ID D2VP64_NAEGR Unreviewed; 459 AA.
AC D2VP64;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Mitochondrial cardiolipin hydrolase {ECO:0000256|ARBA:ARBA00040549};
GN ORFNames=NAEGRDRAFT_58813 {ECO:0000313|EMBL:EFC41378.1};
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:EFC41378.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC41378.1,
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 phospholipase D family. MitoPLD/Zucchini
CC subfamily. {ECO:0000256|ARBA:ARBA00038012}.
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DR EMBL; GG738886; EFC41378.1; -; Genomic_DNA.
DR RefSeq; XP_002674122.1; XM_002674076.1.
DR AlphaFoldDB; D2VP64; -.
DR EnsemblProtists; EFC41378; EFC41378; NAEGRDRAFT_58813.
DR GeneID; 8850669; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_58813; -.
DR eggNOG; ENOG502RYRD; Eukaryota.
DR InParanoid; D2VP64; -.
DR OMA; MYTYSHQ; -.
DR OrthoDB; 5761at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00138; PLDc_SF; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..459
FT /note="Mitochondrial cardiolipin hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003038620"
FT DOMAIN 159..186
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 366..388
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 459 AA; 51555 MW; E5357F46D104ADDE CRC64;
MKAISKISLA TLLCAIILFT TTQLVLADLQ NTTYNSPFLP LNIPRANIGL TPLFSPDHST
KEETELVMSA KKTIDIAIPG FDSWSGCTYP KDGCMGCSAT DLLNNEKFPI FQVLINQIVQ
HGVKVRLLTN KYDDKMCSGK MDLLTYLKIA GADVRYYTTT TFLHAKYITI DGCKSAISSI
NFSQTSFRRN REAGILVNEC NNAAGVVKFS QGVFEYDFFH GVPLDVDYSQ YSKSDIHMIQ
TSTATVTIPE NMHFANCDAS SGDIQEFNDN YNISISASPD YAYGFLMSAL NQVKKSLKIS
IYEISHPDLC DYVIQLGNKG INLKIFASHY VFAKSEALEA YQCYRKLVDN NINVVLSAKQ
CLEFSHEKYW VIDDNILMMS TGNWRGSDYP NPPYVFPPKK GNSSTWRNVN RDFTLRIDGQ
TAILKKFLAV LDNDYQQGYP YSPSTSTSPI KQSINIRNY
//
