NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|937117543|ref|WP_054554874|]
View 

MULTISPECIES: GMP/IMP nucleotidase [Pseudoalteromonas]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-216 1.51e-91

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 PRK14988:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 224  Bit Score: 267.74  E-value: 1.51e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   1 MLNWSKIDTVLLDMDGTLLDLHFDNYFWLTVIPEQYARKHKISLDAAKADILHRYQQVHGQINWYCLDYWQQQLDLPIMA 80
Cdd:PRK14988   4 DIAWQDVDTVLLDMDGTLLDLAFDNYFWQKLVPETLGAQRGISPQEAQEYIRQEYHAVQHTLNWYCLDYWSERLGLDICA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  81 LKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEWQ 160
Cdd:PRK14988  84 MTTEQGPRAVLREDTVPFLEALKASGKRRILLTNAHPHNLAVKLEHTGLDAHLDLLLSTHTFGYPKEDQRLWQAVAEHTG 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 937117543 161 FDKERTLFVDDSPAVLDAAKEFGIGHILAVANPDSQQPHKQFDGFLSTIDFREFIP 216
Cdd:PRK14988 164 LKAERTLFIDDSEPILDAAAQFGIRYCLGVTNPDSGIAEKQYQRHPSLNDYRRLIP 219
 
Name Accession Description Interval E-value
PRK14988 PRK14988
GMP/IMP nucleotidase; Provisional
 1-216 1.51e-91

GMP/IMP nucleotidase; Provisional


Pssm-ID: 237882 [Multi-domain]  Cd Length: 224  Bit Score: 267.74  E-value: 1.51e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   1 MLNWSKIDTVLLDMDGTLLDLHFDNYFWLTVIPEQYARKHKISLDAAKADILHRYQQVHGQINWYCLDYWQQQLDLPIMA 80
Cdd:PRK14988   4 DIAWQDVDTVLLDMDGTLLDLAFDNYFWQKLVPETLGAQRGISPQEAQEYIRQEYHAVQHTLNWYCLDYWSERLGLDICA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  81 LKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEWQ 160
Cdd:PRK14988  84 MTTEQGPRAVLREDTVPFLEALKASGKRRILLTNAHPHNLAVKLEHTGLDAHLDLLLSTHTFGYPKEDQRLWQAVAEHTG 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 937117543 161 FDKERTLFVDDSPAVLDAAKEFGIGHILAVANPDSQQPHKQFDGFLSTIDFREFIP 216
Cdd:PRK14988 164 LKAERTLFIDDSEPILDAAAQFGIRYCLGVTNPDSGIAEKQYQRHPSLNDYRRLIP 219
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-188 8.21e-28

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 104.73  E-value: 8.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   7 IDTVLLDMDGTLLDLHFDNYFWLTVIPEQYARKHKI-----SLDAAKADILHRYQQvhGQINWY-CLDYWQQQLDLPIM- 79
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAeelaeAYRAIEYALWRRYER--GEITFAeLLRRLLEELGLDLAe 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  80 ----ALKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQV 155
Cdd:COG1011   79 elaeAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELA 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 937117543 156 HQEWQFDKERTLFVDDSP-AVLDAAKEFGIGHIL 188
Cdd:COG1011  159 LERLGVPPEEALFVGDSPeTDVAGARAAGMRTVW 192
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 9-188 2.01e-26

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 100.19  E-value: 2.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543    9 TVLLDMDGTLLDLHFD-----NYFWLTVIPEQYARKHKISLDAAkadiLHRYQQVHG----QINWYCLDYwQQQLDLPIM 79
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAiakliNREELGLVPDELGVSAVGRLELA----LRRFKAQYGrtisPEDAQLLYK-QLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   80 ALKrdiqhlIRIREDVPPFLTELRKAGKQLIMLTNAHPDcAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEW 159
Cdd:TIGR01509  76 EAK------LKPLPGVRALLEALRARGKKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKAL 148

