ID C8W5Q7_DESAS Unreviewed; 564 AA.
AC C8W5Q7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Ribonuclease, Rne/Rng family {ECO:0000313|EMBL:ACV64057.1};
GN OrderedLocusNames=Dtox_3326 {ECO:0000313|EMBL:ACV64057.1};
OS Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV64057.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV64057.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP001720; ACV64057.1; -; Genomic_DNA.
DR RefSeq; WP_015758747.1; NC_013216.1.
DR AlphaFoldDB; C8W5Q7; -.
DR STRING; 485916.Dtox_3326; -.
DR KEGG; dae:Dtox_3326; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_9; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000002217; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd04453; S1_RNase_E; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR004659; RNase_E/G.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR002792; TRAM_dom.
DR NCBIfam; TIGR00757; RNaseEG; 1.
DR PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR PANTHER; PTHR30001:SF0; RIBONUCLEASE G; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR Pfam; PF01938; TRAM; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..127
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 499..561
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
SQ SEQUENCE 564 AA; 63657 MW; E5C003187610BD01 CRC64;
MLKEIVVNVG EEETRVAVLE DKVTVEIYIE RAINQRLEGN IFKGKVENVL PGMQAAFVDI
GLDKNAFLYV EDALPSRNPE ENRNSLDLCA NIGDVLKQGQ DLVVQIVKEP IGTKGPRITT
HITLPGRYLV LMPTVDYIGI SRRIADEQER ERLKELAARV KPRDMGLIVR TVAEGVSEEE
LAQDVNVLAK LWRKIINRSN HGPVPNLLHR DLELVHRILR DIFTEDVDRL IIDSRYEYER
VLELLDIIDP QLKIKVSVDE RENLFEEYGI EMELEKAVKR KVWLKCGGYL VIDQAEALTA
IDVNTGKFVG STNLEDTVLR TNLDAALEIA RQLRLRNIGG IIIVDFIDML EDEHRQKVLE
VLEKEIKKDK TKTNLLGITQ LGLVEMTRKK VRPSLSEMLQ KPCPYCEGRG KVLSEETVGI
YFKNEIYQLS RQTPADTILV EANPLVAARL IGSGGSNLRD LENKTGKNLY IRGSANYHIE
SVKIRPLYNK DDIEANIVPV KTGEVLEVCV EEPHASNIND GISRLNGFIL DIEGAGSLVG
ETIPVEIIRV HRTYAKAKVA RTFN
//