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Database: UniProt
Entry: H3GR72_PHYRM
LinkDB: H3GR72_PHYRM
Original site: H3GR72_PHYRM 
ID   H3GR72_PHYRM            Unreviewed;      1016 AA.
AC   H3GR72;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblProtists:Phyra79353};
OS   Phytophthora ramorum (Sudden oak death agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra79353, ECO:0000313|Proteomes:UP000005238};
RN   [1] {ECO:0000313|Proteomes:UP000005238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
RN   [2] {ECO:0000313|EnsemblProtists:Phyra79353}
RP   IDENTIFICATION.
RC   STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra79353};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Sulfur metabolism. {ECO:0000256|ARBA:ARBA00004678}.
CC   -!- SIMILARITY: Belongs to the PPase family.
CC       {ECO:0000256|ARBA:ARBA00006220}.
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DR   EMBL; DS566036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3GR72; -.
DR   STRING; 164328.H3GR72; -.
DR   EnsemblProtists; Phyra79353; Phyra79353; Phyra79353.
DR   VEuPathDB; FungiDB:PSURA_79353; -.
DR   eggNOG; KOG1626; Eukaryota.
DR   eggNOG; KOG4238; Eukaryota.
DR   HOGENOM; CLU_009463_0_0_1; -.
DR   InParanoid; H3GR72; -.
DR   OMA; QGEVDHK; -.
DR   Proteomes; UP000005238; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:InterPro.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR   GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR   CDD; cd02027; APSK; 1.
DR   CDD; cd00412; pyrophosphatase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.80.10; Inorganic pyrophosphatase; 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; IPR008162; Pyrophosphatase.
DR   InterPro; IPR036649; Pyrophosphatase_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR024951; Sulfurylase_cat_dom.
DR   NCBIfam; TIGR00455; apsK; 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   Pfam; PF00719; Pyrophosphatase; 1.
DR   SUPFAM; SSF50324; Inorganic pyrophosphatase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   PROSITE; PS00387; PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005238};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          334..501
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          511..717
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
SQ   SEQUENCE   1016 AA;  113968 MW;  A5A04D76AC39BA75 CRC64;
     MSDALYASVK QEDLELNEGA ASRVFSRGPD HDERRELVKK FVLAALVVMP YLVLIALFAG
     VGSPSVGSSY APSIAVSDLA NQTQVDQVCA DQRLQKLDMQ RNVYYDSSLL TRPQRYAALQ
     QKGATLWFTG LSGSGKSTVG RALEKELLRR RVHTYRLDGD NVRIGLNRDL SFTETDRAES
     VRRVGEMSAL FSEAGVITLV ALVSPFRARR DEVRELHKKM NIPFYEVFVD VPVSVAADRD
     VKGLYKRAIK GEIKDFTGIS SPYEEPLTPE IHLNASSQSL DDEVKMILDK LEAEGLLTGV
     EEPPSGYPGV AVADGGNAVA TFPTLFPDQP RSTRPGNFDE LPRVLLRDED VHWLQVIGEG
     WAAPLRGFMR EGVYLQSLHF SSVLYDSDNL TDGHLALHKS TNFSEYSSEF VSKGQRVNMP
     VPIVLPINDA TKDHIGEFKQ VVLVSPSGEE LALLNEPEIF DHRKEERITR TFGAMDNGHP
     YIAEILKSGE YLLGGEIELL SRVKYNDDLD EYRLTPTELR KRFEEMGADV VLAFQTRNPT
     HAGHAYLMNN AREQLIAQGY KNPVLWLSPL GGWTKEDDVP LDVRVRQHEA ILRDGMLDKE
     STVLAIWPSP MIYAGPREVQ WHAKSRKNAG ASFFVVGRDP AGIKRSDGDK DDIYAGDHGR
     FVLHMAPGME DFNILSFSKV YYDVQDHKMK PMDSSRKQDF LSISGSRMRK MAREGLQKCE
     GDKIPAGWED KPTCVPQGFM VKSGWDIMID YYQNINSPRW IPFATQFSKP VVDTTRSFSS
     EGTFGRTDYK LHFKNDKGEK ISPWHDIPLH PADSKDNSSY NFIVEIPKGI AHKMEVNKED
     RYNPIMQDTT HNGTRGRDYL YGVPFFNYGL FPQTWEDPSV KDESGNGGDN DPLDVIEIGA
     KQLAMGSVNP VKILGSLELV DQGEVDHKIL VLSLADEDAD KINSVADLQS VKPGVLDALV
     DWLKKYKIPE GKSENVFSQE NPTSAEAAIQ IVQETHERWQ KLKAGEISVK DEFWLN
//
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