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Conserved domains on  [gi|1002984370|ref|WP_061429013|]
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MULTISPECIES: HAD-IB family hydrolase [Clostridium]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 4-196 7.30e-51

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member TIGR01490:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 202  Bit Score: 163.28  E-value: 7.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   4 LAIFDVDFTLTSKETLLQLFKFLI-KEDKKNLKFLPRAAFSGLMYGLKFYDEKKVKQSFLK-FIDGVEENDLKILVKKYY 81
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLAsKNILFEELRLPKVLARFEFFLNRGLDYMAYYRAFALdALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  82 DEVLSKIIYKDSIDMMKKLKSEGYKIYLISASPEFYLNELYNIKEVDVIIGTRFSFNE-GKFERKMVGENCKGKEKVRRL 160
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEdGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1002984370 161 KEYLQEHNIevDYKNSYMFSDSLSDKPLLDLVGNAY 196
Cdd:TIGR01490 161 AELLAEEQI--DLKDSYAYGDSISDLPLLSLVGHPY 194
 
Name Accession Description Interval E-value
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 4-196 7.30e-51

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 163.28  E-value: 7.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   4 LAIFDVDFTLTSKETLLQLFKFLI-KEDKKNLKFLPRAAFSGLMYGLKFYDEKKVKQSFLK-FIDGVEENDLKILVKKYY 81
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLAsKNILFEELRLPKVLARFEFFLNRGLDYMAYYRAFALdALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  82 DEVLSKIIYKDSIDMMKKLKSEGYKIYLISASPEFYLNELYNIKEVDVIIGTRFSFNE-GKFERKMVGENCKGKEKVRRL 160
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEdGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1002984370 161 KEYLQEHNIevDYKNSYMFSDSLSDKPLLDLVGNAY 196
Cdd:TIGR01490 161 AELLAEEQI--DLKDSYAYGDSISDLPLLSLVGHPY 194
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 4-196 5.76e-41

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 137.82  E-value: 5.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   4 LAIFDVDFTLTSKETLLQLFKFLIKEDKKNlkFLPRAAFSGLMYGLKF--YDEKKVKQsFLKFIDGVEENDLKILVKKYY 81
Cdd:cd02612     1 LAFFDLDGTLIAGDSFFAFLRFKGIAERRA--PLEELLLLRLMALYALgrLDGAGMEA-LLGFATAGLAGELAALVEEFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  82 DEVLSKIIYKDSIDMMKKLKSEGYKIYLISASPEFYLNELYNIKEVDVIIGTRFSFNEGKFERKMVGENCKGKEKVRRLK 161
Cdd:cd02612    78 EEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLR 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1002984370 162 EYLQEHNIevDYKNSYMFSDSLSDKPLLDLVGNAY 196
Cdd:cd02612   158 EWLAEEGI--DLKDSYAYSDSINDLPMLEAVGHPV 190
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-196 8.80e-35

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 122.64  E-value: 8.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   1 MEKLAIFDVDFTLTSKETLLQLFKFLIKEDKKNLK-FLPRAAFSGLMYGLKFYDEKKVKQSFLKFIDGVEENDLKILVKK 79
Cdd:COG0560     2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRReVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  80 YYDEVlsKIIYKDSIDMMKKLKSEGYKIYLISASPEFYLN---ELYNIKEVdviIGTRFSFNEGKFERKMVGENCKGKEK 156
Cdd:COG0560    82 LFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEpiaERLGIDHV---IANELEVEDGRLTGEVVGPIVDGEGK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1002984370 157 VRRLKEYLQEHNIevDYKNSYMFSDSLSDKPLLDLVGNAY 196
Cdd:COG0560   157 AEALRELAAELGI--DLEQSYAYGDSANDLPMLEAAGLPV 194
HAD pfam12710
haloacid dehalogenase-like hydrolase;
5-189 4.22e-28

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 104.54  E-value: 4.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   5 AIFDVDFTLTSKETLLQLFKFLIKEDK-KNLKFLPRAAFSGLMYGLKFYDEKKVKQSFLKFIDGVEENDLKILVKKYYDE 83
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGpDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  84 VLSKIiYKDSIDMMKKLKSEGYKIYLISASPEFYLN---ELYNIKEVdviIGTRFSFNEGKF--ERKMVGENCKGKEKVR 158
Cdd:pfam12710  81 ALPRL-HPGALELLAAHRAAGDRVVVVTGGLRPLVEpvlAELGFDEV---LATELEVDDGRFtgELRLIGPPCAGEGKVR 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1002984370 159 RLKEYLQEHNIEVDYKNSYMFSDSLSDKPLL 189
Cdd:pfam12710 157 RLRAWLAARGLGLDLADSVAYGDSPSDLPML 187
 
Name Accession Description Interval E-value
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 4-196 7.30e-51

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 163.28  E-value: 7.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   4 LAIFDVDFTLTSKETLLQLFKFLI-KEDKKNLKFLPRAAFSGLMYGLKFYDEKKVKQSFLK-FIDGVEENDLKILVKKYY 81
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLAsKNILFEELRLPKVLARFEFFLNRGLDYMAYYRAFALdALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  82 DEVLSKIIYKDSIDMMKKLKSEGYKIYLISASPEFYLNELYNIKEVDVIIGTRFSFNE-GKFERKMVGENCKGKEKVRRL 160
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEdGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1002984370 161 KEYLQEHNIevDYKNSYMFSDSLSDKPLLDLVGNAY 196
Cdd:TIGR01490 161 AELLAEEQI--DLKDSYAYGDSISDLPLLSLVGHPY 194
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 4-196 5.76e-41

