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Conserved domains on  [gi|6322923|ref|NP_012996|]
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uncharacterized protein YKR070W [Saccharomyces cerevisiae S288C]

Protein Classification

haloacid dehalogenase-like hydrolase domain-containing 5 protein( domain architecture ID 11492672)

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.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 14-348 0e+00

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: 535.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     14 IAFAFDIDGVLFRGKKPIAGASDALKLLNRN----KIPYILLTNGGGFSERARTEFISSKLDVDVSPLQIIQSHTPYKSL 89
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNqgqlKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     90 VNKYS-RILAVGTPSVRGVAEGYGFQDVVHQTDIVRYNRDIAPFSGLSDEQVMEYSRDIPDLTTKKFDAVLVFNDPHDWA 168
Cdd:TIGR01456  81 VNKYEkRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDPFSGMSDEQVMEYSRDIPDLTTKRFDAVLVFNDPVDWA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    169 ADIQIISDAINSENgmlntLRNEKSGKPSIPIYFSNQDLLWANPYKLNRFGQGAFRLLVRRLYLELNGEPLQDYTLGKPT 248
Cdd:TIGR01456 161 ADIQIISDALNSEG-----LPGEKSGKPSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYYTLGKPT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    249 KLTYDFAHHVLIDWEKRLSgkigqsvkqklpllGTKPSTSPFHAVFMVGDNPASDIIGAQNYGWNSCLVKTGVYNEGDDL 328
Cdd:TIGR01456 236 KLTYDFAEDVLIDWEKRLS--------------GTKPSTSPFHALYMVGDNPASDIIGAQNYGWFSCLVKTGVYNGGDDL 301

                         330       340
                  ....*....|....*....|
gi 6322923    329 KECKPTLIVNDVFDAVTKTL 348
Cdd:TIGR01456 302 KECKPTLIVNDVFDAVTKIL 321
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 14-348 0e+00

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: 535.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     14 IAFAFDIDGVLFRGKKPIAGASDALKLLNRN----KIPYILLTNGGGFSERARTEFISSKLDVDVSPLQIIQSHTPYKSL 89
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNqgqlKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     90 VNKYS-RILAVGTPSVRGVAEGYGFQDVVHQTDIVRYNRDIAPFSGLSDEQVMEYSRDIPDLTTKKFDAVLVFNDPHDWA 168
Cdd:TIGR01456  81 VNKYEkRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDPFSGMSDEQVMEYSRDIPDLTTKRFDAVLVFNDPVDWA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    169 ADIQIISDAINSENgmlntLRNEKSGKPSIPIYFSNQDLLWANPYKLNRFGQGAFRLLVRRLYLELNGEPLQDYTLGKPT 248
Cdd:TIGR01456 161 ADIQIISDALNSEG-----LPGEKSGKPSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYYTLGKPT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    249 KLTYDFAHHVLIDWEKRLSgkigqsvkqklpllGTKPSTSPFHAVFMVGDNPASDIIGAQNYGWNSCLVKTGVYNEGDDL 328
Cdd:TIGR01456 236 KLTYDFAEDVLIDWEKRLS--------------GTKPSTSPFHALYMVGDNPASDIIGAQNYGWFSCLVKTGVYNGGDDL 301

                         330       340
                  ....*....|....*....|
gi 6322923    329 KECKPTLIVNDVFDAVTKTL 348
Cdd:TIGR01456 302 KECKPTLIVNDVFDAVTKIL 321
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 14-320 1.81e-42

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: 144.07  E-value: 1.81e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   14 IAFAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSERARTEFISSKLDVDVSPLQIIQSHTPykslvnky 93
Cdd:cd07511   1 FGFAFDIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLSKLLGVEVSPDQVIQSHSP-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   94 srilavgtpsvrgvaegygfqdvvhqtdivrynrdiapfsglsdeqvmeysrdipdlttkkfdavlvfndphdwaadiqi 173
Cdd:cd07511     --------------------------------------------------------------------------------

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  174 isdainsengmlntlrneksgkpsipiyfsnqdllwanpyklnrfgqgafrllvrrlylelngeplqdytlGKPTKLTYD 253
Cdd:cd07511  73 -----------------------------------------------------------------------GKPTELTYD 81

