RPS-BLAST 2.2.9 [May-01-2004]
Query= local sequence: lcl|tmpseq_0 unnamed protein product
(257 letters)
Database: cdd.v2.00
.. This CD alignment includes 3D structure. To display structure, download
Cn3D!
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PSSMs producing significant alignments: |
Score (bits) |
E value |
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gnl|CDD|24304 |
smart00563, PlsC, Phosphate acyltransferases; Function in phos... |
91.2 |
1e-19 |
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gnl|CDD|25778 |
pfam01553, Acyltransferase, Acyltransferase. This family conta... |
83.5 |
2e-17 |
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gnl|CDD|10079 |
COG0204, PlsC, 1-acyl-sn-glycerol-3-phosphate acyltransferase ... |
133 |
3e-32 |
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gnl|CDD|11829 |
COG2121, COG2121, Uncharacterized protein conserved in bacteri... |
38.0 |
0.001 |
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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.
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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
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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.
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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.
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