ID A8U6H2_9LACT Unreviewed; 783 AA.
AC A8U6H2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=CAT7_06091 {ECO:0000313|EMBL:EDP69068.1};
OS Carnobacterium sp. AT7.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=333990 {ECO:0000313|EMBL:EDP69068.1, ECO:0000313|Proteomes:UP000005587};
RN [1] {ECO:0000313|EMBL:EDP69068.1, ECO:0000313|Proteomes:UP000005587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT7 {ECO:0000313|EMBL:EDP69068.1,
RC ECO:0000313|Proteomes:UP000005587};
RA Bartlett D., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP69068.1}.
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DR EMBL; ABHH01000003; EDP69068.1; -; Genomic_DNA.
DR RefSeq; WP_007721460.1; NZ_ABHH01000003.1.
DR AlphaFoldDB; A8U6H2; -.
DR Proteomes; UP000005587; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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..720
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 714..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 605..632
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 714..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 88323 MW; 93310E3D616330B4 CRC64;
MSDKKKLQEA ILVFMTEHKN VSFQVSDISE GMGMTSAADF KTLVSSLAEM EREGKLFLSR
KGHFKLPSND PVLTGVFRAS DRGFGFVAIE DEEKDIYIPP NMTNYALDGD KVTVDIIKPA
EPWSDKGAEG KIKAIVERNF TQLVGEFYAY SEEGIEETGL YGYIDPQDKK ITDIRVFIEA
EGIKPVDGSI VVVEITLYPD DEFPRSMQGI VKKVVGHIND PGIDILTIVY KHGIPTEFSK
EALQQADAVP EKIKETDFEG RRDLRDEVLV TIDGADAKDL DDAVGLKLLD NGNYQLGVHI
ADVSYYVTED SPLDKDAFER GTSVYLTDRV IPMIPQRLSN GICSLNPHVD RLTMSCVMEM
SPDGEIVGHD IFQSVIRTTE RMTYTEVNEI VTDKNQETRE KYSSLVGMFE LMETLHHTLE
KKRKSRGAID FDTKEAKIIV DSVGKPLDIE LRERGVGERM IESFMLSANE TVSEHFSRME
VPLIYRIHEQ PDSDRMQKFM EFVTAFGITV KGTSKDVSPK TLQTVINSVK GKPEEQVVST
MMLRSMKQAK YDVEPLGHFG LGAEFYSHFT SPIRRYPDLI LHRLIRSYGE EGTGSAQKTK
WANRLPEIAE ETSKAERRAV DAERETDALK KTEFMVDKVG QTFEGIIGSV LKFGLFVELP
NTVEGLIHIS NMKDDYFNYI EEQMMLVGER TGVVYRIGQK VKVKITKADP ETREIDFELV
PDPDAPKYDG PKRSTQGRGR GNSQRRGKES SSTYKPKQEG SSKKKSKPFY KDVAKAKKPK
KKN
//
