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Conserved domains on  [gi|320543626|ref|NP_001188874|]
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lipin, isoform C [Drosophila melanogaster]

Protein Classification

phosphatidate phosphatase( domain architecture ID 11151321)

phosphatidate phosphatase is a magnesium-dependent enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 759-983 2.96e-148

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


:

Pssm-ID: 462403  Cd Length: 226  Bit Score: 440.41  E-value: 2.96e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   759 KSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGV 838
Cdd:pfam08235    1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   839 AQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRD 918
Cdd:pfam08235   81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320543626   919 LFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSYCSMTYIVDQLFP 983
Cdd:pfam08235  161 LFPpDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-104 6.22e-56

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


:

Pssm-ID: 461356  Cd Length: 103  Bit Score: 188.52  E-value: 6.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626     1 MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSG 80
Cdd:pfam04571    1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKLGESG 80

                           90       100
                   ....*....|....*....|....
gi 320543626    81 EAFFVeECLEDEDEELPANLATSP 104
Cdd:pfam04571   81 EAFFV-FETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 561-673 2.32e-41

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


:

Pssm-ID: 465292  Cd Length: 98  Bit Score: 146.66  E-value: 2.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   561 VAMSMCGM--SEQGAPPSDEEFDRHLVNYPDVCKSPSIFSSPNLVVRLNGKYYTWMAACPIVMTMITFQKPLTHDAIEQL 638
Cdd:pfam16876    1 VELSLCGGllQGQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320543626   639 MSQtvdgkclpgdekqeavaQADNGGQTKRYWWSW 673
Cdd:pfam16876   81 IKE-----------------ARKNPKKGRRSWFSW 98
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 759-983 2.96e-148

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 462403  Cd Length: 226  Bit Score: 440.41  E-value: 2.96e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   759 KSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGV 838
Cdd:pfam08235    1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   839 AQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRD 918
Cdd:pfam08235   81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320543626   919 LFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSYCSMTYIVDQLFP 983
Cdd:pfam08235  161 LFPpDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 807-962 9.75e-90

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 283.78  E-value: 9.75e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626    807 VVISDIDGTITKSDVLGHILPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLL 886
Cdd:smart00775    1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320543626    887 LNPTSLISAFHREVIEKKPEQFKIACLSDIRDLFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHE 962
Cdd:smart00775   81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPpQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-104 6.22e-56

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


Pssm-ID: 461356  Cd Length: 103  Bit Score: 188.52  E-value: 6.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626     1 MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSG 80
Cdd:pfam04571    1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKLGESG 80

                           90       100
                   ....*....|....*....|....
gi 320543626    81 EAFFVeECLEDEDEELPANLATSP 104
Cdd:pfam04571   81 EAFFV-FETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 561-673 2.32e-41

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


Pssm-ID: 465292  Cd Length: 98  Bit Score: 146.66  E-value: 2.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   561 VAMSMCGM--SEQGAPPSDEEFDRHLVNYPDVCKSPSIFSSPNLVVRLNGKYYTWMAACPIVMTMITFQKPLTHDAIEQL 638
Cdd:pfam16876    1 VELSLCGGllQGQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320543626   639 MSQtvdgkclpgdekqeavaQADNGGQTKRYWWSW 673
Cdd:pfam16876   81 IKE-----------------ARKNPKKGRRSWFSW 98
SMP2 COG5083
Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid ...
 806-992 1.89e-15

Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid maintenance [Lipid transport and metabolism];


Pssm-ID: 444053  Cd Length: 353  Bit Score: 79.12  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626  806 KVVISDIDGTITKSDVLGhILPMVGKDWAQL--GVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSirQGnvmLPDG 883
Cdd:COG5083   186 KTVVFDIDGTLTLNDFEG-VGDYLGGETADAhpYAAEVVQAYADKGYRPIYVTGRPYWLAKDTREWLDT--QG---LPPG 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626  884 PLLLNPTSlisafhREVIEKKPEQFKIAclsDIRDLFPDKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELkhEL 963
Cdd:COG5083   260 ILHTTPSA------TGPIGPDTARYKTA---EIQLLIDDGLNIVRAYGNAATDAEAYANAGIPKSETYIIGEDAGL--RG 328

                         170       180
                  ....*....|....*....|....*....
gi 320543626  964 TQTFQSSYcsmtyivDQLFPPVKLDEASA 992
Cdd:COG5083   329 TQRIDGDY-------SEHFATVVANTPAA 350
pseT PHA02530
polynucleotide kinase; Provisional
 803-874 3.70e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 40.78  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626  803 HNDKVVISDIDGTITKsdvlghilpMVGK---DWAQLG-------VAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRS 872
Cdd:PHA02530  156 GLPKAVIFDIDGTLAK---------MGGRspyDWTKVKedkpnpmVVELVKMYKAAGYEIIVVSGRDGVCEEDTVEWLRQ 226


                  ..
gi 320543626  873 IR 874
Cdd:PHA02530  227 TD 228
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 806-887 9.21e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. 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: 319805  Cd Length: 145  Bit Score: 37.89  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626  806 KVVISDIDGTITKSDVLGHILPMVGKDWAQLG-----------VAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIR 874
Cdd:cd07502     2 KAVIFDLDGTLADTNGRQPYLERRPRDWDAFFeaadhdppnapVIELVKESALTGYEIVYLSGRPERYRRDTLRWLAKHG 81

