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Conserved domains on  [gi|2623440035|ref|WP_319609270|]
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MULTISPECIES: lyase family protein, partial [unclassified Bacillus cereus group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14515 super family cl36389
aspartate ammonia-lyase; Provisional
 1-158 4.41e-115

aspartate ammonia-lyase; Provisional


The actual alignment was detected with superfamily member PRK14515:

Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 333.89  E-value: 4.41e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:PRK14515  233 MGATAVGTGLNADPEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 312

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:PRK14515  313 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 390
 
Name Accession Description Interval E-value
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 1-158 4.41e-115

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 333.89  E-value: 4.41e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:PRK14515  233 MGATAVGTGLNADPEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 312

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:PRK14515  313 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 390
AspA COG1027
Aspartate ammonia-lyase [Amino acid transport and metabolism];
1-158 2.31e-109

Aspartate ammonia-lyase [Amino acid transport and metabolism];


Pssm-ID: 440650 [Multi-domain]  Cd Length: 460  Bit Score: 318.53  E-value: 2.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:COG1027   224 LGGTAIGTGLNAPPGYIELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGL 303

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:COG1027   304 GEINLPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLR 381
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 1-158 5.14e-102

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 299.82  E-value: 5.14e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:cd01357   222 LGGTAIGTGINAPPGYIELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGL 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:cd01357   302 GEINLPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLR 379
aspA TIGR00839
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ...
 1-158 1.62e-92

aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by pfam00206. Fumarate hydratase scores as high as 570 bits against this model. [Energy metabolism, Amino acids and amines]


Pssm-ID: 213564 [Multi-domain]  Cd Length: 468  Bit Score: 275.94  E-value: 1.62e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:TIGR00839 225 LGATAIGTGLNTPPEYSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGL 304

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:TIGR00839 305 NEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLT 382
Lyase_1 pfam00206
Lyase;
1-116 9.00e-48

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 156.76  E-value: 9.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPlVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPrVGL 80
Cdd:pfam00206 199 GGGTAVGTGLNADPEFAELVAKELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGL 276

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIG 116
Cdd:pfam00206 277 VELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
 
Name Accession Description Interval E-value
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 1-158 4.41e-115

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 333.89  E-value: 4.41e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:PRK14515  233 MGATAVGTGLNADPEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 312

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:PRK14515  313 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 390
AspA COG1027
Aspartate ammonia-lyase [Amino acid transport and metabolism];
1-158 2.31e-109

Aspartate ammonia-lyase [Amino acid transport and metabolism];


Pssm-ID: 440650 [Multi-domain]  Cd Length: 460  Bit Score: 318.53  E-value: 2.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:COG1027   224 LGGTAIGTGLNAPPGYIELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGL 303

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:COG1027   304 GEINLPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLR 381
aspA PRK12273
aspartate ammonia-lyase; Provisional
 1-158 3.00e-107

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 313.60  E-value: 3.00e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:PRK12273  229 LGATAIGTGLNAPPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGL 308

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:PRK12273  309 NEINLPAVQAGSSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLR 386
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 1-158 1.25e-106

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 312.30  E-value: 1.25e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:PRK13353  227 LGGTAVGTGLNADPEYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGL 306

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:PRK13353  307 GEINLPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFT 384
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 1-158 5.14e-102

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 299.82  E-value: 5.14e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:cd01357   222 LGGTAIGTGINAPPGYIELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGL 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:cd01357   302 GEINLPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLR 379
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 1-158 2.28e-96

aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176468 [Multi-domain]  Cd Length: 450  Bit Score: 285.09  E-value: 2.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:cd01596   222 LGGTAVGTGLNAPPGYAEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGL 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:cd01596   302 GEINLPANQPGSSIMPGKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFR 379
aspA TIGR00839
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ...
 1-158 1.62e-92

aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by pfam00206. Fumarate hydratase scores as high as 570 bits against this model. [Energy metabolism, Amino acids and amines]


Pssm-ID: 213564 [Multi-domain]  Cd Length: 468  Bit Score: 275.94  E-value: 1.62e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:TIGR00839 225 LGATAIGTGLNTPPEYSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGL 304

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:TIGR00839 305 NEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLT 382
FumC COG0114
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ...
 1-158 9.59e-74

Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439884 [Multi-domain]  Cd Length: 461  Bit Score: 227.60  E-value: 9.59e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:COG0114   227 LGGTAVGTGLNAHPGFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGL 306

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:COG0114   307 GEIRLPANEPGSSIMPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFA 384
fumC PRK00485
fumarate hydratase; Reviewed
 1-158 2.37e-69

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 216.50  E-value: 2.37e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:PRK00485  227 LGGTAVGTGLNAHPGFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGL 306

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:PRK00485  307 GEISLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFA 384
Fumarase_classII cd01362
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ...
 1-158 6.73e-68

Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176465 [Multi-domain]  Cd Length: 455  Bit Score: 212.36  E-value: 6.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGL 80
Cdd:cd01362   223 LGGTAVGTGLNAHPGFAEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGL 302

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:cd01362   303 GELSLPENEPGSSIMPGKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFA 380
PLN00134 PLN00134
fumarate hydratase; Provisional
 2-158 8.23e-63

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 199.53  E-value: 8.23e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   2 GATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLA 81
Cdd:PLN00134  220 GGTAVGTGLNTKKGFDEKIAAAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLG 299

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2623440035  82 EIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:PLN00134  300 ELNLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFR 376
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 1-158 3.60e-53

Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.


