ID A0A1N6FR76_9LACT Unreviewed; 783 AA.
AC A0A1N6FR76;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05878443_0774 {ECO:0000313|EMBL:SIN97734.1};
OS Carnobacterium alterfunditum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=28230 {ECO:0000313|EMBL:SIN97734.1, ECO:0000313|Proteomes:UP000184758};
RN [1] {ECO:0000313|EMBL:SIN97734.1, ECO:0000313|Proteomes:UP000184758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=313 {ECO:0000313|EMBL:SIN97734.1,
RC ECO:0000313|Proteomes:UP000184758};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FSRN01000001; SIN97734.1; -; Genomic_DNA.
DR RefSeq; WP_034547525.1; NZ_FSRN01000001.1.
DR AlphaFoldDB; A0A1N6FR76; -.
DR STRING; 28230.SAMN05878443_0774; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000184758; 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 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 720..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 88262 MW; 523E9884A18488E9 CRC64;
MNDKKTLQEA IIVFMSEHKK ISFQVSDISE GMGMTSAVDF KILVSSLAEM EREGKLFLNK
KGHFKLPSND PVLTGIFRAS DRGFGFVAIE DVEKDIFIPP NMTNYALDGD KVTVDIIKPA
EPWSDKGAEG KIKAIIERNF TQLVGEFYAY SEDGIEETGL YGYIDPQDKK ITDLRVFIES
EGIKPVDGSI VVVEITLYPD DEFPRSMQGI VKKVVGHIND PGIDILTIVY KHGIPTEFSQ
EALKQADEVP EKISESDLEG RRDLRDEVLV TIDGADAKDL DDAVGLKVLD NGNYLLGVHI
ADVSYYVTED SPLDKDAFER GTSVYLTDRV IPMIPQRLSN GICSLNPHVD RLTMSCEMEM
TPDGEIVGHD VFQSVIRTTE RMTYTEVNEI LTDKNLETRK KYSSLVAMFE LMETLHHTLE
VDRKNRGAID FDTKEAKIIV DPTGKPLDIV LRERGVGERL IESFMLAANE TVSEHFSKME
VPLIYRIHEQ PDSDRMQKFM EFVTAFGITV KGTSKDVSPM TLQKIANSVK GKPEEQVVST
MMLRSMKQAK YAVEPLGHFG LGAEFYSHFT SPIRRYPDLI LHRLIRSYGE EGTGSAQKTK
WENRLPAIAE DTSKAERRAV DAERETDALK KTEYMADKVG EIYEGIIGSV LKFGIFVELP
NTVEGLVHIS NMKDDYFNYI EEQMMLVGER TGVVYRIGQK VKVKITKADP ETREIDFELV
PDPDAPKYEG PKHLVKGRGR ENSQRRGKES TSSYKPKQDG SSKKKSKPFY KDAAKNKKSK
NKN
//
