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Conserved domains on  [gi|118601009|ref|NP_067524|]
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bifunctional polynucleotide phosphatase/kinase isoform a [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PNK-3'Pase super family cl31131
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 3-522 0e+00

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


The actual alignment was detected with superfamily member TIGR01663:

Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 818.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009    3 QLGSRGRLWLQS----PTGGPPPIFLPSDGQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGVQE 78
Cdd:TIGR01663   2 EVEAAGKDVAARictlKPGEAEHHFIHLDAGALFLGRGPETGIRDRKCSKRQIELQADLEKATVALKQLGVNPCGTGGLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009   79 LKPGLSGSLSLGDVLYLVNGLYPLTLRWEELSTSGSQPDAPPDTP-GDPEEGEDTEPQKKRVRKSSLGWESLKKLLVFTA 157
Cdd:TIGR01663  82 LKPGGEGELGHGDLLEIVNGLHPLTLQFEETFNPEPEPDKEKAEPlSSQDEKRDAEKPEKRDRKGNPGWENLEKLLIFTA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  158 SGVKPQGKVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKGKVEA 237
Cdd:TIGR01663 162 AGVKGQEKIAGFDLDGTIIKTKSGKVFPKGPDDWQIIFPEIPEKLKELEADGFKICIFTNQGGIARGKINADDFKAKIEA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  238 VLEKLGVPFQVLVATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRLAN-WAPGRKKKDFSCADRLFALNV 316
Cdd:TIGR01663 242 IVAKLGVPFQVFIAIGAGFYRKPLTGMWDHLKEEANDGTEIQEDDCFFVGDAAGRPANgKAAGKKKKDFSCADRLFAANL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  317 GLPFATPEEFFLKWPAARFELPAFDPRTISSAGPLYLPESSSLLSPNPEVVVAVGFPGAGKSTFIQEHLVSAGYVHVNRD 396
Cdd:TIGR01663 322 GIPFATPEEFFLGKPAAGFEKPAFDPRSVQDQGPLCDPDDLALDDAPCEMVIAVGFPGAGKSHFCKKFFQPAGYKHVNAD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  397 TLGSWQRCVSSCQAALRQGKRVVIDNTNPDVPSRARYIQCAKDAGVPCRCFNFCATIEQARHNNRFREMTDPSHAPVSDM 476
Cdd:TIGR01663 402 TLGSTQNCLTACERALDQGKRCAIDNTNPDAASRAKFLQCARAAGIPCRCFLFNAPLAQAKHNIAFRELSDSAHIKIKDM 481

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 118601009  477 VMFSYRKQFEPPTLAEGFLEILEIPFRlQEHLDPALQRLYRQFSEG 522
Cdd:TIGR01663 482 VFNGMKKKFEAPALAEGFIAIHEINFK-PLFADEKLEKLYCMFLEE 526
 
Name Accession Description Interval E-value
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 3-522 0e+00

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 818.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009    3 QLGSRGRLWLQS----PTGGPPPIFLPSDGQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGVQE 78
Cdd:TIGR01663   2 EVEAAGKDVAARictlKPGEAEHHFIHLDAGALFLGRGPETGIRDRKCSKRQIELQADLEKATVALKQLGVNPCGTGGLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009   79 LKPGLSGSLSLGDVLYLVNGLYPLTLRWEELSTSGSQPDAPPDTP-GDPEEGEDTEPQKKRVRKSSLGWESLKKLLVFTA 157
Cdd:TIGR01663  82 LKPGGEGELGHGDLLEIVNGLHPLTLQFEETFNPEPEPDKEKAEPlSSQDEKRDAEKPEKRDRKGNPGWENLEKLLIFTA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  158 SGVKPQGKVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKGKVEA 237
Cdd:TIGR01663 162 AGVKGQEKIAGFDLDGTIIKTKSGKVFPKGPDDWQIIFPEIPEKLKELEADGFKICIFTNQGGIARGKINADDFKAKIEA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  238 VLEKLGVPFQVLVATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRLAN-WAPGRKKKDFSCADRLFALNV 316
Cdd:TIGR01663 242 IVAKLGVPFQVFIAIGAGFYRKPLTGMWDHLKEEANDGTEIQEDDCFFVGDAAGRPANgKAAGKKKKDFSCADRLFAANL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  317 GLPFATPEEFFLKWPAARFELPAFDPRTISSAGPLYLPESSSLLSPNPEVVVAVGFPGAGKSTFIQEHLVSAGYVHVNRD 396
Cdd:TIGR01663 322 GIPFATPEEFFLGKPAAGFEKPAFDPRSVQDQGPLCDPDDLALDDAPCEMVIAVGFPGAGKSHFCKKFFQPAGYKHVNAD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  397 TLGSWQRCVSSCQAALRQGKRVVIDNTNPDVPSRARYIQCAKDAGVPCRCFNFCATIEQARHNNRFREMTDPSHAPVSDM 476
Cdd:TIGR01663 402 TLGSTQNCLTACERALDQGKRCAIDNTNPDAASRAKFLQCARAAGIPCRCFLFNAPLAQAKHNIAFRELSDSAHIKIKDM 481

