV TIDGEDAKDL DDAVSGRKLD NGTYELGVHI ADVSHYVVSQ KAIDREAYKR
GTSVYLVDRV IPMLPEVLSN GICSLNAGED RYAMTCMMEI DTQGKVVNYR IQPSIIHVNR
RCSYKEIYKA LTEDIIPDDL APLMPMIHNL SDIAKTLNDM RRRRGALDFD FPEYKVLLDT
EGIPLRIVRR DRTLAERLIE ECMLIANETV ATHLKNTNRM SVYRIHETPS EEKMSMYQKV
LNYLGQDIRL HLDELEPRVF QHILDAVKGT DIEQVAQIMT LRSMQQAKYS IDNAGHFGLA
SKCYTHFTSP IRRYPDLMVH RLLKADMGWP DGYANRDTKT EFLERAAVHS SEREQVAVAA
ERDTVDLKKT QYMVPFIGEV FEGKISSITS FGMFVELDNG IDGLVHMNMM TDDYYFYDEE
HFLLVGKRTG QIYHLGDTVT VTLVKADVEK RQIDFVLGEV DNLMRIQEMM KNSEGYVGVR
EKKPFGRSGI SKQSKRKGKG HSKSSKRRER YSGLSSVTKH KKGRKDHKAS KKKVKKRKR
//