                         170       180
                  ....*....|....*....|....*....
gi 937117543  160 QFDKERTLFVDDSPAVLDAAKEFGIGHIL 188
Cdd:TIGR01509 149 GLEPSECVFVDDSPAGIEAAKAAGMHTVG 177
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-183 6.43e-18

haloacid dehalogenase-like hydrolase; This family is 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, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 78.01  E-value: 6.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543    7 IDTVLLDMDGTLLDLHF---------DNYFWLTVIPEQYARKHKISLDAAKADILH-RYQQVHGQINWYCLDYWQQQLDL 76
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPvvteaiaelASEHPLAKAIVAAAEDLPIPVEDFTARLLLgKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   77 PIMALKRD----IQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLW 152
Cdd:pfam00702  81 TVVLVELLgviaLADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 937117543  153 QQVHQEWQFDKERTLFVDDSPAVLDAAKEFG 183
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 95-188 2.65e-13

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All 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. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 63.57  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  95 VPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEWQFDKERTLFVDDSPA 174
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                         90
                 ....*....|....
gi 937117543 175 VLDAAKEFGIGHIL 188
Cdd:cd01427   92 DIEAARAAGGRTVA 105
 
Name Accession Description Interval E-value
PRK14988 PRK14988
GMP/IMP nucleotidase; Provisional
 1-216 1.51e-91

GMP/IMP nucleotidase; Provisional


Pssm-ID: 237882 [Multi-domain]  Cd Length: 224  Bit Score: 267.74  E-value: 1.51e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   1 MLNWSKIDTVLLDMDGTLLDLHFDNYFWLTVIPEQYARKHKISLDAAKADILHRYQQVHGQINWYCLDYWQQQLDLPIMA 80
Cdd:PRK14988   4 DIAWQDVDTVLLDMDGTLLDLAFDNYFWQKLVPETLGAQRGISPQEAQEYIRQEYHAVQHTLNWYCLDYWSERLGLDICA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  81 LKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEWQ 160
Cdd:PRK14988  84 MTTEQGPRAVLREDTVPFLEALKASGKRRILLTNAHPHNLAVKLEHTGLDAHLDLLLSTHTFGYPKEDQRLWQAVAEHTG 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 937117543 161 FDKERTLFVDDSPAVLDAAKEFGIGHILAVANPDSQQPHKQFDGFLSTIDFREFIP 216
Cdd:PRK14988 164 LKAERTLFIDDSEPILDAAAQFGIRYCLGVTNPDSGIAEKQYQRHPSLNDYRRLIP 219
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-188 8.21e-28

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 104.73  E-value: 8.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   7 IDTVLLDMDGTLLDLHFDNYFWLTVIPEQYARKHKI-----SLDAAKADILHRYQQvhGQINWY-CLDYWQQQLDLPIM- 79
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAeelaeAYRAIEYALWRRYER--GEITFAeLLRRLLEELGLDLAe 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  80 ----ALKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQV 155
Cdd:COG1011   79 elaeAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELA 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 937117543 156 HQEWQFDKERTLFVDDSP-AVLDAAKEFGIGHIL 188
Cdd:COG1011  159 LERLGVPPEEALFVGDSPeTDVAGARAAGMRTVW 192
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 9-188 2.01e-26

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 100.19  E-value: 2.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543    9 TVLLDMDGTLLDLHFD-----NYFWLTVIPEQYARKHKISLDAAkadiLHRYQQVHG----QINWYCLDYwQQQLDLPIM 79
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAiakliNREELGLVPDELGVSAVGRLELA----LRRFKAQYGrtisPEDAQLLYK-QLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   80 ALKrdiqhlIRIREDVPPFLTELRKAGKQLIMLTNAHPDcAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEW 159
Cdd:TIGR01509  76 EAK------LKPLPGVRALLEALRARGKKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKAL 148

                         170       180
                  ....*....|....*....|....*....
gi 937117543  160 QFDKERTLFVDDSPAVLDAAKEFGIGHIL 188
Cdd:TIGR01509 149 GLEPSECVFVDDSPAGIEAAKAAGMHTVG 177
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-183 6.43e-18

haloacid dehalogenase-like hydrolase; This family is 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, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 78.01  E-value: 6.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543    7 IDTVLLDMDGTLLDLHF---------DNYFWLTVIPEQYARKHKISLDAAKADILH-RYQQVHGQINWYCLDYWQQQLDL 76
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPvvteaiaelASEHPLAKAIVAAAEDLPIPVEDFTARLLLgKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   77 PIMALKRD----IQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLW 152
Cdd:pfam00702  81 TVVLVELLgviaLADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 937117543  153 QQVHQEWQFDKERTLFVDDSPAVLDAAKEFG 183
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
6-214 1.33e-13