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 137.82  E-value: 5.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   4 LAIFDVDFTLTSKETLLQLFKFLIKEDKKNlkFLPRAAFSGLMYGLKF--YDEKKVKQsFLKFIDGVEENDLKILVKKYY 81
Cdd:cd02612     1 LAFFDLDGTLIAGDSFFAFLRFKGIAERRA--PLEELLLLRLMALYALgrLDGAGMEA-LLGFATAGLAGELAALVEEFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  82 DEVLSKIIYKDSIDMMKKLKSEGYKIYLISASPEFYLNELYNIKEVDVIIGTRFSFNEGKFERKMVGENCKGKEKVRRLK 161
Cdd:cd02612    78 EEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLR 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1002984370 162 EYLQEHNIevDYKNSYMFSDSLSDKPLLDLVGNAY 196
Cdd:cd02612   158 EWLAEEGI--DLKDSYAYSDSINDLPMLEAVGHPV 190
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-196 8.80e-35

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 122.64  E-value: 8.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   1 MEKLAIFDVDFTLTSKETLLQLFKFLIKEDKKNLK-FLPRAAFSGLMYGLKFYDEKKVKQSFLKFIDGVEENDLKILVKK 79
Cdd:COG0560     2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRReVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  80 YYDEVlsKIIYKDSIDMMKKLKSEGYKIYLISASPEFYLN---ELYNIKEVdviIGTRFSFNEGKFERKMVGENCKGKEK 156
Cdd:COG0560    82 LFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEpiaERLGIDHV---IANELEVEDGRLTGEVVGPIVDGEGK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1002984370 157 VRRLKEYLQEHNIevDYKNSYMFSDSLSDKPLLDLVGNAY 196
Cdd:COG0560   157 AEALRELAAELGI--DLEQSYAYGDSANDLPMLEAAGLPV 194
HAD pfam12710
haloacid dehalogenase-like hydrolase;
5-189 4.22e-28

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 104.54  E-value: 4.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   5 AIFDVDFTLTSKETLLQLFKFLIKEDK-KNLKFLPRAAFSGLMYGLKFYDEKKVKQSFLKFIDGVEENDLKILVKKYYDE 83
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGpDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  84 VLSKIiYKDSIDMMKKLKSEGYKIYLISASPEFYLN---ELYNIKEVdviIGTRFSFNEGKF--ERKMVGENCKGKEKVR 158
Cdd:pfam12710  81 ALPRL-HPGALELLAAHRAAGDRVVVVTGGLRPLVEpvlAELGFDEV---LATELEVDDGRFtgELRLIGPPCAGEGKVR 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1002984370 159 RLKEYLQEHNIEVDYKNSYMFSDSLSDKPLL 189
Cdd:pfam12710 157 RLRAWLAARGLGLDLADSVAYGDSPSDLPML 187
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 4-192 3.38e-24

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 93.96  E-value: 3.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   4 LAIFDVDFTLTSKETLLQLFKFLIKEDKKNLKFLPRAAFSGLMYglkfydEKKVKQSFLKfidgveenDLKILVKKYYDE 83
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTNDEVIELTRLAPSGRISF------EDALGRRLAL--------LHRSRSEEVAKE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  84 VLSKIIYKD--SIDMMKKLKSEGYKIYLISASPEFYLNELYNIKEVDVIIGTRFSFNE-GKFERKMVGE-NCKGKEKVRR 159
Cdd:TIGR01488  67 FLARQVALRpgARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDnGLLTGPIEGQvNPEGECKGKV 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1002984370 160 LKEYLQEHNIevDYKNSYMFSDSLSDKPLLDLV 192
Cdd:TIGR01488 147 LKELLEESKI--TLKKIIAVGDSVNDLPMLKLA 177
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-185 4.21e-03

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 36.83  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   3 KLAIFDVDFTLT-SKETLLQLFKFLIKEdkKNLKFLPRAAFSGLMyGLkfydekKVKQSFLKFIDGVEENDLKILVKKYY 81
Cdd:COG0546     2 KLVLFDLDGTLVdSAPDIAAALNEALAE--LGLPPLDLEELRALI-GL------GLRELLRRLLGEDPDEELEELLARFR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370  82 DEVLSKII-----YKDSIDMMKKLKSEGYKIYLISASPEFYLNEL---YNIKE-VDVIIGtrfsfnegkferkmvGENC- 151
Cdd:COG0546    73 ELYEEELLdetrlFPGVRELLEALKARGIKLAVVTNKPREFAERLleaLGLDDyFDAIVG---------------GDDVp 137

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1002984370 152 KGKEKVRRLKEYLQEHNIEVDykNSYMFSDSLSD 185
Cdd:COG0546   138 PAKPKPEPLLEALERLGLDPE--EVLMVGDSPHD 169
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-111 5.14e-03

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 36.41  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002984370   6 IFDVDFTL-TSKETLLQLFKFLIKEdkknlkflpraafsglmYGLKFYDEKKV--------KQSFLKF-IDGVEENDLKI 75
Cdd:pfam13419   2 IFDFDGTLlDTEELIIKSFNYLLEE-----------------FGYGELSEEEIlkfiglplREIFRYLgVSEDEEEKIEF 64

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1002984370  76 LVKKYYDEVLSKII--YKDSIDMMKKLKSEGYKIYLIS 111
Cdd:pfam13419  65 YLRKYNEELHDKLVkpYPGIKELLEELKEQGYKLGIVT 102
 
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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