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Database: UniProt
Entry: C4JXH2_UNCRE
LinkDB: C4JXH2_UNCRE
Original site: C4JXH2_UNCRE 
ID   C4JXH2_UNCRE            Unreviewed;       356 AA.
AC   C4JXH2;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Tafazzin family protein {ECO:0000256|RuleBase:RU365062};
GN   ORFNames=UREG_06345 {ECO:0000313|EMBL:EEP81480.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP81480.1, ECO:0000313|Proteomes:UP000002058};
RN   [1] {ECO:0000313|Proteomes:UP000002058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476618; EEP81480.1; -; Genomic_DNA.
DR   RefSeq; XP_002583378.1; XM_002583332.1.
DR   AlphaFoldDB; C4JXH2; -.
DR   STRING; 336963.C4JXH2; -.
DR   GeneID; 8442214; -.
DR   KEGG; ure:UREG_06345; -.
DR   VEuPathDB; FungiDB:UREG_06345; -.
DR   eggNOG; KOG2847; Eukaryota.
DR   HOGENOM; CLU_046747_1_0_1; -.
DR   InParanoid; C4JXH2; -.
DR   OMA; IMRYFKW; -.
DR   OrthoDB; 1387at2759; -.
DR   Proteomes; UP000002058; 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:UP000002058}.
FT   DOMAIN          43..228
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          323..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  40818 MW;  16A59A567206469D CRC64;
     MFQVAALCRG FLYALNTTEV HGQEEFLKLL EERRDHTLRT RGLITVSNHI SVMDDPLMWG
     TVPLHNHWGY QSFNRRWAFG SHDICFSNRA LSAFFTLGQV LPTHRLYHSS YGGLFQPTVT
     QAIRLLSRGP FPTNPHTAPG DMQQWSFQNV CVDPFSEVAT AYTTTSHDSY LAPSAYACNS
     YSWVHIFPEG KIHQSPPKTM RYFKWGVSRL ILEASDCPDV VPIWIEGTDE VMHESRAFPR
     FLPRINKKIS VTFGQRADAE TVFGDLRRRW QKLKAEAEKD GEPAPLGVLN EELMYGEKAV
     ALRKECTMRV RELVLQVRRS RGLPDEDPKA SLAETWAWEG PKREGKMDDD SWVRDI
//
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