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Conserved domains on  [gi|1958769731|ref|XP_038963589|]
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haloacid dehalogenase-like hydrolase domain-containing 5 isoform X4 [Rattus norvegicus]

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 ...
47-315 1.55e-131

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: 378.45  E-value: 1.55e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNSQGQLQVPVVFVTNAGNILQRDKAQELSALLECKVDPDQVILSHSPMKLF 126
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 127 LQYHNKRMLVSGQGPLVENARALGFQNVVTVDDLRIAFPELD----MVDLQRRPKTmviRTRPRSDFPAIEGVLLLGEPV 202
Cdd:TIGR01456  81 VNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYS---RDIPDLTTKRFDAVLVFNDPV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 203 RWETNLQLITDVLLSNGHPGAGLATapyPHLPVLASNMDLLWMAEASMPRFGHGTFLLCLETIYRKITGHELKYEgLMGK 282
Cdd:TIGR01456 158 DWAADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGK 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958769731 283 PSILTYRYAEEVI----RQQAERRGWAAPIRKLYAIG 315
Cdd:TIGR01456 234 PTKLTYDFAEDVLidweKRLSGTKPSTSPFHALYMVG 270
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
47-315 1.55e-131

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: 378.45  E-value: 1.55e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNSQGQLQVPVVFVTNAGNILQRDKAQELSALLECKVDPDQVILSHSPMKLF 126
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 127 LQYHNKRMLVSGQGPLVENARALGFQNVVTVDDLRIAFPELD----MVDLQRRPKTmviRTRPRSDFPAIEGVLLLGEPV 202
Cdd:TIGR01456  81 VNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYS---RDIPDLTTKRFDAVLVFNDPV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 203 RWETNLQLITDVLLSNGHPGAGLATapyPHLPVLASNMDLLWMAEASMPRFGHGTFLLCLETIYRKITGHELKYEgLMGK 282
Cdd:TIGR01456 158 DWAADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGK 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958769731 283 PSILTYRYAEEVI----RQQAERRGWAAPIRKLYAIG 315
Cdd:TIGR01456 234 PTKLTYDFAEDVLidweKRLSGTKPSTSPFHALYMVG 270
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
47-124 2.66e-29

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: 109.79  E-value: 2.66e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769731  47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNsqgqLQVPVVFVTNAGNILQRDKAQELSALLECKVDPDQVILSHSPMK 124
Cdd:cd07511     1 FGFAFDIDGVLVRGKKPIPGAPKALKFLND----NKIPFIFLTNGGGFPESKRADFLSKLLGVEVSPDQVIQSHSPGK 74
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
49-152 3.72e-26

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 100.23  E-value: 3.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  49 LLFDIDGVLVRGHRVIPAALEAFSKLvNSQGqlqVPVVFVTNAGNILQRDKAQELSAlLECKVDPDQVILSHSPMKLFLQ 128
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRAL-RAAG---KPVVFVTNNSSRSREEYAEKLRK-LGFDIDEDEIITSGTAAADYLK 75
                          90       100
                  ....*....|....*....|....*.
gi 1958769731 129 --YHNKRMLVSGQGPLVENARALGFQ 152
Cdd:pfam13344  76 erKFGKKVLVIGSEGLREELEEAGFE 101
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
48-301 1.20e-11

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 63.97  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  48 GLLFDIDGVLVRGHRVIPAALEAFSKLVnsqgQLQVPVVFVTNAGNILQRDKAQELSAL-LEckVDPDQVILSHSPMKLF 126
Cdd:COG0647    10 AFLLDLDGVLYRGDEPIPGAVEALARLR----AAGKPVLFLTNNSSRTPEDVAEKLRRLgIP--VAEDEIVTSGDATAAY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 127 L--QYHNKRMLVSGQGPLVENARALGFqnVVTVDDlriafpeldmvdlqrrpktmvirtrprsdfpAIEGVLL-LGEPVR 203
Cdd:COG0647    84 LaeRHPGARVYVIGEEGLREELEEAGL--TLVDDE-------------------------------EPDAVVVgLDRTFT 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 204 WETnLQLITDvLLSNGhpgaglatapyphLPVLASNMDLLWMAEASmPRFGHGTFLLCLETiyrkITGHELKYeglMGKP 283
Cdd:COG0647   131 YEK-LAEALR-AIRRG-------------APFIATNPDRTVPTEDG-LIPGAGALAAALEA----ATGGEPLV---VGKP 187
                         250
                  ....*....|....*...
gi 1958769731 284 SILTYRYAEEVIRQQAER 301
Cdd:COG0647   188 SPPIYELALERLGVDPER 205
 