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 118601009  477 VMFSYRKQFEPPTLAEGFLEILEIPFRlQEHLDPALQRLYRQFSEG 522
Cdd:TIGR01663 482 VFNGMKKKFEAPALAEGFIAIHEINFK-PLFADEKLEKLYCMFLEE 526
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 165-327 1.29e-94

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. 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: 319766  Cd Length: 154  Bit Score: 284.24  E-value: 1.29e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 165 KVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKGKVEAVLEKLGV 244
Cdd:cd01625    1 KVAAFDLDGTLIKTKSGKVFPTNASDWQILYPSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTPEVFKGKIEAILEKLGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 245 PFQVLVATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRlanwapgrkKKDFSCADRLFALNVGLPFATPE 324
Cdd:cd01625   81 PIQVYAATKKGKYRKPVTGMWDHLKEDLNSGIPINLKDSFYVGDAAGR---------PKDFSDSDRLFAENVGLKFFTPE 151


                 ...
gi 118601009 325 EFF 327
Cdd:cd01625  152 EFF 154
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 165-327 1.83e-87

Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin.


Pssm-ID: 370030  Cd Length: 161  Bit Score: 266.05  E-value: 1.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  165 KVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGR-GKLPAEVFKGKVEAVLEKLG 243
Cdd:pfam08645   1 KIAAFDLDGTLIKTKSGKVFPRNPDDWKWLYPSVPEKLKKLHEDGYKIVIFTNQGGIGRkGKKSLEKFKNKIEAILKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  244 VPFQVLVATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRLanwAPGRKKKDFSCADRLFALNVGLPFATP 323
Cdd:pfam08645  81 VPLQVYAATKKDIYRKPNTGMWDEMKKDYNDGVEIDLEKSFYVGDAAGRP---YDTRRKKDFSDSDRKFALNVGIKFKTP 157


                  ....
gi 118601009  324 EEFF 327
Cdd:pfam08645 158 EEFF 161
COG4639 COG4639
Predicted kinase [General function prediction only];
364-498 2.14e-17

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 79.10  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 364 PEVVVAVGFPGAGKSTFIQEHL-----VSA----GYVHVNRDTLGSWQRCV----SSCQAALRQGKRVVIDNTNPDVPSR 430
Cdd:COG4639    2 LSLVVLIGLPGSGKSTFARRLFaptevVSSddirALLGGDENDQSAWGDVFqlahEIARARLRAGRLTVVDATNLQREAR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118601009 431 ARYIQCAKDAGVPCRCFNFCATIEQARHNNRFREmtdpshAPVSDMVMFSYRKQFE-PPTLAEGFLEIL 498
Cdd:COG4639   82 RRLLALARAYGALVVAVVLDVPLEVCLARNAARD------RQVPEEVIRRMLRRLRrPPLPEEGFRVVY 144
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
170-293 8.39e-07

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 49.43  E-value: 8.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 170 DLDGTLITTRSGkvFPTSPSDWRIlypeIPKKLQ---ELAAEGYKLVIFTNQMGIGRGKLPAEVFkgkvEAVLEKL---- 242
Cdd:PRK08942   9 DRDGVINVDSDG--YVKSPDEWIP----IPGSIEaiaRLKQAGYRVVVATNQSGIARGLFTEAQL----NALHEKMdwsl 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 118601009 243 ---GVPFQVLV----ATHAGLN-RKPVSGMWdhlqEQANEGIPISVEDSVFVGDAAGRL 293
Cdd:PRK08942  79 adrGGRLDGIYycphHPEDGCDcRKPKPGML----LSIAERLNIDLAGSPMVGDSLRDL 133
 
Name Accession Description Interval E-value
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 3-522 0e+00

