NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720417604|ref|XP_030111169|]
View 

haloacid dehalogenase-like hydrolase domain-containing 5 isoform X4 [Mus musculus]

Protein Classification

haloacid dehalogenase-like hydrolase domain-containing 5 protein( domain architecture ID 712250)

haloacid dehalogenase-like hydrolase domain-containing 5 (HDHD5) protein is a member of the haloacid dehalogenase superfamily of enzymes, which are involved in the degradation of halogenated compounds.

Gene Ontology:  GO:0046474

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CECR5 super family cl28371
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 1-151 9.47e-64

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


The actual alignment was detected with superfamily member TIGR01456:

Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 200.10  E-value: 9.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604   1 MDVLLSNGHPGTGLATapyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYRKITGNELKYEgLMGKPSILTYQYA 80
Cdd:TIGR01456 167 SDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGKPTKLTYDFA 242

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417604  81 EDVI----RQQAERRGWAAPIRKLYAIGDNPMSDVYGAN---LFHQYLQMA-NRGEEEQQTGGQQKQRPSATQSCASIL 151
Cdd:TIGR01456 243 EDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGvYNGGDDLKECKPTLIVNDVFDAVTKIL 321
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 1-151 9.47e-64

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 200.10  E-value: 9.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604   1 MDVLLSNGHPGTGLATapyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYRKITGNELKYEgLMGKPSILTYQYA 80
Cdd:TIGR01456 167 SDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGKPTKLTYDFA 242

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417604  81 EDVI----RQQAERRGWAAPIRKLYAIGDNPMSDVYGAN---LFHQYLQMA-NRGEEEQQTGGQQKQRPSATQSCASIL 151
Cdd:TIGR01456 243 EDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGvYNGGDDLKECKPTLIVNDVFDAVTKIL 321
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 70-155 5.62e-30

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5); 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: 319814  Cd Length: 136  Bit Score: 107.86  E-value: 5.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604  70 GKPSILTYQYAEDVIRQQAERRGWAAPIRKLYAIGDNPMSDVYGANLFHQYlqmanrgeeeqqtggqqkqrpsATQSCAS 149
Cdd:cd07511    73 GKPTELTYDFAEHVLQRQAKRLGKTEPFKYVYMVGDNPMSDIRGANLFDRY----------------------VVTGWIS 130


                  ....*.
gi 1720417604 150 ILVCTG 155
Cdd:cd07511   131 ILVRTG 136
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
22-161 1.30e-04

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 41.63  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604  22 LPVLASNMDLLWMAEAKMpRFGHGTFLLCLETIyrkiTGNELKYeglMGKPSILTYQYAEDVIRQQAERrgwaapirkLY 101
Cdd:COG0647   145 APFIATNPDRTVPTEDGL-IPGAGALAAALEAA----TGGEPLV---VGKPSPPIYELALERLGVDPER---------VL 207

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604 102 AIGDNPMSDVYGANlfhqylqmaNRGeeeqqtggqqkqrpsatqsCASILVCTGIYSSQD 161
Cdd:COG0647   208 MVGDRLDTDILGAN---------AAG-------------------LDTLLVLTGVTTAED 239
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 1-151 9.47e-64

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 200.10  E-value: 9.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604   1 MDVLLSNGHPGTGLATapyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYRKITGNELKYEgLMGKPSILTYQYA 80
Cdd:TIGR01456 167 SDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGKPTKLTYDFA 242

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417604  81 EDVI----RQQAERRGWAAPIRKLYAIGDNPMSDVYGAN---LFHQYLQMA-NRGEEEQQTGGQQKQRPSATQSCASIL 151
Cdd:TIGR01456 243 EDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGvYNGGDDLKECKPTLIVNDVFDAVTKIL 321
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 70-155 5.62e-30

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5); 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: 319814  Cd Length: 136  Bit Score: 107.86  E-value: 5.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604  70 GKPSILTYQYAEDVIRQQAERRGWAAPIRKLYAIGDNPMSDVYGANLFHQYlqmanrgeeeqqtggqqkqrpsATQSCAS 149
Cdd:cd07511    73 GKPTELTYDFAEHVLQRQAKRLGKTEPFKYVYMVGDNPMSDIRGANLFDRY----------------------VVTGWIS 130


                  ....*.
gi 1720417604 150 ILVCTG 155
Cdd:cd07511   131 ILVRTG 136
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 1-122 1.14e-24

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 97.01  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604   1 MDVLLSNGHpgtglatapyphLPVLASNMDllwmaeaKMPRFGHGTFLLCLETIYRKITGNELKYEGLMGKPSILTYQYA 80
Cdd:TIGR01460 137 AAYLLAEGD------------VPFIAANRD-------DLVRLGDGRFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAA 197

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720417604  81 EDVIRQQAERRGwaapirklYAIGDNPMSDVYGANLFHQYLQ 122
Cdd:TIGR01460 198 LNLLQARPERRD--------VMVGDNLRTDILGAKNAGFDTL 231
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
22-161 1.30e-04

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 41.63  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604  22 LPVLASNMDLLWMAEAKMpRFGHGTFLLCLETIyrkiTGNELKYeglMGKPSILTYQYAEDVIRQQAERrgwaapirkLY 101
Cdd:COG0647   145 APFIATNPDRTVPTEDGL-IPGAGALAAALEAA----TGGEPLV---VGKPSPPIYELALERLGVDPER---------VL 207

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417604 102 AIGDNPMSDVYGANlfhqylqmaNRGeeeqqtggqqkqrpsatqsCASILVCTGIYSSQD 161
Cdd:COG0647   208 MVGDRLDTDILGAN---------AAG-------------------LDTLLVLTGVTTAED 239
 
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