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Database: UniProt
Entry: A0A0G2DZ76_9PEZI
LinkDB: A0A0G2DZ76_9PEZI
Original site: A0A0G2DZ76_9PEZI 
ID   A0A0G2DZ76_9PEZI        Unreviewed;       438 AA.
AC   A0A0G2DZ76;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:KKY15844.1};
GN   ORFNames=UCDDS831_g07447 {ECO:0000313|EMBL:KKY15844.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY15844.1, ECO:0000313|Proteomes:UP000034182};
RN   [1] {ECO:0000313|EMBL:KKY15844.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY15844.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY15844.1, ECO:0000313|Proteomes:UP000034182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS831 {ECO:0000313|EMBL:KKY15844.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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:KKY15844.1}.
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DR   EMBL; LAQI01000179; KKY15844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2DZ76; -.
DR   Proteomes; UP000034182; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KKY15844.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KKY15844.1}.
SQ   SEQUENCE   438 AA;  46600 MW;  BA288527CFEF05A0 CRC64;
     MLPVSRSAHE GAETANASGI LHRSLKHLPL KVVGASGNYL TLSNGQKILD ATGGAAVSCL
     GHGDKRVQDA ITRQMSEVAY CHSLFFSTSA AEDLGQELVA GTNGAMTKAF IVSSGSEAIE
     AAMKLARQYH LELSPSQPQR TKFIARKESY HGTTLGSLSL GGHVSRRALF EPMLLENISR
     VSACNTYRGK TDGESEQEYV ARLAKELDDE FHRVGPETVC AFVAEPVVGA ALGCVPSVAG
     YFEAVKAVCD KYGALLIMDE IMSGMGRTGT LHAWQQEGVV PDIQTIGKGL GGGYAPVAGV
     LINHRVVDVL QKGTGSFSHG QTYQGHPVAC AAAAQVQRII RDDSLCENVK KMGVYLEKLL
     KQRLADHPNV GDIRGRMEPK YSISIYPGTG TADGKSGDHV LLAPAYNVTE ADVEKIVDLT
     TGVITEFFAE LQGKAVLG
//
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