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Conserved domains on  [gi|21450187|ref|NP_659064|]
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haloacid dehalogenase-like hydrolase domain-containing 5 precursor [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

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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 ...
 47-358 1.45e-147

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: 421.98  E-value: 1.45e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187    47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNSQGQLRVPVVFVTNAGNILQHNKAQELSDLLRCKVDPDQVILSHSPMKLF 126
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   127 LQYHSKQMLVSGQGPLVENARALGFQNVVTIDELRLAFPELD----MVDLQRRPKTMRL-RSDFPAIEGVLLLGEPVRWE 201
Cdd:TIGR01456  81 VNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYSRDIpDLTTKRFDAVLVFNDPVDWA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   202 TNLQLIMDVLLSNGHPGTGLATapyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYRKITGNELKYEgLMGKPSI 281
Cdd:TIGR01456 161 ADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGKPTK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   282 LTYQYAEDVI----RQQAERRGWAAPIRKLYAIGDNPMSDVYGAN---LFHQYLQMA-NRGEEEQQTGGQQKQRPSATQS 353
Cdd:TIGR01456 237 LTYDFAEDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGvYNGGDDLKECKPTLIVNDVFDA 316


                  ....*
gi 21450187   354 CASIL 358
Cdd:TIGR01456 317 VTKIL 321
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 47-358 1.45e-147

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: 421.98  E-value: 1.45e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187    47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNSQGQLRVPVVFVTNAGNILQHNKAQELSDLLRCKVDPDQVILSHSPMKLF 126
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   127 LQYHSKQMLVSGQGPLVENARALGFQNVVTIDELRLAFPELD----MVDLQRRPKTMRL-RSDFPAIEGVLLLGEPVRWE 201
Cdd:TIGR01456  81 VNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYSRDIpDLTTKRFDAVLVFNDPVDWA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   202 TNLQLIMDVLLSNGHPGTGLATapyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYRKITGNELKYEgLMGKPSI 281
Cdd:TIGR01456 161 ADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGKPTK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   282 LTYQYAEDVI----RQQAERRGWAAPIRKLYAIGDNPMSDVYGAN---LFHQYLQMA-NRGEEEQQTGGQQKQRPSATQS 353
Cdd:TIGR01456 237 LTYDFAEDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGvYNGGDDLKECKPTLIVNDVFDA 316


                  ....*
gi 21450187   354 CASIL 358
Cdd:TIGR01456 317 VTKIL 321
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 47-362 1.13e-43

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: 149.08  E-value: 1.13e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187  47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNsqgqLRVPVVFVTNAGNILQHNKAQELSDLLRCKVDPDQVILSHSPmklf 126
Cdd:cd07511   1 FGFAFDIDGVLVRGKKPIPGAPKALKFLND----NKIPFIFLTNGGGFPESKRADFLSKLLGVEVSPDQVIQSHSP---- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 127 lqyhskqmlvsgqgplvenaralgfqnvvtidelrlafpeldmvdlqrrpktmrlrsdfpaiegvlllgepvrwetnlql 206
Cdd:cd07511     --------------------------------------------------------------------------------

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 207 imdvllsnghpgtglatapyphlpvlasnmdllwmaeakmprfghgtfllcletiyrkitgnelkyeglmGKPSILTYQY 286
Cdd:cd07511  73 ----------------------------------------------------------------------GKPTELTYDF 82

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450187 287 AEDVIRQQAERRGWAAPIRKLYAIGDNPMSDVYGANLFHQYlqmanrgeeeqqtggqqkqrpsATQSCASILVCTG 362
Cdd:cd07511  83 AEHVLQRQAKRLGKTEPFKYVYMVGDNPMSDIRGANLFDRY----------------------VVTGWISILVRTG 136
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 49-152 3.79e-23

