ID A0A0W0U0D6_9GAMM Unreviewed; 601 AA.
AC A0A0W0U0D6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=exoribonuclease II {ECO:0000256|ARBA:ARBA00012163};
DE EC=3.1.13.1 {ECO:0000256|ARBA:ARBA00012163};
DE Flags: Fragment;
GN Name=lidP_2 {ECO:0000313|EMBL:KTD01215.1};
GN ORFNames=Lgee_0859 {ECO:0000313|EMBL:KTD01215.1};
OS Legionella geestiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45065 {ECO:0000313|EMBL:KTD01215.1, ECO:0000313|Proteomes:UP000054785};
RN [1] {ECO:0000313|EMBL:KTD01215.1, ECO:0000313|Proteomes:UP000054785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49504 {ECO:0000313|EMBL:KTD01215.1,
RC ECO:0000313|Proteomes:UP000054785};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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 -!- 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:KTD01215.1}.
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DR EMBL; LNYC01000029; KTD01215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0U0D6; -.
DR STRING; 45065.Lgee_0859; -.
DR PATRIC; fig|45065.4.peg.922; -.
DR Proteomes; UP000054785; Unassembled WGS sequence.
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 CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
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:KTD01215.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000054785}.
FT DOMAIN 513..594
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KTD01215.1"
SQ SEQUENCE 601 AA; 67435 MW; F367C0C20A73021F CRC64;
LVLAHEIGVD RRGRPEGKIH EVVEHANASV VGRFFTEHGV SIVIPDNKRL TQDISIPQEF
ANGAKNGQVV LAEVIAYPSK RTQAIGKVAH ILGDHMAPGM EIDVAIHAHG IPSDWPQDVL
DEAARIPLSV DEASLKGRTD LRKLPFVTID GEDAKDFDDA VLAHEKPNGG YQLYVAIADV
SHYVQPDSAL DKEAARRGNS VYFPGRVVPM LPESLSNGIC SLNPHVDRLC MVAEMHISKD
GKITRSRFYR GVIHSKARLT YTKVGTWVQQ DAPPPEHREI WPHLKALHSL FTVLEGMRKS
RGAIDFDTTE TRIEFDEHKK IRNIVPVIRN DAHRLIEECM LAANVATARF LEKAEIPALY
RVHMPPSEDK VLALRQFLNE VGLSLSGGKK PTPRDFQKTM EKLIDRPDKH LVETVMLRSL
KQAQYLAGNE GHFGLAYSAY THFTSPIRRY PDLLIHRAIG HLLDNREAEN FRYSTDDMTR
LGTHCSSTER RADEATRDVV AWLKCEYMQD KVGQVFHGRI SAVTGFGIFV ELDEVYVEGL
VHVTSLKNDY YAFDPSKHRL RGERTGVSYN LGDSLTVLVA RVDLDERKID FEPVEGASQH
G
//