Pssm-ID: 176461 [Multi-domain]  Cd Length: 325  Bit Score: 170.76  E-value: 3.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAiselpLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGprvGL 80
Cdd:cd01334   166 LGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSG---EF 237

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2623440035  81 AEIMLPAR-QPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:cd01334   238 GEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLT 316
PRK12425 PRK12425
class II fumarate hydratase;
2-157 5.66e-51

class II fumarate hydratase;


Pssm-ID: 171490 [Multi-domain]  Cd Length: 464  Bit Score: 168.95  E-value: 5.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   2 GATAVGTGLNADPEYIQAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLA 81
Cdd:PRK12425  226 GGTAVGTGLNAPHGFAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLA 305

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2623440035  82 EIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAF 157
Cdd:PRK12425  306 EVRLPANEPGSSIMPGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNF 381
Lyase_1 pfam00206
Lyase;
1-116 9.00e-48

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 156.76  E-value: 9.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAVGTGLNADPEYIQAVVKHLAAISELPlVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPrVGL 80
Cdd:pfam00206 199 GGGTAVGTGLNADPEFAELVAKELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGL 276

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2623440035  81 AEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIG 116
Cdd:pfam00206 277 VELSLAEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 47-158 6.48e-31

Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.


Pssm-ID: 176466 [Multi-domain]  Cd Length: 231  Bit Score: 111.16  E-value: 6.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035  47 AYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPaRQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLASE 126
Cdd:cd01594   121 AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALK 199

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2623440035 127 AGQLELNVMEPVLVFNLLQSISIMNNGFRAFT 158
Cdd:cd01594   200 GGPERDNEDSPSMREILADSLLLLIDALRLLL 231
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 1-117 9.48e-10

Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.


Pssm-ID: 176463 [Multi-domain]  Cd Length: 435  Bit Score: 55.63  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATA-VGTGLNADPEYIQAvvkhlaaiselpLVGAEDLV----DATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASG 75
Cdd:cd01359   173 LGAGAlAGTTFPIDRERTAE------------LLGFDGPTenslDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2623440035  76 PRvGLAEimLPAR-QPGSSIMPGKVNPVMPEVINQIAFQVIGN 117
Cdd:cd01359   241 EF-GFVE--LPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGA 280
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 2-107 7.50e-09

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 53.23  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   2 GATA-VGTGLNADPEYIQAvvkhlaaiselpLVGAEDLV----DATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASgP 76
Cdd:PRK00855  198 GSAAlAGTTFPIDRERTAE------------LLGFDGVTenslDAVSDRDFALEFLSAASLLMVHLSRLAEELILWSS-Q 264

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2623440035  77 RVGLAEimLPAR-QPGSSIMPGKVNPVMPEVI 107
Cdd:PRK00855  265 EFGFVE--LPDAfSTGSSIMPQKKNPDVAELI 294
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 1-117 2.83e-08

Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439935 [Multi-domain]  Cd Length: 462  Bit Score: 51.64  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATAV-GTGLNADPEYIqavvkhlaaiselplvgAEDL---------VDATQNTDAYTEVSAALKVCMMNMSKIANDLR 70
Cdd:COG0165   196 LGAAALaGTTFPIDRERT-----------------AELLgfdgptensLDAVSDRDFALEFLSAASLIMVHLSRLAEELI 258

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2623440035  71 LMASgPRVGLAEImlparqP-----GSSIMPGKVNPVMPEVINQIAFQVIGN 117
Cdd:COG0165   259 LWSS-SEFGFVEL------PdafstGSSIMPQKKNPDVAELIRGKTGRVIGN 303
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 2-117 1.06e-07

argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 129918 [Multi-domain]  Cd Length: 455  Bit Score: 50.04  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   2 GATAvGTGLNADPEYIQAVVKHLAAIselplvgaEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGpRVGLA 81
Cdd:TIGR00838 196 GALA-GTGFPIDREYLAELLGFDAVT--------ENSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTG-EFGFV 265

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2623440035  82 EimLPAR-QPGSSIMPGKVNPVMPEVINQIAFQVIGN 117
Cdd:TIGR00838 266 E--LPDEfSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 5-102 1.07e-07

Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439786 [Multi-domain]  Cd Length: 436  Bit Score: 49.70  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   5 AVGTgLNADPEYIQAVVKHLAAisELplvGAEDLVDATQNT--DAYTEVSAALKVCMMNMSKIANDLRLMASgPRVGLAE 82
Cdd:COG0015   188 AVGT-YAAHGEAWPEVEERVAE--KL---GLKPNPVTTQIEprDRHAELFSALALIAGSLEKIARDIRLLQR-TEVGEVE 260

