ID G0S699_CHATD Unreviewed; 378 AA.
AC G0S699;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Tafazzin family protein {ECO:0000256|RuleBase:RU365062};
GN ORFNames=CTHT_0025990 {ECO:0000313|EMBL:EGS20763.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS20763.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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; GL988041; EGS20763.1; -; Genomic_DNA.
DR RefSeq; XP_006693059.1; XM_006692996.1.
DR AlphaFoldDB; G0S699; -.
DR SMR; G0S699; -.
DR STRING; 759272.G0S699; -.
DR GeneID; 18256637; -.
DR KEGG; cthr:CTHT_0025990; -.
DR eggNOG; KOG2847; Eukaryota.
DR HOGENOM; CLU_046747_1_0_1; -.
DR OMA; IMRYFKW; -.
DR OrthoDB; 1387at2759; -.
DR Proteomes; UP000008066; 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:EGS20763.1};
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:UP000008066};
KW Transferase {ECO:0000313|EMBL:EGS20763.1}.
FT DOMAIN 65..233
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 378 AA; 42921 MW; 91A9E242BB62FCE6 CRC64;
MSASSPVPQR PSLSWQIKSA LVMGMTGVIS RVFLYGFNKV EVHGLDRFLE LLDSRKDPAN
RKHGLLTVSN HISVVDDPVV WGLLPLTKYA FNPDNLRWTL GAADICFKNK LFASFFTVGQ
VLPCHRLKHS PYGGPFQPAL TQAIRLLSTP NPLLSSNSPT SLPLTYTTDG TDTHPSPLSF
PKLRRHAWVH VFPEGLVHQH ASTDLRYFKW GAARLILESD PVPDIVPMFI DGTQRVMPED
RGFPKFLPRI GKKVRVVFGE VVDYERTFGD LKRQWDALVE RERKRLVKEG GEKAMILLKQ
MMPGELPTDE LKYGKEAREI RIEVARRLRE EVLRLRRELG GYPEPDPSFA FAETWRPDDV
IGAKKYKSRV DGSNINQD
//
