ID T0SEJ9_LACLC Unreviewed; 670 AA.
AC T0SEJ9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=exoribonuclease II {ECO:0000256|ARBA:ARBA00012163};
DE EC=3.1.13.1 {ECO:0000256|ARBA:ARBA00012163};
DE Flags: Fragment;
GN ORFNames=LLT6_09170 {ECO:0000313|EMBL:EQC57417.1};
OS Lactococcus cremoris subsp. cremoris TIFN6.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1234876 {ECO:0000313|EMBL:EQC57417.1, ECO:0000313|Proteomes:UP000015854};
RN [1] {ECO:0000313|EMBL:EQC57417.1, ECO:0000313|Proteomes:UP000015854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIFN6 {ECO:0000313|EMBL:EQC57417.1,
RC ECO:0000313|Proteomes:UP000015854};
RX PubMed=23823494; DOI=10.1038/ismej.2013.108;
RA Erkus O., de Jager V.C., Spus M., van Alen-Boerrigter I.J.,
RA van Rijswijck I.M., Hazelwood L., Janssen P.W., van Hijum S.A.,
RA Kleerebezem M., Smid E.J.;
RT "Multifactorial diversity sustains microbial community stability.";
RL ISME J. 7:2126-2136(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 -!- 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:EQC57417.1}.
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DR EMBL; ATBB01000140; EQC57417.1; -; Genomic_DNA.
DR AlphaFoldDB; T0SEJ9; -.
DR Proteomes; UP000015854; 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; 2.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR011129; CSD.
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; 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; 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; 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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000015854}.
FT DOMAIN 579..662
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT NON_TER 670
FT /evidence="ECO:0000313|EMBL:EQC57417.1"
SQ SEQUENCE 670 AA; 75758 MW; 717F71C2D21518B1 CRC64;
MVQLSELASA LKQTESKGVF SKHPKGFGFV HPEGETDKTN DIYIGQNETK FAMDGDKVTV
KVLYPKTERR GASGQIIKIN ERAVVDTVGT YRSLSNRQAK ALGYKGRIEL FNDRISDTLY
IKQPLTGVQE EDVVSIKVTQ YPTDTKAFEG KITQIIGHKG EVGLDILEVL YAMKIPQEFS
AETLAEAESF SEELTQEDLQ GREDYRNEIT YTIDGEDSKD LDDAIHVKKL SNGHFELGVH
IADVSHYVTE GSSLNEEAYA RATSVYVTDR VVPMLPVRLS NNLCSLNEAQ ERLTMSCLME
IDDKGKIVTY KISPSVIKTT YRMTYSNVNK MIHQGQEGHR EALEKFSKIA DSIEVAVELH
EILETMRKDR GMIEFDESEA KIILDDEGHP IEIVKRDRDT AERMIESFML MANETVALDF
QKKKLPSLYR VHETPKEKAF AKLMEAAAEA GFSLSSDSHQ AINFFADEIK GTSFEKALTY
QLRHTMSTAV YSEKNTKHFG LAATNYTHFT SPIRRYPDLI IHRLLHLYPS DHSNRTKDEW
KERLPEIASH SSDMEHRAVV TERIIDAMKK AEYMLERIGE VYTGTITGVQ KFGIFVALDN
TVEGLVRVPN LHTGTTEELD FDEEMSIIKG KKSETIYQVG KEIKICVIAA NKRKGTVDFE
QIAPEKTSNL
//