ID Q7MQZ6_WOLSU Unreviewed; 653 AA.
AC Q7MQZ6;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=exoribonuclease II {ECO:0000256|ARBA:ARBA00012163};
DE EC=3.1.13.1 {ECO:0000256|ARBA:ARBA00012163};
GN OrderedLocusNames=WS1875 {ECO:0000313|EMBL:CAE10885.1};
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121 {ECO:0000313|Proteomes:UP000000422};
RN [1] {ECO:0000313|EMBL:CAE10885.1, ECO:0000313|Proteomes:UP000000422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 /
RC NCTC 11488 / FDC 602W {ECO:0000313|Proteomes:UP000000422};
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon JM., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571662; CAE10885.1; -; Genomic_DNA.
DR RefSeq; WP_011139668.1; NC_005090.1.
DR AlphaFoldDB; Q7MQZ6; -.
DR STRING; 273121.WS1875; -.
DR KEGG; wsu:WS1875; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_3_7; -.
DR Proteomes; UP000000422; Chromosome.
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; IPR011129; CSD.
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 NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00357; CSP; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR PROSITE; PS01175; RIBONUCLEASE_II; 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:UP000000422}.
FT DOMAIN 49..109
FT /note="Cold shock"
FT /evidence="ECO:0000259|SMART:SM00357"
FT DOMAIN 215..535
FT /note="Ribonuclease II/R"
FT /evidence="ECO:0000259|SMART:SM00955"
SQ SEQUENCE 653 AA; 74127 MW; ED3551200A51AF95 CRC64;
MREFLTTLAL GIKTKDIPRS FLALVETLRE KGALQAKGER IFLDLAFRVG VLDISREGVG
FLESFGSSGK DLLIQKSDLK GAFKGDVVLA RRVYSHKGGR PSAKVVEVLE KKNAILVAYL
DQHAGRIEAL DIKNGLSLPL NASAKSLKAL PPQTVIRLDV REGRIIEVLG VLSDPRVDEK
ISLALFNKSE PFPRECEEQA ESFGRKVEAS MYPARQDFRS LPFCTIDPID AKDHDDAVYF
DAKESILYVA IADVSEYVTP HSPIDKEARV RGFTIYLPHK SIPMLPRNLS ENICSLKPQE
DRLAYVWKIR LHKRTALPLK AELHEAIIRS KQKLSYEEVD EFLEEPKANS TILKELQEPL
LNLYARTKKL RAKRLERGYE FFNEENRLLM DENLNLISIV SEKETPSHSL IEECMLLANI
YSAKHLEKGI FRVHEEPKLE KIEELLWDLR SLGLEAKPKE TLHATIATIQ KEAEAKGIRT
EVDRMIIRSQ AQARYSHQKI GHFGLGFEEY SHFTSPIRRY SDLVLHRLLK AELKGEKRKM
EFYLDALAPL CDSLSALERE SARVEMDYKD RKYARLALER LGEVVEAVVV DEESPPLARA
EGFLKGARIV LGKGLVERLS RVRVRLMDVD VASAKIYGKV VGIIKEKRVQ TGV
//
