ID A1CY25_NEOFI Unreviewed; 449 AA.
AC A1CY25;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 80.
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=NFIA_110210 {ECO:0000313|EMBL:EAW25527.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW25527.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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; DS027685; EAW25527.1; -; Genomic_DNA.
DR RefSeq; XP_001267424.1; XM_001267423.1.
DR AlphaFoldDB; A1CY25; -.
DR STRING; 331117.A1CY25; -.
DR EnsemblFungi; EAW25527; EAW25527; NFIA_110210.
DR GeneID; 4593655; -.
DR KEGG; nfi:NFIA_110210; -.
DR VEuPathDB; FungiDB:NFIA_110210; -.
DR eggNOG; KOG2803; Eukaryota.
DR HOGENOM; CLU_031246_0_0_1; -.
DR OMA; QCKYINA; -.
DR OrthoDB; 5474784at2759; -.
DR UniPathway; UPA00558; UER00742.
DR Proteomes; UP000006702; 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 Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 32..155
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 449 AA; 50531 MW; 9EEF1D4F24F1C239 CRC64;
MSVLPGELVP APGHWPVDPQ DDVPIREDRI WVDGCFDFSH HGHAGAMLQA RRLGNELYVG
VHSDEAILEN KGPTVMTLEE RVAAVEACRW ATRCIPRAPY VTSLSWVSHY GCKYVVHGDD
ITSDSNGEDC YRFVKAAGRF RVVKRTPGIS TTDLVGRMLL CTKGHFIKSV KDTLAGVEGS
DNQEERKQFG VELMQRIRDY ATDESGLRPG PQVWTWTGSK PAKVSDTVEE AGTFETLVNG
KAIKPGQRVV YVDGGFDLFS SGHIEFLRQV LELEELEGRQ RGWYDSEQVE KRLHDFGEDY
PPAYVVAGIH DDDVINHWKG FNYPIMNIFE RGLCVLQCRY IHAVIFSAPF SPSQPYLEAM
PFGVPDVVYH GPTTFIPLTY DPYTAPKRMG IFSQISDHAF QHVNAGEIVD RILRSREAYE
ERQRAKLQKG IIEELVRSEE KSLAGERGA
//