ID A0A0K1EPS4_CHOCO Unreviewed; 348 AA.
AC A0A0K1EPS4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Ribosomal protein S6 modification protein {ECO:0000313|EMBL:AKT42819.1};
GN Name=rimK {ECO:0000313|EMBL:AKT42819.1};
GN ORFNames=CMC5_070470 {ECO:0000313|EMBL:AKT42819.1};
OS Chondromyces crocatus.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC Chondromyces.
OX NCBI_TaxID=52 {ECO:0000313|EMBL:AKT42819.1, ECO:0000313|Proteomes:UP000067626};
RN [1] {ECO:0000313|EMBL:AKT42819.1, ECO:0000313|Proteomes:UP000067626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm c5 {ECO:0000313|EMBL:AKT42819.1,
RC ECO:0000313|Proteomes:UP000067626};
RA Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT high potential for natural compound synthesis and the genetic basis for the
RT loss of fruiting body formation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP012159; AKT42819.1; -; Genomic_DNA.
DR RefSeq; WP_050434384.1; NZ_CP012159.1.
DR AlphaFoldDB; A0A0K1EPS4; -.
DR STRING; 52.CMC5_070470; -.
DR KEGG; ccro:CMC5_070470; -.
DR PATRIC; fig|52.7.peg.7732; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000067626; Chromosome.
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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000067626}.
FT DOMAIN 104..287
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 327..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 37081 MW; D4EDB2A5592992B5 CRC64;
MRVLVLSRNA SLYSTSRIVL AARARGHDVS IIDPLDFQIV VSRGGPSVLV GGAAVPRFDI
VIPRIGASIT NYGLAVVRQF DLMGVPVLNG AVSIARSRDK LRALQLLTRR KLEVPTTVCA
RSPAGVEAAL GLVGGCPAII KLQQGTQGIG TMIAETPQAV HSLLETFWAM GQDIVLQEYV
RESKGRDLRV IVVGGRVIAC MRRVAKPGEF RSNLHRGGTG DGVRLPRTYR SVAIRAAKAM
GLEVAGVDML ESKSGPKILE INSSPGLEGV ERTTGIDVAG AIISYAETYA ATHGRISRKL
VEARLNGVIH EERMPRRIAL ATSPEVRTAR RKGAAMTNGS SRAGRAAS
//
