ID G1X558_ARTOA Unreviewed; 311 AA.
AC G1X558;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=choline-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00026101};
DE EC=2.7.7.15 {ECO:0000256|ARBA:ARBA00026101};
GN ORFNames=AOL_s00054g2 {ECO:0000313|EMBL:EGX51698.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX51698.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX51698.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- SIMILARITY: Belongs to the cytidylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010101}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX51698.1}.
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DR EMBL; ADOT01000082; EGX51698.1; -; Genomic_DNA.
DR RefSeq; XP_011119620.1; XM_011121318.1.
DR AlphaFoldDB; G1X558; -.
DR STRING; 756982.G1X558; -.
DR GeneID; 22890715; -.
DR eggNOG; KOG2804; Eukaryota.
DR HOGENOM; CLU_034585_5_2_1; -.
DR InParanoid; G1X558; -.
DR OMA; DIYKPCK; -.
DR OrthoDB; 5474784at2759; -.
DR Proteomes; UP000008784; 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; CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR10739:SF13; GH25855P-RELATED; 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:UP000008784}.
FT DOMAIN 34..152
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT REGION 273..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 35539 MW; 516F3F6AA805AE62 CRC64;
MLMVFSTFSI LGEYLYTRIS PLALLILVYM TRHHHRHMRQ LEQAKKAFPN TYLLVGIPND
IETHKRKGLT VLTDKERAET LRHCKWVDEV IEDAPWIVTP SFLEKHAIDY VAHDDEPYAG
ADTDDIYKPC KEAGKFLVTQ RTEGISTTYI ITKIVRDYDK YITRQLRRGT PRQDLNVSWL
KKNELDIKRH AVELRDSIKT NWTTTGRELR GEIGKFWSPQ PQTLPALSIP DNATSSSIDQ
IDIGRSASPH TDFATGYSLG LIGGVRSWMQ VRSSSNRGSK ATSAENSDQS DEEDLTRKSI
SPTREQMDQT I
//