ID A0A1H1YEY5_9MICO Unreviewed; 401 AA.
AC A0A1H1YEY5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=SSU ribosomal protein S6P modification protein {ECO:0000313|EMBL:SDT19596.1};
GN ORFNames=SAMN04489721_2733 {ECO:0000313|EMBL:SDT19596.1};
OS Agromyces flavus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=589382 {ECO:0000313|EMBL:SDT19596.1, ECO:0000313|Proteomes:UP000199482};
RN [1] {ECO:0000313|Proteomes:UP000199482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 202695 {ECO:0000313|Proteomes:UP000199482};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT629755; SDT19596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1YEY5; -.
DR STRING; 589382.SAMN04489721_2733; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000199482; Chromosome i.
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:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; 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 Gene3D; 3.30.70.1450; Regulator of K+ conductance, C-terminal domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
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 Pfam; PF02080; TrkA_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF116726; TrkA C-terminal domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51202; RCK_C; 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 104..287
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 296..380
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
FT REGION 379..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43678 MW; FE43BE075095B703 CRC64;
MKLAILSRAP QAYSTQRLRA AAQQRGHDVK VLNTLRFGID LSGPEPDLQY RGRPLSDYDA
VLPRIGNSIT YFGTAVVRQF EQMDVYTPNT ANGITNARDK LRATQILSRH GIGMPATTFV
RNRADLRPAI ERVGGAPVVI KLLEGTQGIG VILAPEVKVA EAIIETLHST KQNVLIQRFI
GESRGRDIRA LVVGDRVVAA MRRVASGDEF RSNVHRGGTV EPVALSAEYE QAAVRSAQIM
GLKVAGVDML EGNEGPLVME VNSSPGLQGI ETATNLDVAG AIIDYIANQV AFPEIDVRQR
LTVSTGYGVA ELLVHGAADL VGKTLGDSGL WDRDITVLTL HRGTSVIPNP RKGVVLEAED
RLLCFGKLEE MRSMIPERRR RRQKVRRLPK EPIPAPVEVA G
//
