ID A0A2M8MZM7_9RHOB Unreviewed; 749 AA.
AC A0A2M8MZM7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:PJF09675.1};
GN ORFNames=CUR21_07190 {ECO:0000313|EMBL:PJF09675.1};
OS Pseudorhodobacter sp. MZDSW-24AT.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudorhodobacter.
OX NCBI_TaxID=2052957 {ECO:0000313|EMBL:PJF09675.1, ECO:0000313|Proteomes:UP000230388};
RN [1] {ECO:0000313|EMBL:PJF09675.1, ECO:0000313|Proteomes:UP000230388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MZDSW-24AT {ECO:0000313|EMBL:PJF09675.1,
RC ECO:0000313|Proteomes:UP000230388};
RA Mayilraj S.;
RT "Pseudorhodobacter sp. nov., strain MZDSW-24AT genome sequence and
RT assembly.";
RL Submitted (NOV-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}.
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:PJF09675.1}.
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DR EMBL; PGOI01000007; PJF09675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8MZM7; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000230388; 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 Reference proteome {ECO:0000313|Proteomes:UP000230388};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 627..708
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 718..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 81823 MW; 2F90DF5E684CC0B9 CRC64;
MEQMPSKEQI LQWISENPGL AAKRDIAKAF GIKGAARIEL KRILGELAEE GQIARKGRSY
RDPEGLPPVS ILVITGPDAQ GDVFARPMEW GGAGEAPRIL FLAKKGDPAL AAGDRILARL
SPADVGEYQY EARLIRHIGT NPLRVLGVFR AGAEGGRIVP IDKGQDKEWR VGRDMTLGAK
DGELVEGEAV GRRNMGLPQA RITAVLGDPS GPKAVSLIAI HQHGIPDQFP DAVIAEADRA
LPAPLEGRTD LRDLPLCTID PADARDRDDA VYAEADTEPG NPGGFVVWVA IADVAYYVRP
GSALDREARK RGNSTYFPDR VVPMLPDVLS GDLCSLHQHV DRACLAVRMR LDAKGAKISH
RFVRGIMRSV ASLSYEQVQA AIDGAPDAVT APLLDPVLRP LYAAYAATKL ARAARQPLDL
DLPERKIELS EAGEVRSVSF KERFDAHRLI EEFMILANVA AAEELVRLKQ PLLFRVHEEP
TPEKLDALRE VAEASGFVLA KGQVLQTRHL NSLLAAAQGT EFDELLNIST LRSMTQAYYF
PQNFGHFGLA LKNYAHFTSP IRRYSDLIVH RALIAGHGWG KDGLSASDIE QLEDTAKLIS
DSERRSMAAE RDTTDRYLAA YLADRVGADF TGRISGVQRF GLFVKLDETG ADGLIPIRSV
GREFFHYDQD SQTLTGADTG LTIGIGQRVT VRLAEAVPVT GGIMLELLEI EGGALPRAQP
RRGRFAPRKP GKAAAKEAKV KRKVLRKRR
//