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 818.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009    3 QLGSRGRLWLQS----PTGGPPPIFLPSDGQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGVQE 78
Cdd:TIGR01663   2 EVEAAGKDVAARictlKPGEAEHHFIHLDAGALFLGRGPETGIRDRKCSKRQIELQADLEKATVALKQLGVNPCGTGGLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009   79 LKPGLSGSLSLGDVLYLVNGLYPLTLRWEELSTSGSQPDAPPDTP-GDPEEGEDTEPQKKRVRKSSLGWESLKKLLVFTA 157
Cdd:TIGR01663  82 LKPGGEGELGHGDLLEIVNGLHPLTLQFEETFNPEPEPDKEKAEPlSSQDEKRDAEKPEKRDRKGNPGWENLEKLLIFTA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  158 SGVKPQGKVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKGKVEA 237
Cdd:TIGR01663 162 AGVKGQEKIAGFDLDGTIIKTKSGKVFPKGPDDWQIIFPEIPEKLKELEADGFKICIFTNQGGIARGKINADDFKAKIEA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  238 VLEKLGVPFQVLVATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRLAN-WAPGRKKKDFSCADRLFALNV 316
Cdd:TIGR01663 242 IVAKLGVPFQVFIAIGAGFYRKPLTGMWDHLKEEANDGTEIQEDDCFFVGDAAGRPANgKAAGKKKKDFSCADRLFAANL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  317 GLPFATPEEFFLKWPAARFELPAFDPRTISSAGPLYLPESSSLLSPNPEVVVAVGFPGAGKSTFIQEHLVSAGYVHVNRD 396
Cdd:TIGR01663 322 GIPFATPEEFFLGKPAAGFEKPAFDPRSVQDQGPLCDPDDLALDDAPCEMVIAVGFPGAGKSHFCKKFFQPAGYKHVNAD 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  397 TLGSWQRCVSSCQAALRQGKRVVIDNTNPDVPSRARYIQCAKDAGVPCRCFNFCATIEQARHNNRFREMTDPSHAPVSDM 476
Cdd:TIGR01663 402 TLGSTQNCLTACERALDQGKRCAIDNTNPDAASRAKFLQCARAAGIPCRCFLFNAPLAQAKHNIAFRELSDSAHIKIKDM 481

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 118601009  477 VMFSYRKQFEPPTLAEGFLEILEIPFRlQEHLDPALQRLYRQFSEG 522
Cdd:TIGR01663 482 VFNGMKKKFEAPALAEGFIAIHEINFK-PLFADEKLEKLYCMFLEE 526
DNA-3'-Pase TIGR01664
DNA 3'-phosphatase; This model represents a family of proteins and protein domains which ...
 152-328 3.02e-95

DNA 3'-phosphatase; This model represents a family of proteins and protein domains which catalyze the dephosphorylation of DNA 3'-phosphates. It is believed that this activity is important for the repair of single-strand breaks in DNA caused by radiation or oxidative damage. This domain is often (TIGR01663), but not always linked to a DNA 5'-kinase domain. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is usually replaced by an arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Alternatively, there is an additional conserved aspartate downstream of the ususal site which may indicate slightly different fold in this region.


Pssm-ID: 211680  Cd Length: 166  Bit Score: 286.27  E-value: 3.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  152 LLVFTASGVKPQGKVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVF 231
Cdd:TIGR01664   1 LFVFTADGPKPQSKVAAFDLDGTLITTRSGKVFPTSASDWRFLYPEIPAKLQELDDEGYKIVIFTNQSGIGRGKLSAESF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  232 KGKVEAVLEKLGVPFQVLVATHAGLNRKPVSGMWDHLQEQANEgiPISVEDSVFVGDAAGRlanwapgrkKKDFSCADRL 311
Cdd:TIGR01664  81 KNKIEAFLEKLKVPIQVLAATHAGLYRKPMTGMWEYLQSQYNS--PIKMTRSFYVGDAAGR---------KLDFSDADIK 149

                         170
                  ....*....|....*..
gi 118601009  312 FALNVGLPFATPEEFFL 328
Cdd:TIGR01664 150 FAKNLGLEFKYPEEFFL 166
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 165-327 1.29e-94

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. 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: 319766  Cd Length: 154  Bit Score: 284.24  E-value: 1.29e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 165 KVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKGKVEAVLEKLGV 244
Cdd:cd01625    1 KVAAFDLDGTLIKTKSGKVFPTNASDWQILYPSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTPEVFKGKIEAILEKLGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 245 PFQVLVATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRlanwapgrkKKDFSCADRLFALNVGLPFATPE 324
Cdd:cd01625   81 PIQVYAATKKGKYRKPVTGMWDHLKEDLNSGIPINLKDSFYVGDAAGR---------PKDFSDSDRLFAENVGLKFFTPE 151


                 ...
gi 118601009 325 EFF 327
Cdd:cd01625  152 EFF 154
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 165-327 1.83e-87

Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin.


