ID A0A0G0L7A3_9BACT Unreviewed; 304 AA.
AC A0A0G0L7A3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Ribosomal protein S6 modification protein {ECO:0000313|EMBL:KKQ87908.1};
GN ORFNames=UT09_C0008G0013 {ECO:0000313|EMBL:KKQ87908.1};
OS Parcubacteria group bacterium GW2011_GWF2_38_8.
OC Bacteria.
OX NCBI_TaxID=1618961 {ECO:0000313|EMBL:KKQ87908.1, ECO:0000313|Proteomes:UP000034262};
RN [1] {ECO:0000313|EMBL:KKQ87908.1, ECO:0000313|Proteomes:UP000034262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ87908.1}.
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DR EMBL; LBVM01000008; KKQ87908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0L7A3; -.
DR PATRIC; fig|1618961.3.peg.269; -.
DR Proteomes; UP000034262; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR HAMAP; MF_01552; RimK; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR023533; RimK.
DR InterPro; IPR041107; Rimk_N.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR PANTHER; PTHR21621:SF7; RIBOSOMAL PROTEIN S6--L-GLUTAMATE LIGASE; 1.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF18030; Rimk_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 107..290
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 304 AA; 32617 MW; CA598EB9F6B30554 CRC64;
MRIGILSRNA RLYSTTRLVE AAQKRGHNVK VVDVLKCYMN ITANKPTVFY KPKDKKEKLE
FDAVIPRIGA SVTTYGTAVL RQFEVGGVYS VNESVAISRS RDKLRAHQLL ARKGVGMPMT
GYAHAANATE DLIEFVGGAP LIVKVLKSTH GSGVVLAETN NAAESVINAF RGLDADFLVQ
EFIKEAGGSD IRCFVIGDKV IAAMQRQAKE GEYRSNLHMG GTAAIVRLRP DERALAVRAA
GVMGLDVAGV DIIRSAHGPL VLEVNSSPGL KGIETSTGKD VAGAIIEYVE KDALKGPNKM
KGRG
//