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 92.91  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187    49 LLFDIDGVLVRGHRVIPAALEAFSKLvNSQGqlrVPVVFVTNAGNILQHNKAQELSDlLRCKVDPDQVILSHSPMKLFLQ 128
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRAL-RAAG---KPVVFVTNNSSRSREEYAEKLRK-LGFDIDEDEIITSGTAAADYLK 75

                          90       100
                  ....*....|....*....|....*.
gi 21450187   129 --YHSKQMLVSGQGPLVENARALGFQ 152
Cdd:pfam13344  76 erKFGKKVLVIGSEGLREELEEAGFE 101
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
48-368 2.09e-13

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 69.75  E-value: 2.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187  48 GLLFDIDGVLVRGHRVIPAALEAFSKLvNSQGqlrVPVVFVTNAGNIlqhnKAQELSDLLR---CKVDPDQVILSHSPMK 124
Cdd:COG0647  10 AFLLDLDGVLYRGDEPIPGAVEALARL-RAAG---KPVLFLTNNSSR----TPEDVAEKLRrlgIPVAEDEIVTSGDATA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 125 LFL--QYHSKQMLVSGQGPLVENARALGFqnVVTIDElrlafpeldmvdlqrrpktmrlrsdfpAIEGVLL-LGEPVRWE 201
Cdd:COG0647  82 AYLaeRHPGARVYVIGEEGLREELEEAGL--TLVDDE---------------------------EPDAVVVgLDRTFTYE 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 202 TnLQLIMDvLLSNGhpgtglatapyphLPVLASNMDLLWMAEAKmPRFGHGTFLLCLETiyrkITGNELKYeglMGKPSI 281
Cdd:COG0647 133 K-LAEALR-AIRRG-------------APFIATNPDRTVPTEDG-LIPGAGALAAALEA----ATGGEPLV---VGKPSP 189

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 282 LTYQYAEDVIRQQAERrgwaapirkLYAIGDNPMSDVYGANlfhqylqmaNRGeeeqqtggqqkqrpsatqsCASILVCT 361
Cdd:COG0647 190 PIYELALERLGVDPER---------VLMVGDRLDTDILGAN---------AAG-------------------LDTLLVLT 232


                ....*..
gi 21450187 362 GIYSSQD 368
Cdd:COG0647 233 GVTTAED 239
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 47-358 1.45e-147

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: 421.98  E-value: 1.45e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187    47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNSQGQLRVPVVFVTNAGNILQHNKAQELSDLLRCKVDPDQVILSHSPMKLF 126
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   127 LQYHSKQMLVSGQGPLVENARALGFQNVVTIDELRLAFPELD----MVDLQRRPKTMRL-RSDFPAIEGVLLLGEPVRWE 201
Cdd:TIGR01456  81 VNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYSRDIpDLTTKRFDAVLVFNDPVDWA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   202 TNLQLIMDVLLSNGHPGTGLATapyPHLPVLASNMDLLWMAEAKMPRFGHGTFLLCLETIYRKITGNELKYEgLMGKPSI 281
Cdd:TIGR01456 161 ADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGKPTK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   282 LTYQYAEDVI----RQQAERRGWAAPIRKLYAIGDNPMSDVYGAN---LFHQYLQMA-NRGEEEQQTGGQQKQRPSATQS 353
Cdd:TIGR01456 237 LTYDFAEDVLidweKRLSGTKPSTSPFHALYMVGDNPASDIIGAQnygWFSCLVKTGvYNGGDDLKECKPTLIVNDVFDA 316


                  ....*
gi 21450187   354 CASIL 358
Cdd:TIGR01456 317 VTKIL 321
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 50-329 9.27e-68