Pssm-ID: 370030  Cd Length: 161  Bit Score: 266.05  E-value: 1.83e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  165 KVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGR-GKLPAEVFKGKVEAVLEKLG 243
Cdd:pfam08645   1 KIAAFDLDGTLIKTKSGKVFPRNPDDWKWLYPSVPEKLKKLHEDGYKIVIFTNQGGIGRkGKKSLEKFKNKIEAILKKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  244 VPFQVLVATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRLanwAPGRKKKDFSCADRLFALNVGLPFATP 323
Cdd:pfam08645  81 VPLQVYAATKKDIYRKPNTGMWDEMKKDYNDGVEIDLEKSFYVGDAAGRP---YDTRRKKDFSDSDRKFALNVGIKFKTP 157


                  ....
gi 118601009  324 EEFF 327
Cdd:pfam08645 158 EEFF 161
FHA_PNKP cd22736
forkhead associated (FHA) domain found in bifunctional polynucleotide phosphatase/kinase (PNKP) ...
 9-108 3.26e-56

forkhead associated (FHA) domain found in bifunctional polynucleotide phosphatase/kinase (PNKP) and similar proteins; PNKP (EC 3.1.3.32/EC 2.7.1.78), also called DNA 5'-kinase/3'-phosphatase, or polynucleotide kinase-3'-phosphatase, plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNKP ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. PNKP contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438788  Cd Length: 99  Bit Score: 183.06  E-value: 3.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009   9 RLWLQSPTGGPPPIFLPsDGQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGVQELKPGLSGSLS 88
Cdd:cd22736    1 RCWLVSVDGGHPPIFLP-DGQALVLGRGPETRVTDRKCSRTQVELVADYESRTVAVTQLGVNPSSVGEQELKPGLSGSLK 79

                         90       100
                 ....*....|....*....|
gi 118601009  89 LGDVLYLVNGLYPLTLRWEE 108
Cdd:cd22736   80 EGQTLYLVNGLYPLTLRFEE 99
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 165-309 2.23e-47

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 161.03  E-value: 2.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  165 KVAAFDLDGTLITtrsgKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPaEVFKGKVEAVLEKLGV 244
Cdd:TIGR01662   1 KAVVLDLDGTLTD----DVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFS-RSFSGRVARRLEELGV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118601009  245 PFQVLVAthAGLNRKPVSGMWDHLQEQANEgipISVEDSVFVGDAAGRLANWAPGRKKKDFSCAD 309
Cdd:TIGR01662  76 PIDILYA--CPGCRKPKPGMFLEALKRFNE---IDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
FHA_APTX_PNKP cd22716
forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase ...
 11-108 4.13e-40

forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase/kinase (PNKP), and similar proteins; The subfamily includes aprataxin and PNKP. Aprataxin (EC 3.6.1.71/EC 3.6.1.72), also called forkhead-associated domain histidine triad-like protein (FHA-HIT), is a DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair, and base excision repair. It catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. It can also hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, it catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA but has higher specific activity with 5'-linked adenosine (AppDNA). PNKP (EC 3.1.3.32/EC 2.7.1.78), also called DNA 5'-kinase/3'-phosphatase, or polynucleotide kinase-3'-phosphatase, plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNKP ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. Both aprataxin and PNKP contain an FHA domain at their N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438768 [Multi-domain]  Cd Length: 97  Bit Score: 140.11  E-value: 4.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  11 WLQSPTGGPPPIFLPsDGQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGVQELKPGLSGSLSLG 90
Cdd:cd22716    1 ILVCCSSSHPPIPLP-DGVPVILGRGPQTQITDKRCSRQQVELTANYEKRYVLVKQLGPNPSSVGGKLLEKGDEAELSPG 79

                         90
                 ....*....|....*...
gi 118601009  91 DVLYLVNGLYPLTLRWEE 108
Cdd:cd22716   80 ETLHLLNGKYPHTVYFEG 97
FHA_2 pfam17913
FHA domain; This entry represents a divergent FHA domain which in PNK binds to phosphorylated ...
 11-107 6.99e-39

FHA domain; This entry represents a divergent FHA domain which in PNK binds to phosphorylated segment of XRCC1.


Pssm-ID: 436135 [Multi-domain]  Cd Length: 97  Bit Score: 137.04  E-value: 6.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009   11 WLQSPTGGPPPIFLPsDGQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGVQELKPGLSGSLSLG 90
Cdd:pfam17913   2 YLVSLEGTHPPIPLP-HGQPVVIGRGPETGITDKKCSRNQVELKADCEKRYVKVKQLGANPSGLNGFKLKKGESYELKHG 80

