ID A4EFC5_9RHOB Unreviewed; 751 AA.
AC A4EFC5;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 87.
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=RCCS2_06909 {ECO:0000313|EMBL:EBA13597.1};
OS Roseobacter sp. CCS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA13597.1, ECO:0000313|Proteomes:UP000003535};
RN [1] {ECO:0000313|EMBL:EBA13597.1, ECO:0000313|Proteomes:UP000003535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS2 {ECO:0000313|EMBL:EBA13597.1,
RC ECO:0000313|Proteomes:UP000003535};
RA Mary Ann M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) 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}.
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:EBA13597.1}.
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DR EMBL; AAYB01000001; EBA13597.1; -; Genomic_DNA.
DR RefSeq; WP_008231381.1; NZ_AAYB01000001.1.
DR AlphaFoldDB; A4EFC5; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000003535; 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; 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 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 628..709
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 716..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..751
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 82188 MW; 8E1E0448D59336BC CRC64;
MTRIPSKAEI LAWISEHPTK AAKRDIAKAF GIKGAARIDL KRLLKELEEE GKLTKRRSSY
RDAEDLPPVA VLEVVGADAD GDLFARPLEW KGEGAEPRIL MMLRSSDPAL GAGDRILGRL
TVDQTEDHSH TARMIRRIGT NPQRILGVFR AGSEGGRVLP IDKGADKQWT VAAGATGGAK
DGELVEAEQA GPKGRMGLPK ARIVARLGDP TEPRAVSLIA IHQHGIPDHF PDDVVAEADA
AKPAGLKGRK DLRDLPLVTI DPWDARDHDD ACFVEPDPDP KNAGGFIIWV AIADVAHYVT
PGSELDREAR KRGNSTYFPD RVVPMLPDRL SGDLCSLHEG VERACLAVAM RVDMAGNKID
HAFHRGLMKS VASLNYEEVQ AAVDGQPNDK TAPLMDDIIT PLYDAYAALT KARAQRQPLE
LDLPERQIVL DDNGKVTSVQ YKERLDAHRL IEEFMVLANV AAAETLVAKK SPLLFRVHEE
PSPEKLEALR EVATASGLVL AKGQVLKTAH LNKLLKGAAG TENDELINMA TLRSMTQAYY
FPENFGHFGL ALRAYAHFTS PIRRYADLIV HRALIKAHGW GDDGLSAWDM EHLTDTAKQI
SDTERRSMTA ERDTTDRYLA AFLSDRIGAE LTGRISGIAK FGVFVKLDET GADGMIPIRT
LGREYFHYDA ETQTLMGSDT GVVIGLGQRV TVKLAEAAPV TGGLIVELLT LEDRIMPKGP
SRGRGKPPRR KVGSARKKAA KTARKVKRTR K
//
