ID R5IFI4_9BACT Unreviewed; 769 AA.
AC R5IFI4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=BN796_02013 {ECO:0000313|EMBL:CCY35511.1};
OS Alistipes sp. CAG:831.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1262698 {ECO:0000313|EMBL:CCY35511.1, ECO:0000313|Proteomes:UP000018094};
RN [1] {ECO:0000313|EMBL:CCY35511.1, ECO:0000313|Proteomes:UP000018094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:831 {ECO:0000313|Proteomes:UP000018094};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY35511.1}.
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DR EMBL; CAYB010000063; CCY35511.1; -; Genomic_DNA.
DR AlphaFoldDB; R5IFI4; -.
DR STRING; 1262698.BN796_02013; -.
DR Proteomes; UP000018094; 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; 3.
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:UP000018094};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 647..728
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 87022 MW; 167F5576E5A9AD29 CRC64;
MTRKKRPSSR PRGKGGKNQT PDQKAMQKEL NLKRKERSGG KKKSKGKKEH FNKEELTGTV
SMTREGYGFV EVPDRDTDIF VPQHKMRGAL NGDIVKVLTT KAKGVGKDGK PKRIEGEVIT
VLERSSKPHI GVLQISRGEA WLIMESRNMP YDISIPLKEI DRCFGEDGQR TWKPGDVSGL
KAAVIVTDWP RKASAPTGRI VDVLGEPGAN DTEMHAILAE YGLPYRFEPE VEAAAEAVPD
RITPKDISER RDFRKVTTFT IDPADAKDFD DALSYRELGD GNIEVGVHIA DVTHYVTPGS
VIDKCAYERG TSVYLVDRTV PMLPEKLSNN LCSLRPGEEK LCFSAVFDIA PTGTVKKTWL
GRTVIKSDYR FNYDEAQAII ETGQGPLAKE IQTLHKIASV LRKKRFTAGA IAFERPEMKV
EVDETGKPIR VYEKISKEAN WLIEEFMLLA NRAVAEYVGK VPKTKKAKTF VYRVHEDPNE
EKLGVLRKFV RLFGYDFPME PGAMEDGQKK EEPKRFPEGV KVKEIKGKNV AQRINNLLGT
VKGRPEEEAV VMMALRSMAR AHYTTDNVGH YGLAFKYYTH FTSPIRRYPD MMVHRLLAMY
LAGVESQNKE YYETCCQYAS QREQIATEAE RSSIKYKLCE YMQDKVGQIF PGTVSGLTEW
GLYVETEPDK VEGMVPVRDI PGDFYQFDEE TYSIVGRSRG RRFTMGDKVW IRVVRASLEQ
KIIDYELVEM EDDKGLIQSD EPQSVSQQPA AEQPAPAKPA SRRTRKRSK
//
