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Database: UniProt
Entry: D2V9U5_NAEGR
LinkDB: D2V9U5_NAEGR
Original site: D2V9U5_NAEGR 
ID   D2V9U5_NAEGR            Unreviewed;       368 AA.
AC   D2V9U5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC46201.1};
GN   ORFNames=NAEGRDRAFT_65632 {ECO:0000313|EMBL:EFC46201.1};
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:EFC46201.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC46201.1,
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).
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DR   EMBL; GG738859; EFC46201.1; -; Genomic_DNA.
DR   RefSeq; XP_002678945.1; XM_002678899.1.
DR   AlphaFoldDB; D2V9U5; -.
DR   EnsemblProtists; EFC46201; EFC46201; NAEGRDRAFT_65632.
DR   GeneID; 8850573; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_65632; -.
DR   eggNOG; ENOG502S2XU; Eukaryota.
DR   InParanoid; D2V9U5; -.
DR   OMA; FIMQFVN; -.
DR   OrthoDB; 6541at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR14969:SF58; PAP2 SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR14969; SPHINGOSINE-1-PHOSPHATE PHOSPHOHYDROLASE; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..368
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003037386"
FT   TRANSMEM        73..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          123..229
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01569"
SQ   SEQUENCE   368 AA;  41885 MW;  F232A5294C1C9307 CRC64;
     MMKQLSLLFV LFLTLSSVMM MVSADSTTTT LGEKSYCINE LDDSFINKCH RQVPTNFLTM
     VANFVVQWVN PRTLAITAVI FLLAIPVLQI ASVRRDSQII RHTLAKFLHN KIVILNFLHR
     VCYTLVLDVA LYTVFRQIRP CSCTTDGGNT FQHFGSRYGM PSGDAMSGAI FGIFLFDVAP
     YHGWLARAFA IIIIPIVCLE RVVLGYHTVA QVTVGSCMGI ALHYYSTRAP QFMIFFDGIV
     QIVLGAILLQ VDPSLVNERD SMNNLFSWYV WGVSFQIYVF MEIGRYYFKK KNFKKIRYSL
     QHLISTKQIG EEVDSDIDHE KDTKHLDAQM DVTKLTDFGF TCISFTLMSI INFFSTAIGQ
     EGWLTKMH
//
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