ID N1QKM1_SPHMS Unreviewed; 1210 AA.
AC N1QKM1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Copper transport protein 86 {ECO:0000256|ARBA:ARBA00022406};
GN ORFNames=SEPMUDRAFT_146748 {ECO:0000313|EMBL:EMF17806.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF17806.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF17806.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF17806.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR EMBL; KB456260; EMF17806.1; -; Genomic_DNA.
DR RefSeq; XP_016765927.1; XM_016903837.1.
DR AlphaFoldDB; N1QKM1; -.
DR STRING; 692275.N1QKM1; -.
DR GeneID; 27900974; -.
DR eggNOG; KOG2676; Eukaryota.
DR HOGENOM; CLU_005559_2_0_1; -.
DR OMA; FIMHNEH; -.
DR OrthoDB; 1438872at2759; -.
DR Proteomes; UP000016931; 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:UP000016931};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 999..1072
FT /note="Ataxin-10"
FT /evidence="ECO:0000259|Pfam:PF09759"
FT REGION 226..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..584
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 134419 MW; 926F9609B75F782C CRC64;
MGQRDATSIM KAHSVFLRLV LPPYTIHFKS AGYMKDVTLE MLDKKVCKEI LRRSAKDPAV
REAIGLDAKF WEDFCTLLKA AIPSLERRSF TIWDPSSVDY ESTSGALIAS HHPGLWKDLE
RLNDLVSISR NVLTVGDRAQ DLAASFSIDA EVFRLVNCCV RVTARGYDGD ADTGDEEKWQ
WIVNGYKKLL ITSLQFLNNL VAQNERRKLM LWVSLFDNTT ESVLAPEDVP ETSSASLTDV
PSNPTSKPPH PLSSEDFLIA YGTNGVEEVS TEGAEPLWDN TPFSDYPLPK EALEGREKLE
RKERFDGNGY ALFVKRLKDI QIEDYQLERK RGPNYGEAHL EFPRRWAELN DDDHEYWQGL
FDDAMAKYRQ DLAVYEAKMI AVTETQPVLR SDVPVAEQTR QVERKIAMLE EQLAEKYKSE
NADIAPLEPP IYGQDGHLTF DNESLQSRPV VADDMRMLFT AEAGTKILES GKSELMKRLE
GYDAGPNPDL ISPMSPQSGP IDPVSSTDLA TNPLRQATDA QLDLQRASRS PSAVGSHVAE
EHSRDNGPAE DAFDGSVDEE CDENGEEEES QEEAEEEEEE DYPGSTEDGR GLLTDVPLIL
GPSEIEVLPM LIMSGIVPPT SLPPALSNDE RNALMNMHTV RTHLLLSQSN GRNLLRELLI
FVAAWDLREE ELYFKFMVKI MEAILKNGLM PYAYHAFRDR SRSKDIISPA QAVIMKLLTC
IFRARGDAAK HAVATNAQNK TNQATGHTLT HAVVPSHARN NGSAPPNMPS RVDLHILNFI
FTEFRQHIIP QTCALIFLQG QIHAGRASPE DFPLNLWDME RMYEGVYQYL EFFAVLTEEG
VWKGILGEWE MASELVTLLR ELEGGIPKMG SVVPQVPRRV SSHPPQRAMS VDAGTMHHSS
RMASQSAQGH YAPPGSPAPA PTLAHPPTQA PVAVERPFDV ASQDTTLPPL PLHPPINGAG
PAFEPETPMA YPEDNLPSMA QELQHDQDEP SDFEWRNLKK LTVLVLSSLI WKNRTVQDQV
RRYGGLEALV GCCRADEHNP YIREHAIMCL RFAVEGCEEN SRVIKQMAAS QAPKPVEGGQ
VTLPNKTEAP SEIPSEIPSE ILDTSGYESF MDNKGQVGLR RKEATSHPAA HGPPAASSSN
SGMSSAGVQK PRLSNTKLTA ERAAELMSSA LSSLPLGDRM VTDKQKAEAL AKLDRAFEST
ERVLGRGRRS
//
