ID A0A1Q9CSX4_SYMMI Unreviewed; 721 AA.
AC A0A1Q9CSX4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487};
DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487};
DE AltName: Full=CDP-diacylglycerol synthase {ECO:0000256|ARBA:ARBA00029893};
DE AltName: Full=CDP-diglyceride pyrophosphorylase {ECO:0000256|ARBA:ARBA00032396};
DE AltName: Full=CDP-diglyceride synthase {ECO:0000256|ARBA:ARBA00033406};
GN Name=cdsA {ECO:0000313|EMBL:OLP85997.1};
GN ORFNames=AK812_SmicGene32952 {ECO:0000313|EMBL:OLP85997.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP85997.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP85997.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP85997.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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 -!- 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:OLP85997.1}.
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DR EMBL; LSRX01000942; OLP85997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9CSX4; -.
DR OrthoDB; 5481516at2759; -.
DR UniPathway; UPA00557; UER00614.
DR Proteomes; UP000186817; Unassembled WGS sequence.
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; 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.
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:0000313|EMBL:OLP85997.1};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OLP85997.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 176..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 721 AA; 80622 MW; B1FD618C411C086E CRC64;
MQDGTSKARL VLENNMLVSF SLYTLLLMVS VLSLRKGLYK YQITQYTWTM VTICIVVFQT
QAVFHLIYAG LFWFVLPSSL VICNDIMAYY CGQLFGKKLI RRRFLELSPN KTWEGFLGSA
VCTMLFALWF SRKLCAYKWM TCVKREEESL FPRHARHFPF RTSMCGGADA CAGGGISPRA
GELPPSPALS KERERERECS SGETNFADLL NRHNMPRGTY PPTESTQPAT TDAEPTQPTK
AQTYYPYWDP RKSARQRGAT AAEARRASET WPVHQHLLRA ANSIQATHYR QMMHLNRQAT
ESWSEWHVRS LRTARARMHR EGMQRWSTFI LQRIWSLWGH MARGGDEVNN MIRWKDLRFW
RAEQQKPART RVRHAGRFNP GGDVERAIEA IAGTSWGEVA QQRQVWQALQ QRFVERLDVP
WATGRQGSIH DNLHPNTSNT SKTKRAAQLG DLSQSGNKER YYAAPYNPET DPWHEEEDDP
HQAQPLPAQI TAADLAFRFG YPWYDAQGNL VLPSPAVPGS SHWRGPPLQD PTDHAAHPQP
SGGTTQSHSS HTLGGATEPQ QAPHQQASAS GTSSHQPQAA AGGATPAGRP KSRKPRPQQA
AASNTAPMGD TPSTQPDPQL KLRLTAPDPP QQPPTFGAWA VSQDTATPSD WIPPPWDTTE
ASHNTQSTQH PGNLPTHDLG AQALELTLAG ETLKQTPQQP AAKGGEQRRQ ESLQAPDPSQ
I
//
