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Database: UniProt
Entry: F2Q3Z0_TRIEC
LinkDB: F2Q3Z0_TRIEC
Original site: F2Q3Z0_TRIEC 
ID   F2Q3Z0_TRIEC            Unreviewed;       545 AA.
AC   F2Q3Z0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=ethanolamine-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00024221};
DE            EC=2.7.7.14 {ECO:0000256|ARBA:ARBA00024221};
DE   AltName: Full=CTP:phosphoethanolamine cytidylyltransferase {ECO:0000256|ARBA:ARBA00031473};
GN   ORFNames=TEQG_07859 {ECO:0000313|EMBL:EGE08858.1};
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   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from ethanolamine: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00024191}.
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00010101}.
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DR   EMBL; DS995788; EGE08858.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2Q3Z0; -.
DR   VEuPathDB; FungiDB:TEQG_07859; -.
DR   eggNOG; KOG2803; Eukaryota.
DR   HOGENOM; CLU_031246_0_0_1; -.
DR   UniPathway; UPA00558; UER00742.
DR   Proteomes; UP000009169; Unassembled WGS sequence.
DR   GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02174; CCT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR041723; CCT.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR044608; Ect1/PCYT2.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   PANTHER; PTHR45780; ETHANOLAMINE-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR45780:SF2; ETHANOLAMINE-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 2.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          126..249
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          27..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  60975 MW;  4B853EE0C4F7930F CRC64;
     MTYRPDKGRC LVIHRVEVGK VELAPKRARR RNETRQAQER TEEIRWRAPP GGSTELGHGV
     VDGWITRDHL LFSATAVCWC AVCAVVQLCS CSVEMAAFER GALPRQGQWP ADPQEDVEIS
     KDRIWVDGCF DFSHHGHAGA MLQARRLGKE LLVGVHSDEE ISDNKGPTVM TLAERIAAVD
     ACRWSTKSIP YAPYVTSLDW ISHYGCQYVV HGDDITSDSD GNDCYRFVKE AGRFLVVKRT
     PGISTTDLVG RMLLCTKTHF IKSLLAYITG KEGSGTPEEM EEAGKSHFQR IRDYATDETG
     LRPGPEVWHW NGPSTLSSTP ATGGAHEQLQ QLVEGVKPKP GQKIVYVDGG FDLFSSGHIE
     FLRCVHSAEE KEGEARGWFH PDQVAQRVKE HGEDYGPAYI VAGVHDDEVI NRWKGLNYPI
     MNIFERGLCV LQCRYINTVV FAAPFTPTEA YLSALPFGMA DVVYHGPTTF IPLTFDPYEE
     PRKLGIFKEI GNHQFQNVNA GEIVQRIMTA RAAFEERQRI KMLKSINEAE VKKQEEVAKL
     SGQGN
//
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