ID S7Q5A3_MYOBR Unreviewed; 330 AA.
AC S7Q5A3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=D623_10007384 {ECO:0000313|EMBL:EPQ18578.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ18578.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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; KE164547; EPQ18578.1; -; Genomic_DNA.
DR AlphaFoldDB; S7Q5A3; -.
DR UniPathway; UPA00558; UER00742.
DR Proteomes; UP000052978; 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 CDD; cd02173; ECT; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
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; 2.
DR PANTHER; PTHR45780; ETHANOLAMINE-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR45780:SF2; ETHANOLAMINE-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR Pfam; PF01467; CTP_transf_like; 2.
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 ECO:0000313|EMBL:EPQ18578.1};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPQ18578.1}.
FT DOMAIN 1..114
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT DOMAIN 182..243
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 330 AA; 37587 MW; E3DA90DC37A7EA59 CRC64;
MVHYGHSNQL RQARAMGDYL IVGVHTDEEI SKHKGPPVFT QEERYKMVQA IKWVDEVVPA
APYVTTLETL DKYSCDFYDI TLTVDGRDTY EEVKQAGRYR ECKRTQGVST TDLVGRMLLM
TKAHHSSQEM SSEYRAYADS FGKCPGGRNP WTGVSQFLQT SRKIIQFASG KEPQPGDTII
YVAGAFDLFH IGHVDFLAKV HGLVERPYVI AGLHFDQEVN HYKGKNYPIM NLHERTLSVL
ACRVDLVCHG KTEIMPDKDG SDPYQEPKKR GIFRQIDSGS DLTTDLIVQR IIKNRLEYEA
RNQKKEAKEL AFLEAMKQQE EPPERGSHSA
//
