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Database: UniProt
Entry: R9PDI3_PSEHS
LinkDB: R9PDI3_PSEHS
Original site: R9PDI3_PSEHS 
ID   R9PDI3_PSEHS            Unreviewed;       352 AA.
AC   R9PDI3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Tafazzin family protein {ECO:0000256|RuleBase:RU365062};
GN   ORFNames=PHSY_007039 {ECO:0000313|EMBL:GAC99438.1};
OS   Pseudozyma hubeiensis (strain SY62) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC99438.1, ECO:0000313|Proteomes:UP000014071};
RN   [1] {ECO:0000313|Proteomes:UP000014071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX   PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA   Konishi M., Hatada Y., Horiuchi J.;
RT   "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT   hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT   mannosylerythritol lipids.";
RL   Genome Announc. 1:E0040913-E0040913(2013).
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; DF238831; GAC99438.1; -; Genomic_DNA.
DR   RefSeq; XP_012193025.1; XM_012337635.1.
DR   AlphaFoldDB; R9PDI3; -.
DR   STRING; 1305764.R9PDI3; -.
DR   GeneID; 24112304; -.
DR   eggNOG; KOG2847; Eukaryota.
DR   HOGENOM; CLU_046747_0_0_1; -.
DR   OrthoDB; 1387at2759; -.
DR   Proteomes; UP000014071; 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:InterPro.
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   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:UP000014071}.
FT   DOMAIN          57..183
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          313..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  38799 MW;  4328FAF4FB16BD3C CRC64;
     MSSSAVSGSS SNLTIRAVAA FSRNLLRFGC RKVTVRGLER FLSHLHSSSR LSSNTGLLTY
     CNHISVLDEP TIWGSLPASS FRNADTVRWT LGASDIMFTS SLLSKFFRSG QCIETHRGGG
     IHQAAIDDSI SKLDAGKWIH LFPEGYVNVS TSTRLRRFKW GISRMLIEAE KMPVVMPIWI
     TGFDKLMPEP RDKPKWLPRW GADVTIDFGE PISDTIGPII KAIKETGEAA PQHLLPHELC
     QSETDAEPLA GEENDRSIPT QVATTWSTSN LIRSHADLKG NSASLKLALA RSQLAAVLRH
     HLGLVGVDQR RADGFPHPEQ DGELVHTQSL RSAEKHAQNN VLRDGERKKV GV
//
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