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Database: UniProt
Entry: A0A0L0DV49_THETB
LinkDB: A0A0L0DV49_THETB
Original site: A0A0L0DV49_THETB 
ID   A0A0L0DV49_THETB        Unreviewed;       305 AA.
AC   A0A0L0DV49;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Tafazzin family protein {ECO:0000256|RuleBase:RU365062};
GN   ORFNames=AMSG_01980 {ECO:0000313|EMBL:KNC55966.1};
OS   Thecamonas trahens ATCC 50062.
OC   Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX   NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC55966.1, ECO:0000313|Proteomes:UP000054408};
RN   [1] {ECO:0000313|EMBL:KNC55966.1, ECO:0000313|Proteomes:UP000054408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC55966.1,
RC   ECO:0000313|Proteomes:UP000054408};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA   Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC         phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-
CC         acyl-sn-glycero-3-phosphocholine + a cardiolipin;
CC         Xref=Rhea:RHEA:33731, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC         ChEBI:CHEBI:62237, ChEBI:CHEBI:64743;
CC         Evidence={ECO:0000256|ARBA:ARBA00024570};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC         Evidence={ECO:0000256|ARBA:ARBA00024570};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC         Evidence={ECO:0000256|ARBA:ARBA00024570};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC       {ECO:0000256|ARBA:ARBA00004137}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00024323}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00024323}; Intermembrane side
CC       {ECO:0000256|ARBA:ARBA00024323}.
CC   -!- SIMILARITY: Belongs to the taffazin family.
CC       {ECO:0000256|ARBA:ARBA00010524, ECO:0000256|RuleBase:RU365062}.
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DR   EMBL; GL349440; KNC55966.1; -; Genomic_DNA.
DR   RefSeq; XP_013761013.1; XM_013905559.1.
DR   AlphaFoldDB; A0A0L0DV49; -.
DR   STRING; 461836.A0A0L0DV49; -.
DR   EnsemblProtists; KNC55966; KNC55966; AMSG_01980.
DR   GeneID; 25561693; -.
DR   eggNOG; KOG2847; Eukaryota.
DR   OMA; GKHITIM; -.
DR   OrthoDB; 1387at2759; -.
DR   Proteomes; UP000054408; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   InterPro; IPR000872; Tafazzin.
DR   PANTHER; PTHR12497:SF0; TAFAZZIN; 1.
DR   PANTHER; PTHR12497; TAZ PROTEIN TAFAZZIN; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   PRINTS; PR00979; TAFAZZIN.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:KNC55966.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:KNC55966.1}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..305
FT                   /note="Tafazzin family protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005537875"
FT   DOMAIN          101..232
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   305 AA;  33654 MW;  433715339DB250C7 CRC64;
     MLSKLFSSLS LSFTTSALPA PHCPHAKPEK TYHDVVDVPG IHKLPSSDHN VGWSMLSTVS
     IATAWTLASI HCNGFVTPHV YNEKALEDAV YFRSRKPGQG LITVANHVSE FDPGFIPMTL
     RWITCLRPRL VRWTLAAEDQ LFTNLASSYY FQSLKVLPVT RGGGVMQPNM LRAVDKLNGS
     SAWVNIFPEG RISMDHAPDE IPPLLPIKLG VGRLITECDT PPMVLPIYQE GMNVTKPPDK
     APIFSRDIHV HVAVGEPIEL ADILEQAAAE AWDDRRTWAA IAVRIGEAFA VMREEMAVRR
     AASGL
//
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