ID E1V4Q0_HALED Unreviewed; 646 AA.
AC E1V4Q0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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:CBV42988.1};
GN OrderedLocusNames=HELO_3104 {ECO:0000313|EMBL:CBV42988.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV42988.1, ECO:0000313|Proteomes:UP000008707};
RN [1] {ECO:0000313|Proteomes:UP000008707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC {ECO:0000313|Proteomes:UP000008707};
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
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; FN869568; CBV42988.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V4Q0; -.
DR STRING; 768066.HELO_3104; -.
DR KEGG; hel:HELO_3104; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000008707; 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, ECO:0000313|EMBL:CBV42988.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722}.
FT DOMAIN 563..644
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 646 AA; 72648 MW; 0C6A8E8657C58D5B CRC64;
MLQNNSALAQ LKQQIRDNTP RVEGVIKATE RGFGFLETED GTSYFVPPPA MKQVLHGDRV
GAILHEEGEK KSVEPDTLIE QGLERFIARV RKRDGRLAVI PDHPSISNAL KARVKRSLDE
ASLDDGDWVE ARLVRHPLKP DDRAFFAQID ELVAKHDNPA VPWRVTLARH ALEQASPDGG
DDWPLRDEGL QREDLTEAPF FTIDDAKTRD MDDALRIEPR DNGGWRLTVA IADPTAYVAE
GDGVDLEART RAFTVYLPGQ NVTMLPEHLA DDLCSLWEGQ DRPALACALD VEADGSLGDY
RFFAATVRSH ARLAYDDVSD WLEGQGEWAP EPAIGEQLKA LRDLTEARTA WRAEHALVFK
DRPDYVFDLD DAGNVLNIRT EQRRIANRMI EESMIAANAC CAHLLAEHVG HGIFNVHRAF
EPEKAEAARE FLADQDIEVA LEALTELPRY KELKRELEGR DDAWLDARLR RFQGFTSMSA
RPGPHFGLGL AAYATWTSPI RKYGDMVNHR LIKRVLKGEQ APAEASLELT EQLTERRRLN
RMAERDVKDW LYVRYLGPHA ESGEAFNAEI IAINRGGMRV RLTANGATAF VPAPLMHSDR
DKVVIDDKEG RIQIEGEERF KLGDHVRVAL TEAREETRSL VGRPAD
//