ID A0A108U6V6_9GAMM Unreviewed; 827 AA.
AC A0A108U6V6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=AZ78_1194 {ECO:0000313|EMBL:KWS03646.1};
OS Lysobacter capsici AZ78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS03646.1, ECO:0000313|Proteomes:UP000023435};
RN [1] {ECO:0000313|EMBL:KWS03646.1, ECO:0000313|Proteomes:UP000023435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ78 {ECO:0000313|EMBL:KWS03646.1,
RC ECO:0000313|Proteomes:UP000023435};
RX PubMed=24762937;
RA Puopolo G., Sonego P., Engelen K., Pertot I.;
RT "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT to Plant-Pathogenic Oomycetes.";
RL Genome Announc. 2:0-0(2014).
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|ARBA:ARBA00004496,
CC 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:KWS03646.1}.
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; JAJA02000001; KWS03646.1; -; Genomic_DNA.
DR RefSeq; WP_036113900.1; NZ_JAJA02000001.1.
DR AlphaFoldDB; A0A108U6V6; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000023435; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 2.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
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; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
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 724..805
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91581 MW; 87F2E0F26D4F7156 CRC64;
MTKKTKSTKT GKPGSSKTSP TGAGPAPSKK GGAKPPAARP PWLPDNLQHG ASKTPRKKAA
SGPASFLPQV PGPAIKGPAA KAPPFHDPYA DREASRYEQP IASRELILQT LAAADGPMSA
ETLAEQLKLS EPDRADALGK RLGAMIRDGQ LIRNRKGDFA PAAQMDLIPG VVIANPDGFG
FLRPESGVGD DLFLPPYEMR KAMHGDRVLV SVTGMDRRGR REGAIVEVLE RRLNRLIGRF
TVEQGISYVV PDDRRIQRNV QIPPDARMDA QNGQLVVCEL VQAPDHKRPP IGRVLAVLGD
KLTASLAVQA AIHGHEIPDV FPQETLDEAA AVPLTVPESV AAQRVDLRKL PLVTIDGEDA
KDFDDAVYCE SNRDGFRLVV AIADVSHYVR PGTPLDDEAQ KRATSVYFPG FVVPMLPETL
SNGICSLNPK VDRLCFVCDM QIDREGQVTE SKFYEAVMNS HARLTYTTVW NAVGDVPEEL
KSEAHAQIGS LLPNIERLHQ LFHVLLKARQ KRGAIEFESS EVRFVLGSNG EVTQAGMLQR
NDAHKLIEEC MIAANVEAAK YLIAQEVPAP YRIHDRPPEQ KYADLQEFLK EFKLRMPAWN
QVEPRDFTAL LKKIRERPDA ALIESVLLRS QSLAVYAPEN VGHFGLALHA YAHFTSPIRR
YPDLLVHRAI KHALSGAKPS AYGYSPRQMS ALALQCSERE RRADEAEREV DERYRAAWME
QHVGGEFEGT ISGVTSFGLF IELDESKVNG LVHVTQLPHD YYHFDPIRKT LKGERTAREF
RLGDRVAIVV LKASVEDRKI DFRLVEERGA KPLPPRGQPA KRPKQKY
//
