ID A0A1G1Z438_9BACT Unreviewed; 645 AA.
AC A0A1G1Z438;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 17.
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=A3E61_00165 {ECO:0000313|EMBL:OGY58457.1};
OS Candidatus Colwellbacteria bacterium RIFCSPHIGHO2_12_FULL_43_12.
OC Bacteria; Candidatus Colwellbacteria.
OX NCBI_TaxID=1797688 {ECO:0000313|EMBL:OGY58457.1, ECO:0000313|Proteomes:UP000178259};
RN [1] {ECO:0000313|EMBL:OGY58457.1, ECO:0000313|Proteomes:UP000178259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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:OGY58457.1}.
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DR EMBL; MHIW01000026; OGY58457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1Z438; -.
DR Proteomes; UP000178259; Unassembled WGS sequence.
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; 2.40.50.700; -; 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; 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; SM00357; CSP; 2.
DR SMART; SM00955; RNB; 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 564..645
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 645 AA; 73676 MW; F1B5A21A2C73EA3C CRC64;
MDKVTKKSVN TGIISITSKG RGYILSSGFA EDVQVEPQFL NTALHGDEVE FSLFPQAEKE
RLTGEIIKIL KRAKMEFVGT IDKRKGSNIS FLIPDDNRMY IDIFLPFNES KDIQNNSKVL
VRISKWDDPK KNPQGKVLRI LGKKGDNDVE MESIVLEKGF QMQFPHKVEE EAKLLGRHAK
TVSQKDISER RDFRNVTTFT IDPEDAKDFD DAISFKEIQD GLFEIGVHIA DVSHYIKEGG
QLDKEARYRG TSIYLVDRTV PMLPEILSND ICSLNPNEDK LTFATVLTIS KDGHIKNVWF
GRTIINSNKR FVYEEAQKVM DDKRGPYYYE LNELNKLAKI FKERRMKIGG LDFDREEVKF
KLDAKGKPIS IFEKPRLDVH KLVEEFMVLA NTEVASYLSK EVKRINKGAA IYRIHDVPKK
KAIDDLLSLL RALGHEVEAE GENITSKELN NLLKNIKGKP EESLVNTVAM RSMAKAIYSV
DNIGHYGLAL ENYTHFTSPI RRYADILVHR ILEKHLKGGS LTDEEIAWHH KVSIELSSRE
TDAAEAERSS VYYKQIQYMM ERIGSTYSGI ISGITNWGVY VEETQTKANG MVKFQNMKND
FYVLSRETYS LTGTKTKKKY SIGDEVKIKV IGGDLEKKTL DYAFV
//
