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Conserved domains on  [gi|1242568306|gb|ATA89107|]
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haloacid dehalogenase [Capnocytophaga stomatis]

Protein Classification

HAD family hydrolase( domain architecture ID 11436852)

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-214 1.44e-31

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: 114.36  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYEIDFLKSAYKEIARFACNSEDCESLYDKILDIYHQG-----------EDAFSFLVNKFPHLTKEKLL 72
Cdd:COG1011     2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALwrryergeitfAELLRRLLEELGLDLAEELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  73 EMYRNHFPNL-KLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDERNFTIFQEE 151
Cdd:COG1011    82 EAFLAALPELvEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALER 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242568306 152 -GID--EYFYIADNPKKDFIIPNKLNWTSIclldkgWnIHPQNFNLEKDLLPRHKVDDLTNIIDII 214
Cdd:COG1011   162 lGVPpeEALFVGDSPETDVAGARAAGMRTV------W-VNRSGEPAPAEPRPDYVISDLAELLELL 220
 
Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-214 1.44e-31

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: 114.36  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYEIDFLKSAYKEIARFACNSEDCESLYDKILDIYHQG-----------EDAFSFLVNKFPHLTKEKLL 72
Cdd:COG1011     2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALwrryergeitfAELLRRLLEELGLDLAEELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  73 EMYRNHFPNL-KLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDERNFTIFQEE 151
Cdd:COG1011    82 EAFLAALPELvEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALER 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242568306 152 -GID--EYFYIADNPKKDFIIPNKLNWTSIclldkgWnIHPQNFNLEKDLLPRHKVDDLTNIIDII 214
Cdd:COG1011   162 lGVPpeEALFVGDSPETDVAGARAAGMRTV------W-VNRSGEPAPAEPRPDYVISDLAELLELL 220
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 86-178 3.32e-13

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 63.33  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  86 DGAEIIFNFCKsKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDERNFT-IFQEEGI--DEYFYIADN 162
Cdd:cd04305    12 PGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDyALNQLGVkpEETLMVGDS 90

                          90
                  ....*....|....*.
gi 1242568306 163 PKKDFIIPNKLNWTSI 178
Cdd:cd04305    91 LESDILGAKNAGIKTV 106
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-141 4.54e-12

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 61.83  E-value: 4.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   6 IIFDLDDTLIYEIDFLKSAYKEiarfACNSEDCESLYDKILDIY--HQGEDAFSFL-VNKFPHLTKEKLLEMYRNHF--P 80
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNY----LLEEFGYGELSEEEILKFigLPLREIFRYLgVSEDEEEKIEFYLRKYNEELhdK 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242568306  81 NLKLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPD 141
Cdd:pfam13419  77 LVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPD 137
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 4-166 1.67e-11

HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 61.26  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYE-----------IDFLKSAY-------------KEIARFACNSEDceSLYDKILDIYhqgEDAFSFL 59
Cdd:TIGR02253   3 KAIFFDLDDTLIDTsglaekarrnaIEVLIEAGlnvdfeeayeellKLIKEYGSNYPT--HFDYLIRRLW---EEYNPKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  60 VNKF---PHLTKEKLLEMYRNHFPNLKLndgaeiifnfCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFG 136
Cdd:TIGR02253  78 VAAFvyaYHKLKFAYLRVYPGVRDTLME----------LRESGYRLGIITDGLPVKQWEKLERLGVRDFFDAVITSEEEG 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1242568306 137 SSKPDERNFTIFQEE-GID--EYFYIADNPKKD 166
Cdd:TIGR02253 148 VEKPHPKIFYAALKRlGVKpeEAVMVGDRLDKD 180
PRK09449 PRK09449
dUMP phosphatase; Provisional
 99-166 1.71e-05

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 44.12  E-value: 1.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242568306  99 NYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDERnftIFqeegiDEYFYIADNPKKD 166
Cdd:PRK09449  110 KVKMGIITNGFTELQQVRLERTGLRDYFDLLVISEQVGVAKPDVA---IF-----DYALEQMGNPDRS 169
 
Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-214 1.44e-31

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: 114.36  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYEIDFLKSAYKEIARFACNSEDCESLYDKILDIYHQG-----------EDAFSFLVNKFPHLTKEKLL 72
Cdd:COG1011     2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALwrryergeitfAELLRRLLEELGLDLAEELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  73 EMYRNHFPNL-KLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDERNFTIFQEE 151
Cdd:COG1011    82 EAFLAALPELvEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALER 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242568306 152 -GID--EYFYIADNPKKDFIIPNKLNWTSIclldkgWnIHPQNFNLEKDLLPRHKVDDLTNIIDII 214
Cdd:COG1011   162 lGVPpeEALFVGDSPETDVAGARAAGMRTV------W-VNRSGEPAPAEPRPDYVISDLAELLELL 220
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 86-178 3.32e-13

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 63.33  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  86 DGAEIIFNFCKsKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDERNFT-IFQEEGI--DEYFYIADN 162
Cdd:cd04305    12 PGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDyALNQLGVkpEETLMVGDS 90

                          90
                  ....*....|....*.
gi 1242568306 163 PKKDFIIPNKLNWTSI 178
Cdd:cd04305    91 LESDILGAKNAGIKTV 106
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-141 4.54e-12

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 61.83  E-value: 4.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   6 IIFDLDDTLIYEIDFLKSAYKEiarfACNSEDCESLYDKILDIY--HQGEDAFSFL-VNKFPHLTKEKLLEMYRNHF--P 80
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNY----LLEEFGYGELSEEEILKFigLPLREIFRYLgVSEDEEEKIEFYLRKYNEELhdK 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242568306  81 NLKLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPD 141
Cdd:pfam13419  77 LVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPD 137
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 4-166 1.67e-11

HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 61.26  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYE-----------IDFLKSAY-------------KEIARFACNSEDceSLYDKILDIYhqgEDAFSFL 59
Cdd:TIGR02253   3 KAIFFDLDDTLIDTsglaekarrnaIEVLIEAGlnvdfeeayeellKLIKEYGSNYPT--HFDYLIRRLW---EEYNPKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  60 VNKF---PHLTKEKLLEMYRNHFPNLKLndgaeiifnfCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFG 136
Cdd:TIGR02253  78 VAAFvyaYHKLKFAYLRVYPGVRDTLME----------LRESGYRLGIITDGLPVKQWEKLERLGVRDFFDAVITSEEEG 147

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1242568306 137 SSKPDERNFTIFQEE-GID--EYFYIADNPKKD 166
Cdd:TIGR02253 148 VEKPHPKIFYAALKRlGVKpeEAVMVGDRLDKD 180
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
4-141 8.73e-11

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 59.17  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYEIDFLKSAYKEiarfACNSEDCESL-YDKILDIYHQG-EDAFSFLVNKFPHLTKEKLLEMYRNHF-- 79
Cdd:COG0546     2 KLVLFDLDGTLVDSAPDIAAALNE----ALAELGLPPLdLEELRALIGLGlRELLRRLLGEDPDEELEELLARFRELYee 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242568306  80 ---PNLKLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPD 141
Cdd:COG0546    78 ellDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPK 142
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 94-189 2.26e-08

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are 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 include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 50.75  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  94 FCKSKNYKIGLI--TDGRsvtQRNKLKSLDIENIFDKIIISEEFGSSKPDERnftIFQE--EGI----DEYFYIADNPKK 165
Cdd:cd16415    18 DLKEKGLKLAVVsnFDRR---LRELLEALGLDDYFDFVVFSYEVGYEKPDPR---IFQKalERLgvspEEALHVGDDLKN 91

                          90       100
                  ....*....|....*....|....
gi 1242568306 166 DFIIPNKLNWTSIcLLDKGWNIHP 189
Cdd:cd16415    92 DYLGARAVGWHAL-LVDREGALHE 114
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 6-162 1.06e-07

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: 49.70  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   6 IIFDLDDTLIYEIDFLKSAYKEIARFAcnsEDCESLYDKILDIYHQGEDAFsflvnkfpHLTKEKLLEMYRNHFP----- 80
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEF---GLDPASFKALKQAGGLAEEEW--------YRIATSALEELQGRFWseyda 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  81 NLKLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGsSKPDERNF-TIFQEEGID-EYFY 158
Cdd:TIGR01549  71 EEAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPG-SKPEPEIFlAALESLGVPpEVLH 149


