ID E6ZPT6_SPORE Unreviewed; 306 AA.
AC E6ZPT6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=GDT1 family protein {ECO:0000256|RuleBase:RU365102};
GN ORFNames=sr15312 {ECO:0000313|EMBL:CBQ69243.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ69243.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ69243.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU365102}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU365102}.
CC -!- SIMILARITY: Belongs to the GDT1 family. {ECO:0000256|ARBA:ARBA00009190,
CC ECO:0000256|RuleBase:RU365102}.
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DR EMBL; FQ311435; CBQ69243.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZPT6; -.
DR EnsemblFungi; CBQ69243; CBQ69243; sr15312.
DR VEuPathDB; FungiDB:sr15312; -.
DR eggNOG; KOG2881; Eukaryota.
DR HOGENOM; CLU_040186_0_0_1; -.
DR OrthoDB; 180756at2759; -.
DR Proteomes; UP000008867; Chromosome 14.
DR GO; GO:0005801; C:cis-Golgi network; IEA:EnsemblFungi.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0005797; C:Golgi medial cisterna; IEA:EnsemblFungi.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015369; F:calcium:proton antiporter activity; IEA:EnsemblFungi.
DR GO; GO:0010486; F:manganese:proton antiporter activity; IEA:EnsemblFungi.
DR GO; GO:0032468; P:Golgi calcium ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0030026; P:intracellular manganese ion homeostasis; IEA:EnsemblFungi.
DR InterPro; IPR001727; GDT1-like.
DR InterPro; IPR049555; GDT1-like_CS.
DR PANTHER; PTHR12608:SF1; TRANSMEMBRANE PROTEIN 165; 1.
DR PANTHER; PTHR12608; TRANSMEMBRANE PROTEIN HTP-1 RELATED; 1.
DR Pfam; PF01169; UPF0016; 2.
DR PROSITE; PS01214; UPF0016; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365102};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365102};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365102}.
FT TRANSMEM 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365102"
FT TRANSMEM 75..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365102"
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365102"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365102"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365102"
FT TRANSMEM 257..275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365102"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 31670 MW; 63E254D4C7B3C0E1 CRC64;
MEATANGSGS ALDLLMSTTG ESSAGLSSSA WGALGEAWKD DPRALWSSYA MIIVSEIGDK
TFLIAAILAM RQSKLVVFSG AFASLAVMSV LSALLGVMFP SLLPKSLTNL LAAGLFLVFG
LKMVKDGLGM SGDEIQEEWQ EAEREIDQED GTAHELQSLE SGLASPSPSP KDSGMAHTLR
DGTRNLCGLC FSPVFAQAFI LTFLGEWGDR SQIATIALAA AHNVALVCVG TIAGHACCTG
LAVLGGSWLA SRISVKHVTL GGACMFLVFA VVYAWEAYHE PAGELDVAQV VAAAKGAVGA
RAAAGV
//
