ID A9GZQ2_GLUDA Unreviewed; 781 AA.
AC A9GZQ2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 112.
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:CAP53987.1};
GN OrderedLocusNames=GDI0044 {ECO:0000313|EMBL:CAP53987.1};
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP53987.1, ECO:0000313|Proteomes:UP000001176};
RN [1] {ECO:0000313|EMBL:CAP53987.1, ECO:0000313|Proteomes:UP000001176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 /
RC PAl5 {ECO:0000313|Proteomes:UP000001176};
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B.,
RA Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G.,
RA Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C.,
RA Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
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; AM889285; CAP53987.1; -; Genomic_DNA.
DR RefSeq; WP_012222292.1; NC_011365.1.
DR STRING; 272568.GDI0044; -.
DR KEGG; gdi:GDI0044; -.
DR KEGG; gdj:Gdia_1646; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_1_5; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000001176; Chromosome.
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:UP000001176};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
SQ SEQUENCE 781 AA; 83615 MW; 93BFB3B254033DDC CRC64;
MGGRNPSDPQ PTACPSPDVP PTDPRPPAPP QPGGGLPDRE ALRRFVTEAS GRVGKREIAR
AFNLGPEHKA ALRAMLRELA LEGTLVPAGA RRFRASAAMP EAALVQVTGT DPDGDPIARP
VVWDGDGPAP VVFMHPEQKG RPALAPGERV VARLKRLGPG RYEGRTLRRL TDAPGRIVGV
FRPTTLYDGP GPLAPPRRHA EAGRLVPADR RAKAEWIIPA GETMGAEAEE VVVAEPLPLA
GSGLKPARIV ARLGPMGDAR SVSLLAIHTH SIPDQFPAEA LSEAERARGV SPEGREDLRD
VPLITIDGED ARDFDDAVYA EPDGDGFRLI VAIADVAHYV RPGSALDREA RRRGNSVYFP
DRVVPMLPEA LSNGWCSLRP GEDRGCLFAE IFIDAAGNKT RHRFGRGIMR SAARLTYDQA
QAIVGNVEES QQETGLPDGL INTLFTAWRA LSTARARRGT LDLDVPERVV RLDTSGRITA
IEPRPRHDSH RLIEEFMVLA NVAAAEELER RRRPCLYRIH APPSPERAEA MRDSLSAMGF
DLPPPGALRA RDLGAVLARA AQGEASGPAS GTPVSGTLVS ETILRAQSQA EYSPDNIGHF
GLALPAYAHF TSPIRRYADL LVHRALIGMG TQPADGMPAA DAACLDEIGE QVSTAERRAA
LAERETTERY VAAWLADRVG AEFSGHVSGV TRFGAFVTLT QTGATGLVPV STLPDDVWTH
DEKTQTLRGR HGGLALRLGQ PVTVRLVEAT PVTGGLLFAL VGANPAAASG PARRARGTRP
R
//
