ID G0UY93_TRYCI Unreviewed; 416 AA.
AC G0UY93;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ethanolamine phosphotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TCIL3000_10_11390 {ECO:0000313|EMBL:CCC94360.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC94360.1};
RN [1] {ECO:0000313|EMBL:CCC94360.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC94360.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR EMBL; HE575323; CCC94360.1; -; Genomic_DNA.
DR AlphaFoldDB; G0UY93; -.
DR VEuPathDB; TriTrypDB:TcIL3000_10_11390; -.
DR OrthoDB; 198583at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR014472; CHOPT.
DR PANTHER; PTHR10414; ETHANOLAMINEPHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR10414:SF68; ETHANOLAMINEPHOSPHOTRANSFERASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 189..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 416 AA; 46006 MW; 8DDA105FACEEDCC2 CRC64;
MVGKVDMTDI LVSFRCKERV SAVPPQASYL FEYILCPIYE RVASMYPSTW SPNKVTLTGI
FATTISSLLM LTSMPVNTAF EPPHVTVVPA SYYLNSSFKR KAASGPSPLH PSMLQPPFSR
VFTPTSLLLL CGFLNLVYCI ADNTDGCLAR RLRKASNVGE YMDHGLDCVT SLMSTCVSMS
VIGFSFPNIA VTVALVAMLT ILSHTLNYER NIFVWGNRFV SVDEAMLFFF LVNWVSLLFP
GLGTATLSPP ILDMFLPQPL AQLLYPLRYI DAALIGCWIS QCFVLISISA KNWCMLFRMQ
TLASFLSLVF LFAIVPYHTL HMEKEGLAAY TLGPLSYVSV WIITLACTLS SIVHIPIYAR
CAGQLQTELL PLAGVIFIFL TFSSFPAVAM VLAVVWHIGQ ICCNVSRLKA LGVKTE
//