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: 214.88  E-value: 9.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187    50 LFDIDGVLVRGHRVIPAALEAFSKLVNSQgqlrVPVVFVTNAGNILQHNKAQELSDLLRCKVDPDQVILSHSPMKLFL-Q 128
Cdd:TIGR01460   2 LFDIDGVLWLGHKPIPGAAEALNRLRAKG----KPVVFLTNNSSRSEEDYAEKLSSLLGVDVSPDQIITSGSVTKDLLrQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   129 YHSKQ-MLVSGQGPLVENARALGFQNVVTIDelrlafpeLDMVDLQRrpktmrlrsdfpaIEGVLLLGEPVRWETNLQLI 207
Cdd:TIGR01460  78 RFEGEkVYVIGVGELRESLEGLGFRNDFFDD--------IDHLAIEK-------------IPAAVIVGEPSDFSYDELAK 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187   208 MDVLLSNGHpgtglatapyphLPVLASNMDllwmaeaKMPRFGHGTFLLCLETIYRKITGNELKYEGLMGKPSILTYQYA 287
Cdd:TIGR01460 137 AAYLLAEGD------------VPFIAANRD-------DLVRLGDGRFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAA 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 21450187   288 EDVIRQQAERRGwaapirklYAIGDNPMSDVYGANLFHQYLQ 329
Cdd:TIGR01460 198 LNLLQARPERRD--------VMVGDNLRTDILGAKNAGFDTL 231
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 47-362 1.13e-43

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: 149.08  E-value: 1.13e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187  47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNsqgqLRVPVVFVTNAGNILQHNKAQELSDLLRCKVDPDQVILSHSPmklf 126
Cdd:cd07511   1 FGFAFDIDGVLVRGKKPIPGAPKALKFLND----NKIPFIFLTNGGGFPESKRADFLSKLLGVEVSPDQVIQSHSP---- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 127 lqyhskqmlvsgqgplvenaralgfqnvvtidelrlafpeldmvdlqrrpktmrlrsdfpaiegvlllgepvrwetnlql 206
Cdd:cd07511     --------------------------------------------------------------------------------

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 207 imdvllsnghpgtglatapyphlpvlasnmdllwmaeakmprfghgtfllcletiyrkitgnelkyeglmGKPSILTYQY 286
Cdd:cd07511  73 ----------------------------------------------------------------------GKPTELTYDF 82

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450187 287 AEDVIRQQAERRGWAAPIRKLYAIGDNPMSDVYGANLFHQYlqmanrgeeeqqtggqqkqrpsATQSCASILVCTG 362
Cdd:cd07511  83 AEHVLQRQAKRLGKTEPFKYVYMVGDNPMSDIRGANLFDRY----------------------VVTGWISILVRTG 136
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 49-152 3.79e-23

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 92.91  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187    49 LLFDIDGVLVRGHRVIPAALEAFSKLvNSQGqlrVPVVFVTNAGNILQHNKAQELSDlLRCKVDPDQVILSHSPMKLFLQ 128
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRAL-RAAG---KPVVFVTNNSSRSREEYAEKLRK-LGFDIDEDEIITSGTAAADYLK 75

                          90       100
                  ....*....|....*....|....*.
gi 21450187   129 --YHSKQMLVSGQGPLVENARALGFQ 152
Cdd:pfam13344  76 erKFGKKVLVIGSEGLREELEEAGFE 101
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
48-368 2.09e-13

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 69.75  E-value: 2.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187  48 GLLFDIDGVLVRGHRVIPAALEAFSKLvNSQGqlrVPVVFVTNAGNIlqhnKAQELSDLLR---CKVDPDQVILSHSPMK 124
Cdd:COG0647  10 AFLLDLDGVLYRGDEPIPGAVEALARL-RAAG---KPVLFLTNNSSR----TPEDVAEKLRrlgIPVAEDEIVTSGDATA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 125 LFL--QYHSKQMLVSGQGPLVENARALGFqnVVTIDElrlafpeldmvdlqrrpktmrlrsdfpAIEGVLL-LGEPVRWE 201
Cdd:COG0647  82 AYLaeRHPGARVYVIGEEGLREELEEAGL--TLVDDE---------------------------EPDAVVVgLDRTFTYE 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 202 TnLQLIMDvLLSNGhpgtglatapyphLPVLASNMDLLWMAEAKmPRFGHGTFLLCLETiyrkITGNELKYeglMGKPSI 281
Cdd:COG0647 133 K-LAEALR-AIRRG-------------APFIATNPDRTVPTEDG-LIPGAGALAAALEA----ATGGEPLV---VGKPSP 189

