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Database: UniProt
Entry: M0MJB5_9EURY
LinkDB: M0MJB5_9EURY
Original site: M0MJB5_9EURY 
ID   M0MJB5_9EURY            Unreviewed;       449 AA.
AC   M0MJB5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=C449_05896 {ECO:0000313|EMBL:EMA45771.1};
OS   Halococcus saccharolyticus DSM 5350.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA45771.1, ECO:0000313|Proteomes:UP000011669};
RN   [1] {ECO:0000313|EMBL:EMA45771.1, ECO:0000313|Proteomes:UP000011669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA45771.1,
RC   ECO:0000313|Proteomes:UP000011669};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA45771.1}.
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DR   EMBL; AOMD01000016; EMA45771.1; -; Genomic_DNA.
DR   RefSeq; WP_006077039.1; NZ_AOMD01000016.1.
DR   AlphaFoldDB; M0MJB5; -.
DR   STRING; 1227455.C449_05896; -.
DR   PATRIC; fig|1227455.4.peg.1202; -.
DR   InParanoid; M0MJB5; -.
DR   OrthoDB; 200216at2157; -.
DR   Proteomes; UP000011669; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd00303; retropepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 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; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR008503; Put_Zn_protease.
DR   PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF08443; RimK; 1.
DR   Pfam; PF05618; Zn_protease; 1.
DR   SUPFAM; SSF50630; Acid proteases; 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:UP000011669}.
FT   DOMAIN          106..287
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          305..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  48652 MW;  B9E1D7B502F80038 CRC64;
     MTNADDPVRV GVLSLHNSKE TKAILNAVED LGHTPVWLRR ENTAVSIRDS EVGVEPEIDV
     VANRLLLSNT EEPAEGLGLA ATFERIRPML NRPGPTLTAI HKFATAARLA DWNVRVPDAL
     LALSNDRLNR GREQFGDVGV YKTAIGTHGG GTWKVDLDEP VNPKVGNRQA FLQELIERDA
     TEHRDLRVYV VDDRMVGAMH RYAPEGDWRT NVALGGAVEN VTDDIPDEAR ETALYAADVM
     DLDYVGVDLI EGTDGWHVLE MNPTAGFKGL YEATGKSPAP YIAKLAIERV GGEVDDDRVA
     EIATTLDDSR PSSMPRPERP APGQTPLIGY IEDVVVSGTS GSRSALAKSD TGATRTSIDT
     SLAAEIGAGP IKSMTRVRSG SSKSGKARPV VDLVVGIGGT QHTVTASVED RSHMSYPLLL
     GRDILQHYQV DVRRRADSDE TAEAERLEE
//
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