ID Q2S597_SALRD Unreviewed; 596 AA.
AC Q2S597;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Ribonuclease, Rne/Rng family subfamily {ECO:0000313|EMBL:ABC44436.1};
GN OrderedLocusNames=SRU_0489 {ECO:0000313|EMBL:ABC44436.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44436.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC44436.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP000159; ABC44436.1; -; Genomic_DNA.
DR RefSeq; WP_011403267.1; NC_007677.1.
DR RefSeq; YP_444634.1; NC_007677.1.
DR AlphaFoldDB; Q2S597; -.
DR SMR; Q2S597; -.
DR STRING; 309807.SRU_0489; -.
DR EnsemblBacteria; ABC44436; ABC44436; SRU_0489.
DR KEGG; sru:SRU_0489; -.
DR PATRIC; fig|309807.25.peg.512; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_10; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000008674; 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; 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 NCBIfam; TIGR00757; RNaseEG; 1.
DR PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR PANTHER; PTHR30001:SF0; RIBONUCLEASE G; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 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:UP000008674};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..142
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 412..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 66918 MW; 2300B86E1C9C935D CRC64;
MSKEIVFNVG NEQTRIAIVE DGKLVELYIE NAEHKRTIGN LYLGQIRKVM PSIQAAFVDI
GQEQDAFLHF SDLSDNLPYL LDFLGLEAPT VEAIDVPKGK KDWDKRPSDL LNRGQTILVQ
VTKEPISNKG SRISTDISLA GRFLVLVPLQ NYVAVSRKIT DDEERRRLES LASSLVPDGV
GVIVRTVAQD RDAKSLDKDM KLLMERWRRV EKRLKDKPSP PELVHEDVDM ASSIVRDEFS
EEYDRILVDH EGLYSSIQSY VRAVGPQLVD RVELHEGDQP VFESVGIQHG ADRAFKDRVE
LPSGGYLFIE KTEAMHVVDV NSGRSGKGKS QAENSLNVNL EAARVIARQI RLRDLGGIIV
VDFIDLRDED DKKKVYDEVK KGFEEDRAVT KVLPMSDFGL VEITRQRLRP SITTTFSSAN
GTPSDDGDDG ADPEELRQAE RKIQSLEKEV EKREREVKRL KAEDDTPDEE VTALRQKIQA
LEDKLEAARA QQTAENATPR PSSSDGSAAS AEGDAAPDEL VEDIEQWLVA HSDTHRAVTL
RVHPFVAAFL RRPVPTYTTR WFMEHLVRVH VEADTEVPPH TFQVTDESGA PLPESP
//