ID A0A090D0I6_9BACT Unreviewed; 743 AA.
AC A0A090D0I6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=vacB {ECO:0000313|EMBL:CDR35052.1};
GN Synonyms=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN ORFNames=CSEC_2246 {ECO:0000313|EMBL:CDR35052.1};
OS Criblamydia sequanensis CRIB-18.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC Criblamydia.
OX NCBI_TaxID=1437425 {ECO:0000313|EMBL:CDR35052.1, ECO:0000313|Proteomes:UP000031552};
RN [1] {ECO:0000313|EMBL:CDR35052.1, ECO:0000313|Proteomes:UP000031552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR35052.1,
RC ECO:0000313|Proteomes:UP000031552};
RA Linke B.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDR35052.1, ECO:0000313|Proteomes:UP000031552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR35052.1,
RC ECO:0000313|Proteomes:UP000031552};
RA Bertelli C., Goesmann A., Greub G.;
RT "Criblamydia sequanensis harbors a mega-plasmid encoding arsenite
RT resistance.";
RL Submitted (SEP-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}.
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:CDR35052.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCEJ010000012; CDR35052.1; -; Genomic_DNA.
DR RefSeq; WP_053332027.1; NZ_CCEJ010000012.1.
DR AlphaFoldDB; A0A090D0I6; -.
DR STRING; 1437425.CSEC_2246; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000031552; 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; 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; 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:UP000031552};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 629..699
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 724..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..743
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 84862 MW; 8BDA0B5B09ADA72E CRC64;
MAKKTKKSKE DRLKENLLKT IREFLSSKKA RPLSFEELIQ KLKILPEHAP LINELLQSLL
NEGEVSFSSG RYSYESSIGN EDLLKGTIKM HPRGFGFVIP EDRSAFPEDI FIPRHFTMNA
VDGDKVEVLV SSLPQHDKGP EGKVLNILER SRRHLAGIIR EFGENEEPIV YVPMLGANQR
VILKQEGQKL LTVGDRIVIE VLEWGTKQSV TIARLLHKIG HISDPKCDIP AAIEEYDLKN
SFSPLVLKEA EKFGKRIKPS DLKGRRDLRN EVTFTIDPDT AKDFDDALTL TKDKKGHYFL
GVHIADVSHY VRAGSYLDEE AKNRANSTYF PGVCVPMLPK ELSENLCSLK ANVARLTASV
FMEFDPAGEL VSYSIDRSVI KSVKRLTYRE AFAILQGKKK SPLKENLELM VELCRLLKRK
RIDRGSVDLA LPDLVVLVDP QGNPTGIDTV EYDITHQLVE EFMLKANEMV ATHLDNLGKN
LAFRVHDEPA SENIQDFVKL TRSFGFEMPD KPTSYAIQKL FNEAVKSPYG QYLATSYIRR
MKMAYYSPEN IGHYGLGLTH YCHFTSPIRR YADLIVHRIL FGDEDNLEYL EEATLHCSEQ
ERVSAKAEMS VILLKKLRLI QKEFIKDPYQ EYNAVVTSIK PFGITIEVLP HLLDGFIHIS
EIGNDFFDYD EQKMQLRGKR SKVTYNMGDT VTAVLKSIDL IMQESRWEIL PKEGEKNLAA
LKPKKSRKDF KNVKKSKRNR KKR
//
