ID A0A061D0N5_BABBI Unreviewed; 439 AA.
AC A0A061D0N5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|RuleBase:RU003938};
GN ORFNames=BBBOND_0105220 {ECO:0000313|EMBL:CDR94213.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR94213.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001698,
CC ECO:0000256|RuleBase:RU003938};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00005119, ECO:0000256|RuleBase:RU003938}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185,
CC ECO:0000256|RuleBase:RU003938}.
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DR EMBL; LK391707; CDR94213.1; -; Genomic_DNA.
DR RefSeq; XP_012766399.1; XM_012910945.1.
DR AlphaFoldDB; A0A061D0N5; -.
DR STRING; 5866.A0A061D0N5; -.
DR EnsemblProtists; CDR94213; CDR94213; BBBOND_0105220.
DR GeneID; 24562754; -.
DR KEGG; bbig:BBBOND_0105220; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0105220; -.
DR OMA; FFAYMYF; -.
DR OrthoDB; 5481516at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000033188; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR13773:SF8; PHOSPHATIDATE CYTIDYLYLTRANSFERASE, PHOTORECEPTOR-SPECIFIC; 1.
DR Pfam; PF01148; CTP_transf_1; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU003938};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003938};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003938};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 49556 MW; 1267D1360E1DCBB4 CRC64;
MMPAFRRSSS IRDTRGHSKS DNAELGDTCW SRILSNNLAI RIVLGLIIAG GTVFVICLGP
IYGSILILLL INMAYYEMVS LYDKVIQQHK QATGEEVSSK TGSVTGKFKK RVRIYVITEA
FDVFSFISLE TYFLLTTMVG ISFPWLLPRL ARKHPNIAPI CGFVLSYHHL LLFISFFCGV
VKFILSLEKG RSRQQFLRFA FIIMALLYVV IQSMMIIANL YYGMVWFLLP HAMIALNDVM
AYFFGKMFGR TPLISLSPNK TLEGFLGAFV STSLVVGMVT PTIMNFQPMV CPVNNFDFTP
FAWMTTTCEP ESIYKTSAYI LPTWAANVLG MKEVLYKPCF VHVMILTLFA SLFAPFGGFL
ASGFKRALKV KDFSDTIPGH GGMMDRFDCH ILMGTFTYLY LKTFVRRSNY SPDAVMKVIA
KMAPKDRTML LEKLQEAFG
//
