ID K8WVZ5_9GAMM Unreviewed; 820 AA.
AC K8WVZ5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=OO7_00525 {ECO:0000313|EMBL:EKT61582.1};
OS Providencia sneebia DSM 19967.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141660 {ECO:0000313|EMBL:EKT61582.1, ECO:0000313|Proteomes:UP000010290};
RN [1] {ECO:0000313|EMBL:EKT61582.1, ECO:0000313|Proteomes:UP000010290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19967 {ECO:0000313|EMBL:EKT61582.1,
RC ECO:0000313|Proteomes:UP000010290};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
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 -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-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:EKT61582.1}.
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DR EMBL; AKKN01000001; EKT61582.1; -; Genomic_DNA.
DR RefSeq; WP_008914011.1; NZ_CM001773.1.
DR AlphaFoldDB; K8WVZ5; -.
DR PATRIC; fig|1141660.3.peg.105; -.
DR HOGENOM; CLU_002333_7_0_6; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000010290; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 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; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 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:UP000010290};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 645..726
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 732..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 93397 MW; C14E263EA634581E CRC64;
MSHDPFQERE AEKYESPIPS REFILELLSK RTTPAKREEI AQLLNLSSEE DLEALRRRLR
AMERDGQLVF TRRQCYALPE RLDLLKGKVI GHRDGYGFLR VEGKKEDYYL SQDEMKRAMH
GDVILAQAYG QDRKGRTEVR VVRVLEPRNN QIVGRYFIEA GLGFVVPDDS RLSFDILIPK
EDIKGARMGN VVVVELVTRP QRRAQAVGKI VEILGEDMGT AMAVEIALRT HEIPHTWPPQ
VDKQIADLSE HVPESAKKGR VDLRDLPLVT IDGEDARDFD DAVHCAPKKG GGWRLWVAIA
DVSYYVRPQT ALDDEARSRG NSVYFPSQVI PMLPEVLSNG LCSLNPGVDR LCMVCEMTVS
ATGRLSSYKF YEAVMNSHAR LTYTKVWKIL QGDEELREHY KALVPHIESL HKLYQALDEA
RIERGAISFE SEEAKFIFNA ERRIERIDPV VRNDAHKLIE ECMILANIAA ARFVEKNNEP
ALYRVHDRPK EDSVLNLRSV FSELGLTLPG GMTPEPKDYA QVMNEVAERP DHELLQTMIL
RSMKQAIYDP ENRGHFGLAL KSYAHFTSPI RRYPDLALHR GIKYLLAKEQ GHADHRWTPT
GGWHYDMDSM LQLGEHCSLT ERRADEATRD VADWLKCDFM QDQVGKVFTG LITSVTGFGF
FVRLNDLFID GLVHVSTLDN DYYRYDGVGQ RLIGESSSTT YRLGDEVEVR VEAVHMDERT
IDFALISTTR KAKNPGKTAR DRMKKEVKGA TKAARNKRDV SKEKNFEPDS AFRRSEKKGK
STDKKAESKN KGKKASDKTK KISAKLKEKH AAKKSQKKEG
//
