ID A0A0G0JQP7_9BACT Unreviewed; 308 AA.
AC A0A0G0JQP7;
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, ribosomal protein S6 modification protein {ECO:0000313|EMBL:KKQ69077.1};
GN Name=rimK1 {ECO:0000313|EMBL:KKQ69077.1};
GN ORFNames=US89_C0004G0121 {ECO:0000313|EMBL:KKQ69077.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_38_29.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619066 {ECO:0000313|EMBL:KKQ69077.1, ECO:0000313|Proteomes:UP000033957};
RN [1] {ECO:0000313|EMBL:KKQ69077.1, ECO:0000313|Proteomes:UP000033957}
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:KKQ69077.1}.
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DR EMBL; LBUS01000004; KKQ69077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JQP7; -.
DR STRING; 1619066.US89_C0004G0121; -.
DR PATRIC; fig|1619066.4.peg.385; -.
DR Proteomes; UP000033957; 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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR041107; Rimk_N.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 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 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 109..295
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 308 AA; 34390 MW; 8E8C40E8E9EEA60F CRC64;
MKIAVLTFES IDRKSSKEDS RIVQAARELG HKARIFRADK CQLVYDRHNP RVFYDGSVFP
DYDVIIPRVG LLRNIELQAA LVKQLQLMGF PVVNTFHAIS RAKNKLRTMQ ILDHFDIPIP
KTIVVRDLKY INADILKQVN AFPVILKTPF GSYGSGVVIA ESKRAVMSAL SFLWKQSGVN
IILLQEYMKE SKGKDVRVFV VGNKVVATMI RSAKKGEFRS NIELGGKGEK TVLTKREIDV
AIKSVKVLKL EIGGVDIIRS KKGPLVLEVN ANPGFKSLEE VTGVDVAKAI VEYAVEKAKL
VKLTKEEA
//