ID A0A285IXV5_9GAMM Unreviewed; 791 AA.
AC A0A285IXV5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ORFNames=SAMN06297280_2222 {ECO:0000313|EMBL:SNY52802.1};
OS Arsukibacterium tuosuense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Arsukibacterium.
OX NCBI_TaxID=1323745 {ECO:0000313|EMBL:SNY52802.1, ECO:0000313|Proteomes:UP000219353};
RN [1] {ECO:0000313|EMBL:SNY52802.1, ECO:0000313|Proteomes:UP000219353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12461 {ECO:0000313|EMBL:SNY52802.1,
RC ECO:0000313|Proteomes:UP000219353};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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}.
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DR EMBL; OBEB01000004; SNY52802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285IXV5; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000219353; 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; 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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 640..721
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 744..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 88945 MW; CCC25C6A27092FE4 CRC64;
MTVNDPHLAR EQEKYDNPIP SREFILEHIE KRQQPAYFEE LVTELALTDD DAIFALKKRL
RAMERDGQLI FTKSKRYGLV DHMDLVKGVV MGHREGFGFL KLEQGGPDWY LPYHEMQRVL
PGDKVLATAA AMKSKDKVEA RVVRVLEPRT EPVVGRYYKD SAVCVVVPDD PRITQDIMIP
EGEQGAARHG QIVLVEITQR PSKRVSAVGK VIEVLGEHMA PGMEIEVAIR NHQIPHEFPE
SVLQQVAKYG EQVPEEAKLG RVDLTKLPLV TIDGEDARDF DDAVYAEAKE NGGWKLWVAI
ADVSAYVKPD TPLDRSALER GNSVYFPDHV VPMLPEALSN GLCSLNPHTD RLCFVAEMHI
SASGKLESYQ FYEAVMHSAA RFTYNKVHAI LQGDPELRKQ YQANLTNLET LYSLYKKLAK
VRGQRGAIEF ETVETRFIFN SHRKIEQIVP VHRNEAHKII EECMIMANVA SARFVEKHEA
HALFRVHERP DGDRFANFRR FLAELGIEAN LSSEPTPLEL TQVLANLADR PDRELIETTM
LRSMKQAVYQ GDNQGHFGLA LEAYAHFTSP IRRYPDLVLH RAIKAILVKQ NQKVNGERAY
SEKEITHFGE QCSMTERRAD DATREVSDWL KCEYMQDHLG AEFDGVVATV TNFGLFVRLS
DLYIEGLVHV TSLQNDYYRF DAERQVLNGE HSGVSYRMGD QVKVKVLAVS LESRKIDLAV
VGEPKHNVSG RAVKASRNAA FAEKEAKAAG AGRRSGKGGG KVAAKPAAKA ADKPKTAKGG
SKKPRRRAKK S
//