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Database: UniProt
Entry: R7ZSH8_9BACT
LinkDB: R7ZSH8_9BACT
Original site: R7ZSH8_9BACT 
ID   R7ZSH8_9BACT            Unreviewed;       692 AA.
AC   R7ZSH8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=ADIS_2491 {ECO:0000313|EMBL:EON77042.1};
OS   Lunatimonas lonarensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX   NCBI_TaxID=1232681 {ECO:0000313|EMBL:EON77042.1, ECO:0000313|Proteomes:UP000013909};
RN   [1] {ECO:0000313|EMBL:EON77042.1, ECO:0000313|Proteomes:UP000013909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK24 {ECO:0000313|EMBL:EON77042.1,
RC   ECO:0000313|Proteomes:UP000013909};
RA   Singh A.;
RT   "A novel strain isolated from Lonar lake, Maharashtra, India.";
RL   Submitted (FEB-2013) 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}.
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:EON77042.1}.
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DR   EMBL; AQHR01000068; EON77042.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7ZSH8; -.
DR   STRING; 1232681.ADIS_2491; -.
DR   PATRIC; fig|1288963.3.peg.2483; -.
DR   Proteomes; UP000013909; 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; 2.40.50.140; Nucleic acid-binding proteins; 3.
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; 2.
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:UP000013909};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          611..692
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   692 AA;  79693 MW;  9F490FBD03BCD150 CRC64;
     MNFLENHFGE EFSERQLSKQ LKLRVAKEKQ DLSDVLLELL SAGKVSKNAR NAFSTTADPE
     FVEGEVDYVN ARFAFVIPKS MTKAEDDILV REKDLKNALD GDTVRVMVFP GRAHNGRREG
     KVLEILSRCR DEFVGRVEIS PRYAFVVPDF KKMHRDIFVK KSDLLGAQHN QKVVVKLTEW
     NEQDKNPTGA IVRILGTAGE HEVEIHSIMA EFGLPFDYPE EAEAEADQIA EAIGADEIKG
     RRDFRGVPTF TIDPADAKDF DDAISYRKLD NGNYEVGVHI ADVTHYVRPN TLLEREAYHR
     ATSVYLVDRT IPMLPERLSN GLCSLRPNED KLTFSCVFEI TEDAAVLDFW IGRTVIHSDR
     RFAYEEAQEN IDQQSGDFYG ELTLLNGLAK KLRAERFKKG AINFETVEVK FKLDDKGKPL
     GLIIKERKDI HKMIEEFMLL ANRTVAEFIF NRNKGKDTFV YRIHDYPDLE KLTTFAGFAR
     KFGHELSITD ERTVSKTLNK LMDDIVGKPE QNVLEQLAIR SMAKAKYTTE PKLHFGLAFK
     HYTHFTSPIR RYPDMMVHRL LQHYLDGGKN MENQSWEEKC THSSEREKRA SDAERASIKY
     KQVEFMQLAE VKDYDGIVTG VTEWGVYVEI TETKCEGMVR LQDIKDDYYD FDERNMRLVG
     SKNKRIITLG DKVSVRVLKT DIDRRTIDLE FV
//
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