ID A0A178MUB2_9PROT Unreviewed; 744 AA.
AC A0A178MUB2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=A6A04_00550 {ECO:0000313|EMBL:OAN52223.1};
OS Paramagnetospirillum marisnigri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=1285242 {ECO:0000313|EMBL:OAN52223.1, ECO:0000313|Proteomes:UP000078428};
RN [1] {ECO:0000313|EMBL:OAN52223.1, ECO:0000313|Proteomes:UP000078428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-1 {ECO:0000313|EMBL:OAN52223.1,
RC ECO:0000313|Proteomes:UP000078428};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-2016) 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:OAN52223.1}.
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DR EMBL; LWQT01000044; OAN52223.1; -; Genomic_DNA.
DR RefSeq; WP_068491044.1; NZ_LWQT01000044.1.
DR AlphaFoldDB; A0A178MUB2; -.
DR STRING; 1285242.A6A04_00550; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000078428; 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:UP000078428};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 638..719
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 718..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 82485 MW; 70C97F224A3D73DB CRC64;
MTKPPHKAPK HVPIPSKQEV LDFIKSSPGR VGKRELARAF GLRGSDKIDL KAILRELERE
GAVERGQKKR FARPGALPDV GVVEIIGTDA DGELLARPLA WEHDGRPPRI FMAPFRQGEP
ALGVGDRALC KLRRLRDDTY EARAIRVVGE ARARVLGVFE SNPDGSGRLR PTSRKEKAEY
LVPKGESNGA EAGELVLADI MPGRLYGLRQ VSVKERLGLM GAPRSVSLVA IHANDIPFEF
PEAALKQAAA EGAAPMGHRT DLRAMPLVTI DGEDARDFDD AVWAEPDPDP NNAGGWHCLV
AIADVSWYVR PGDALDKEAF KRGNSVYFPD RVVPMLPEEL SNGWCSLKPD EDRPCLAVHF
WLDKLGNKLR HRFVRGMMRS VARLTYARVQ AAKDGNPDEQ TAPLLAPVIE PLYGAWNALF
LARKQRGVLE LDLPERKVVL DESGKIAKIE ERERFDSHRL IEDFMISANV CAAETLEQIR
QPCMYRVHDL PSAEKLDSLR EFLGSMELKL AKGQVLRPEH FNRILEAVAD TPNAHLVNEV
ILRSQAQAVY QPENIGHFGL GLAKYAHFTS PIRRYADLLV HRALVTGLKF GDGGLPADAV
VDFPDWGEHI SMTERRAATA EREAVDRYVT AYLADRVGAV FNAKVSGVTR FGLFVTLEGT
GADGLVPISS LPEDFYVHDE THHCLVGKRT RKTFQLGQRL DVVLREANTL TGSMVFNLDG
APERGARPPR RGPAPFRPPK RKGR
//
