ID   A0A0G2EDA8_9EURO        Unreviewed;       894 AA.
AC   A0A0G2EDA8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 26.
DE   RecName: Full=Copper transport protein 86 {ECO:0000256|ARBA:ARBA00022406};
GN   ORFNames=UCRPC4_g04176 {ECO:0000313|EMBL:KKY20474.1};
OS   Phaeomoniella chlamydospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX   NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY20474.1, ECO:0000313|Proteomes:UP000053317};
RN   [1] {ECO:0000313|EMBL:KKY20474.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY20474.1};
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.
RN   [2] {ECO:0000313|EMBL:KKY20474.1, ECO:0000313|Proteomes:UP000053317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY20474.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential protein which may be involved in threonine
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00002048}.
CC   -!- SIMILARITY: Belongs to the CTR86 family.
CC       {ECO:0000256|ARBA:ARBA00007516}.
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:KKY20474.1}.
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DR   EMBL; LCWF01000096; KKY20474.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2EDA8; -.
DR   OrthoDB; 1438872at2759; -.
DR   Proteomes; UP000053317; Unassembled WGS sequence.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR019156; Ataxin-10_domain.
DR   PANTHER; PTHR13255; ATAXIN-10; 1.
DR   PANTHER; PTHR13255:SF0; ATAXIN-10; 1.
DR   Pfam; PF09759; Atx10homo_assoc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          790..887
FT                   /note="Ataxin-10"
FT                   /evidence="ECO:0000259|Pfam:PF09759"
FT   REGION          363..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..473
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  99805 MW;  28B1BFF65EC3917A CRC64;
     MEERPKVTAP ELLLKIVLTG TQMHYEHPGM VEEGPLERML NNGKVILYKS HQESEVRQNL
     GFSAAIWQGL TDVLIFAIPD LEKKSFSWKN SPESNFNGSC SDLIASNYHG IIKDIERLND
     LCTIARNLLA TTRKAQNLAA EKGFDQQILR LIHVCVKVTS AGFDGDNTAR NEEKWQKVVT
     LYKRLLITCL QFLHNFIMHN EHRKLVLWLD LFGNSQHHQN ESPRPSTPSS VEQIAQVGLA
     QGGQEARIKS TVDNLPLTGI PTSEDGLGYN IDDIHALFDL MSTDKPPDGT TQEAARLLMD
     KIRNDMERLS GLSASQLDEN PDALLKVGAA LRAQLPAKDF PRGAKPLTAQ QVRKAIVSID
     KKAQTAQSKD TNWSDLPNLN QYGNSSVRNT ELTEEDMSMP RSSQSAAETL QEAKDELMAR
     LQDVAPHLTE AETQQELERN STQASVQLED SGEAPTESVH EIEEDDEDDE DYRSSSDQER
     GLLTDVPLVL GPTEIEALPM IIQAGIVDSF GLKGGERIGS KNMQAVRCHI LLAQEAGRNV
     LRELLIFIAA WDLPDDEFYF KMMVQIMEAI LSNGLMSHAY SDFGQAKDII SPAQAVVIKI
     LTHIFRSKYS PTSINGDSQQ NITPRLPAQL TRVDVLTVRY VFTVFRGNII PETCALIYLQ
     GQIRTGRALA EDFPLNLWDM ERVYEGVYQF LEFFAVLTES NDWKSLLVDW EIVYDLVTLL
     KELDWSIPKP ALTSQIPAPG KGQNSTIGKQ TQPAVSVERP YDQDPDTGAD AGSPSLGTED
     PAEFEWRNLK KLIVLVLSSL VWKSPVVQNQ IREYGGVETI LSCTVFDAHN PYIKEHAVMC
     LKFLLEGNRE NQEIVDQLEA REVVSTAEEV LEEMGVEARI EGGKVKLAAR PKPA
//