ID A0A0X8X7Y8_HALHR Unreviewed; 746 AA.
AC A0A0X8X7Y8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:BAU57200.1};
GN ORFNames=HH1059_05160 {ECO:0000313|EMBL:BAU57200.1};
OS Halorhodospira halochloris (Ectothiorhodospira halochloris).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=1052 {ECO:0000313|EMBL:BAU57200.1, ECO:0000313|Proteomes:UP000218890};
RN [1] {ECO:0000313|Proteomes:UP000218890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-1059 {ECO:0000313|Proteomes:UP000218890};
RA Tsukatani Y.;
RT "Halorhodospira halochloris DSM-1059 complete genome sequence.";
RL Submitted (FEB-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|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}.
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DR EMBL; AP017372; BAU57200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X8X7Y8; -.
DR KEGG; hhk:HH1059_05160; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000218890; 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; 2.
DR HAMAP; MF_01895; RNase_R; 1.
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; 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:UP000218890};
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 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 83926 MW; 025970D9CDA5C331 CRC64;
MAKRKAKTPH KDPYKEREQA KYDNPIPSRE YLLELLAANR RPLGRREIAA ELGLESPEQL
EALRRRLRAM ERDGQLVRNR RRGYLLVDHR ELVRGRVIGK PDGAGFLLAD GKDQRVSLSP
RQMRSLLHAD RAVVRVTGKD EHGNPVGELV EILERGNKQI TGRFFEEHGV GFLVPENKRI
HHDVLLSADG RGGAENGDLA VAEVLAQPTE RRQPIGRITR ILGQTINVGE EDEVAARIHS
VPLEWPDGVE REAAAFGATV AEEDKQGRTD LRKVPLVTID GADAKDFDDA IFCEPTAKGW
RLLVAIADVS HYVRPGSVLD AEARNRGNSV YFPRSVVPML PEVLSNGLCS LNPQVDRLCV
VCDVLLQGDG KILRSRFYRA VMRSAARLTY EQAAAAVVEQ DETVRADLDP QVLKLLENTH
RLYQTLRQAR ERRGAIDFDT TETVMRFDDE GRVVAVEPTV RNDFHRAIEE CMITANVCAA
KFLRKHKVPS LYRVHEHPSE ERLEQLRGFL AQVGLELGGG DQPTGLDYAK VMKAAKDRPD
RHLIETVLLR SMQAAEYRPD NAGHFGLALE AYTHFTSPIR RYPDLAVHRG IGHIIDGHRG
PSFPLSHNDL LTLGEHCSMT ERRADEATRD AEMTLKCEYL ADHLGEEFPG VIAAVTSFGL
FVQLEGVYVD GLVHITNLES DFFHYDQVGH CLIGDRTGKE YRLSDRVLVR VARVDKEDRK
IDLEMLDHPL DKKGRKRRKG KNKGGK
//
