ID G4YTK3_PHYSP Unreviewed; 471 AA.
AC G4YTK3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Aspartyl/asparaginy/proline hydroxylase domain-containing protein {ECO:0000259|Pfam:PF05118};
GN ORFNames=PHYSODRAFT_296378 {ECO:0000313|EMBL:EGZ24231.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ24231.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ24231.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ24231.1,
RC ECO:0000313|Proteomes:UP000002640};
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).
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000256|ARBA:ARBA00007730}.
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DR EMBL; JH159152; EGZ24231.1; -; Genomic_DNA.
DR RefSeq; XP_009519519.1; XM_009521224.1.
DR AlphaFoldDB; G4YTK3; -.
DR EnsemblProtists; EGZ24231; EGZ24231; PHYSODRAFT_296378.
DR GeneID; 20641366; -.
DR KEGG; psoj:PHYSODRAFT_296378; -.
DR InParanoid; G4YTK3; -.
DR OMA; FEQINIP; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10605:SF56; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE; 1.
DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT DOMAIN 106..205
FT /note="Aspartyl/asparaginy/proline hydroxylase"
FT /evidence="ECO:0000259|Pfam:PF05118"
FT ACT_SITE 250
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 352
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 360
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
SQ SEQUENCE 471 AA; 54985 MW; 3B5E7B9A66256C84 CRC64;
MTAIPQVPLE HKKVPMQELP EEVAKDFAMV VPVQENIDIS LLQKRILAGG RELWDPANQK
DNVPVRRAGH DTWGIGKVVF VFCDDYLKNV FTFPWYHSWQ KELAPIFEQI NIPVNRIVRC
ILASMPPGAD IPVHHDTGSW VHFTHRMHIP VFTSPDIDFM VGPNDQNMQR YEFKQGNLYE
LNNISRHRVK NNWDQHRVHM IFDYVDEGFP LNRMDLKQGT TVWQTRRSVD LSTDYGKRVP
PSFVVIGAQK AGTTSLYDYI LQHDLVWPAK RKETHYFDWR WNKELPDAST PEGAKQHLRY
FEDTYLERKI LYRFPSLMSG EATPSYMLGG ETVINRMKQV IPHCRKIMAI MRNPVERAYS
HYSMTADTEG SEKQLRNRGH HHLKGRSFEQ IVDDEIEELS KLGVHPDMDF EEFDEKVMRK
QLEFDHGAHS FVARGLYALQ LAGWIEAYGK ENVLLLTLDE FKSTEKLHVR S
//