ID D5CRS8_SIDLE Unreviewed; 773 AA.
AC D5CRS8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=Slit_1427 {ECO:0000313|EMBL:ADE11664.1};
OS Sideroxydans lithotrophicus (strain ES-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Sideroxydans.
OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE11664.1, ECO:0000313|Proteomes:UP000001625};
RN [1] {ECO:0000313|EMBL:ADE11664.1, ECO:0000313|Proteomes:UP000001625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE11664.1,
RC ECO:0000313|Proteomes:UP000001625};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL Submitted (MAR-2010) 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; CP001965; ADE11664.1; -; Genomic_DNA.
DR RefSeq; WP_013029562.1; NC_013959.1.
DR AlphaFoldDB; D5CRS8; -.
DR STRING; 580332.Slit_1427; -.
DR KEGG; slt:Slit_1427; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_4; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000001625; 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; 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; 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; 3.
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:UP000001625};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 639..720
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 745..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 86527 MW; 1BF07F52BD25C834 CRC64;
MTKKKKNIRE LDPFLERERE QYEQPLPSRE YILQILAEKG VPLEQDELCV LLQIEHHEQD
LFNRRLRAME RDGQIMRNRK RAICVVDKLD LIKGKVQGHP DGFGFLIPED GSPDLVLSAK
EMHKALHGDT VMARIGGEDR RGRREASIVE VLEPANTRVV GRLYEEHGIQ FVVAENRRIS
QDFLVAPGES GGAKAGQVVM LEIMQQPSKH AQPIGRIVEV LGNYADPGME IEIALRKHDL
PNEFPHDAEK QAKAFSPEVK PADYAGRESV AQLPLVTIDG ETARDFDDAV YCEPNAKGFR
LVVAIADVSA YVKSGDALDK EAINRGNSVY FPRRVIPMLP EELSNGLCSL NPNVERLCMV
CDMQISADGE IQKHRFYPSV MFSHARLTYT KVADMLENPQ GENAREYAAV LPHINNLYKL
FQTLLQAREK RGAIDFETVE TQMIFNAQGK IEKIVPVVRN DAHKLIEECM LAANVCAAAF
LKEHDHPVLY RVHEGPTPEK LEAVREFFKE FGLQLGGGDD PQASDYSKLL KQIKGRPDAG
LLQTVMLRSL RQAVYAPENV GHFGLGYEAY AHFTSPIRRY PDLLVHRAIK AVLEGKQYKP
KLKWAELGVH CSMTERRADD ATRDVEAWLK CFYMRDHLGS VFDGSISSVT GFGLFVALDE
LYVEGLVHVS ELGADYYHFD PAKHQMLGER TGKRYRLGDR VRVKVVRVDM ESTKIDFVLE
TGPAASGSDE ASGIQGIDVG AWGAASPKKA KITEKSGKTS KSPKTGKSGK RHG
//
