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Conserved domains on  [gi|768022775|ref|XP_011544428|]
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haloacid dehalogenase-like hydrolase domain-containing 5 isoform X1 [Homo sapiens]

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

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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 ...
42-292 1.28e-142

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: 406.57  E-value: 1.28e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775   42 QVDADQVILSHSPMKLFSEYHEKRMLVSGQGPVMENAQGLGFRNVVTVDELRMAFPLLD----MVDLERRLKTTPLPRND 117
Cdd:TIGR01456  64 DVSPLQVIQSHSPYKSLVNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYSRDIPDLT 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775  118 FPRIEGVLLLGEPVRWETSLQLIMDVLLSNGSPGAGLATppyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYQK 197
Cdd:TIGR01456 144 TKRFDAVLVFNDPVDWAADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLE 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775  198 VTGKELRYEgLMGKPSILTYQYAEDLI----RRQAERRGWAAPIRKLYAVGDNPMSDVYGAN---LFHQYLQKATHDGAP 270
Cdd:TIGR01456 221 LNGKPLQYY-TLGKPTKLTYDFAEDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGVYNGGD 299
                         250       260
                  ....*....|....*....|..
gi 768022775  271 ELGAGGTRQQQPSASQSCISIL 292
Cdd:TIGR01456 300 DLKECKPTLIVNDVFDAVTKIL 321
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
42-292 1.28e-142

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: 406.57  E-value: 1.28e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775   42 QVDADQVILSHSPMKLFSEYHEKRMLVSGQGPVMENAQGLGFRNVVTVDELRMAFPLLD----MVDLERRLKTTPLPRND 117
Cdd:TIGR01456  64 DVSPLQVIQSHSPYKSLVNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYSRDIPDLT 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775  118 FPRIEGVLLLGEPVRWETSLQLIMDVLLSNGSPGAGLATppyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYQK 197
Cdd:TIGR01456 144 TKRFDAVLVFNDPVDWAADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLE 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775  198 VTGKELRYEgLMGKPSILTYQYAEDLI----RRQAERRGWAAPIRKLYAVGDNPMSDVYGAN---LFHQYLQKATHDGAP 270
Cdd:TIGR01456 221 LNGKPLQYY-TLGKPTKLTYDFAEDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGVYNGGD 299
                         250       260
                  ....*....|....*....|..
gi 768022775  271 ELGAGGTRQQQPSASQSCISIL 292
Cdd:TIGR01456 300 DLKECKPTLIVNDVFDAVTKIL 321
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
210-296 4.89e-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: 111.71  E-value: 4.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775 210 GKPSILTYQYAEDLIRRQAERRGWAAPIRKLYAVGDNPMSDVYGANLFHQYlqkathdgapelgaggtrqqqpsASQSCI 289
Cdd:cd07511   73 GKPTELTYDFAEHVLQRQAKRLGKTEPFKYVYMVGDNPMSDIRGANLFDRY-----------------------VVTGWI 129

                 ....*..
gi 768022775 290 SILVCTG 296
Cdd:cd07511  130 SILVRTG 136
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
43-84 3.83e-04

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 39.37  E-value: 3.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 768022775   43 VDADQVILSHSPMKLF--SEYHEKRMLVSGQGPVMENAQGLGFR 84
Cdd:pfam13344  58 IDEDEIITSGTAAADYlkERKFGKKVLVIGSEGLREELEEAGFE 101
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
42-292 1.28e-142

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: 406.57  E-value: 1.28e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775   42 QVDADQVILSHSPMKLFSEYHEKRMLVSGQGPVMENAQGLGFRNVVTVDELRMAFPLLD----MVDLERRLKTTPLPRND 117
Cdd:TIGR01456  64 DVSPLQVIQSHSPYKSLVNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYSRDIPDLT 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775  118 FPRIEGVLLLGEPVRWETSLQLIMDVLLSNGSPGAGLATppyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYQK 197
Cdd:TIGR01456 144 TKRFDAVLVFNDPVDWAADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLE 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775  198 VTGKELRYEgLMGKPSILTYQYAEDLI----RRQAERRGWAAPIRKLYAVGDNPMSDVYGAN---LFHQYLQKATHDGAP 270
Cdd:TIGR01456 221 LNGKPLQYY-TLGKPTKLTYDFAEDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGVYNGGD 299
                         250       260
                  ....*....|....*....|..
gi 768022775  271 ELGAGGTRQQQPSASQSCISIL 292
Cdd:TIGR01456 300 DLKECKPTLIVNDVFDAVTKIL 321
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
42-267 1.64e-49

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: 165.96  E-value: 1.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775   42 QVDADQVILSHSPMKLFSE-YHE-KRMLVSGQGPVMENAQGLGFRNvvtvdelrMAFPLLDMVDlerrlkttplprndFP 119
Cdd:TIGR01460  58 DVSPDQIITSGSVTKDLLRqRFEgEKVYVIGVGELRESLEGLGFRN--------DFFDDIDHLA--------------IE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775  120 RIEGVLLLGEPVRWETSLQLIMDVLLSNGSpgaglatppyphLPVLASNMDllwmaeaKMPRFGHGTFLLCLETIYQKVT 199
Cdd:TIGR01460 116 KIPAAVIVGEPSDFSYDELAKAAYLLAEGD------------VPFIAANRD-------DLVRLGDGRFRPGAGAIAAGIK 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768022775  200 GKELRYEGLMGKPSILTYQYAEDLIRRQAERRGwaapirklYAVGDNPMSDVYGANLFHQYLQKATHD 267
Cdd:TIGR01460 177 ELSGREPTVVGKPSPAIYRAALNLLQARPERRD--------VMVGDNLRTDILGAKNAGFDTLLVLTG 236
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
210-296 4.89e-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: 111.71  E-value: 4.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768022775 210 GKPSILTYQYAEDLIRRQAERRGWAAPIRKLYAVGDNPMSDVYGANLFHQYlqkathdgapelgaggtrqqqpsASQSCI 289
Cdd:cd07511   73 GKPTELTYDFAEHVLQRQAKRLGKTEPFKYVYMVGDNPMSDIRGANLFDRY-----------------------VVTGWI 129

                 ....*..
gi 768022775 290 SILVCTG 296
Cdd:cd07511  130 SILVRTG 136
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
43-84 3.83e-04

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 39.37  E-value: 3.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 768022775   43 VDADQVILSHSPMKLF--SEYHEKRMLVSGQGPVMENAQGLGFR 84
Cdd:pfam13344  58 IDEDEIITSGTAAADYlkERKFGKKVLVIGSEGLREELEEAGFE 101
 
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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