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Database: UniProt
Entry: A5E3T1_LODEL
LinkDB: A5E3T1_LODEL
Original site: A5E3T1_LODEL 
ID   A5E3T1_LODEL            Unreviewed;       514 AA.
AC   A5E3T1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=choline-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00026101};
DE            EC=2.7.7.15 {ECO:0000256|ARBA:ARBA00026101};
GN   ORFNames=LELG_04269 {ECO:0000313|EMBL:EDK46089.1};
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK46089.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK46089.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL YB-4239 {ECO:0000313|EMBL:EDK46089.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Kodira C., Zeng Q., Yandava C., Alvarado L., O'leary S., Kurtzman C.,
RA   Reedy J., Heitman J.;
RT   "The genome sequence of Lodderomyces elongisporus.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDK46089.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL YB-4239 {ECO:0000313|EMBL:EDK46089.1};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00010101}.
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DR   EMBL; CH981529; EDK46089.1; -; Genomic_DNA.
DR   RefSeq; XP_001524298.1; XM_001524248.1.
DR   AlphaFoldDB; A5E3T1; -.
DR   STRING; 379508.A5E3T1; -.
DR   GeneID; 5231605; -.
DR   KEGG; lel:LELG_04269; -.
DR   VEuPathDB; FungiDB:LELG_04269; -.
DR   eggNOG; KOG2804; Eukaryota.
DR   HOGENOM; CLU_034585_0_1_1; -.
DR   InParanoid; A5E3T1; -.
DR   OMA; KWIHGED; -.
DR   OrthoDB; 5474784at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IEA:InterPro.
DR   CDD; cd02174; CCT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR041723; CCT.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR045049; Pcy1-like.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   PANTHER; PTHR10739:SF13; CHOLINE-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR10739; CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT   DOMAIN          154..281
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..90
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  59357 MW;  8085E5C551F26684 CRC64;
     MARLPRRKAI ENELNGHGAP LTRTLSIESI SSLFKRNRKR KLEDDSSVKS SSPTTDNEDA
     ELSKYEDEVE ENDDDDDDDD NEEEEEDKDK DGNDQEGRGG NRRAKKRRIK TKEEEEFEEK
     ERKLDEELPE EYRKFRPRGF RFNIPPKDKP IRIYADGVFD LFHLGHMKQL EQAKKSFENV
     ELVCGIPSDK ETHKRKGLTV LTDEQRCETL KHCKWVDEVI PNAPWCVTPE FLREHNIDYV
     AHDDLPYASS DSDDIYKPIK EQGMFLTTQR TEGISTSDII TKIIRDYDKY LMRNFARGAT
     RKELNVSWLK KNELEFKKHI NDFRTYWMRN KLNINNVSRD LYFEIREFMR GKKFDVQQYL
     ENQQKQQQKH KNQQLITNGS QGPSRSGSIS DFEDSTSYKG GSPLTDFASK YIGNANKELN
     NAGKVILKWI HGEDDSDEEE IKPIVIKPVH KARRRSSSSS SSIKPRLINN SATTNANTNA
     TTTTTKGTLS GAAVKSTPKK GSSTPRKTPQ KKAY
//
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