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Database: UniProt
Entry: A0A316VKP3_9BASI
LinkDB: A0A316VKP3_9BASI
Original site: A0A316VKP3_9BASI 
ID   A0A316VKP3_9BASI        Unreviewed;       318 AA.
AC   A0A316VKP3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FA14DRAFT_159687 {ECO:0000313|EMBL:PWN37824.1};
OS   Meira miltonrushii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX   NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN37824.1, ECO:0000313|Proteomes:UP000245771};
RN   [1] {ECO:0000313|EMBL:PWN37824.1, ECO:0000313|Proteomes:UP000245771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN37824.1,
RC   ECO:0000313|Proteomes:UP000245771};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|RuleBase:RU003750}.
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DR   EMBL; KZ819602; PWN37824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316VKP3; -.
DR   STRING; 1280837.A0A316VKP3; -.
DR   InParanoid; A0A316VKP3; -.
DR   OrthoDB; 5472855at2759; -.
DR   Proteomes; UP000245771; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   PANTHER; PTHR15362:SF4; CDP-DIACYLGLYCEROL--INOSITOL 3-PHOSPHATIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR15362; PHOSPHATIDYLINOSITOL SYNTHASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245771};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        71..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        206..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   318 AA;  35513 MW;  B54D2748524D2218 CRC64;
     MARSSRVSKA AGQISPSDVE SEKGTITRNA NSRTSSTNSV TRRTVHANGE EEEILDSEEA
     VRLANAAQEN VFLFVPNLIG YARVILAALS LYYMKSNPKT CTLLYGFSSL LDAADGVAAR
     RLGQATKFGA VLDMVTDRCA TACLLCFLTT AYPRCAIIFQ GLITLDFSSH YIHMYSSLIT
     GSSSHKLVTS DVSWILWYYY NDSRTLFFYC AGNELFFVCL YLMDFYPTPL GLKPEWFLWP
     LGKGVASSLV LEAARNPKSI QAYFFKMIAE LTWPQIVAVI TFPIFFVKQI INAVQFWKAA
     KVLVGIDLAE RAKNRQKK
//
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