                          90       100
                  ....*....|....*....|
gi 2623440035  83 IMLPARQPGSSIMPGKVNPV 102
Cdd:COG0015   261 EPFAKGQVGSSAMPHKRNPI 280
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 5-107 4.95e-07

Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176467 [Multi-domain]  Cd Length: 381  Bit Score: 47.88  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   5 AVGTGLNADPEyIQAVVKHLAAISELplvGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMAsgpRVGLAEIM 84
Cdd:cd01595   178 AVGTHASLGPK-GPEVEERVAEKLGL---KVPPITTQIEPRDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVE 250

                          90       100
                  ....*....|....*....|....*
gi 2623440035  85 LPAR--QPGSSIMPGKVNPVMPEVI 107
Cdd:cd01595   251 EPFEkgQVGSSTMPHKRNPIDSENI 275
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 36-121 5.56e-06

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 44.97  E-value: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035  36 EDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAeIMLPARQPgSSIMPGKVNPVMPEVINQIAFQVI 115
Cdd:PRK06705  230 ENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGIT-VARPYVQI-SSIMPQKRNPVSIEHARAITSSAL 307


                  ....*.
gi 2623440035 116 GNDHTI 121
Cdd:PRK06705  308 GEAFTV 313
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 5-107 1.98e-05

Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).


Pssm-ID: 176464 [Multi-domain]  Cd Length: 387  Bit Score: 43.31  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   5 AVGTGLNADPEYIQAVVKHLAaiselplVGAEDLvdATQ--NTDAYTEVSAALKVCMMNMSKIANDLRLMaSGPRVGLAE 82
Cdd:cd01360   180 AVGTYANLGPEVEERVAEKLG-------LKPEPI--STQviQRDRHAEYLSTLALIASTLEKIATEIRHL-QRTEVLEVE 249

                          90       100
                  ....*....|....*....|....*
gi 2623440035  83 IMLPARQPGSSIMPGKVNPVMPEVI 107
Cdd:cd01360   250 EPFSKGQKGSSAMPHKRNPILSENI 274
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 46-107 1.09e-04

prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.


Pssm-ID: 176469 [Multi-domain]  Cd Length: 437  Bit Score: 41.08  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2623440035  46 DAYTEVSAALKVCMMNMSKIANDLRLMAsgpRVGLAEIMLPAR--QPGSSIMPGKVNPVMPEVI 107
Cdd:cd01597   224 DRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPFAkgRGGSSTMPHKRNPVGCELI 284
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 5-111 1.09e-04

adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273345 [Multi-domain]  Cd Length: 435  Bit Score: 41.18  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   5 AVGTGLNADPEyiqavvkhlaaISELPLVGAEDLVDATQNT-------DAYTEVSAALKVCMMNMSKIANDLRLMAsgpR 77
Cdd:TIGR00928 186 AVGTHAAAYPL-----------VEEVEERVTEFLGLKPVPIstqieprDRHAELLDALALLATTLEKFAVDIRLLQ---R 251

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2623440035  78 VGLAEIMLPA--RQPGSSIMPGKVNPVMPEVINQIA 111
Cdd:TIGR00928 252 TEHFEVEEPFgkGQVGSSAMPHKRNPIDFENVCGLA 287
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 63-130 1.89e-04

Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176471 [Multi-domain]  Cd Length: 436  Bit Score: 40.38  E-value: 1.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035  63 SKIANDLRLMAsgprvGLAEIMLP--ARQPGSSIMPGKVNPVMPEVINQIAFQVIGndhticLASEAGQL 130
Cdd:cd03302   247 HKIATDIRLLA-----NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN------LASNAAQT 305
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 61-117 2.55e-04

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 39.63  E-value: 2.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2623440035  61 NMSKIANDLRLMAsGPRVGLAEIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGN 117
Cdd:PRK08937   29 SLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY 84
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 1-116 5.65e-04

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 39.06  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2623440035   1 MGATA-VGTGLNADPEyiqaVVKHLAAISElplvGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRL--MASgpr 77
Cdd:PRK02186  602 LGAGAgGGTTFPIDPE----FVARLLGFEQ----PAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLwtTRE--- 670

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2623440035  78 vgLAEIMLPAR-QPGSSIMPGKVNPVMPEVINQIAFQVIG 116
Cdd:PRK02186  671 --FALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAG 708
PLN02646 PLN02646
argininosuccinate lyase
 39-117 5.70e-04

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 38.94  E-value: 5.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2623440035  39 VDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLaeIMLPARQPGSSIMPGKVNPVMPEVINQIAFQVIGN 117
Cdd:PLN02646  240 IDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFV--TPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGD 316
PRK12308 PRK12308
argininosuccinate lyase;
39-107 8.95e-03

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 35.53  E-value: 8.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2623440035  39 VDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGpRVGLAEiMLPARQPGSSIMPGKVNPVMPEVI 107
Cdd:PRK12308  226 LDSVSDRDHVMELMSVASISMLHLSRLAEDLIFYNSG-ESGFIE-LADTVTSGSSLMPQKKNPDALELI 292
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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