Name Accession Description Interval E-value
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
47-315 1.55e-131

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: 378.45  E-value: 1.55e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNSQGQLQVPVVFVTNAGNILQRDKAQELSALLECKVDPDQVILSHSPMKLF 126
Cdd:TIGR01456   1 FGFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLKIPYIFLTNGGGFSERARAEEISSLLGVDVSPLQVIQSHSPYKSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 127 LQYHNKRMLVSGQGPLVENARALGFQNVVTVDDLRIAFPELD----MVDLQRRPKTmviRTRPRSDFPAIEGVLLLGEPV 202
Cdd:TIGR01456  81 VNKYEKRILAVGTGSVRGVAEGYGFQNVVHQDEIVRYFRDIDpfsgMSDEQVMEYS---RDIPDLTTKRFDAVLVFNDPV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 203 RWETNLQLITDVLLSNGHPGAGLATapyPHLPVLASNMDLLWMAEASMPRFGHGTFLLCLETIYRKITGHELKYEgLMGK 282
Cdd:TIGR01456 158 DWAADIQIISDALNSEGLPGEKSGK---PSIPIYFSNQDLLWANEYKLNRFGQGAFRLLLERIYLELNGKPLQYY-TLGK 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958769731 283 PSILTYRYAEEVI----RQQAERRGWAAPIRKLYAIG 315
Cdd:TIGR01456 234 PTKLTYDFAEDVLidweKRLSGTKPSTSPFHALYMVG 270
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
50-303 4.80e-59

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: 190.62  E-value: 4.80e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  50 LFDIDGVLVRGHRVIPAALEAFSKLVNSQgqlqVPVVFVTNAGNILQRDKAQELSALLECKVDPDQVILSHSPMKLFL-- 127
Cdd:TIGR01460   2 LFDIDGVLWLGHKPIPGAAEALNRLRAKG----KPVVFLTNNSSRSEEDYAEKLSSLLGVDVSPDQIITSGSVTKDLLrq 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 128 QYHNKRMLVSGQGPLVENARALGFQNVVtvddlriaFPELDMVDLQRrpktmvirtrprsdfpaIEGVLLLGEPVRWETN 207
Cdd:TIGR01460  78 RFEGEKVYVIGVGELRESLEGLGFRNDF--------FDDIDHLAIEK-----------------IPAAVIVGEPSDFSYD 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 208 LQLITDVLLSNGHpgaglatapyphLPVLASNMDllwmaeaSMPRFGHGTFLLCLETIYRKITGHELKYEGLMGKPSILT 287
Cdd:TIGR01460 133 ELAKAAYLLAEGD------------VPFIAANRD-------DLVRLGDGRFRPGAGAIAAGIKELSGREPTVVGKPSPAI 193
                         250
                  ....*....|....*.
gi 1958769731 288 YRYAEEVIRQQAERRG 303
Cdd:TIGR01460 194 YRAALNLLQARPERRD 209
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
47-124 2.66e-29

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: 109.79  E-value: 2.66e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958769731  47 FGLLFDIDGVLVRGHRVIPAALEAFSKLVNsqgqLQVPVVFVTNAGNILQRDKAQELSALLECKVDPDQVILSHSPMK 124
Cdd:cd07511     1 FGFAFDIDGVLVRGKKPIPGAPKALKFLND----NKIPFIFLTNGGGFPESKRADFLSKLLGVEVSPDQVIQSHSPGK 74
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
49-152 3.72e-26

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 100.23  E-value: 3.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  49 LLFDIDGVLVRGHRVIPAALEAFSKLvNSQGqlqVPVVFVTNAGNILQRDKAQELSAlLECKVDPDQVILSHSPMKLFLQ 128
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRAL-RAAG---KPVVFVTNNSSRSREEYAEKLRK-LGFDIDEDEIITSGTAAADYLK 75
                          90       100
                  ....*....|....*....|....*.
gi 1958769731 129 --YHNKRMLVSGQGPLVENARALGFQ 152
Cdd:pfam13344  76 erKFGKKVLVIGSEGLREELEEAGFE 101
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
48-301 1.20e-11

