ID A0A291P9E2_9GAMM Unreviewed; 646 AA.
AC A0A291P9E2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Exoribonuclease 2 {ECO:0000256|ARBA:ARBA00013374};
DE EC=3.1.13.1 {ECO:0000256|ARBA:ARBA00012163};
DE AltName: Full=Exoribonuclease II {ECO:0000256|ARBA:ARBA00031208};
GN Name=rnb {ECO:0000313|EMBL:ATJ83478.1};
GN ORFNames=BEI_2491 {ECO:0000313|EMBL:ATJ83478.1};
OS Halomonas beimenensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=475662 {ECO:0000313|EMBL:ATJ83478.1, ECO:0000313|Proteomes:UP000219993};
RN [1] {ECO:0000313|EMBL:ATJ83478.1, ECO:0000313|Proteomes:UP000219993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTU-111 {ECO:0000313|EMBL:ATJ83478.1,
RC ECO:0000313|Proteomes:UP000219993};
RX PubMed=29026163;
RA Chen Y.H., Lin S.S., Shyu Y.T.;
RT "Revealing the Saline Adaptation Strategies of the Halophilic Bacterium
RT Halomonas beimenensis through High-throughput Omics and Transposon
RT Mutagenesis Approaches.";
RL Sci. Rep. 7:13037-13037(2017).
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC {ECO:0000256|ARBA:ARBA00009925}.
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DR EMBL; CP021435; ATJ83478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291P9E2; -.
DR KEGG; hbe:BEI_2491; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000219993; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR Gene3D; 2.40.50.640; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR011804; RNase_II.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02062; RNase_B; 1.
DR PANTHER; PTHR23355:SF37; EXORIBONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 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 Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000219993}.
FT DOMAIN 563..646
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 646 AA; 72429 MW; 625BC707FAE02EFA CRC64;
MLQNNSVLAQ LKQQIRDNTP RVEGVIKATD RGFGFLETDD GESYFVPPPA MKQVLHGDRV
EAVLHEEGDK KSVEPDTLVE TGMERFIARL QKRDGRLAVV PDHPSVNNVL KARVKRSLDE
ASLGDGDWVV ARLVRHPLKP EDRGFFTQVD ELVAKTDDPA VPWRVTLARH ALEQECPDAG
DDWPLRDEGL EREDLTGEPF FTIDGEKTRD MDDALRVTPR EGGGWTLTVA IADPTAYVEE
GHAADLEART RAFTVYLPGQ NVTMLPETLA DDLCSLWEDR DRPVLACALD IEADGSLGDY
RFFAATARSH AKLVYDRVSD WLEGQGDWAP SEAIGEQLKA LAELTEARTA WRAEHALVFK
DRPDYVFDLD EAGNVLDIRT EERRIANRMI EESMIAANAC CAHLLAEHVG HGIFNVHRAF
EPDKAEAAHE FLTAQDIAVA PEALTELPRY RELKRELEGR DDAWLDARLR RFQGFTSMSA
KPGPHFGLGL PAYATWTSPI RKYGDMVNHR LIKRVLKGEQ APAEASQQLT EQLTERRRLN
RMAERDVKDW LYVRYLGPSA EAGEAFEAEI IAINRGGMRV RLTANGATAF VPAPLMHGDR
DKVVIDDKEG RIQIEGVERF KLGDTIRVAL TEAREETRSL VGRPAE
//
