ID I1DUU1_9GAMM Unreviewed; 780 AA.
AC I1DUU1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:GAB57819.1};
GN ORFNames=RNAN_0789 {ECO:0000313|EMBL:GAB57819.1};
OS Rheinheimera nanhaiensis E407-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB57819.1, ECO:0000313|Proteomes:UP000004374};
RN [1] {ECO:0000313|EMBL:GAB57819.1, ECO:0000313|Proteomes:UP000004374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB57819.1,
RC ECO:0000313|Proteomes:UP000004374};
RX PubMed=23209246; DOI=10.1128/JB.01922-12;
RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA Zhang Y.-Z.;
RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT Sea.";
RL J. Bacteriol. 194:7001-7002(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 -!- 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:GAB57819.1}.
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DR EMBL; BAFK01000003; GAB57819.1; -; Genomic_DNA.
DR RefSeq; WP_008218925.1; NZ_BAFK01000003.1.
DR AlphaFoldDB; I1DUU1; -.
DR STRING; 562729.RNAN_0789; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000004374; Unassembled WGS sequence.
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; 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:UP000004374};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 640..721
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 738..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 87909 MW; 9245B842715F8743 CRC64;
MTVNDPHLAR EQEKYDNPIP SREFILEHIE KRQSPAYFDE LVQELGLTDD DAIFALKKRL
RAMERDGQLI YTKNRRYGLV DNMDLVKGTV LGHREGFGFL KLEQGGPDWF IPNFEMQRLL
HGDVVLATAQ SVNSKDKTEA RIVRVLEPRS EPIVGRYYKD FALGVVVPDD PRITQDIVIP
DGEQGAARHG QVVLVEVTQR PSKRVNAVGK VTEVLGEHMA PGMEIEIAIR NHQIPHVFSD
AVLQQVAKYG EDVPAAAKQG RVDLTQLGLI TIDGEDARDF DDAVYAEAKD NGGWRLWVAI
ADVSSYVLPD TPLDKSALER GNSVYFPDHV VPMLPEALSN GLCSLNPHVD RLCLVADMHI
SANGKLESYQ FYEAVMHSRA RLTYNKVHKI LQGDPELRAQ YNDNLTNIET LYALYKKLAK
VRGQRGAIEF ETVETRFIFN SHRKIEQIVP VHRVESHKII EECMIMANVA AARFIEKHEA
HTLFRVHERP DGDRFDNFRR FLAELGIEAD LPSEPTPLEL TELLNRIGER PDRELIETTM
LRSMKQAVYQ GDNQGHFGLA LEAYAHFTSP IRRYPDLVLH RGIKAILAKQ GQKVTGARAY
TEAEIAPLGE QCSMTERRAD DATREVADWL KCEYMQDHLG SEFEGVVSTV TSFGLFVRLT
ELYIEGLVHV TSLQNDYYHF DTERHVLTGE HSKVSYRMGD LLKVKVAAVN LEARKIDLVL
VGEPKRFVNK ADIKASKQAA AQKGAKRGSA KGAKAPAKAE AKPKGARNIT ARKKPRRKAK
//
