ID A0A3M7LFC4_9FLAO Unreviewed; 717 AA.
AC A0A3M7LFC4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ECO:0000313|EMBL:RMZ60795.1};
GN ORFNames=D1632_02115 {ECO:0000313|EMBL:RMZ60795.1};
OS Chryseobacterium nematophagum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2305228 {ECO:0000313|EMBL:RMZ60795.1, ECO:0000313|Proteomes:UP000267524};
RN [1] {ECO:0000313|EMBL:RMZ60795.1, ECO:0000313|Proteomes:UP000267524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUb275 {ECO:0000313|EMBL:RMZ60795.1,
RC ECO:0000313|Proteomes:UP000267524};
RA Page A., Roberts M., Felix M.-A., Weir W.;
RT "Chryseobacterium nematophagum: a novel matrix digesting pathogen of
RT nematodes.";
RL Submitted (AUG-2018) 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:RMZ60795.1}.
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DR EMBL; QWIV01000005; RMZ60795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7LFC4; -.
DR Proteomes; UP000267524; 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; 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; 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 635..716
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 717 AA; 82128 MW; B6DCE51C696C2A73 CRC64;
MSKKRKYISH KNELKLMEIG RLILRFMNVN PTKIYNYKQI SDGIDYKNPR QRELVVQALH
KLQASEKIKE AERGKYIVNL KIAGTLTGII DFNQSGNAYV SVEGLEEDIF IHSKNVKDAL
QGDKVLIITY HYKGKKLEGS VLEVLERTRT EFVGTLQMVA HKDFGFVVCD KKAINTDIFI
PKGKFGGAED GNKVIVKMTE WKPGDKNPEG EIIQVLGAPG EHETEIHSIL AEYGLPYEFP
EEVERDADKI DRSINEEEVS KRWDMRGICT FTIDPKDAKD FDDALSIRKL ENGNWEIGVH
IADVSHYVIP GTILDDEAYE RATSVYLVDR VVPMLPEVLS NDVCSLRPHE DKFTFSAVFE
LNDNAEIQKQ WFGRTVIHSD RRFTYEEAQE RIESHKGDLS EEILVLDKLA KIMRQKRIKD
GAITFDRSEV RFNLDENNEP IGVYFKISKD SNHLIEEFML LANKKVSEFV SLNRKGDITQ
NTFIYRVHDD PDPAKLESLR DFVSTFGYKM DLANTKKVAE SLNKLLHDVK GKGEENMIET
LAMRSMSKAV YSTEPIGHYG LGFEYYTHFT SPIRRYPDLI AHRLLQHYLD GGKSPSKPEL
EEKAKHCSSM ERLAADAERD SIKFMQVKFM EKHLGETFNG VISGVAEFGF WVEIPENGAE
GLIKLRDLVD DSYMYDAKTH AVYGTRHGKK YQLGDQVQIK VVKANLIQKQ LDFKIVD
//
