ID A0A1W6CYC4_9RHOB Unreviewed; 757 AA.
AC A0A1W6CYC4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=B0A89_09730 {ECO:0000313|EMBL:ARJ69862.1};
OS Paracoccus contaminans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ69862.1, ECO:0000313|Proteomes:UP000193017};
RN [1] {ECO:0000313|EMBL:ARJ69862.1, ECO:0000313|Proteomes:UP000193017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC {ECO:0000313|Proteomes:UP000193017};
RA Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT "Genome sequence of Paracoccus contaminans isolated from a water
RT microcosm.";
RL Submitted (MAR-2017) 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|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; CP020612; ARJ69862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6CYC4; -.
DR STRING; 1945662.B0A89_09730; -.
DR KEGG; pcon:B0A89_09730; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000193017; Chromosome.
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; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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 InterPro; IPR036388; WH-like_DNA-bd_sf.
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; 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; 2.
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:UP000193017};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 634..715
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 723..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 83660 MW; 6EE8CCB72B1D2446 CRC64;
MTPFPTRQQI LDWIAENPDA TAKRDIAKAF NIKGSARIEL KRLLKELEAE GAVERRRRSY
QGPERLPPVT VVEILPPDAD GDLFARPLEW QGTAPMPRIL FAPRKADPAV APGERVLVRL
VPAEGEDHHY QARLMRRIGI AVHRVVGIFR KAAEGGRILP IDKGADRQWQ VRADATLDAQ
DGELVEAEQV GSRNRPGLAQ ARIIERLGDP SAPRAVSLIA IHQHGIPDDF PDAVIAEADA
QRPAPMDGRE DLRRLPLVTI DPADARDHDD AVAAMPDDDP RNPGGMVIWV AIADVAHYVR
PQSALDREAR HRGNSTYFPD RVVPMLPDVL SGDLCSLHEG VDRPVIAVRM RLDAQGNKIG
HDFHRGMMNS LASLSYEQAQ AAQDGAPDEV TGPLMDSVIG PLFAAYDLLR AARARRQPLE
LDLPERRIEL TPEGRVKSVA FRDRFDAHRL IEEFMVLANV AAAEELIRLR RPLLFRVHEE
PSPEKLNALR DVAEASGFAL AKGQVLQPAQ LNRLLAQAQG TDFDELINVS TLRSMTQAYY
NAQNFGHFGL ALKNYAHFTS PIRRYSDLIV HRALIAAHGW GGGKAGKTDG LSAQDIEMLD
ETAQKISDTE RRSMAAERDT TDRYLAAYLA DRVGSEFTGR VSGVQRFGAF VRLDETGADG
LLPIREIGRE YFHFDRDAQT LVGADTGTTI GIGQRVTVRL AEAIPTTGGL VLELVELDGR
SMAQGARPRR GKAPRRRDAQ SAKAGEARAR KLRRIRK
//