ID A0A1D3D1B6_9EIME Unreviewed; 415 AA.
AC A0A1D3D1B6;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Putative transmembrane protein {ECO:0000313|EMBL:OEH77230.1};
GN ORFNames=cyc_05276 {ECO:0000313|EMBL:OEH77230.1};
OS Cyclospora cayetanensis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Cyclospora.
OX NCBI_TaxID=88456 {ECO:0000313|EMBL:OEH77230.1, ECO:0000313|Proteomes:UP000095192};
RN [1] {ECO:0000313|EMBL:OEH77230.1, ECO:0000313|Proteomes:UP000095192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHN_HEN01 {ECO:0000313|EMBL:OEH77230.1,
RC ECO:0000313|Proteomes:UP000095192};
RX PubMed=27129308; DOI=10.1186/s12864-016-2632-3;
RA Liu S., Wang L., Zheng H., Xu Z., Roellig D.M., Li N., Frace M.A., Tang K.,
RA Arrowood M.J., Moss D.M., Zhang L., Feng Y., Xiao L.;
RT "Comparative genomics reveals Cyclospora cayetanensis possesses coccidia-
RT like metabolism and invasion components but unique surface antigens.";
RL BMC Genomics 17:316-316(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GDT1 family.
CC {ECO:0000256|ARBA:ARBA00009190}.
CC -!- SIMILARITY: Belongs to the GILT family.
CC {ECO:0000256|ARBA:ARBA00005679}.
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:OEH77230.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JROU02001166; OEH77230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3D1B6; -.
DR VEuPathDB; ToxoDB:cyc_05276; -.
DR VEuPathDB; ToxoDB:LOC113146703; -.
DR VEuPathDB; ToxoDB:LOC34621657; -.
DR InParanoid; A0A1D3D1B6; -.
DR Proteomes; UP000095192; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR InterPro; IPR001727; GDT1-like.
DR InterPro; IPR004911; Interferon-induced_GILT.
DR PANTHER; PTHR12608:SF1; TRANSMEMBRANE PROTEIN 165; 1.
DR PANTHER; PTHR12608; TRANSMEMBRANE PROTEIN HTP-1 RELATED; 1.
DR Pfam; PF03227; GILT; 1.
DR Pfam; PF01169; UPF0016; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000095192};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 415 AA; 45666 MW; DF8A27FC28B16BEC CRC64;
MRCTKSESSD KTGPHVGTRW HVFAGGFLAL AVMTLLAAAG GRVIPLFLKQ ELRTVFMAAL
LVLFGLKMLY DAMIYEENNE EPEELKEVSR PEHGAALVGP SRLLRAARYF FSPIFIQAAS
LTLMAEWGDR SQLATFALAA DRSASAVCLG AILGHGLCTG LAVLGGNVLA KRISERLVLL
IGGICFLSFA LFTVVDELFS SGGGMAVLNP AFLICFFTSV LVNGHDHQSI RRKFKIMKEN
ELRLLGEPQV KVEILWVGNA AESDGVVECQ HGAEECQLNT LSACGLKKLQ GEPESRLSFI
EWKSVGRFSR RFEYDYVPWV IVNGRHMPSS EANLTIALCE EYATHTTPVL QVVAIPLVPS
SAHYLMEYTT LLLILRLGSN RPHICSTLSK VGAASFLDEG QRCYREQQRD HGENE
//