                  ....
gi 1242568306 159 IADN 162
Cdd:TIGR01549 150 VGDN 153
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-141 1.91e-07

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 49.44  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYEIDFLKSAYKEIAR---FACNSEDCESL----YDKILDIYHQGEDafsflvnkfPHLTKEKLLEMYR 76
Cdd:COG0637     3 KAVIFDMDGTLVDSEPLHARAWREAFAelgIDLTEEEYRRLmgrsREDILRYLLEEYG---------LDLPEEELAARKE 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242568306  77 NHF------PNLKLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPD 141
Cdd:COG0637    74 ELYrellaeEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPD 144
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-163 2.82e-07

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: 49.12  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYEIDFLKSAYKEIAR----FACNSEDCESLYDKILDIYH----------QGEDAFSFLVNKFPHLTKE 69
Cdd:pfam00702   2 KAVVFDLDGTLTDGEPVVTEAIAELASehplAKAIVAAAEDLPIPVEDFTArlllgkrdwlEELDILRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  70 KLLEMYRNHFP---NLKLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDERNFT 146
Cdd:pfam00702  82 VVLVELLGVIAladELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYL 161

                         170       180
                  ....*....|....*....|
gi 1242568306 147 -IFQEEGID--EYFYIADNP 163
Cdd:pfam00702 162 aALERLGVKpeEVLMVGDGV 181
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 4-166 3.35e-07

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 49.03  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   4 KYIIFDLDDTLIYEIDFLKSAYKEI--ARFACNSEDCESLY----DKILDIYHQGE--------DAFSFLVNKFPHLTKE 69
Cdd:TIGR02254   2 KTLLFDLDDTILDFQAAEALALRLLfeDQGIPLTEDMFAQYkeinQGLWRAYEEGKitkdevvnTRFSALLKEYNTEADE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  70 KLLE------MYRNHfpnlKLNDGAEIIFNFCKSKnYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDER 143
Cdd:TIGR02254  82 ALLNqkylrfLEEGH----QLLPGAFELMENLQQK-FRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKE 156

                         170       180
                  ....*....|....*....|....*..
gi 1242568306 144 NFTIFQEEGI----DEYFYIADNPKKD 166
Cdd:TIGR02254 157 IFNYALERMPkfskEEVLMIGDSLTAD 183
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 6-180 2.22e-06

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: 46.26  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   6 IIFDLDDTLI-YEIDFLKSAYKEIARF---------ACNSEDCESLYDKILDIYHQGEDAFSFLVNKFPHLTKEKLlemy 75
Cdd:TIGR01509   2 ILFDLDGVLVdTEFAIAKLINREELGLvpdelgvsaVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQIEEEA---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  76 rnhfpNLKLNDGAEIIFNFCKSKNYKIGLITDGRSVTQRnKLKSLDIENIFDKIIISEEFGSSKPDERNF-TIFQEEGID 154
Cdd:TIGR01509  78 -----KLKPLPGVRALLEALRARGKKLALLTNSPRAHKL-VLALLGLRDLFDVVIDSSDVGLGKPDPDIYlQALKALGLE 151

                         170       180
                  ....*....|....*....|....*....
gi 1242568306 155 --EYFYIADNPKKdfIIP-NKLNWTSICL 180
Cdd:TIGR01509 152 psECVFVDDSPAG--IEAaKAAGMHTVGV 178
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 92-180 8.29e-06

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: 43.15  E-value: 8.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  92 FNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDER-NFTIFQEEGID--EYFYIADNPkKDFI 168
Cdd:cd01427    16 LKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKpLLLLLLKLGVDpeEVLFVGDSE-NDIE 94

                          90
                  ....*....|..
gi 1242568306 169 IPNKLNWTSICL 180
Cdd:cd01427    95 AARAAGGRTVAV 106
PRK09449 PRK09449
dUMP phosphatase; Provisional
 99-166 1.71e-05

