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Database: UniProt
Entry: A0A1V6YK76_PENNA
LinkDB: A0A1V6YK76_PENNA
Original site: A0A1V6YK76_PENNA 
ID   A0A1V6YK76_PENNA        Unreviewed;       448 AA.
AC   A0A1V6YK76;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
DE            EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269};
GN   ORFNames=PENNAL_c0018G00035 {ECO:0000313|EMBL:OQE87849.1},
GN   PNAL_LOCUS10116 {ECO:0000313|EMBL:CAG8311944.1};
OS   Penicillium nalgiovense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE87849.1, ECO:0000313|Proteomes:UP000191691};
RN   [1] {ECO:0000313|EMBL:OQE87849.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|EMBL:OQE87849.1};
RA   Nielsen J.C., Nielsen J.;
RT   "Uncovering the secondary metabolism of Penicillium species provides
RT   insights into the evolution of 6-MSA pathways.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000191691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
RN   [3] {ECO:0000313|EMBL:CAG8311944.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Branca A.L. A.;
RL   Submitted (JUL-2021) 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         ECO:0000256|PIRNR:PIRNR018269, 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|PIRNR:PIRNR018269,
CC       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|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}.
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:OQE87849.1}.
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DR   EMBL; CAJVNV010000632; CAG8311944.1; -; Genomic_DNA.
DR   EMBL; MOOB01000018; OQE87849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6YK76; -.
DR   STRING; 60175.A0A1V6YK76; -.
DR   OMA; FFAYMYF; -.
DR   OrthoDB; 5481516at2759; -.
DR   UniPathway; UPA00557; UER00614.
DR   Proteomes; UP000191691; Unassembled WGS sequence.
DR   Proteomes; UP001153461; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
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   PIRSF; PIRSF018269; PC_trans_euk; 1.
DR   PROSITE; PS01315; CDS; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018269};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018269};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR018269};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|PIRNR:PIRNR018269}.
FT   TRANSMEM        65..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        164..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        193..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        217..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        259..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   TRANSMEM        327..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR018269"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  51029 MW;  B819D2B7CB10980C CRC64;
     MSKSRRNVRF QHRSNDERRL SVSSDVSDAP SEPTSPGKNG NVSKPPTITE EKPPQSEYEK
     KKQTFITRTI WTFVMIAGFF VALFSGHIYI IALITGIQII SFKEVIAIAS IPNKEKNLRF
     TKSLNWYFLA TTMYFLYGES VIYYFKHILL VDKVLLPLAN HHRFISFTLY VMGFVFFVGS
     LQKGHYRFQF TQFAWTHMAL YLIVVQAHFV MNNIFEGMIW FFLPAALVIT NDIFAYVCGI
     SFGKTQLIQL SPKKTVEGFL GAWACTVAFG YFMTNLLIRY KYFICPVNDL GSNVLTGLEC
     VPNPVFTLQP YSLEVFGLDK TFWVEPIQFH ILAFATFASL IAPFGGFFAS GLKRTFKIKD
     FGESIPGHGG ITDRMDCQFI MGFFSFMYYH SFIAVYKASV GDIIETAING LTVDEQLEVV
     RGLGKYLYNQ GAVSESILDC LVTELKRR
//
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