ID F4QST4_9CAUL Unreviewed; 791 AA.
AC F4QST4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-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 ECO:0000313|EMBL:EGF89804.1};
GN ORFNames=ABI_42270 {ECO:0000313|EMBL:EGF89804.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF89804.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-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|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL883080; EGF89804.1; -; Genomic_DNA.
DR RefSeq; WP_006275000.1; NZ_GL883080.1.
DR AlphaFoldDB; F4QST4; -.
DR STRING; 715226.ABI_42270; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_1_5; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000006512; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
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; 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; 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 655..736
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 87708 MW; FE5BF8C66B70639B CRC64;
MKQKKPFRAV KADAPRAPSG LPDDKTLLEA LQASREVDVG DLAKQFGLKG EDRRALRQRL
KALADGGKLD KRGRKTFGAM GQLPETGVVE VVEQDIDGEL WARWGKPDAL KQRSGSATQN
EAVPLARLAP LKKSVQQTPP KLGDRLYVRF EKAADGWIAH LIKILDQGAP KLVGVVRIGK
REIRLESVIR KEKDSYILTG SNLDTLEDGD VVVAAPVGGT HRFGPKPARV LEVIGKEDSP
KIASVMAIHS HGLPIGFQTS TEDEAKSAQA PGLGKRTDLR DLPFVTIDPV DAKDHDDAVY
AHADDDAANP DGWVVWVAIA DVAHYVTPGS SLDRDARDKG NSTYFPDRVE PMLPHVLSSG
LCSLQEGENR ATLAVRMVFD REGRKISHKF VRGLMRSAAK LSYEQAQAAI DGTPDDKTGP
ILDSLLKPLW AAHACLTRGR QVRQPLQINS PERRVYLDKD GNVERIERRV SLDAMQLIEE
MMIQANVSAA ETLQKHKTPL IYRVHEAPSL EKINNLADFL ATLGLPWAKG EPPRTPRFNQ
LLESQKEGPH AEIINEVVLR TQMQAHYSPE NFGHFGLNLD HYGHFTSPIR RYADLVVHRA
LIRALKLGDD GLTDYEIKTL QDTAEHITAT ERRSMQAERE AIERYIASYL HDKVGATFQG
RIVGVTRFGL FVKLTDTGAD GIIPVSSLRD DYYVHDDVQH ALIGERHGYR WRLGATIEVE
LMEAMPITGG LVFKVLSEPE VGDPGAPRPR LGMRNRVKTP NVRGKPTKKP GFRDEPKGPK
PGVKNMKKKK R
//