                          90
                  ....*....|....*..
gi 118601009   91 DVLYLVNGLYPLTLRWE 107
Cdd:pfam17913  81 DVLELLNGKHPHRVEFN 97
FHA_APTX-like cd22671
forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase ...
 11-105 2.25e-25

forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase/kinase (PNKP), aprataxin and PNK-like factor (APLF), and similar proteins; The family includes aprataxin, PNKP, and APLF. Aprataxin (EC 3.6.1.71/EC 3.6.1.72), also called forkhead-associated domain histidine triad-like protein (FHA-HIT), is a DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair, and base excision repair. It catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. It can also hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, it catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA but has higher specific activity with 5'-linked adenosine (AppDNA). PNKP (EC 3.1.3.32/EC 2.7.1.78), also called DNA 5'-kinase/3'-phosphatase, or polynucleotide kinase-3'-phosphatase, plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNKP ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. APLF, also called apurinic-apyrimidinic endonuclease APLF, PNK and APTX-like FHA domain-containing protein, or XRCC1-interacting protein 1 (XIP1), is a novel apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease with conserved zinc-finger-like motifs involved in single-strand and double-strand DNA break repair. It is recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. It can introduce nicks at hydroxyuracil and other types of pyrimidine base damage. Together with PARP3, APLF promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). Members of this family contain an FHA domain at their N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438723 [Multi-domain]  Cd Length: 101  Bit Score: 100.08  E-value: 2.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  11 WLQSPTGGP-PPIFLPsDGQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGV-----QELKPGLS 84
Cdd:cd22671    1 FLRPVDGGGgPPIELK-EGGPTVLGRGPLLGIRDKRVSRKQAEITVDDDTGSVTVTQLGTNPSFVNRadgegKVLKKGES 79

                         90       100
                 ....*....|....*....|.
gi 118601009  85 GSLSLGDVLYLVNGLYPLTLR 105
Cdd:cd22671   80 VELKDGDVISLLPGKYPFRVE 100
FHA_APTX cd22735
forkhead associated (FHA) domain found in aprataxin and similar proteins; Aprataxin (EC 3.6.1. ...
 11-108 9.78e-24

forkhead associated (FHA) domain found in aprataxin and similar proteins; Aprataxin (EC 3.6.1.71/EC 3.6.1.72), also called forkhead-associated domain histidine triad-like protein (FHA-HIT), is a DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair, and base excision repair. It catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. It can also hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, it catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA but has higher specific activity with 5'-linked adenosine (AppDNA). Mutations in the gene APTX have been associated with ataxia-ocular apraxia. Aprataxin contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438787  Cd Length: 100  Bit Score: 95.63  E-value: 9.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  11 WLQSPTGGPPPIFLPSDgQALVLGRGPLTQVTDRKCSRNQVELIADPESRTVAVKQLGVNPSTVGVQELKPGLSGSLSLG 90
Cdd:cd22735    4 WLVSKDGRHLRIRLPHL-EAVVIGRGPETKITDKKCSRHQVQLKADCNKGYVKVKQLGVNPTSIDLVDIGKDEEVKLKPG 82

                         90
                 ....*....|....*...
gi 118601009  91 DVLYLVNGLYPLTLRWEE 108
Cdd:cd22735   83 QVLHIVNQLYPYIVEFEE 100
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 366-488 1.30e-21

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 90.83  E-value: 1.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  366 VVVAVGFPGAGKSTFIQEHLVSAGYVHVNRDTL-----------GSWQRCVSS---------CQAALRQGKRVVIDNTNP 425
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELGAVRLSSDDErkrlfgegrpsISYYTDATDrtyerlhelARIALRAGRPVILDATNL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118601009  426 DVPSRARYIQCAKDAGVPCRCFNFCATIEQARHNNRFREMTDPSHAPVSDMVMFSYRKQFEPP 488
Cdd:pfam13671  81 RRDERARLLALAREYGVPVRIVVFEAPEEVLRERLAARARAGGDPSDVPEEVLDRQKARFEPP 143
COG4639 COG4639
Predicted kinase [General function prediction only];
364-498 2.14e-17

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 79.10  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 364 PEVVVAVGFPGAGKSTFIQEHL-----VSA----GYVHVNRDTLGSWQRCV----SSCQAALRQGKRVVIDNTNPDVPSR 430
Cdd:COG4639    2 LSLVVLIGLPGSGKSTFARRLFaptevVSSddirALLGGDENDQSAWGDVFqlahEIARARLRAGRLTVVDATNLQREAR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118601009 431 ARYIQCAKDAGVPCRCFNFCATIEQARHNNRFREmtdpshAPVSDMVMFSYRKQFE-PPTLAEGFLEIL 498
Cdd:COG4639   82 RRLLALARAYGALVVAVVLDVPLEVCLARNAARD------RQVPEEVIRRMLRRLRrPPLPEEGFRVVY 144
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 169-288 1.52e-15

