ID R9PQ83_AGAAL Unreviewed; 641 AA.
AC R9PQ83;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ORFNames=AALB_3637 {ECO:0000313|EMBL:GAD03557.1};
OS Agarivorans albus MKT 106.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Agarivorans.
OX NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD03557.1, ECO:0000313|Proteomes:UP000014461};
RN [1] {ECO:0000313|EMBL:GAD03557.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT Marine Bacterium.";
RL Genome Announc. 1:e00367-13(2013).
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}.
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:GAD03557.1}.
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DR EMBL; BARX01000029; GAD03557.1; -; Genomic_DNA.
DR RefSeq; WP_016403324.1; NZ_BARX01000029.1.
DR AlphaFoldDB; R9PQ83; -.
DR STRING; 1331007.AALB_3637; -.
DR Proteomes; UP000014461; Unassembled WGS sequence.
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 SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAD03557.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000014461}.
FT DOMAIN 560..641
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT COILED 316..352
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 641 AA; 72678 MW; 5D95285C5EED962A CRC64;
MLKDNPLLAQ LKQQIRETIP TVEGVVKATE KNFGFLQTDN KKSYFISPPM MKKLIHGDRI
SAAIRENNGK EAAEPETLVE AALDTFVARV KFVDKRTKLQ VDHPLINQLL SAKVIKDSGF
SIKQGDWVLA RLVKHALKEQ HFQAEIFEFI AESDDNFARW KATTKKHQLA WDQPELTEDL
AIIDQQVERR DLTNELFFTI DGENTKDMDD AVSITREAEH WKLKVAIADP SAYINSESKL
EKAAKQRAFT LYLPARTVPM MPSKLANEHC SLVADQVRPA LVCEMLIGLD GELQENAEFY
LATVQSKHRL NYNQVSDFIE QKATELESNA ELAEALQQLN LFSEQRNQWR AENTSVFGDQ
ADYEFVLDNK GQVIDILRQS RRSANRMIEE AMVAANICGG RFLDEKLGFG VFACHSGFKE
EKLDGLVELL AKFKLPVERE KLNDLDYFCQ LRRTIAATGD KCLDQLVKRH FNFGVYNEKC
LPHFGLGEAK YATWTSPIRK YSDLLNHRLI KSVINGETPS SPLSEELSEH LSDNRKKQKF
AEREMANYLY CEYFAEQDPN TCLLAEISNI NRGGLNIRLV DSGASAFVPK TKLAGKDEEL
TIESELGRLA TKDKQYCVGD TISVKIVEVK KLQQSIVAAP C
//