ID A0A1E4MIG2_9SPHN Unreviewed; 782 AA.
AC A0A1E4MIG2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=ABT11_03780 {ECO:0000313|EMBL:ODU71306.1};
OS Novosphingobium sp. SCN 66-18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1660121 {ECO:0000313|EMBL:ODU71306.1, ECO:0000313|Proteomes:UP000094170};
RN [1] {ECO:0000313|EMBL:ODU71306.1, ECO:0000313|Proteomes:UP000094170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU71306.1}.
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; MEGD01000005; ODU71306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4MIG2; -.
DR Proteomes; UP000094170; 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 PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 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 657..738
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 746..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 86340 MW; AEFA5FE3A6422A60 CRC64;
MRCDSSDVRL ELRAAKRHMA WMPFPKTLRP EPGLPTRQQV LDFIARSDEP AGKREIARAF
GLKGQEKIAL KALLKDMAEE GLIDGNRTAF HRMGGVPRVT VLRVVDTEDG EAIAIPDSWH
PDDGAPPPRL RLVEQRGKQR QQALRVGDRV LARTEEAGKG WIAHAMKKLP AQTDQMLGVV
EIDGAGKGWL APVDKRVRNA VPISDLGQAE AGHLVLAEPA GRSPRAGLKV TTVLGDPLAP
RAFSLIAIHK YGIPFSFTEK AIEEARLAAA LPLSEDHRED LRHLPIVAID PIDARDHDDA
IWAEPDGEGG FRALVAIADV SFYVRPGGAL DRDARKRGNS VYFPDRVVPM LPEVLSADVC
SLKAGSDRAA MACHMTIDAQ GRVTSWRFTR ALVRIAEVIA YEEAQRRIDA DEAEAHLVNL
WAAWRLLEKA RKDRDPLELD LPERRVMLDE QGRIAEVALR ERLDAHRVVE DFMVTANVAA
AKALEAKVAP VVYRIHEPPT REKLIALKEY LATFDRKLAL GQVITPSLFN RMLKDVTDDA
EKALVMEAVL RSQTQAYYGP RNAGHFGLSL GSYAHFTSPI RRYSDLLVHR ALVDAYDLEQ
PRPKDHDLPP ATGLADRDRN DLARVSEAIS ASERRAMEAE RETIDRYVAA WLAGRVGEVF
DTRITGVQKF GLFATIIGLG GDGLVPVSVL GAERFAYDEK AQVLEGESSG EQFAMGMILK
LRLAEANPLT GALKFEPVDV AEGVSRIERR GGKLPGKPKP KGKFAVGKRG RPSNIRHQGK
RK
//
