ID K1V3B8_TRIAC Unreviewed; 404 AA.
AC K1V3B8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phosphatidylserine decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1Q2_07453 {ECO:0000313|EMBL:EKC98439.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98439.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98439.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98439.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKC98439.1}.
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DR EMBL; AMBO01000391; EKC98439.1; -; Genomic_DNA.
DR AlphaFoldDB; K1V3B8; -.
DR STRING; 1220162.K1V3B8; -.
DR eggNOG; KOG2419; Eukaryota.
DR HOGENOM; CLU_043195_0_0_1; -.
DR InParanoid; K1V3B8; -.
DR OrthoDB; 1109500at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR PANTHER; PTHR10067:SF17; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 2.
PE 4: Predicted;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 43309 MW; 07B96C96730C144F CRC64;
MTGPPPQAPP PSTGPNQAPN QQPSAPTAFS DAADSWEAKA LAASLGHVVE NVGLHFLGGG
KEYPAPSEAQ KNLESVHPTL KEARQAVASF FPSSETLDKG TSGYVGAITT SSLKLIIRKL
CHGPQNGAQG LRADAALCVA SRTSAIKLTA DVRIGMHLLF VSGRGKIQQM LKTQSVREGK
LYDATGPQVK QHIAKFIATY QLDTSQLLEQ DLDKYPLVPG ARPIASADDP SVIDSPADCR
LSCFDTVSDA TKFWVKGKQF TIPHLLGAID DDTAKGFTDV SGDNATTATS QKQPANAPSD
PKSEIAKNPK VTNNTNISDQ KQDQALQSFL RHSDYALAVA RLAPQDYHRF HSPVDGVLVS
QTECMDLGIV RLHHVELRAA AATRKHAPHA ELQPRSRAPR QSQQ
//
