ID D2W2A0_NAEGR Unreviewed; 472 AA.
AC D2W2A0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC36787.1};
GN ORFNames=NAEGRDRAFT_59916 {ECO:0000313|EMBL:EFC36787.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC36787.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC36787.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|RuleBase:RU003750}.
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DR EMBL; GG738925; EFC36787.1; -; Genomic_DNA.
DR RefSeq; XP_002669531.1; XM_002669485.1.
DR AlphaFoldDB; D2W2A0; -.
DR EnsemblProtists; EFC36787; EFC36787; NAEGRDRAFT_59916.
DR GeneID; 8862926; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_59916; -.
DR InParanoid; D2W2A0; -.
DR OrthoDB; 5496479at2759; -.
DR Proteomes; UP000006671; 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 Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 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 SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
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 47..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 472 AA; 53826 MW; 25101F7FBE369EF9 CRC64;
MTLTTTSCLY IDSEGNWVDN NHPKRTAPKV GDYITHRVRL SFFDLCLYYA NIVDYLRIVM
VVVALIALIV NDEMNLGCNW SSISISVLVF GSVLLDWVDG PLARNFGQSS VMGCGWDWLA
DILTQLCLAI WCMSLSSDYK IFKLFTVLLT AVEISTGIFD FAVSAQGVYP SMHNTENLPW
YAIVEHWLTP NHSYNNLGII CWLVNTLYPI TVFLQLPSIV SNSLIPFAIL YAWHECTQCV
FIVVNWKETA VTLHQEGIEH VRKCNDTEIE MLKTAHEATL NTPVELDDEA TKINEITWVN
LYNNGKISPV FENHPLQKEF HDWVKSLVKS NWLDEQDRII LSYGFITAPK NGNVTQDWHF
DYGENVSNLF IPLCDVTEKN GTQFIRGPLR QDMPPGEYFP RPFEIMTEEK SECLQVCQVV
CKAFNLLKLH PGVCHRGIAN GENYDRVMFF LSTNPTPLDI GEEGYLNKAT YD
//
