ID A0A1U9N9E0_9GAMM Unreviewed; 664 AA.
AC A0A1U9N9E0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=exoribonuclease II {ECO:0000256|ARBA:ARBA00012163};
DE EC=3.1.13.1 {ECO:0000256|ARBA:ARBA00012163};
GN ORFNames=B0D95_07280 {ECO:0000313|EMBL:AQT59910.1};
OS Cellvibrio sp. PSBB023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT59910.1, ECO:0000313|Proteomes:UP000189646};
RN [1] {ECO:0000313|EMBL:AQT59910.1, ECO:0000313|Proteomes:UP000189646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB023 {ECO:0000313|EMBL:AQT59910.1,
RC ECO:0000313|Proteomes:UP000189646};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP019799; AQT59910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9N9E0; -.
DR STRING; 1945512.B0D95_07280; -.
DR KEGG; ceb:B0D95_07280; -.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000189646; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR PANTHER; PTHR23355:SF37; EXORIBONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000189646}.
FT DOMAIN 572..652
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 664 AA; 74868 MW; 3CE44EE4C7FFFD4A CRC64;
MLNKDALQQL SQLKSSIVAA KDIAQGTVRT TTKRFGFLIL DDGREAFIDP EQMMRVLPDD
RVEAEINTNS KGQFEAKLTQ LIKPGLSEFV GKYVNKGSTD FVEPDVPNFN RWLFIPPQER
KGYKVGDLIH CSIARHPFNS EGKTQVHILN RIGTPDEPGV ESRYTIAKFQ MPFEWQSQAQ
SQAGGINWSP LTFDNGELDL THLPFVTIDS ENTRDMDDAI YIATTEAGWE LITAIADPSK
HIEFGSPLEL AARARASTHY LLGQTVTMLP VDLSHDTYSL VPEQKRPALI CRMHIGRDGT
INQFEFAEAL IRSQSKLSYQ GVYDALTAEV SSLGAPAHIH DMLVELKAFA QARAQYRQQH
ALVMEDRPDY AFVLNDVKKI DHIEKRERNI AHRMIEEAML VTNICAGELF LQHPGCGIFS
SHVGFRPERL NDALSLIQED RPDLTPGDLT KLEHFTTLFR ELRLNADNNP VNSRLHSLLQ
RMLQAGSLTF DPVAHFGLGF NAYAMVTSPI RRYNDLFNHL AIKRILRGQP PLELNDKKQF
AEQLQQQLNN GRQACRYVES WLGCQYANQH VGSVHSGSIA LVNSFGIGIK LDDWGLDGYA
LLAPKDGEVK AQFDSRRLSL TIEGNTYRLD DKVHVLVNNV DIEKRKINLE LISEETASRL
SVWL
//