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187 282 LTYQYAEDVIRQQAERrgwaapirkLYAIGDNPMSDVYGANlfhqylqmaNRGeeeqqtggqqkqrpsatqsCASILVCT 361
Cdd:COG0647 190 PIYELALERLGVDPER---------VLMVGDRLDTDILGAN---------AAG-------------------LDTLLVLT 232


                ....*..
gi 21450187 362 GIYSSQD 368
Cdd:COG0647 233 GVTTAED 239
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 48-159 1.26e-09

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319833 [Multi-domain]  Cd Length: 252  Bit Score: 58.35  E-value: 1.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187  48 GLLFDIDGVLVRGHRVIPAALEAFSKLvnsqGQLRVPVVFVTNAGNIlqhNKAQELSDLLR--CKVDPDQVILSHSPMKL 125
Cdd:cd07531   2 GYIIDLDGTIGKGVTLIPGAVEGVKTL----RRLGKKIIFLSNNSTR---SRRILLERLRSfgIEVGEDEILVSSYVTAR 74

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21450187 126 FLQYHSK--QMLVSGQGPLVENARALGFQNVVTIDE 159
Cdd:cd07531  75 FLAREKPnaKVFVTGEEGLIEELRLAGLEIVDKYDE 110
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 48-151 1.43e-06

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 49.13  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187  48 GLLFDIDGVLVRGHRVIPAALEAFSKLVNSQgqlrVPVVFVTNagNILQhnKAQELSDLLR---CKVDPDQVILSHSPMK 124
Cdd:cd07530   2 GYLIDLDGTVYRGGTAIPGAVEFIERLREKG----IPFLFLTN--NSTR--TPEDVAAKLAemgIDVPEEDVYTSALATA 73

                        90       100
                ....*....|....*....|....*....
gi 21450187 125 LFL--QYHSKQMLVSGQGPLVENARALGF 151
Cdd:cd07530  74 QYLaeQLPGAKVYVIGEEGLRTALHEAGL 102
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 48-167 2.48e-04

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 42.74  E-value: 2.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450187  48 GLLFDIDGVLVRGHRVIPAALEAFSKLvNSQGQlrvPVVFVTNagNILQhnKAQELSDLLR---CKVDPDQVILSHSPMK 124
Cdd:cd07508   1 LVISDCDGVLWHDERAIPGAAEFLEAL-KEAGK---KIVFVSN--NSSR--SRQDYAEKFRkfgVDVPEDQIVTSAKATA 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 21450187 125 LFLQYH--SKQMLVSGQGPLVENARALGFQNVVTIDELRLAFPEL 167
Cdd:cd07508  73 RFLRSRkfGKKVYVLGEEGLKEELRAAGFRIAGGPSKGIETYAEL 117
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 48-119 2.77e-04

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 42.27  E-value: 2.77e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21450187  48 GLLFDIDGVLVRGHRVIPAALEAFSKLVNSqgqlRVPVVFVTNAGNILQHNKAQELSDlLRCKVDPDQVILS 119
Cdd:cd07509   2 AVLLDLSGTLYISGAAIPGAAEALKRLRHA----GLKVRFLTNTTKESRRTLAERLQR-LGFDVSEEEIFTS 68
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 48-90 8.67e-04

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It belongs to the UmpH/NagD phosphatase family, and 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: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 40.83  E-value: 8.67e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 21450187  48 GLLFDIDGVLVRGHRVIPAALEAFSKLVNSQGQLrvpvVFVTN 90
Cdd:cd07510   3 TFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRL----VFVTN 41
 
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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