GenomeNet

Database: UniProt
Entry: A0A5B0LTQ3_PUCGR
LinkDB: A0A5B0LTQ3_PUCGR
Original site: A0A5B0LTQ3_PUCGR 
ID   A0A5B0LTQ3_PUCGR        Unreviewed;       499 AA.
AC   A0A5B0LTQ3;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   05-FEB-2025, entry version 16.
DE   SubName: Full=Squalene epoxidase {ECO:0000313|EMBL:KAA1067439.1};
GN   Name=ERG1_4 {ECO:0000313|EMBL:KAA1067439.1};
GN   Synonyms=ERG1_1 {ECO:0000313|EMBL:KAA1137778.1};
GN   ORFNames=PGT21_005560 {ECO:0000313|EMBL:KAA1067439.1}, PGTUg99_016480
GN   {ECO:0000313|EMBL:KAA1137778.1};
OS   Puccinia graminis f. sp. tritici.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=56615 {ECO:0000313|EMBL:KAA1067439.1, ECO:0000313|Proteomes:UP000324748};
RN   [1] {ECO:0000313|Proteomes:UP000324748, ECO:0000313|Proteomes:UP000325313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21-0 {ECO:0000313|EMBL:KAA1067439.1}, and Ug99
RC   {ECO:0000313|EMBL:KAA1137778.1, ECO:0000313|Proteomes:UP000325313};
RA   Li F., Upadhyaya N.M., Sperschneider J., Matny O., Nguyen-Phuc H., Mago R.,
RA   Raley C., Miller M.E., Silverstein K.A.T., Henningsen E., Hirsch C.D.,
RA   Visser B., Pretorius Z.A., Steffenson B.J., Schwessinger B., Dodds P.N.,
RA   Figueroa M.;
RT   "Emergence of the Ug99 lineage of the wheat stem rust pathogen through
RT   somatic hybridization.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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:KAA1067439.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; VSWC01000184; KAA1067439.1; -; Genomic_DNA.
DR   EMBL; VDEP01000005; KAA1137778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5B0LTQ3; -.
DR   OrthoDB; 73846at2759; -.
DR   Proteomes; UP000324748; Unassembled WGS sequence.
DR   Proteomes; UP000325313; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR050838; Ketopantoate_reductase.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 2.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324748}.
FT   DOMAIN          3..169
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          252..345
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   DOMAIN          391..427
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          181..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  55661 MW;  87D6E2DA745B7CA2 CRC64;
     MRIHCIGPGS IGSLICFHLQ SITPITLLLR SRQAQHRRSI PTLSIQLEQQ DRTRTATGFT
     YEFLNKQQQQ PIESLIVTTK APHVLESLQR VRHRLSANST VLLLHNGLGV VEELIETCFQ
     EPSSRPTFVL ATTSHGVYRI DKGLPGTQAG SHGRFCHAGL GDIRLGVLPN TTIRNCLERL
     RGHSNQPSSN DDGQNLQDDN PLLNPHSRTK PVLEEHLPDI EPETRSLHYT LSSLLNPLMI
     KELNTKWLPM GDFQTSALIK LTVNAAINPI SALLETRNEA LYRESSFESL CRQVCQEASA
     VFAAQAGQPF RPHHSLSAPN LQRVVNDIVL ATRANISSMC SDIRTLATNR ISPHKTLSKA
     NLNRIAASQA PIKIPNYQSL ISGQEEKSVK ETSTEIDYIN GYICRLGSQF NVDTPLNQSL
     SDLVKLKSFA IKRAQVLPKL QRVNRRLKIN RPEDNPATPD QLDLFEKPEN HPGSHQLDLF
     EKPENNHLAD NQASVVDKS
//
DBGET integrated database retrieval system