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322923  254 FAHHVLIDWEKRLsgkigqsvkqklpllgtkPSTSPFHAVFMVGDNPASDIIGAQNY------GWNSCLVKTG 320
Cdd:cd07511  82 FAEHVLQRQAKRL------------------GKTEPFKYVYMVGDNPMSDIRGANLFdryvvtGWISILVRTG 136
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 16-114 3.38e-29

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 108.32  E-value: 3.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     16 FAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSERARTEFIsSKLDVDVSPLQIIQSHTPYKSLV---NK 92
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKL-RKLGFDIDEDEIITSGTAAADYLkerKF 79

                          90       100
                  ....*....|....*....|..
gi 6322923     93 YSRILAVGTPSVRGVAEGYGFQ 114
Cdd:pfam13344  80 GKKVLVIGSEGLREELEEAGFE 101
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
15-342 2.40e-28

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 110.58  E-value: 2.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   15 AFAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGgfseRARTEFISSKLD---VDVSPLQII----------Q 81
Cdd:COG0647  10 AFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNS----SRTPEDVAEKLRrlgIPVAEDEIVtsgdataaylA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   82 SHTPYKslvnkysRILAVGTPSVRGVAEGYGFQDVVhqtdivrynrdiapfsglsDEQVmeysrdipdlttkkfDAVLVF 161
Cdd:COG0647  86 ERHPGA-------RVYVIGEEGLREELEEAGLTLVD-------------------DEEP---------------DAVVVG 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  162 NDPHDWAADIQIISDAInsENGmlntlrneksgkpsIPIYFSNQDLLWANPYKLnRFGQGAFrllVRRLYLELNGEPlqd 241
Cdd:COG0647 125 LDRTFTYEKLAEALRAI--RRG--------------APFIATNPDRTVPTEDGL-IPGAGAL---AAALEAATGGEP--- 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  242 YTLGKPTKLTYDFAhhvlidwekrlsgkigqsvkqkLPLLGTKPSTspfhaVFMVGDNPASDIIGAQNYGWNSCLVKTGV 321
Cdd:COG0647 182 LVVGKPSPPIYELA----------------------LERLGVDPER-----VLMVGDRLDTDILGANAAGLDTLLVLTGV 234

                       330       340
                ....*....|....*....|..
gi 6322923  322 YNEGD-DLKECKPTLIVNDVFD 342
Cdd:COG0647 235 TTAEDlEAAPIRPDYVLDSLAE 256
PRK09449 PRK09449
dUMP phosphatase; Provisional
 293-315 5.50e-04

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 40.65  E-value: 5.50e-04
                         10        20
                 ....*....|....*....|...
gi 6322923   293 VFMVGDNPASDIIGAQNYGWNSC 315
Cdd:PRK09449 171 VLMVGDNLHSDILGGINAGIDTC 193
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 14-348 0e+00

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: 535.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     14 IAFAFDIDGVLFRGKKPIAGASDALKLLNRN----KIPYILLTNGGGFSERARTEFISSKLDVDVSPLQIIQSHTPYKSL 89
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNqgqlKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     90 VNKYS-RILAVGTPSVRGVAEGYGFQDVVHQTDIVRYNRDIAPFSGLSDEQVMEYSRDIPDLTTKKFDAVLVFNDPHDWA 168
Cdd:TIGR01456  81 VNKYEkRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDPFSGMSDEQVMEYSRDIPDLTTKRFDAVLVFNDPVDWA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    169 ADIQIISDAINSENgmlntLRNEKSGKPSIPIYFSNQDLLWANPYKLNRFGQGAFRLLVRRLYLELNGEPLQDYTLGKPT 248
Cdd:TIGR01456 161 ADIQIISDALNSEG-----LPGEKSGKPSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYYTLGKPT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    249 KLTYDFAHHVLIDWEKRLSgkigqsvkqklpllGTKPSTSPFHAVFMVGDNPASDIIGAQNYGWNSCLVKTGVYNEGDDL 328
Cdd:TIGR01456 236 KLTYDFAEDVLIDWEKRLS--------------GTKPSTSPFHALYMVGDNPASDIIGAQNYGWFSCLVKTGVYNGGDDL 301

                         330       340
                  ....*....|....*....|
gi 6322923    329 KECKPTLIVNDVFDAVTKTL 348
Cdd:TIGR01456 302 KECKPTLIVNDVFDAVTKIL 321
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 16-320 6.55e-76