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 66.77  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   6 KIDTVLLDMDGTLLD---LHFDnyFWltvipEQYARKHKISLDAAkadilhRYQQVHGQINWYCLDYWQQQLDLP----- 77
Cdd:COG0637    1 MIKAVIFDMDGTLVDsepLHAR--AW-----REAFAELGIDLTEE------EYRRLMGRSREDILRYLLEEYGLDlpeee 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  78 IMALKRDI------QHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHqP- 150
Cdd:COG0637   68 LAARKEELyrellaEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPD-Pd 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937117543 151 LWQQVHQEWQFDKERTLFVDDSPAVLDAAKEFGighILAVANPDSQQPHKQFDGFLSTI-DFREF 214
Cdd:COG0637  147 IYLLAAERLGVDPEECVVFEDSPAGIRAAKAAG---MRVVGVPDGGTAEEELAGADLVVdDLAEL 208
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 95-188 2.65e-13

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All 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. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 63.57  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  95 VPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEWQFDKERTLFVDDSPA 174
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                         90
                 ....*....|....
gi 937117543 175 VLDAAKEFGIGHIL 188
Cdd:cd01427   92 DIEAARAAGGRTVA 105
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-189 1.26e-12

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 64.18  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   7 IDTVLLDMDGTLLDLHFDNY---------FWLTVIP-EQYARKHKISLDAAKADILHRYQQvhgqinwyclDYWQQQLDL 76
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAaalnealaeLGLPPLDlEELRALIGLGLRELLRRLLGEDPD----------EELEELLAR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  77 PIMALKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEH-QPLWQQV 155
Cdd:COG0546   71 FRELYEEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKpEPLLEAL 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 937117543 156 hQEWQFDKERTLFVDDSPAVLDAAKEFGIGHILA 189
Cdd:COG0546  151 -ERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGV 183
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 7-184 4.60e-11

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 59.67  E-value: 4.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   7 IDTVLLDMDGTLLDLHFDnyfwltvipEQYARKHKISLDAAKADIL-HRYQQVHGQIN---WYCLDYWQQ-----QLDLP 77
Cdd:cd02603    1 IRAVLFDFGGVLIDPDPA---------AAVARFEALTGEPSEFVLDtEGLAGAFLELErgrITEEEFWEElreelGRPLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  78 IMALKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTA-IDNYLDGVISTHQYGVSKEHQPLWQQVH 156
Cdd:cd02603   72 AELFEELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPrRGDLFDGVVESCRLGVRKPDPEIYQLAL 151

                        170       180
                 ....*....|....*....|....*...
gi 937117543 157 QEWQFDKERTLFVDDSPAVLDAAKEFGI 184
Cdd:cd02603  152 ERLGVKPEEVLFIDDREENVEAARALGI 179
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
10-190 1.01e-09

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 55.67  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   10 VLLDMDGTLLD-----LHFDNY----FWLTVIPEQYARKHkISLDAAkaDILHRY---QQVHGQINWYcLDYWQQQLDlp 77
Cdd:pfam13419   1 IIFDFDGTLLDteeliIKSFNYlleeFGYGELSEEEILKF-IGLPLR--EIFRYLgvsEDEEEKIEFY-LRKYNEELH-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   78 imalkrdiQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQ 157
Cdd:pfam13419  75 --------DKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALE 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 937117543  158 EWQFDKERTLFVDDSPAVLDAAKEFGIgHILAV 190
Cdd:pfam13419 147 QLGLKPEEVIYVGDSPRDIEAAKNAGI-KVIAV 178
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 94-184 3.93e-08

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 51.89  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  94 DVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEWQFDKERTLFVDDSP 173
Cdd:cd02588   95 DVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASHA 174

                         90
                 ....*....|.
gi 937117543 174 AVLDAAKEFGI 184
Cdd:cd02588  175 WDLAGARALGL 185
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 10-185 2.87e-07

