ID A0A1F4PKX5_9BACT Unreviewed; 312 AA.
AC A0A1F4PKX5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=A3F66_01935 {ECO:0000313|EMBL:OGB84308.1};
OS candidate division TM6 bacterium RIFCSPHIGHO2_12_FULL_32_22.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1802375 {ECO:0000313|EMBL:OGB84308.1, ECO:0000313|Proteomes:UP000178609};
RN [1] {ECO:0000313|EMBL:OGB84308.1, ECO:0000313|Proteomes:UP000178609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGB84308.1}.
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DR EMBL; METJ01000026; OGB84308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4PKX5; -.
DR Proteomes; UP000178609; 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:SF2; COENZYME GAMMA-F420-2:ALPHA-L-GLUTAMATE LIGASE; 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 108..292
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 312 AA; 35262 MW; C75EC4467752DBFC CRC64;
MVKNLWILSK DNSLGYENSR LIQECVNQAI DVKLVHPDNF DILVNRDDRK SVIYNGESIN
LPDLLLCRTG SDTDYFSLSI IRQLERLGIK TANNSYAIER VKDKLYAAQI LAQNGLPTPK
TMLVKFPIKP VYVEKHIGFP CVVKVITGSF GQGVYLSKDS DSFKDLMELV HSLKPPTSII
LQEFISYKPG SDLRVWVVGN KVLGAMLRCS TDGNFKANIS RGGKGELFPI NKEIEFLAKE
TARVLDLEIA GIDLLFDKDG YKICEANSAP GFEGFEYFCK QNIAKEVIDY CKNLNKSSHF
IYKEKHLKDL NY
//