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 63.97  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  48 GLLFDIDGVLVRGHRVIPAALEAFSKLVnsqgQLQVPVVFVTNAGNILQRDKAQELSAL-LEckVDPDQVILSHSPMKLF 126
Cdd:COG0647    10 AFLLDLDGVLYRGDEPIPGAVEALARLR----AAGKPVLFLTNNSSRTPEDVAEKLRRLgIP--VAEDEIVTSGDATAAY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 127 L--QYHNKRMLVSGQGPLVENARALGFqnVVTVDDlriafpeldmvdlqrrpktmvirtrprsdfpAIEGVLL-LGEPVR 203
Cdd:COG0647    84 LaeRHPGARVYVIGEEGLREELEEAGL--TLVDDE-------------------------------EPDAVVVgLDRTFT 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 204 WETnLQLITDvLLSNGhpgaglatapyphLPVLASNMDLLWMAEASmPRFGHGTFLLCLETiyrkITGHELKYeglMGKP 283
Cdd:COG0647   131 YEK-LAEALR-AIRRG-------------APFIATNPDRTVPTEDG-LIPGAGALAAALEA----ATGGEPLV---VGKP 187
                         250
                  ....*....|....*...
gi 1958769731 284 SILTYRYAEEVIRQQAER 301
Cdd:COG0647   188 SPPIYELALERLGVDPER 205
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
48-194 2.57e-11

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: 62.97  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  48 GLLFDIDGVLVRGHRVIPAALEAFSKLvnsqGQLQVPVVFVTNAGNILQRDKAQEL-SALLEckVDPDQVILSHSPMKLF 126
Cdd:cd07531     2 GYIIDLDGTIGKGVTLIPGAVEGVKTL----RRLGKKIIFLSNNSTRSRRILLERLrSFGIE--VGEDEILVSSYVTARF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731 127 L--QYHNKRMLVSGQGPLVENARALGFQNV----------------VTVDDLRIAFPELdmvdlqrRPKTMVIRTRPRSD 188
Cdd:cd07531    76 LarEKPNAKVFVTGEEGLIEELRLAGLEIVdkydeaeyvvvgsnrkITYELLTKAFRAC-------LRGARYIATNPDRI 148

                  ....*.
gi 1958769731 189 FPAIEG 194
Cdd:cd07531   149 FPAEDG 154
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
48-151 1.25e-08

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: 54.91  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  48 GLLFDIDGVLVRGHRVIPAALEAFSKLVNSqgqlQVPVVFVTNAGNILQRDKAQELSAlLECKVDPDQVILSHSPMKLFL 127
Cdd:cd07530     2 GYLIDLDGTVYRGGTAIPGAVEFIERLREK----GIPFLFLTNNSTRTPEDVAAKLAE-MGIDVPEEDVYTSALATAQYL 76
                          90       100
                  ....*....|....*....|....*.
gi 1958769731 128 --QYHNKRMLVSGQGPLVENARALGF 151
Cdd:cd07530    77 aeQLPGAKVYVIGEEGLRTALHEAGL 102
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
48-152 2.35e-05

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: 45.43  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958769731  48 GLLFDIDGVLVRGHRVIPAALEAFSKLvnsqGQLQVPVVFVTNAGNILQRDKAqELSALLECKVDPDQVILSHSPMKLFL 127
Cdd:cd07508     1 LVISDCDGVLWHDERAIPGAAEFLEAL----KEAGKKIVFVSNNSSRSRQDYA-EKFRKFGVDVPEDQIVTSAKATARFL 75
                          90       100
                  ....*....|....*....|....*..
gi 1958769731 128 QYH--NKRMLVSGQGPLVENARALGFQ 152
Cdd:cd07508    76 RSRkfGKKVYVLGEEGLKEELRAAGFR 102
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
48-119 2.55e-05

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: 44.96  E-value: 2.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958769731  48 GLLFDIDGVLVRGHRVIPAALEAFSKLvNSQGqlqVPVVFVTNAGNILQRDKAQELSAlLECKVDPDQVILS 119
Cdd:cd07509     2 AVLLDLSGTLYISGAAIPGAAEALKRL-RHAG---LKVRFLTNTTKESRRTLAERLQR-LGFDVSEEEIFTS 68
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
48-90 7.48e-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: 7.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958769731  48 GLLFDIDGVLVRGHRVIPAALEAFSKLVNSQGQLqvpvVFVTN 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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