ID   K9ITE8_DESRO            Unreviewed;       604 AA.
AC   K9ITE8;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   13-SEP-2023, entry version 26.
DE   SubName: Full=Putative bifunctional atp sulfurylase/adenosine 5'-phosphosulfate kinase {ECO:0000313|EMBL:JAA52368.1};
DE   Flags: Fragment;
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC   Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA52368.1};
RN   [1] {ECO:0000313|EMBL:JAA52368.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:JAA52368.1};
RA   Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA   Ribeiro J.M.C.;
RT   "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT   and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT   Desmodus rotundus.";
RL   Submitted (NOV-2012) 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}.
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DR   EMBL; GABZ01001157; JAA52368.1; -; mRNA.
DR   AlphaFoldDB; K9ITE8; -.
DR   UniPathway; UPA00097; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   HAMAP; MF_00065; Adenylyl_sulf_kinase; 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:SF17; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE 1; 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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:JAA52368.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          213..365
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          374..596
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAA52368.1"
SQ   SEQUENCE   604 AA;  68514 MW;  D785065E3549891E CRC64;
     GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL SGAGKTTVSM ALEEYLVCHG
     IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF ADAGLVCITS FISPYTQDRN
     NARQIHEGAS LPFFEVFVDA PLHVCEQRDV KGLYKKARAG EIKGFTGIDS EYEKPEAPEL
     VLKTDSCDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP ENKLHLAKTD AETLPALKIN
     KVDMQWVQVL AEGWATPLNG FMREREYLQC LHFDCLLDGG VINLSVPIVL SAAREDKERL
     DGCTAFALIY EGRRVAILRN PEFFEHRKEE RCARQWGTTC KNHPYIKMVM EQGDWLIGGD
     LQVLDRIYWN DGLDQYRLTP AELKQKFKDM NADAVFAFQL RNPVHNGHAL LMQDTHKQLL
     ERGYRRPVLL LHPLGGWTKD DDVPLMWRMK QHAAVLEEGI LNPETTVVAI FPSPMMYAGP
     TEVQWHCRAR MVAGANFYIV GRDPAGMPHP DTGKDLYEPT HGAKVLTMAP GLITLEIVPF
     RVAAYNKKKK RMDYYDSDHH EDFEFISGTR MRKLARDGQK PPDGFMAPKA WTVLLQYYKS
     LEKA
//