ID C0QIZ5_DESAH Unreviewed; 519 AA.
AC C0QIZ5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Rne1 {ECO:0000313|EMBL:ACN13785.1};
DE EC=3.1.4.- {ECO:0000313|EMBL:ACN13785.1};
GN Name=rne1 {ECO:0000313|EMBL:ACN13785.1};
GN OrderedLocusNames=HRM2_06710 {ECO:0000313|EMBL:ACN13785.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN13785.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN13785.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP001087; ACN13785.1; -; Genomic_DNA.
DR RefSeq; WP_012663033.1; NC_012108.1.
DR AlphaFoldDB; C0QIZ5; -.
DR STRING; 177437.HRM2_06710; -.
DR KEGG; dat:HRM2_06710; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_7; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000000442; 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 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; IPR048583; RNase_E_G_thioredoxin-like.
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; PF20833; RNase_E_G_Thio; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACN13785.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 431..513
FT /note="RNase E/G thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF20833"
FT REGION 83..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 59120 MW; 19CB61E16A54E230 CRC64;
MLKELVVNAA EHETRVALLE NGTIAELFIE QDDESNITGN IYKGKIQRVL PGMQAAFVDI
GLAQAAFLYV DDIYDETSQE LARRFEQESD ADPNDPDLKP VDDTPIPMEW KPSFTTEASI
EDLVTEGQEI LVQISKSPIG TKGPRVTAHI SLPGRFMVLM PTVDHVGISK RITADSERTR
LKELLTSVRQ DNFGYIFRTA AQGIDEQRLK KEIAFLTKTW ESIQKKNKTS AAPTLLYRDL
TVTFRAVRDL LTDEADKLVI DSKIGYESVL SFLDKLMPDI HVSVELYQGK EPIFDAYNIE
GDITRALKKK VWLKSGGYII IDPTEALVAI DVNTGRYVGK HNFDETILKT NLEAVKEIAY
QIRLRNIGGI IIIDFIDMKR TQHKEKVMNL LIETLKRDKA QTNVLPLSEL GLVQMTRKRV
RKNLTRTLCE PCFYCGGDGM LLSKRSICYK IHRDLMSEAN DIMGNMFTVK VHPEIAQLLH
GEQEHLIISL EREIRRPITI YPDPQYHIEE YHIFETLAK
//