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Database: UniProt
Entry: A2BIU1_HYPBU
LinkDB: A2BIU1_HYPBU
Original site: A2BIU1_HYPBU 
ID   A2BIU1_HYPBU            Unreviewed;       297 AA.
AC   A2BIU1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Glutathione synthase-RimK/ribosomal protein S6 modification (Glutaminyl transferase) {ECO:0000313|EMBL:ABM79897.1};
GN   OrderedLocusNames=Hbut_0019 {ECO:0000313|EMBL:ABM79897.1};
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM79897.1, ECO:0000313|Proteomes:UP000002593};
RN   [1] {ECO:0000313|EMBL:ABM79897.1, ECO:0000313|Proteomes:UP000002593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC   {ECO:0000313|Proteomes:UP000002593};
RX   PubMed=17350933;
RA   Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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DR   EMBL; CP000493; ABM79897.1; -; Genomic_DNA.
DR   RefSeq; WP_011821214.1; NC_008818.1.
DR   AlphaFoldDB; A2BIU1; -.
DR   STRING; 415426.Hbut_0019; -.
DR   EnsemblBacteria; ABM79897; ABM79897; Hbut_0019.
DR   GeneID; 4782952; -.
DR   KEGG; hbu:Hbut_0019; -.
DR   eggNOG; arCOG01589; Archaea.
DR   HOGENOM; CLU_054353_2_0_2; -.
DR   OrthoDB; 33241at2157; -.
DR   Proteomes; UP000002593; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000002593};
KW   Transferase {ECO:0000313|EMBL:ABM79897.1}.
FT   DOMAIN          110..292
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   297 AA;  32914 MW;  A4DFFAE89B23E070 CRC64;
     MAKIAVLHHT PRPTWSSRQL LKAIADTGST PLYILWNYIS AELGTPSCPL KYRGRCLNVD
     AIIVRGLGRG LSIERYAVRR AILEAAESWG YVVVNPPEGL FRARDKFTSL RILQEAGIPV
     PRTLVTEDPT TALHAVEQLG DVVFKPIIGS LGLGSFRVKD TDTAYHIINL LLTLNQPLYI
     QKYLEKPGNR DLRVFVVGDH VVAAMYRIAP RNSWKTNIAQ GAKPVPATVR DEVAKAVIRA
     VKVLGLVYAG VDVIEYDENR YAVIEVNASP LWRGLQSATG VNPARYIVEK VLELVKK
//
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