NCBI Conserved Domain Search
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RPS-BLAST 2.2.9 [May-01-2004] Query= local sequence: lcl|tmpseq_0 unnamed protein product (257 letters) Database: cdd.v2.00
gnl|CDD|24304 smart00563, PlsC, Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family gnl|CDD|25778 pfam01553, Acyltransferase, Acyltransferase. This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene gnl|CDD|10079 COG0204, PlsC, 1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid metabolism] gnl|CDD|11829 COG2121, COG2121, Uncharacterized protein conserved in bacteria [Function unknown]
 Domain Relatives
    .. This CD alignment includes 3D structure. To display structure, download Cn3D!
  PSSMs producing significant alignments: Score
(bits)
E
value
 
gnl|CDD|24304 smart00563, PlsC, Phosphate acyltransferases; Function in phos... 91.2 1e-19
gnl|CDD|25778 pfam01553, Acyltransferase, Acyltransferase. This family conta... 83.5 2e-17
  gnl|CDD|10079 COG0204, PlsC, 1-acyl-sn-glycerol-3-phosphate acyltransferase ... 133 3e-32
  gnl|CDD|11829 COG2121, COG2121, Uncharacterized protein conserved in bacteri... 38.0 0.001


gnl|CDD|24304, smart00563, PlsC, Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.
             CD-Length = 118 residues,  98.3% aligned
             Score = 91.2 bits (226), Expect = 1e-19
Query:  76   CVILSKHQSTWETFFLSGFFEPLSQ----VLKRELLYVPFFGWALALLKPIAIDRSQPKL  131
Sbjct:  1    ALVVANHQSFLDPLVLSALLPRKLRRVRFVAKKELFYVPLLGWLLRLAGAIFIDRSRGRK  60

Query:  132  ALKQLAKQGDECLKKGAWVLIFPEGTRIPVGQMGKFSRGGTALAVNAGLPVLPIAHN  188
Sbjct:  61   DRAALREAV-RLLREGEWLLIFPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIR  116


gnl|CDD|25778, pfam01553, Acyltransferase, Acyltransferase. This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.
             CD-Length = 132 residues,  98.5% aligned
             Score = 83.5 bits (206), Expect = 2e-17
Query:  62   RYEVRGLENIPEK-PCVILSKHQSTWETFFLSGFF----EPLSQVLKRELLYVPFFGWAL  116
Sbjct:  1    RIRVHGLENLPEAGPAIVVANHQSWLDPLVLSLLLYKRPDRPVFIAKKILLTDPLLGPLM  60

Query:  117  ALLKPIAIDRSQPKLALKQLAKQGDECLKKGAWVLIFPEGTRIPVGQMGKFSRGGTALAV  176
Sbjct:  61   RLLGLIFIDRENKKRALEALREAVELLRKGELPVLIFPEGTRSRNGRLLPFKKGAFHLAV  120

Query:  177  NAGLPVLPIA  186
Sbjct:  121  QAGVPIVPVA  130


gnl|CDD|10079, COG0204, PlsC, 1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid metabolism]
             CD-Length = 255 residues,  92.2% aligned
             Score =  133 bits (334), Expect = 3e-32
Query:  12   FYLLLSASAFVWGTLSFFIAPILPFRARYRFVVQNWCRFAIWLTRVVAGIRYEVRGLENI  71
Sbjct:  1    LRLALLLILVILFLLLPLPLALIALFRLRRPVLRRWLRFLVLLLLLLFGLRVEVEGLENL  60

Query:  72   PE-KPCVILSKHQSTWETFFLSGFF---EPLSQVLKRELLYVPFFGWALALLKPIAIDRS  127
Sbjct:  61   PKGGPALVVANHQSFLDPLLLSLALPRRGPVRFVAKKELFKVPLLGWLLRLLGAIPVDRE  120

Query:  128  QPKLALKQLAKQGDECLKKGAWVLIFPEGTRIPVGQ-MGKFSRGGTALAVNAGLPVLPIA  186
Sbjct:  121  NPDDETLRAAVA--RLKAGGRSLVIFPEGTRSRGGEELLPFKRGAARLALEAGVPIVPVA  178

Query:  187  HNAGQYWPKAGWAKYPGTIQVVIGPAMHAEGEGPRAIAELNQRAEAWVSETMAEISPIQQ  246
Sbjct:  179  IVGAE---ELFPSLKKGKVKVRIGPPIDISALPEPLLPELAEAVEQLARPILLELLPRYA  235


gnl|CDD|11829, COG2121, COG2121, Uncharacterized protein conserved in bacteria [Function unknown]
             CD-Length = 214 residues,  96.7% aligned
             Score = 38.0 bits (88), Expect = 0.001
Query:  33   ILPFRARYRFVVQNWCRFAIWLTRVV-AGIRYEVRGLENIP---EKPCVILSKHQSTWET  88
Sbjct:  1    LKKFLKNSKFVISILTSLLYGYLRLVYLTSRWKAGGADNNALANEKPGIVAFWHGQ----  56

Query:  89   FFLSGFFEP--------LSQVLKRELLYVPFFGWALALLKPIAIDRSQPKLALKQLAKQG  140
Sbjct:  57   LALGPFAFPKGKKIYAMVSPSRDGELIARL-----LEKFGLRVIRGSSNKGGISAL-RAL  110

Query:  141  DECLKKGAWVLIFPEGTRIPVGQMGKFSRGGTALAVNAGLPVLPIAHNAGQYWPKAGWAK  200
Sbjct:  111  LKALKQGKSIAITPDGPKGPVHKIGD---GIIALAQKSGVPIIPVGVATSRCWRLKTWDK  167

Query:  201  YP-----GTIQVVIGPAMHAEGEGPRAIAELNQRAEAWVSETMAE  240
Sbjct:  168  TIIPLPFGKIKIVLGEPIEVDAD-----KDKEELEEKRQEVSLAL  207

Citing CD-Search: Marchler-Bauer A, Anderson JB, DeWeese-Scott C, Fedorova ND, Geer LY, He S, Hurwitz DI, Jackson JD, Jacobs AR, Lanczycki CJ, Liebert CA, Liu C, Madej T, Marchler GH, Mazumder R, Nikolskaya AN, Panchenko AR, Rao BS, Shoemaker BA, Simonyan V, Song JS, Thiessen PA, Vasudevan S, Wang Y, Yamashita RA, Yin JJ, and Bryant SH (2003), "CDD: a curated Entrez database of conserved domain alignments", Nucleic Acids Res. 31:383-387.