ID A0A0P0N2R6_9CREN Unreviewed; 194 AA.
AC A0A0P0N2R6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=CDP-alcohol phosphatidyltransferase {ECO:0000313|EMBL:ALL00943.1};
GN ORFNames=Pdsh_01180 {ECO:0000313|EMBL:OWJ55445.1}, Pyrde_0895
GN {ECO:0000313|EMBL:ALL00943.1};
OS Pyrodictium delaneyi.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=1273541 {ECO:0000313|EMBL:ALL00943.1, ECO:0000313|Proteomes:UP000058613};
RN [1] {ECO:0000313|EMBL:ALL00943.1, ECO:0000313|Proteomes:UP000058613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Su06 {ECO:0000313|EMBL:ALL00943.1,
RC ECO:0000313|Proteomes:UP000058613};
RA Jung J.-H., Lin J., Holden J.F., Park C.-S.;
RT "Complete genome sequence of hyperthermophilic archaeon Pyrodictium
RT delaneyi Su06.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OWJ55445.1, ECO:0000313|Proteomes:UP000196694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hulk {ECO:0000313|EMBL:OWJ55445.1,
RC ECO:0000313|Proteomes:UP000196694};
RA Demey L.M., Miller C., Manzella M., Reguera G., Kashefi K.;
RT "The draft genome of the hyperthermophilic archaeon 'Pyrodictium delaneyi
RT strain Hulk', an iron and nitrate reducer, reveals the capacity for sulfate
RT reduction.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|RuleBase:RU003750}.
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DR EMBL; CP013011; ALL00943.1; -; Genomic_DNA.
DR EMBL; NCQP01000001; OWJ55445.1; -; Genomic_DNA.
DR RefSeq; WP_055408601.1; NZ_NCQP01000001.1.
DR AlphaFoldDB; A0A0P0N2R6; -.
DR STRING; 1273541.Pyrde_0895; -.
DR GeneID; 26099232; -.
DR KEGG; pdl:Pyrde_0895; -.
DR OrthoDB; 9904at2157; -.
DR Proteomes; UP000058613; Chromosome.
DR Proteomes; UP000196694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Pfam; PF01066; CDP-OH_P_transf; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 194 AA; 20600 MW; 610F66C96844116C CRC64;
MLGRLRGRVR VVLEAAAAPL AVLPADFYTV LGLAGALAYL WAAHSGNVGL AALLLAVSGL
LDALDGAVAR LRGEAGPRGA YLDSLLDRVA DIAYAAGFLA LGYPVWSVLV FLTGALLTSY
ARARYESLAG RSMEGIGLLE RSDRLAAQLI VLLVHARLGL EAAARLYTVL AVLAWITFAE
RLVRGYTQLP RRQS
//
