ID F2PGX1_TRIEC Unreviewed; 392 AA.
AC F2PGX1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=sn-1,2-diacylglycerol cholinephosphotransferase {ECO:0000313|EMBL:EGE01139.1};
GN ORFNames=TEQG_00191 {ECO:0000313|EMBL:EGE01139.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441}.
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DR EMBL; DS995718; EGE01139.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PGX1; -.
DR VEuPathDB; FungiDB:TEQG_00191; -.
DR eggNOG; KOG2877; Eukaryota.
DR HOGENOM; CLU_035066_5_0_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
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; IPR014472; CHOPT.
DR PANTHER; PTHR10414:SF37; BB IN A BOXCAR, ISOFORM C; 1.
DR PANTHER; PTHR10414; ETHANOLAMINEPHOSPHOTRANSFERASE; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF015665; CHOPT; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EGE01139.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 392 AA; 44049 MW; CFCF9708BD83225B CRC64;
MDVVRKLAGL EDSLTDETLA PLKSYKYSSV DKSYISRYIL KHYWNAFVEL LPLWIAPNMV
TLLGFGFIVG NVVLLEIYMP DLVGPAPSWV YYSFAIGIWM YSTMDNVDGK QARRTGTSSP
LGELFELIPC LPMFFSTWET YHTHTLYLGY FNGPTEGLII ATTIIIVAGY YGPEIYSRPL
ADGIGYADLI GNVTFLDIWV FVLLTSFFTA HLPECVYNVV QARRRNGLPV LPIFLEWTSI
IISTISAISW VYSPYSFILK DNHLVLFAVT LCFVFGRMTT KIILAHLTRQ PFPYWTVLIT
PLIGGAVLVN LPAIGLPAVG ATVELWYLWG YLAFAFAAYM HWALYVIGRI TAFLDINCLT
IKKRRASLNG SALGDITNSK MQAAFNKPVK LN
//