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 74.36  E-value: 1.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 169 FDLDGTLITtRSGKVfpTSPSDWRiLYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKG---KVEAVLEKLGVP 245
Cdd:COG0241    8 LDRDGTINE-DVGYV--KSPEEFE-FLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAvhaKMLELLAAEGGR 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 118601009 246 F-QVLVATHAG----LNRKPVSGMWDHLQEQANegipISVEDSVFVGD 288
Cdd:COG0241   84 IdAIYYCPHHPddncDCRKPKPGMLLQAAERLG----IDLSNSYMIGD 127
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 165-298 2.37e-11

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 61.39  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 165 KVAAFDLDGTLITTRsgkVFPTSPSDWrILYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKG---KVEAVLEK 241
Cdd:cd07503    1 KALFLDRDGVINVDV---PYVHKPEDL-EFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEAlhdKMRELLAS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118601009 242 LGVPF-QVLVATHA----GLNRKPVSGMWdhlqEQANEGIPISVEDSVFVGDA-----AGRLANWAP 298
Cdd:cd07503   77 QGVEIdDIYYCPHHpddgCPCRKPKPGML----LDAAKELGIDLARSFVIGDRlsdiqAARNAGCKG 139
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 169-267 2.16e-10

histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.


Pssm-ID: 273737  Cd Length: 147  Bit Score: 58.95  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  169 FDLDGTLITTRSGKvFPTSPSDWRiLYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAE---VFKGKVEAVLEKLGVP 245
Cdd:TIGR01656   5 LDRDGVINEDTVSD-YPRSLDDWQ-LRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEafrAPNGRLLELLRQLGVA 82

                          90       100
                  ....*....|....*....|....*..
gi 118601009  246 FQ-VLVATH--AGLN--RKPVSGMWDH 267
Cdd:TIGR01656  83 VDgVLFCPHhpADNCscRKPKPGLILE 109
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
366-515 3.72e-10

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 58.77  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 366 VVVAVGFPGAGKSTF---IQEHLvsaGYVHVNRDT-----LGSW---------------QRCVSSCQAALRQGKRVVIDN 422
Cdd:COG0645    1 LILVCGLPGSGKSTLaraLAERL---GAVRLRSDVvrkrlFGAGlaplerspeatartyARLLALARELLAAGRSVILDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 423 TNPDVPSRARYIQCAKDAGVPCRCFNFCATIEQARHNNRFR-EMTDPSHApvSDMVMFSYRKQFEPPTLAEGFLEILEip 501
Cdd:COG0645   78 TFLRRAQREAFRALAEEAGAPFVLIWLDAPEEVLRERLEARnAEGGDSDA--TWEVLERQLAFEEPLTEDEGFLLVVD-- 153

                        170
                 ....*....|....
gi 118601009 502 frlQEHLDPALQRL 515
Cdd:COG0645  154 ---TSGLEEALAAL 164
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 166-296 1.31e-07

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All 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. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 49.70  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 166 VAAFDLDGTLITTRSgkvfptspsdwrilypeipkkLQELAAEGYKLVIFTNQmgigrgklpaevFKGKVEAVLEKLGVP 245
Cdd:cd01427    1 AVLFDLDGTLLAVEL---------------------LKRLRAAGIKLAIVTNR------------SREALRALLEKLGLG 47

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118601009 246 --FQVLVATHAGLNRKPVSGMWDHLQEQANegipISVEDSVFVGD-----AAGRLANW 296
Cdd:cd01427   48 dlFDGIIGSDGGGTPKPKPKPLLLLLLKLG----VDPEEVLFVGDsendiEAARAAGG 101
HAD-SF-IIIC TIGR01681
HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the ...
 165-214 8.16e-07

HAD-superfamily phosphatase, subfamily IIIC; This model represents the IIIC subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. Subfamily III (also including IIIA - TIGR01662 and IIIB - pfam03767) contains sequences which do not contain either of the insert domains (between the 1st and 2nd conserved catalytic motifs, subfamily I - TIGR01493, TIGR01509, TIGR01549, TIGR01488, TIGR01494, TIGR01658, TIGR01544 and TIGR01545, or between the 2nd and 3rd, subfamily II - TIGR01460 and TIGR01484). Subfamily IIIC contains five relatively distantly related clades: a family of viral proteins (TIGR01684), a family of eukaryotic proteins called MDP-1 and a family of archaeal proteins most closely related to MDP-1 (TIGR01685), a family of bacteria including the Streptomyces FkbH protein (TIGR01686), and a small clade including the Pasteurella BcbF and EcbF proteins. The overall lack of species overlap among these clades may indicate a conserved function, but the degree of divergence between the clades and the differences in archetecture outside of the domain in some clades warns against such a conclusion. No member of this subfamily is characterized with respect to function, however the MDP-1 protein is a characterized phosphatase. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in subfamily IIIC.


