ID   A0A139IC85_9PEZI        Unreviewed;       464 AA.
AC   A0A139IC85;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC579_3434 {ECO:0000313|EMBL:KXT12205.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12205.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT12205.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12205.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC       family. {ECO:0000256|ARBA:ARBA00008903}.
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:KXT12205.1}.
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DR   EMBL; LFZO01000160; KXT12205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IC85; -.
DR   STRING; 113226.A0A139IC85; -.
DR   Proteomes; UP000073492; Unassembled WGS sequence.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR   PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT   REGION          83..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  51094 MW;  FB0801A6A3955CBF CRC64;
     MPLQILTNDD VSKILHSFTK EDILELQQSL ADALHWYSTS SDGNDCCSDY QPERTVLKRK
     DGTTSIYMPA SGMTGQGVKV LNVTPPDANG LPALQETYSD GDSRSSISSA SRQSIDSRRS
     GSSSLPTTLS EVTDGTGSLS LTSANDGSPS AIRGSLTLLD NMGNTTGLLN AGEITAFRTA
     LASTMLLKKR HSVNDVTVFG AGRQAYWHMR LALLLRGDEI RHLNIVTRSF ESARKCIMRL
     YNPQPDDPDY VNHVGEKYNS KTKKNILTPS HTEYERLIKE YVRASNVIFC CTPSTTPLFP
     ATHLTNPEGR KKGRYISCIG SYKPHMIELH PDVLRYAVAP HHEHKHIHKR QTEGGAILVD
     TVSGCLKEAG EVIQAKLMPD QVVELGELFM LKRDADRKAR ERGEKVDVGK DGCALQDNSG
     LKDWLTRGNV IYKSVGLGLM DIVVGNELLR CARERGVGMT VDNF
//