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 44.12  E-value: 1.71e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242568306  99 NYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPDERnftIFqeegiDEYFYIADNPKKD 166
Cdd:PRK09449  110 KVKMGIITNGFTELQQVRLERTGLRDYFDLLVISEQVGVAKPDVA---IF-----DYALEQMGNPDRS 169
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 6-108 3.10e-05

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 42.92  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   6 IIFDLDDTLIYE--IDflksaykEIARFAcnsedceSLYDKILDIYHQ---GEDAF--SFL--VNKFPHLTKEKLLEMYr 76
Cdd:cd07500     2 IVFDMDSTLIQQevID-------ELAAEA-------GVGEEVAAITERamrGELDFeeSLRerVALLKGLPESVLDEVY- 66

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1242568306  77 nhfPNLKLNDGAEIIFNFCKSKNYKIGLITDG 108
Cdd:cd07500    67 ---ERLTLTPGAEELIQTLKAKGYKTAVVSGG 95
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 6-141 5.55e-05

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: 42.65  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   6 IIFDLDDTLIYEIDFLKSAYKEIARfacnsedcESLYDKILDiyhqgEDAFSF-------LVNKFPHLTKEKLLEMYRNH 78
Cdd:cd02616     4 ILFDLDGTLIDTNELIIKSFNHTLK--------EYGLEGYTR-----EEVLPFigpplreTFEKIDPDKLEDMVEEFRKY 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306  79 fpNLKLNDGAEIIF-------NFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPD 141
Cdd:cd02616    71 --YREHNDDLTKEYpgvyetlARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPD 138
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-108 1.59e-04

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: 41.36  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   1 MRNKYIIFDLDDTLIYE--IDflksaykEIARFA-----CNSEDCESLYDKILDIYHQGEDAFS----FLVNKFPHLTKE 69
Cdd:COG0560     1 RKMRLAVFDLDGTLIAGesID-------ELARFLgrrglVDRREVLEEVAAITERAMAGELDFEeslrFRVALLAGLPEE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1242568306  70 KLLEMYRNHFPNL-KLNDGAEIIFNFCKSKNYKIGLITDG 108
Cdd:COG0560    74 ELEELAERLFEEVpRLYPGARELIAEHRAAGHKVAIVSGG 113
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 1-141 2.25e-04

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 40.78  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   1 MRNKYIIFDLDDTLIYEIDFLKSAYKEIarfacnsedceslYDKILDIYHQGEDAFSF----LVNKFPHLTKEKLLEM-- 74
Cdd:PRK13288    1 MKINTVLFDLDGTLINTNELIISSFLHT-------------LKTYYPNQYKREDVLPFigpsLHDTFSKIDESKVEEMit 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1242568306  75 -YRNHfpNLKLNDgaEIIFNF---------CKSKNYKIGLITDGRSVTQRNKLKSLDIENIFDKIIISEEFGSSKPD 141
Cdd:PRK13288   68 tYREF--NHEHHD--ELVTEYetvyetlktLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPD 140
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 6-141 2.69e-04

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 39.93  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   6 IIFDLDDTLIyeidflksaykeiarfacnseDCESLYdkildiYHqgedAFSFLVNKFPHLTKEKLLEMYrnhfPNLKLN 85
Cdd:cd16423     2 VIFDFDGVIV---------------------DTEPLW------YE----AWQELLNERRNELIKRQFSEK----TDLPPI 46

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1242568306  86 DGAEIIFNFCKSKNYKIGLITD-GRSVTQRNkLKSLDIENIFDKIIISEEFGSSKPD 141
Cdd:cd16423    47 EGVKELLEFLKEKGIKLAVASSsPRRWIEPH-LERLGLLDYFEVIVTGDDVEKSKPD 102
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 5-126 2.88e-03

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: 37.33  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242568306   5 YIIFDLDDTLIYEidflKSAYKEIARFACNSEDCESLYDKILDIYHQGEDAFSFLVNKFPHLTKEKLLEMYrnHFPNLKL 84
Cdd:TIGR01488   1 LAIFDFDGTLTRQ----DSLIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRSEEVAKEF--LARQVAL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1242568306  85 NDGAEIIFNFCKSKNYKIGLITDGRSVTQRNKLKSLDIENIF 126
Cdd:TIGR01488  75 RPGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVF 116
 
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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