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Database: UniProt
Entry: G9KF56_MUSPF
LinkDB: G9KF56_MUSPF
Original site: G9KF56_MUSPF 
ID   G9KF56_MUSPF            Unreviewed;       606 AA.
AC   G9KF56;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=3'-phosphoadenosine 5'-phosphosulfate synthase 2 {ECO:0000313|EMBL:AES03531.1};
DE   Flags: Fragment;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|EMBL:AES03531.1};
RN   [1] {ECO:0000313|EMBL:AES03531.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lungs {ECO:0000313|EMBL:AES03531.1};
RX   PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA   Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA   Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA   Farooqui A., Kelvin D.J.;
RT   "Sequencing, annotation, and characterization of the influenza ferret
RT   infectome.";
RL   J. Virol. 87:1957-1966(2013).
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; JP014933; AES03531.1; -; mRNA.
DR   AlphaFoldDB; G9KF56; -.
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: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:SF16; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE 2; 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   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          208..370
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          378..600
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AES03531.1"
FT   NON_TER         606
FT                   /evidence="ECO:0000313|EMBL:AES03531.1"
SQ   SEQUENCE   606 AA;  68584 MW;  CE47BBA36655C3AE CRC64;
     ESQQKSTNVV YQAHHVSRNK RGQVVGTRGG FRGCTVWLTG LSGAGKTTIS FALEEYLVSH
     AIPCYSLDGD NVRHGLNKNL GFSPGDREEN IRRIAEVAKL FADAGLVCIT SFISPFTKDR
     ENARKIHESA GLPFFEIFVD APLNICESRD VKGLYKRARA GEIKGFTGID SDYEKPETPE
     RVLKTNLSSV SDCVQQVVEL LQEQNIVPHT IMKGVHELFV PENKLDQVRA EAEALPSLEI
     TKLDLQWVQV LSEGWATPLK GFMREKEYLQ AIHFDTLLDD GVINMSIPIV LPVSTDDKTR
     LEGRSEFVLT HGGRRVAVLR DPEFYQPYEH RKEERCSRVW GTMCAKHPHI KMVMESGDWL
     VGGDLHVLER IRWNDGLDQY RLTPLELKQK CKEMNADAVF AFQLRNPVHN GHALLMQDTR
     RRLLERGYKH PVLLLHPLGG WTKDDDVPLA WRMKQHAAVL EEGVLDPKST IVAIFPSPML
     YAGPTEVQWH CRSRMIAGVN FYIVGRDPAG MPNPETKKDL YEPTHGGKVL SMAPGLTSVE
     IIPFRVAAYN KAKKAMDFYD PARHNEFDFI SGTRMRKLAR EGENPPDGFM APKAWKVLTD
     YYRSLE
//
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