                          90
                  ....*....|...
gi 320543626  875 qgnvmLPDGPLLL 887
Cdd:cd07502    82 -----IPDDALHM 89
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 759-983 2.96e-148

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 462403  Cd Length: 226  Bit Score: 440.41  E-value: 2.96e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   759 KSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGV 838
Cdd:pfam08235    1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   839 AQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRD 918
Cdd:pfam08235   81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320543626   919 LFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSYCSMTYIVDQLFP 983
Cdd:pfam08235  161 LFPpDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 807-962 9.75e-90

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 283.78  E-value: 9.75e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626    807 VVISDIDGTITKSDVLGHILPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLL 886
Cdd:smart00775    1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320543626    887 LNPTSLISAFHREVIEKKPEQFKIACLSDIRDLFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHE 962
Cdd:smart00775   81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPpQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-104 6.22e-56

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


Pssm-ID: 461356  Cd Length: 103  Bit Score: 188.52  E-value: 6.22e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626     1 MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSG 80
Cdd:pfam04571    1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKLGESG 80

                           90       100
                   ....*....|....*....|....
gi 320543626    81 EAFFVeECLEDEDEELPANLATSP 104
Cdd:pfam04571   81 EAFFV-FETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 561-673 2.32e-41

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


Pssm-ID: 465292  Cd Length: 98  Bit Score: 146.66  E-value: 2.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   561 VAMSMCGM--SEQGAPPSDEEFDRHLVNYPDVCKSPSIFSSPNLVVRLNGKYYTWMAACPIVMTMITFQKPLTHDAIEQL 638
Cdd:pfam16876    1 VELSLCGGllQGQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320543626   639 MSQtvdgkclpgdekqeavaQADNGGQTKRYWWSW 673
Cdd:pfam16876   81 IKE-----------------ARKNPKKGRRSWFSW 98
SMP2 COG5083
Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid ...
 806-992 1.89e-15

Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid maintenance [Lipid transport and metabolism];


Pssm-ID: 444053  Cd Length: 353  Bit Score: 79.12  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626  806 KVVISDIDGTITKSDVLGhILPMVGKDWAQL--GVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSirQGnvmLPDG 883
Cdd:COG5083   186 KTVVFDIDGTLTLNDFEG-VGDYLGGETADAhpYAAEVVQAYADKGYRPIYVTGRPYWLAKDTREWLDT--QG---LPPG 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626  884 PLLLNPTSlisafhREVIEKKPEQFKIAclsDIRDLFPDKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELkhEL 963
Cdd:COG5083   260 ILHTTPSA------TGPIGPDTARYKTA---EIQLLIDDGLNIVRAYGNAATDAEAYANAGIPKSETYIIGEDAGL--RG 328

                         170       180
                  ....*....|....*....|....*....
gi 320543626  964 TQTFQSSYcsmtyivDQLFPPVKLDEASA 992
Cdd:COG5083   329 TQRIDGDY-------SEHFATVVANTPAA 350
APP1_cat pfam09949
Phosphatidate phosphatase APP1, catalytic domain; This entry represents a conserved region ...
 808-923 3.50e-04

Phosphatidate phosphatase APP1, catalytic domain; This entry represents a conserved region found in Phosphatidate phosphatase APP1 from yeast, which contains the catalytic motif DXDX(T/V), present in other Mg+2-dependent phosphatases. This domain has a weak sequence similarity to the haloacid dehalogenase-like domain. APP1 catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol and may play a role in vesicular trafficking through its phosphatidate phosphatase activity at cortical actin patches.


Pssm-ID: 462930  Cd Length: 153  Bit Score: 42.10  E-value: 3.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626   808 VISDIDGTITKSDVLGhilPMVG----------KDWAQLGVAQLFSKI-EQNGYKLLYLSARAIGQSRVTREYLRsirqg 876
Cdd:pfam09949    1 VISDIDDTIKVTGVTS---PLRAlfntffvnalTRVPIPGMPELYRALsASPGNPFFYVSNSPWNLYPFLRDFLE----- 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 320543626   877 NVMLPDGPLLLNP-----TSLISAFHrevieKKPEQFKIACLSDIRDLFPDK 923
Cdd:pfam09949   73 RHGYPPGSLLLRDygstdTSLLRSGL-----TPSAEHKRASIERILRDFPNR 119
pseT PHA02530
polynucleotide kinase; Provisional
 803-874 3.70e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 40.78  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626  803 HNDKVVISDIDGTITKsdvlghilpMVGK---DWAQLG-------VAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRS 872
Cdd:PHA02530  156 GLPKAVIFDIDGTLAK---------MGGRspyDWTKVKedkpnpmVVELVKMYKAAGYEIIVVSGRDGVCEEDTVEWLRQ 226


                  ..
gi 320543626  873 IR 874
Cdd:PHA02530  227 TD 228
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 806-887 9.21e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. 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: 319805  Cd Length: 145  Bit Score: 37.89  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543626  806 KVVISDIDGTITKSDVLGHILPMVGKDWAQLG-----------VAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIR 874
Cdd:cd07502     2 KAVIFDLDGTLADTNGRQPYLERRPRDWDAFFeaadhdppnapVIELVKESALTGYEIVYLSGRPERYRRDTLRWLAKHG 81

                          90
                  ....*....|...
gi 320543626  875 qgnvmLPDGPLLL 887
Cdd:cd07502    82 -----IPDDALHM 89
 
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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