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: 233.76  E-value: 6.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     16 FAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSERARTEFISSKLDVDVSPLQIIQSHTPYKSLVNKY-- 93
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLLGVDVSPDQIITSGSVTKDLLRQRfe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     94 -SRILAVGTPSVRGVAEGYGFQDvvhqtdivrynrdiapfsglsdeqvmEYSRDIPDLTTKKFDAVLVFNDPHDWAADIQ 172
Cdd:TIGR01460  81 gEKVYVIGVGELRESLEGLGFRN--------------------------DFFDDIDHLAIEKIPAAVIVGEPSDFSYDEL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    173 IISDAINSENGMlntlrneksgkpsiPIYFSNQDllwanpyKLNRFGQGAFRLLVRRLYLELNGEPLQDYT-LGKPTKLT 251
Cdd:TIGR01460 135 AKAAYLLAEGDV--------------PFIAANRD-------DLVRLGDGRFRPGAGAIAAGIKELSGREPTvVGKPSPAI 193

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322923    252 YDFAHHVLIDWEKRlsgkigqsvkqklpllgtkpstspfHAVfMVGDNPASDIIGAQNYGWNSCLVKTG 320
Cdd:TIGR01460 194 YRAALNLLQARPER-------------------------RDV-MVGDNLRTDILGAKNAGFDTLLVLTG 236
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 14-320 1.81e-42

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: 144.07  E-value: 1.81e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   14 IAFAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSERARTEFISSKLDVDVSPLQIIQSHTPykslvnky 93
Cdd:cd07511   1 FGFAFDIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLSKLLGVEVSPDQVIQSHSP-------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   94 srilavgtpsvrgvaegygfqdvvhqtdivrynrdiapfsglsdeqvmeysrdipdlttkkfdavlvfndphdwaadiqi 173
Cdd:cd07511     --------------------------------------------------------------------------------

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  174 isdainsengmlntlrneksgkpsipiyfsnqdllwanpyklnrfgqgafrllvrrlylelngeplqdytlGKPTKLTYD 253
Cdd:cd07511  73 -----------------------------------------------------------------------GKPTELTYD 81

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322923  254 FAHHVLIDWEKRLsgkigqsvkqklpllgtkPSTSPFHAVFMVGDNPASDIIGAQNY------GWNSCLVKTG 320
Cdd:cd07511  82 FAEHVLQRQAKRL------------------GKTEPFKYVYMVGDNPMSDIRGANLFdryvvtGWISILVRTG 136
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 16-114 3.38e-29

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 108.32  E-value: 3.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923     16 FAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSERARTEFIsSKLDVDVSPLQIIQSHTPYKSLV---NK 92
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKL-RKLGFDIDEDEIITSGTAAADYLkerKF 79

                          90       100
                  ....*....|....*....|..
gi 6322923     93 YSRILAVGTPSVRGVAEGYGFQ 114
Cdd:pfam13344  80 GKKVLVIGSEGLREELEEAGFE 101
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
15-342 2.40e-28

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 110.58  E-value: 2.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   15 AFAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGgfseRARTEFISSKLD---VDVSPLQII----------Q 81
Cdd:COG0647  10 AFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNS----SRTPEDVAEKLRrlgIPVAEDEIVtsgdataaylA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   82 SHTPYKslvnkysRILAVGTPSVRGVAEGYGFQDVVhqtdivrynrdiapfsglsDEQVmeysrdipdlttkkfDAVLVF 161
Cdd:COG0647  86 ERHPGA-------RVYVIGEEGLREELEEAGLTLVD-------------------DEEP---------------DAVVVG 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  162 NDPHDWAADIQIISDAInsENGmlntlrneksgkpsIPIYFSNQDLLWANPYKLnRFGQGAFrllVRRLYLELNGEPlqd 241
Cdd:COG0647 125 LDRTFTYEKLAEALRAI--RRG--------------APFIATNPDRTVPTEDGL-IPGAGAL---AAALEAATGGEP--- 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  242 YTLGKPTKLTYDFAhhvlidwekrlsgkigqsvkqkLPLLGTKPSTspfhaVFMVGDNPASDIIGAQNYGWNSCLVKTGV 321
Cdd:COG0647 182 LVVGKPSPPIYELA----------------------LERLGVDPER-----VLMVGDRLDTDILGANAAGLDTLLVLTGV 234

