ID A0A0C5VLY8_9GAMM Unreviewed; 846 AA.
AC A0A0C5VLY8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=YC6258_02335 {ECO:0000313|EMBL:AJQ94373.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ94373.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ94373.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ94373.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) 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; CP007142; AJQ94373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C5VLY8; -.
DR STRING; 1445510.YC6258_02335; -.
DR KEGG; gsn:YC6258_02335; -.
DR PATRIC; fig|1445510.3.peg.2291; -.
DR HOGENOM; CLU_002333_7_0_6; -.
DR Proteomes; UP000032266; 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; 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:UP000032266};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 699..780
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 786..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 95693 MW; 3B204A0ADD854CBD CRC64;
MELCLSGPAS ILFYLNHLLA TMPINYSYKR TATISRQKKN RAAIKDPHAR REAENYADPI
PSREFILTHL QERNGPASHP ELCQALNLTT DNQIEALRRR LIAMVRDGQI RCSRNGAFGL
IDKMNLAKGR VQGHQDGYGF LIAEDGRKDI YLNSNQMSCV FDGDVVLVRE TERDFRGRME
GKIVDVLERN THQLVCRYHE QSGIGFGCPE NRKIHHDILI KPGTSAGATD GDIVLIEIVE
QPRFRHQPIG KVVEVMGKHL DPGMEIDIAL QTFAIPHDWP EEVEQQARLF KSDVSSKDKQ
GRVDLSKYPL VTIDGEDARD FDDAVYARRT REGDWKLFVA IADVSHYVKP DSALDQEAFN
RGTSVYFPER VVPMLPEVLS NGLCSLNPHV DRLAICCEMT FGPRGALKEY KFYEALIHSH
ARLTYNQVAA MLMDPDLEKA DALRQQFSDV LPSLETLHEL YKVLRKLRNK RGAIDFETQE
TRIVFNDNQK IDRIVPVERN DAHKLIEECM LAANTCAADF LNTLDIPALY RVHAGPSFEK
LENLRSYLAE LGLEIGGGLK PSPADYQKLL LQIKDRDDFD LIQTVLLRSL SQAVYQPQNE
GHFGLGYDAY THFTSPIRRY PDLLVHRAIH SVIHSGRRTS LVKRVKDTPK ADSAVSYPYD
LAKMLMFGEH CSMTERRADE ATWDVIAWLK CEYIEDHIGD VFTGTVASVV TFGLFVQLDE
IFVEGLIHVT SLNSDYYVFD PAGHRLVGER TRTVYSLGDK VSVRVARVNL DERKIDFELE
NQIKTARRTA ASRKSSTKTS KESGKKPAAK ASKHKSKSKS GKASKHAPKA DFGKTRSRSK
RKKTNG
//
