ID G0W837_NAUDC Unreviewed; 452 AA.
AC G0W837;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=choline-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00026101};
DE EC=2.7.7.15 {ECO:0000256|ARBA:ARBA00026101};
GN Name=NDAI0C02880 {ECO:0000313|EMBL:CCD23948.1};
GN OrderedLocusNames=NDAI_0C02880 {ECO:0000313|EMBL:CCD23948.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD23948.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD23948.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010101}.
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DR EMBL; HE580269; CCD23948.1; -; Genomic_DNA.
DR RefSeq; XP_003669191.1; XM_003669143.1.
DR AlphaFoldDB; G0W837; -.
DR STRING; 1071378.G0W837; -.
DR GeneID; 11496284; -.
DR KEGG; ndi:NDAI_0C02880; -.
DR eggNOG; KOG2804; Eukaryota.
DR HOGENOM; CLU_034585_0_2_1; -.
DR OMA; CGIPSDE; -.
DR OrthoDB; 5474784at2759; -.
DR Proteomes; UP000000689; Chromosome 3.
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:UP000000689}.
FT DOMAIN 149..276
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT REGION 25..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..442
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 52391 MW; 0DB64C8BE89BF303 CRC64;
MAKESRTSSL KKSTLLQLHL TKLFQKTRKR KHESDTDDQE QLSTPELRSH DNEHAHNHSH
NNHNHNGQDR SDSGNVDDSS DDHSSTVSTT PNRKRRRLSN TTTEKDQDLI MFEKRENELD
AKLPEELRKY RPKGFPFNLP PKDRPIRIYA DGVFDLFHLG HMKQLEQCKK ALPNVTLICG
IPSDEVTHKL KGLTVLTDKQ RCETLKHCRW VDEVIEDAPW CVTPEFLEKH NIDYVAHDDI
PYASAGSDDV YKPIKQAGKF LVTQRTNGIS TSDIITKIIR DYDKYLMRNF ARGATRQELN
VSWLKKNELE FKKHIKDFRS YFKKNQENLN NSSRDLYFEV REILLRKTLG NKLYMKLVGN
SENLDDIVNG SVKGIAAKSR KLLRARSPAS EFASEYTGPN LEEENHDNPF DPADAVEGTE
DEGDEDDDEE EEEEEEYYDS NEDEPEDKKL KK
//
