ID A0A1C2HI94_9RHOB Unreviewed; 753 AA.
AC A0A1C2HI94;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=BFP70_12360 {ECO:0000313|EMBL:OCX63436.1};
OS Thioclava sp. SK-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX63436.1, ECO:0000313|Proteomes:UP000094269};
RN [1] {ECO:0000313|EMBL:OCX63436.1, ECO:0000313|Proteomes:UP000094269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-1 {ECO:0000313|EMBL:OCX63436.1,
RC ECO:0000313|Proteomes:UP000094269};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Thioclava sp. strain SK-1.";
RL Submitted (AUG-2016) 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|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:OCX63436.1}.
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DR EMBL; MDHA01000051; OCX63436.1; -; Genomic_DNA.
DR RefSeq; WP_066011992.1; NZ_MDHA01000051.1.
DR AlphaFoldDB; A0A1C2HI94; -.
DR STRING; 1889770.BFP70_12360; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000094269; 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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; 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; 2.
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:UP000094269};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 628..709
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 164..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..753
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 83299 MW; 18D24EFD21AB45F5 CRC64;
MTQIPSREQI LDWLADHPGA SSKRDIAKAF DVKGAAKIEL KKILRAMQDE GVIEKRRRSF
RDRSTLPPVS VLEVLRADSL GDLWARPVEW DGDTAEPLIL VISKPADALG AGDRILARVA
PTPDAQYDYE ARPIRKIGVA RHAIVGIFRK TAEGGRIMPI DKKSSDKEWR VPAAATDDAR
DGELVEAEQT GPKGRMGLPQ ARVIARLGDP SAPRAVSLIA IHQHDIPDDF PDAVVAEADA
AQPADLTGRE DLTHMPFITI DPADARDHDD ACLVEYDDDP DNEDGMLIWV AIADVAHYVT
PGSQLDREAR KRGNSSYFPD RVVPMLPDVL SGDLCSLHEG VTRAVIAVRM KIDADGNKIN
HRFSRALIRS AASLSYEQVQ AAQDGAPDAQ CEPLMDDVIA PCYDAFAALS RARVIRQPLE
LDLPERKIVL SDDGKVASIQ FKDRLDAHKL IEEFMVLANV AAAEELERLK RPLLYRVHEE
PSQDKLENLR EVAVASGFTL AKGQVLRTSH LNHLLEQAVG SEFNELINIS TLRTMTQAYY
FPKNFGHFGL ALRSYAHFTS PIRRYSDLIV HRALISGHRW GDDGLSDWDI ENLEETAKQI
SDTERRSMVA ERDTTDRYLA AYLSERVGNE FRGRVSGVQK FGLFVRLDET GADGLIPIRS
VGREYFHFDG DAQMLIGSES RVQIGVGQRV LVRLAEATPV TGGLMLDLLE LDGKAISQGG
RGKGRGKGGP RKIGAYKAKA KAKTRTVQRR RSK
//