                       330       340
                ....*....|....*....|..
gi 6322923  322 YNEGD-DLKECKPTLIVNDVFD 342
Cdd:COG0647 235 TTAEDlEAAPIRPDYVLDSLAE 256
Hydrolase_like pfam13242
HAD-hyrolase-like;
244-343 1.31e-15

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 70.72  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    244 LGKPTKLTYDFAHHVLidwekrlsgkigqsvkqklpllgtkpsTSPFHAVFMVGDNPASDIIGAQNYGWNSCLVKTGVYN 323
Cdd:pfam13242   2 CGKPNPGMLERALARL---------------------------GLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTR 54

                          90       100
                  ....*....|....*....|.
gi 6322923    324 EGDDLK-ECKPTLIVNDVFDA 343
Cdd:pfam13242  55 PADLEKaPIRPDYVVDDLAEA 75
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 15-344 1.20e-10

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: 61.14  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   15 AFAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSERARTEFISsKLDVDVSPLQIIQShtpykslvnkys 94
Cdd:cd07509   2 AVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQ-RLGFDVSEEEIFTS------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   95 rilavgTPSVRGVAEGygfqdvvhqtdivRYNRdiaPFSgLSDEQVMEysrDIPDLTTKKFDAVLVFNDPHDWaaDIQII 174
Cdd:cd07509  69 ------LTAARQYLEE-------------KGLR---PHL-LVDDDALE---DFIGIDTSDPNAVVIGDAGEHF--NYQTL 120

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  175 SDAInsenGMLntlrneKSGKPSIPIyfsNQDLLWANPYKLnRFGQGAFrllVRRLYLELNGEPLqdyTLGKPTKLTYdf 254
Cdd:cd07509 121 NRAF----RLL------LDGAPLIAL---HKGRYYKRKDGL-ALDPGAF---VTGLEYATGIKAT---VVGKPSPEFF-- 178

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  255 ahhvlidwekrlsgkigqsvKQKLPLLGTKPStspfHAVfMVGDNPASDIIGAQNYGWNSCLVKTGVYNEGDDLK-ECKP 333
Cdd:cd07509 179 --------------------LSALRSLGVDPE----EAV-MIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKpNVPP 233

                       330
                ....*....|.
gi 6322923  334 TLIVNDVFDAV 344
Cdd:cd07509 234 DLTADSFADAV 244
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 16-123 3.73e-08

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized 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: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 53.60  E-value: 3.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   16 FAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGggfSERARTEFIS--SKLDVDVSPLQIIQSHTPYKSLVNK- 92
Cdd:cd16422   2 FIFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNN---SSKNLADYVEklNRLGIDAGLDRVFTSGEATIDHLKKe 78

                        90       100       110
                ....*....|....*....|....*....|...
gi 6322923   93 --YSRILAVGTPSVRGVAEGYGFQDVVHQTDIV 123
Cdd:cd16422  79 fiKPKIFLLGTKSLREEFEKAGFTLDGDDIDVV 111
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 18-344 6.91e-08

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: 53.14  E-value: 6.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   18 FDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSERARTE-FISSKLDVD----VSPLQII----QSHTPYKs 88
Cdd:cd07508   4 SDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEkFRKFGVDVPedqiVTSAKATarflRSRKFGK- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   89 lvnkysRILAVGTPSVRGVAEGYGFQdvvhqtdivrynrdiapFSGLSDEQVMEYSRDIPDLTTKK-FDAVLVFNDPH-D 166
Cdd:cd07508  83 ------KVYVLGEEGLKEELRAAGFR-----------------IAGGPSKGIETYAELVEHLEDDEnVDAVIVGSDFKlN 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  167 WAADIQIISDAINSENGMLNTlrneksgkpsipiyfsNQDLLWanPYKLNRFGQGAFRLLVrRLYLELNGEPLqdyTLGK 246
Cdd:cd07508 140 FAKLRKACRYLRNPGCLFIAT----------------APDRIH--PLKDGGPIPGTGAFAA-AVEAATGRQPL---VLGK 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  247 PTKLTYDFAhhvlidwekrlsgkigqsvkqkLPLLGTKPSTspfhaVFMVGDNPASDIIGAQNYGWNSCLVKTGVYNEGD 326
Cdd:cd07508 198 PSPWLGELA----------------------LEKFGIDPER-----VLFVGDRLATDVLFGKACGFQTLLVLTGVTTLED 250

