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Database: UniProt
Entry: A0A0J7L6H6_LASNI
LinkDB: A0A0J7L6H6_LASNI
Original site: A0A0J7L6H6_LASNI 
ID   A0A0J7L6H6_LASNI        Unreviewed;       551 AA.
AC   A0A0J7L6H6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Bifunctional 3-phosphoadenosine 5-phosphosulfate synthetase {ECO:0000313|EMBL:KMQ98168.1};
GN   ORFNames=RF55_1479 {ECO:0000313|EMBL:KMQ98168.1};
OS   Lasius niger (Black garden ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Lasius; Lasius.
OX   NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ98168.1, ECO:0000313|Proteomes:UP000036403};
RN   [1] {ECO:0000313|EMBL:KMQ98168.1, ECO:0000313|Proteomes:UP000036403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:KMQ98168.1};
RA   Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT   "Lasius niger genome sequencing.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC       {ECO:0000256|ARBA:ARBA00005050}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC       adenylyltransferase family. {ECO:0000256|ARBA:ARBA00009290}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC       family. {ECO:0000256|ARBA:ARBA00007268}.
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:KMQ98168.1}.
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DR   EMBL; LBMM01000514; KMQ98168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J7L6H6; -.
DR   STRING; 67767.A0A0J7L6H6; -.
DR   PaxDb; 67767-A0A0J7L6H6; -.
DR   OrthoDB; 22780at2759; -.
DR   UniPathway; UPA00097; -.
DR   Proteomes; UP000036403; Unassembled WGS sequence.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniPathway.
DR   CDD; cd02027; APSK; 1.
DR   CDD; cd00517; ATPS; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR024951; Sulfurylase_cat_dom.
DR   InterPro; IPR002650; Sulphate_adenylyltransferase.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   NCBIfam; TIGR00339; sopT; 1.
DR   PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   Pfam; PF14306; PUA_2; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          145..300
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          309..534
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
SQ   SEQUENCE   551 AA;  63066 MW;  47A2D93ADB0CF7B2 CRC64;
     MRTGLNRNLG FSKEDREENV RRVAEVARLF ADAGIITLCS FVSPFAADRK MAREIHRNAD
     LPFFEIFVEA SLRVCESRDV KGLYKKARQG IIKGFTGIDQ SYDVPVTPDL IVNTENATVR
     QSTDLVVDFL QRKHVIPKSG DPFKQPFREL FVKEDRLEDI RKEMKALPAL EIQEIDMQWV
     QVLAEGWAAP LKGFMRENEY LQTQHFNCLY ENGIPINQSI PIVLAISTAD KERYFDASAL
     VLRYQGKDVA ILRNPEFYHH RKEERCCRQF GTNDPRHPYV RIIRESGDWL VGGDLEVVER
     IRWNDGLDHY RLTPNEIRIR CQEIGADAVF AFQLRNPIHN GHALLMQDTR RHLVEERGFK
     KPVLLLHPLG GWTKDDDVPL PIRIQQHQAV LEDGILHKDT ILAIFPSPMC YAGPTEVQWH
     AKARMIAGAN FYIVGRDPAG VSHPDKSATP DGNLYDATHG ARVLSMAPGL QNLEIIPFRV
     AAYDAKVKKM SFFEAERQQD FIFISGTKMR ALAKNGEDPP EGFMAPKAWK IVAKYYQTAH
     TCRREANYQN E
//
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