ID F2SVH2_TRIRC Unreviewed; 464 AA.
AC F2SVH2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
GN ORFNames=TERG_06543 {ECO:0000313|EMBL:EGD90316.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD90316.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001698,
CC ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005119, ECO:0000256|PIRNR:PIRNR018269,
CC ECO:0000256|RuleBase:RU003938}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185,
CC ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}.
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; GG700655; EGD90316.2; -; Genomic_DNA.
DR AlphaFoldDB; F2SVH2; -.
DR STRING; 559305.F2SVH2; -.
DR VEuPathDB; FungiDB:TERG_06543; -.
DR InParanoid; F2SVH2; -.
DR OMA; FFAYMYF; -.
DR OrthoDB; 5481516at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR13773:SF8; PHOSPHATIDATE CYTIDYLYLTRANSFERASE, PHOTORECEPTOR-SPECIFIC; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
DR PIRSF; PIRSF018269; PC_trans_euk; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018269};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018269};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR018269};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR018269}.
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 230..251
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 272..290
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 52836 MW; 9B03F3EF3A95AD9D CRC64;
MGKSRRNLRA QESLATSPET TNYPSSEDSD ASDVQSPSRE DTSVIPQKME ATQTTSEKEQ
QPQPQQPLSD FEKKRQTFIT RTIWTFVMIA GFFVIIFAGH LYLIIVVTAI QIVSFKEVIA
IANVPSKARN LKFTKSLNWY FLVTTMYFLY GESVLYYFKH ILLVDRILLP FATHHRFISF
MLYLIGFVFF VATLQKGHYK FQFTQFAWTH MALYLIVVQA HFVLNNIFEG LIWFCIPVSL
VITNDIFAYI CGITFGRTQL IKLSPKKTVE GFVGAWVCTV IFGYGATILL KQYKYFTCPV
NDLGSNLLTG LECTPNPCFK AQPYTMPEWT HINKTFHIAP VQFHVFVLST FASLIAPFGG
FFASGLKRTF KIKDFGESIP GHGGITDRMD CQFIMGLFAY MYYHSFIAVH KASVGGVIEN
AITGLTVDEQ IELIKGLSKY LYNQGVVSES LVECLNGDYR RLRR
//