Pssm-ID: 273752 [Multi-domain]  Cd Length: 128  Bit Score: 48.19  E-value: 8.16e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 118601009  165 KVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVI 214
Cdd:TIGR01681   1 KVIVFDLDNTLWTGENIVVGEDPIIDLEVTIKEIRDKLQTLKKNGFLLAL 50
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
170-293 8.39e-07

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 49.43  E-value: 8.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 170 DLDGTLITTRSGkvFPTSPSDWRIlypeIPKKLQ---ELAAEGYKLVIFTNQMGIGRGKLPAEVFkgkvEAVLEKL---- 242
Cdd:PRK08942   9 DRDGVINVDSDG--YVKSPDEWIP----IPGSIEaiaRLKQAGYRVVVATNQSGIARGLFTEAQL----NALHEKMdwsl 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 118601009 243 ---GVPFQVLV----ATHAGLN-RKPVSGMWdhlqEQANEGIPISVEDSVFVGDAAGRL 293
Cdd:PRK08942  79 adrGGRLDGIYycphHPEDGCDcRKPKPGML----LSIAERLNIDLAGSPMVGDSLRDL 133
pseT PHA02530
polynucleotide kinase; Provisional
 364-485 9.26e-07

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 50.79  E-value: 9.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 364 PEVVVAVGFPGAGKSTFIQEHL-VSAGYVHVNRDTL-------GSW---------QRCVSSCQ-----AALRQGKRVVID 421
Cdd:PHA02530   2 MKIILTVGVPGSGKSTWAREFAaKNPKAVNVNRDDLrqslfghGEWgeykftkekEDLVTKAQeaaalAALKSGKSVIIS 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118601009 422 NTNPdVPSRARYIQ-CAKDAGVPCRCFNFCATIEQARHNNRFR-EMTDPSHAPVSdmvMFSYRKQF 485
Cdd:PHA02530  82 DTNL-NPERRRKWKeLAKELGAEFEEKVFDVPVEELVKRNRKRgERAVPEDVLRS---MFKQMKEY 143
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 170-288 1.43e-06

histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the scope of this model are bifunctional proteins with a histidinol phosphatase domain followed by an imidazoleglycerol-phosphate dehydratase domain. These enzymatic domains catalyze the ninth and seventh steps, respectively, of histidine biosynthesis. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 130328 [Multi-domain]  Cd Length: 161  Bit Score: 48.17  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  170 DLDGTLITTrsgkvfptSPSDWRI-------LYPEIPKKLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKG---KVEAVL 239
Cdd:TIGR01261   7 DRDGTLIEE--------PPSDFQVdaleklrFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGphnLMLQIF 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118601009  240 EKLGVPFQ-VLVATH----AGLNRKPVSGMWDH-LQEQAnegipISVEDSVFVGD 288
Cdd:TIGR01261  79 RSQGIIFDdVLICPHfpddNCDCRKPKIKLLEPyLKKNL-----IDKARSYVIGD 128
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 194-288 1.74e-06

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: 48.87  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 194 LYPEIPKKLQELAAEGYKLVIFTNQmgigrgklPAEVFkgkvEAVLEKLGV--PFQ-VLVATHAGLnRKPVSGMWDHLQE 270
Cdd:COG1011   94 PYPDALELLEALKARGYRLALLTNG--------SAELQ----EAKLRRLGLddLFDaVVSSEEVGV-RKPDPEIFELALE 160

                         90
                 ....*....|....*...
gi 118601009 271 QANegipISVEDSVFVGD 288
Cdd:COG1011  161 RLG----VPPEEALFVGD 174
FHA_APLF cd22717
forkhead associated (FHA) domain found in aprataxin and PNK-like factor (APLF) and similar ...
 15-81 4.84e-05

forkhead associated (FHA) domain found in aprataxin and PNK-like factor (APLF) and similar proteins; APLF, also called apurinic-apyrimidinic endonuclease APLF, PNK and APTX-like FHA domain-containing protein, or XRCC1-interacting protein 1 (XIP1), is a novel apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease with conserved zinc-finger-like motifs involved in single-strand and double-strand DNA break repair. It is recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. It can introduce nicks at hydroxyuracil and other types of pyrimidine base damage. Together with PARP3, APLF promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). APLF contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438769 [Multi-domain]  Cd Length: 99  Bit Score: 42.27  E-value: 4.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  15 PTGGPPPIFLPSDgqALVLGRGPLTQVTDRKCSRNQVELiaDPESRTVAVKQLGVNP---STVGVQELKP 81
Cdd:cd22717    6 PVDGGKRIELPPG--ETTIGRGPFLGITDKRVSRNHAIL--EVVDGKLRIKPTHTNPcfyQPSGKSKLIP 71
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
170-288 5.86e-05