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 48.87  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   10 VLLDMDGTLLDLHFdnyfWLTVIPEQY-ARKHKIS-------LDAAKADIL-HRYQ---QVHGQINWYCLDYWQQQLDLP 77
Cdd:TIGR01428   4 LVFDVYGTLFDVHS----VAERAAELYgGRGEALSqlwrqkqLEYSWLRTLmGPYKdfwDLTREALRYLLGRLGLEDDES 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   78 IMALKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDcaMLKF--EHTAIDNYLDGVISTHQYGVSKEHQPLWQQV 155
Cdd:TIGR01428  80 AADRLAEAYLRLPPHPDVPAGLRALKERGYRLAILSNGSPA--MLKSlvKHAGLDDPFDAVLSADAVRAYKPAPQVYQLA 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 937117543  156 HQEWQFDKERTLFVDDSPAVLDAAKEFGIG 185
Cdd:TIGR01428 158 LEALGVPPDEVLFVASNPWDLGGAKKFGFK 187
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 9-188 4.44e-05

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 42.36  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   9 TVLLDMDGTLLDLH------FDNYFWLTVIPEQYARKHKISLDAAKADILHRYQQVHGQinwycldywQQQldlpIMALK 82
Cdd:cd07523    1 NFIWDLDGTLLDSYpamtkaLSETLADFGIPQDLETVYKIIKESSVQFAIQYYAEVPDL---------EEE----YKELE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  83 RDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHpDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLWQQVHQEWQFD 162
Cdd:cd07523   68 AEYLAKPILFPGAKAVLRWIKEQGGKNFLMTHRD-HSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLN 146

                        170       180
                 ....*....|....*....|....*.
gi 937117543 163 KERTLFVDDSPAVLDAAKEFGIGHIL 188
Cdd:cd07523  147 PEETVMIGDRELDIEAGHNAGISTIL 172
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 9-183 5.91e-05

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 42.00  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543    9 TVLLDMDGTLLDLHFdnyFWLTVIPEqyaRKHKISLDAAKADILHryqQVHGQIN----WYCLDYWQQqldlpimaLKRD 84
Cdd:TIGR01549   1 AILFDIDGTLVDIKF---AIRRAFPQ---TFEEFGLDPASFKALK---QAGGLAEeewyRIATSALEE--------LQGR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   85 IQHLIRIRE----DVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEHQPLwQQVHQEWQ 160
Cdd:TIGR01549  64 FWSEYDAEEayirGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGSKPEPEIF-LAALESLG 142

                         170       180
                  ....*....|....*....|...
gi 937117543  161 fDKERTLFVDDSPAVLDAAKEFG 183
Cdd:TIGR01549 143 -VPPEVLHVGDNLNDIEGARNAG 164
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 7-184 1.95e-04

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 41.11  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543   7 IDTVLLDMDGTLLDLHFD-----NYFWLTVIPEQYARKhkisldaakaDILHRY-QQVHGQINWYCLDYWQQQLDLPIMA 80
Cdd:cd02616    1 ITTILFDLDGTLIDTNELiiksfNHTLKEYGLEGYTRE----------EVLPFIgPPLRETFEKIDPDKLEDMVEEFRKY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543  81 LKRDIQHLIRIREDVPPFLTELRKAGKQLIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYGVSKEH-QPLW---QQVH 156
Cdd:cd02616   71 YREHNDDLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDpEPVLkalELLG 150

                        170       180
                 ....*....|....*....|....*...
gi 937117543 157 QEwqfdKERTLFVDDSPAVLDAAKEFGI 184
Cdd:cd02616  151 AE----PEEALMVGDSPHDILAGKNAGV 174
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 109-188 3.80e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 36.84  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937117543 109 LIMLTNAHPDCAMLKFEHTAIDNYLDGVISTHQYG-VSKEHQPLWQQVHQEWQFDKERTLFVDDSPAVLDAAKEFGIGHI 187
Cdd:cd02604   99 KIIFTNASKNHAIRVLKRLGLADLFDGIFDIEYAGpDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTV 178


                 .
gi 937117543 188 L 188
Cdd:cd02604  179 L 179
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH