GenomeNet

Database: UniProt
Entry: A0A8H4C508_COLGL
LinkDB: A0A8H4C508_COLGL
Original site: A0A8H4C508_COLGL 
ID   A0A8H4C508_COLGL        Unreviewed;       764 AA.
AC   A0A8H4C508;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   02-APR-2025, entry version 13.
DE   SubName: Full=Meiotically up-regulated protein 72 {ECO:0000313|EMBL:KAF3797292.1};
GN   ORFNames=GCG54_00009263 {ECO:0000313|EMBL:KAF3797292.1};
OS   Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=474922 {ECO:0000313|EMBL:KAF3797292.1, ECO:0000313|Proteomes:UP000613401};
RN   [1] {ECO:0000313|EMBL:KAF3797292.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lc1 {ECO:0000313|EMBL:KAF3797292.1};
RX   PubMed=32202483;
RA   Fu F.F., Hao Z., Wang P., Lu Y., Xue L.J., Wei G., Tian Y., Baishi H.,
RA   Xu H., Shi J., Cheng T., Wang G., Yi Y., Chen J.;
RT   "Genome sequence and comparative analysis of Colletotrichum gloeosporioides
RT   isolated from Liriodendron leaves.";
RL   Phytopathology 110:1260-1269(2020).
RN   [2] {ECO:0000313|EMBL:KAF3797292.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Lc1 {ECO:0000313|EMBL:KAF3797292.1};
RA   Fu F.-F., Chen J.;
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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:KAF3797292.1}.
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DR   EMBL; WVTB01000117; KAF3797292.1; -; Genomic_DNA.
DR   RefSeq; XP_045256456.1; XM_045409211.1.
DR   GeneID; 69016396; -.
DR   OMA; IWVGATN; -.
DR   Proteomes; UP000613401; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR   FunFam; 3.40.50.720:FF:000424; Meiotically up-regulated gene 72 protein; 1.
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; IPR013752; KPA_reductase.
DR   InterPro; IPR051402; KPR-Related.
DR   InterPro; IPR013332; KPR_N.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR21708:SF25; PROTEIN PAM1-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000613401}.
FT   DOMAIN          14..168
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          202..325
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          330..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..381
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..409
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..493
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..512
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..641
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..738
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  83052 MW;  82C9A80FC12B9FD1 CRC64;
     MAEENNSSEL MSVCSVGGNP VSAFLSWRLQ ATNACDVTLV WKSGYDHVAQ YGISFKSPIF
     GNERFKPRHV VRVPEEAANT VGPFDYVILC IKALPDVYDL AAVIDAVVTP QHTCILVNTT
     HTLGVEAAIE ERFPTNVVLS LVSNAELSQL GQSEFEHKGS TEIWVGPSSK NDNIPPAIQE
     DMAQALAMTL TTGQVDCKVS QNIRQQQYER VIGPIAFHPA SVIFETANHT QLLEKIGVRD
     LVNDVIDELF ALATAHGCKF APDFKQKTID EMTKPTPTES IMWQDYIARR PMEVETYLGS
     PIKLAKEARI PVPRIETLYA VLHNLNIVNR QRPPKPVDGM GAPGSPTSQS PAPRMSTQNG
     ARPMNGNGMP PRGPRPRNSS NLGPPPPGMR RPPMNGGPPN GYPRGPPGPG SRAASRRGSL
     EGNELEEFSH LMLYDDIPEG GEPGYVPGPD GSDLTMRERE LELRQRELAM REREMRMRSR
     GPPPRRGPHP GPHPMRNSAQ AFDDEDDDDD YFDPMSGPPP PMIDPENFDM MSVTSRKNRK
     QAPPPPNRAQ YHKNEIYDSA APPVRTSRFR PNFGRNRSSQ IANMPPMNEN ILDDPLLSMT
     SNRYGAVDRG AMNAGSRANS LTASRLDEMQ MGGPMQMGMN GAFPRRASQS PGNPYSPSIR
     GGSGRPSPPN GYGGPSMNGR PSPPNGVRQP VPRYPPGHGN AVAPQQVEQH VGVSGLLPPK
     QKNVRSLTGS ASASAGSGES QPDTEPSAHS SQSSLGARPP IGVR
//
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