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 45.17  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 170 DLDGTLITTrsgkvfPtsPSDWRI-------LYPE-IP--KKLQELaaeGYKLVIFTNQMGIGRGKLPAEVFKG---KVE 236
Cdd:PRK05446   8 DRDGTLIEE------P--PTDFQVdsldklaFEPGvIPalLKLQKA---GYKLVMVTNQDGLGTDSFPQEDFDPphnLMM 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118601009 237 AVLEKLGVPF-QVLVATH----AGLNRKPVSGMwdhLQEQANEGiPISVEDSVFVGD 288
Cdd:PRK05446  77 QIFESQGIKFdEVLICPHfpedNCSCRKPKTGL---VEEYLAEG-AIDLANSYVIGD 129
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
194-321 1.98e-04

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 42.61  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 194 LYPEIPKKLQELAAEGYKLVIFTNqmgigrgKLPAEvfkgkVEAVLEKLGV--PFQVLVATHAGLNRKPVSGMWDHLQEQ 271
Cdd:COG0546   85 LFPGVRELLEALKARGIKLAVVTN-------KPREF-----AERLLEALGLddYFDAIVGGDDVPPAKPKPEPLLEALER 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 118601009 272 ANegipISVEDSVFVGDaagrlanwapgrkkkdfSCADRLFALNVGLPFA 321
Cdd:COG0546  153 LG----LDPEEVLMVGD-----------------SPHDIEAARAAGVPFI 181
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 168-256 8.66e-04

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 40.83  E-value: 8.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009  168 AFDLDGTLIttrsgkvfptsPSDWRILYPEIPKKLQELAAEGYKLVIFTnqmgigrGKLPAEvfkgkVEAVLEKLGVPFq 247
Cdd:TIGR01484   3 FFDLDGTLL-----------DPNAHELSPETIEALERLREAGVKVVIVT-------GRSLAE-----IKELLKQLNLPL- 58


                  ....*....
gi 118601009  248 VLVATHAGL 256
Cdd:TIGR01484  59 PLIAENGAL 67
PRK06769 PRK06769
HAD-IIIA family hydrolase;
170-264 1.99e-03

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 39.33  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 170 DLDGTLittrSGKVFPTSPSDWRiLYPEIPKKLQELAAEGYKLVIFTNQMGIGRGklpaEVFKGKVEAVLEKLGVPfQVL 249
Cdd:PRK06769  10 DRDGTI----GGDTTIHYPGSFT-LFPFTKASLQKLKANHIKIFSFTNQPGIADG----IATIADFVQELKGFGFD-DIY 79

                         90
                 ....*....|....*....
gi 118601009 250 VATH---AGLN-RKPVSGM 264
Cdd:PRK06769  80 LCPHkhgDGCEcRKPSTGM 98
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 153-339 2.46e-03

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 39.61  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 153 LVFTASGVKPQGKVAAFDLDGTLittrsgKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVIFTNQmgigrgklPAevfk 232
Cdd:cd07512   52 RAFAAAGEDLDGPLHDALLARFL------DHYEADPPGLTRPYPGVIEALERLRAAGWRLAICTNK--------PE---- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 233 GKVEAVLEKLGV--PFQVLVATHAGLNRKPVSGMWDHLQEQANEGipisVEDSVFVGDaagrlanwapgrkkkdfSCADR 310
Cdd:cd07512  114 APARALLSALGLadLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGD----VSRALMVGD-----------------SETDA 172

                        170       180
                 ....*....|....*....|....*....
gi 118601009 311 LFALNVGLPFATPEEFFLKWPAArfELPA 339
Cdd:cd07512  173 ATARAAGVPFVLVTFGYRHAPVA--ELPH 199
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
194-295 3.19e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 39.02  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601009 194 LYPEIPKKLQELAAEGYKLVIFTNQMgigrgklpaEVFkgkVEAVLEKLGVP--FQVLVATHAGLNRKPVSGMWDHLQEQ 271
Cdd:PRK13222  94 LYPGVKETLAALKAAGYPLAVVTNKP---------TPF---VAPLLEALGIAdyFSVVIGGDSLPNKKPDPAPLLLACEK 161

                         90       100
                 ....*....|....*....|....*....
gi 118601009 272 ANegipISVEDSVFVGD-----AAGRLAN 295
Cdd:PRK13222 162 LG----LDPEEMLFVGDsrndiQAARAAG 186
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 169-247 6.04e-03

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 36.29  E-value: 6.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118601009  169 FDLDGTLIttRSGKvfptspsdwriLYPEIPKKLQELAAEGYKLVIFTNqmgiGRGKLPAEVFKgkveaVLEKLGVPFQ 247
Cdd:pfam13344   3 FDIDGVLW--RGGE-----------PIPGAAEALRALRAAGKPVVFVTN----NSSRSREEYAE-----KLRKLGFDID 59
 
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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