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Database: UniProt
Entry: A0A166UDL7_9PEZI
LinkDB: A0A166UDL7_9PEZI
Original site: A0A166UDL7_9PEZI 
ID   A0A166UDL7_9PEZI        Unreviewed;       468 AA.
AC   A0A166UDL7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=UbiD family decarboxylase {ECO:0000313|EMBL:KZL73278.1};
GN   ORFNames=CT0861_10168 {ECO:0000313|EMBL:KZL73278.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL73278.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL73278.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL73278.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-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:KZL73278.1}.
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DR   EMBL; LFIV01000046; KZL73278.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166UDL7; -.
DR   STRING; 708197.A0A166UDL7; -.
DR   OrthoDB; 470839at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   InterPro; IPR023401; ODC_N.
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:UP000076552}.
FT   REGION          375..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  51170 MW;  FBC63E3BCB66236A CRC64;
     MVLTVLTDDQ IKAILADLTA DEFEGFRKTI STALHEYSTN THNIEDGTYH QPGRISTENL
     RTGATTLYMP SVGPQGMGCK VVTLSSGKAT QDPSKPSIQP TGAVTLLSPE GQPVGFLHAK
     TLTAFRTALT STCLLARRGQ VKTVTVFGVG LQAYWHVRLA LLIRGSTIKH VNVINRRFSD
     HARVFLRQFY EVPQHIKERE GWAEATFSIL TPGYGEFKRL QREQIRDADV VYCCTPSTED
     LFEAEVLTNH EGRRKGRLVA AIGSYTPKMR ELPEGLLLQA TKHEKPHWHF HKHAPEGGVI
     VVDTLDGALK EAGEVIAAGL QPTQLVELGE LIMLRRIHEE EEAAEAEADG ETASIAPSEL
     DKLDFSGTPS IKSAFTGSDA ASASDSRSSI SKDSTTGSHS SRGPSMLRRS SSQRSSDKHK
     KEDALVKWLR DGTVIYKSVG LGLMDLAVGM HMVQLAREKG VGTQVEGF
//
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