GenomeNet

Database: UniProt
Entry: A0A3M6V6W4_9STRA
LinkDB: A0A3M6V6W4_9STRA
Original site: A0A3M6V6W4_9STRA 
ID   A0A3M6V6W4_9STRA        Unreviewed;       524 AA.
AC   A0A3M6V6W4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   22-FEB-2023, entry version 13.
DE   RecName: Full=Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding domain-containing protein {ECO:0000259|SMART:SM00846};
GN   ORFNames=DD238_006197 {ECO:0000313|EMBL:RMX62024.1};
OS   Peronospora effusa.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Peronospora.
OX   NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX62024.1, ECO:0000313|Proteomes:UP000282087};
RN   [1] {ECO:0000313|EMBL:RMX62024.1, ECO:0000313|Proteomes:UP000282087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R14 {ECO:0000313|EMBL:RMX62024.1,
RC   ECO:0000313|Proteomes:UP000282087};
RA   Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA   Reyes Chin-Wo S., Mou B., Michelmore R.;
RT   "Comparative genomics of downy mildews reveals potential adaptations to
RT   biotrophy.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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:RMX62024.1}.
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; QLLG01000818; RMX62024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6V6W4; -.
DR   STRING; 542832.A0A3M6V6W4; -.
DR   VEuPathDB; FungiDB:DD237_002324; -.
DR   Proteomes; UP000282087; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43454; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43454:SF1; GP_DH_N DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282087}.
FT   DOMAIN          153..314
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   524 AA;  57414 MW;  E248AEEF16CC7FB2 CRC64;
     MSEPSLSSTQ INTLRDSELE QWKTQENAAD LMVPLIGRLY RENNVVSVIF GKGLVHKNSI
     DLIKLHNFVC KYVGQHMHPT ETLVVLLALV HYAPNARGMR IDLGRTFVLM EKEVRDVQAQ
     LTSDARDAKV RELGELLNDK MASFASAPAF TPSDVILYGF GRIGRLLARL LIEKSGPGVK
     LMLRAIVVRK GTKEDLMKRA SLLRRDSVHG PFHGSITFNE EANAIIANGN LIQIIYSDGP
     DKCDYTKYGI NNAVVIDNTG RWRDADALGL HLKSPGVSKV ILTAPAKGNV PTIVAGVNEH
     MITSTDNIFS AASCTTNAIA PPLFALDKKF GIVGGHIETV HSFTNDQNLI DNYHMKERRG
     RSAVLNMVIT ETGAAAAVVK CLPSLKDKLT ANAIRVPTPN VSLAILNVQL DPAKAEGITK
     EAINSFMHRV SLDSPLQNQI DFVNSAEVAS SDFIGSRAAG TVDGKATIVD GTKVILYVWY
     DNEFGYSCQV VRTLQHLMGI NHAHFPVKEQ VAEIDRSLNL TWDT
//
DBGET integrated database retrieval system