                       330
                ....*....|....*...
gi 6322923  327 DLKECKPTLIVNDVFDAV 344
Cdd:cd07508 251 LQAYIDHELVPDYYADSL 268
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 15-82 1.54e-07

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: 51.82  E-value: 1.54e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322923   15 AFAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGggfSERARtEFISSKL---DVDVSPLQIIQS 82
Cdd:cd07530   2 GYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNN---STRTP-EDVAAKLaemGIDVPEEDVYTS 68
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
222-342 1.35e-05

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 45.69  E-value: 1.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923  222 AFRLLVRRLYLELngeplqdytLGKPTKLtYDFAHHVLIDWEKR------LSGKIGQSVKQKLPLLG------------- 282
Cdd:COG0546  66 ELLARFRELYEEE---------LLDETRL-FPGVRELLEALKARgiklavVTNKPREFAERLLEALGlddyfdaivggdd 135

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322923  283 ---TKPSTSPFHA-----------VFMVGDNPaSDIIGAQNYGWNSCLVKTGvYNEGDDLKECKPTLIVNDVFD 342
Cdd:COG0546 136 vppAKPKPEPLLEalerlgldpeeVLMVGDSP-HDIEAARAAGVPFIGVTWG-YGSAEELEAAGADYVIDSLAE 207
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 284-339 2.55e-05

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: 44.63  E-value: 2.55e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322923  284 KPSTSPFHAVF-----------MVGDNPASDIIGAQNYGWNSCLVKTGVYNEGDDLkecKPTLIVND 339
Cdd:COG1011 149 KPDPEIFELALerlgvppeealFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEP---RPDYVISD 212
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 275-344 7.32e-05

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 43.70  E-value: 7.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322923    275 KQKLPLLGTKPstspfHAVFMVGDNPASDIIGAQNYGWNSCLVKTGVYNEGDDLK-ECKPTLIVNDVFDAV 344
Cdd:TIGR01458 186 LEALRATGCEP-----EEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPSDEEKiNVPPDLTCDSLPHAV 251
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 253-315 9.74e-05

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: 40.99  E-value: 9.74e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322923  253 DFAHHVLIdwekrlSGKIGQSvkqklpllgtKPSTSPFHAVF-----------MVGDNPASDIIGAQNYGWNSC 315
Cdd:cd04305  49 KYFDHIVI------SEEVGVQ----------KPNPEIFDYALnqlgvkpeetlMVGDSLESDILGAKNAGIKTV 106
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 16-65 1.18e-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: 43.14  E-value: 1.18e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 6322923   16 FAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGggfSERARTEF 65
Cdd:cd07510   4 FLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNN---STKSREAY 50
PRK09449 PRK09449
dUMP phosphatase; Provisional
 293-315 5.50e-04

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 40.65  E-value: 5.50e-04
                         10        20
                 ....*....|....*....|...
gi 6322923   293 VFMVGDNPASDIIGAQNYGWNSC 315
Cdd:PRK09449 171 VLMVGDNLHSDILGGINAGIDTC 193
PRK14166 PRK14166
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 264-322 1.67e-03

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 172654 [Multi-domain]  Cd Length: 282  Bit Score: 39.62  E-value: 1.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923   264 KRLSGKIGQSVKQKLPLLGTKpSTSPFHAVFMVGDNPASDI-IGAQNYGWNSCLVKTGVY 322
Cdd:PRK14166   7 KALSAKIKEELKEKNQFLKSK-GIESCLAVILVGDNPASQTyVKSKAKACEECGIKSLVY 65
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 18-60 2.07e-03

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: 39.09  E-value: 2.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6322923   18 FDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSER 60
Cdd:cd07531   5 IDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRR 47
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 217-316 3.67e-03

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: 38.24  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322923    217 RFGQGAFRLLVR-----RLYLELNG-EPLQDYTLGKpTKLTyDFAHHVLIDWE---KRLSGKIGQSVKQKLPllgtKPST 287
Cdd:TIGR02254  97 QLLPGAFELMENlqqkfRLYIVTNGvRETQYKRLRK-SGLF-PFFDDIFVSEDagiQKPDKEIFNYALERMP----KFSK 170

                          90       100
                  ....*....|....*....|....*....
gi 6322923    288 SpfhAVFMVGDNPASDIIGAQNYGWNSCL 316
Cdd:TIGR02254 171 E---EVLMIGDSLTADIKGGQNAGLDTCW 196
 
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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