ID   M0G186_9EURY            Unreviewed;       325 AA.
AC   M0G186;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Sulfate adenylyltransferase {ECO:0000313|EMBL:ELZ64594.1};
GN   ORFNames=C459_08695 {ECO:0000313|EMBL:ELZ64594.1};
OS   Haloferax sp. ATCC BAA-645.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1227463 {ECO:0000313|EMBL:ELZ64594.1, ECO:0000313|Proteomes:UP000011673};
RN   [1] {ECO:0000313|EMBL:ELZ64594.1, ECO:0000313|Proteomes:UP000011673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-645 {ECO:0000313|EMBL:ELZ64594.1,
RC   ECO:0000313|Proteomes:UP000011673};
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:ELZ64594.1}.
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DR   EMBL; AOLE01000019; ELZ64594.1; -; Genomic_DNA.
DR   RefSeq; WP_008573632.1; NZ_AOLE01000019.1.
DR   AlphaFoldDB; M0G186; -.
DR   PATRIC; fig|1227463.4.peg.1748; -.
DR   Proteomes; UP000011673; Unassembled WGS sequence.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43196; SULFATE ADENYLYLTRANSFERASE SUBUNIT 2; 1.
DR   PANTHER; PTHR43196:SF1; SULFATE ADENYLYLTRANSFERASE SUBUNIT 2; 1.
DR   Pfam; PF01507; PAPS_reduct; 2.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   4: Predicted;
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ELZ64594.1};
KW   Transferase {ECO:0000313|EMBL:ELZ64594.1}.
FT   DOMAIN          50..118
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   DOMAIN          165..231
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   325 AA;  37564 MW;  25160AA60DCFBD1D CRC64;
     MSEAESFPDY LDVDYTDGEG ETPEDYPSIE DKIEKAIEVT KQGLEQYENP AVMWTGGKDS
     TLTLYFIKEV AERYDLEVPP AVFIDHYQHF DEIMDFVEHW ADEWDLDVIW ARNEDVGAYV
     DENGLEPGDD IPVSELSEHN QHHIRNILEY EEDTFPFLLD TYVGNHLLKT VALNDTLEEY
     DIDGVISGVR WDEQEARADE TFFSPRHDPD IYPPHDRIQP ILQFEESAVW DAFWYFAVPD
     TVENYPEDGY VPTSDTDLPE GVTQEDVPVS PKYFAGFRSL GSEVSTDKSA EEPAWLQDME
     NTTERAGRAQ DKEDLMERLR DLGYM
//