RPS-BLAST 2.2.9 [May-01-2004]
Query= local sequence: lcl|tmpseq_0 unnamed protein product
(178 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|25595 |
pfam00702, Hydrolase, haloacid dehalogenase-like hydrolase. Th... |
49.6 |
2e-07 |
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gnl|CDD|10116 |
COG0241, HisB, Histidinol phosphatase and related phosphatases... |
199 |
2e-52 |
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gnl|CDD|10417 |
COG0546, Gph, Predicted phosphatases [General function predict... |
59.4 |
2e-10 |
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gnl|CDD|10431 |
COG0560, SerB, Phosphoserine phosphatase [Amino acid transport... |
36.1 |
0.003 |
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gnl|CDD|10517 |
COG0647, NagD, Predicted sugar phosphatases of the HAD superfa... |
36.0 |
0.003 |
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gnl|CDD|25595, pfam00702, Hydrolase, haloacid dehalogenase-like hydrolase. This family are structurally different from the alpha/ beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment. The rest of the fold is composed of the core alpha/beta domain.
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CD-Length = 197 residues, only 51.8% aligned
Score = 49.6 bits (117), Expect = 2e-07
Query: 30 PIPSSIEAIARLSQAGWTVAVATNQSGIARGYYDLAVLEAMHARLRELVAEQGGEVGLIV 89
Sbjct: 96 LYPGAREALKALKERGIKLAILTNGDRA-------------NAEAVLELLGLADLFDVIV 142
Query: 90 YCPHGPDDGCDCRKPKPGMLRQIGKHYGVDLSGIWFVGDSIGDLEAARAVDCQPVLVKTG 149
Sbjct: 143 DS-----DDVGPVKPKPEIFLLALERLGVKPEEVLMVGDGVNDAPALAAAGVGVAMVNGG 197
gnl|CDD|10116, COG0241, HisB, Histidinol phosphatase and related phosphatases [Amino acid transport and metabolism]
CD-Length = 181 residues, 94.5% aligned
Score = 199 bits (507), Expect = 2e-52
Query: 1 MSRSLLILDRDGVINLDSDDYIKTLDEWIPIPSSIEAIARLSQAGWTVAVATNQSGIARG 60
Sbjct: 3 KDQKALFLDRDGTINIDKGDYVDSLDDFQFIPGVIPALLKLQRAGYKLVVVTNQSGIGRG 62
Query: 61 YYDLAVLEAMHARLRELVAEQGGEVGLIVYCPHGPDDGCDCRKPKPGMLRQIGKHYGVDL 120
Sbjct: 63 YFTEADFDKLHNKMLKILASQGVKIDGILYCPHHPEDNCDCRKPKPGMLLSALKEYNIDL 122
Query: 121 SGIWFVGDSIGDLEAARAVDCQPVLVKTGKGVRTLGKPLPEGTLIFDDLAAVA 173
Sbjct: 123 SRSYVVGDRLTDLQAAENAGIKGVLVLTGIGVTTDGA--GRAKWVFDSLAEFA 173
gnl|CDD|10417, COG0546, Gph, Predicted phosphatases [General function prediction only]
CD-Length = 220 residues, only 64.1% aligned
Score = 59.4 bits (143), Expect = 2e-10
Query: 19 DDYIKTLDEWIPIPSSIEAIARLSQAGWTVAVATNQSGIARGYYDLAVLEAMHARLRELV 78
Sbjct: 79 LTAYAELLESRLFPGVKELLAALKSAGYKLGIVTNKP---------------ERELDILL 123
Query: 79 AEQG-GEVGLIVYCPHGPDDGCDCRKPKPGMLRQIGKHYGVDLSGIWFVGDSIGDLEAAR 137
Sbjct: 124 KALGLADYFDVIVG----GDDVPPPKPDPEPLLLLLEKLGLDPEEALMVGDSLNDILAAK 179
Query: 138 AVDCQPVLVKTGKGVRTLGKPLPEGTLIFDDLAAVASALLQ 178
Sbjct: 180 AAGVPAVGVTWGYNSREELAQA-GADVVIDSLAELLALLAE 219
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gnl|CDD|10431, COG0560, SerB, Phosphoserine phosphatase [Amino acid transport and metabolism]
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CD-Length = 212 residues, only 63.7% aligned
Score = 36.1 bits (83), Expect = 0.003
Query: 15 NLDSDDYIKTLDEWIPI-PSSIEAIARLSQAGWTVAVAT-NQSGIARGYYDLAVLEAMHA 72
Sbjct: 62 GLPVEVLEEVREEFLRLTPGAEELVAALKAAGAKVVIISGGFTFLVEPIAER--LGIDYV 119
Query: 73 RLRELVAEQGGEVGLIVYCPHGPDDGCDCRKPKPGMLRQIGKHYGVDLSGIWFVGDSIGD 132
Sbjct: 120 VANELEIDDGKLTGRVVGPI------CD-GEGKAKALRELAAELGIPLEETVAYGDSAND 172
Query: 133 LEAARAVDCQPVLVKTGKGVRTLGK 157
Sbjct: 173 LPMLEAAG-LPIAVNPKPKLRALAD 196
gnl|CDD|10517, COG0647, NagD, Predicted sugar phosphatases of the HAD superfamily [Carbohydrate transport and metabolism]
CD-Length = 269 residues, only 28.3% aligned
Score = 36.0 bits (83), Expect = 0.003
Query: 103 KPKPGMLRQIGKHYGVDLSGIWFVGDSI-GDLEAARAVDCQPVLVKTGK-GVRTLGKPLP 160
Sbjct: 190 KPSPAIYEAALEKLGLDRSEVLMVGDRLDTDILGAKAAGLDTLLVLTGVSSAEDLDRAEV 249
Query: 161 EGTLIFDDLAAVASAL 176
Sbjct: 250 KPTYVVDSLAELITAL 265
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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