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
//