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Conserved domains on  [gi|74205305|dbj|BAE23156|]
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unnamed protein product [Mus musculus]

Protein Classification

phosphatidylserine synthase; phospholipase D family protein( domain architecture ID 10332450)

phosphatidylserine synthase catalyzes de novo synthesis of phosphatidylserine from CDP-diacylglycerol and L-serine; phospholipase D family protein similar to Escherichia coli cardiolipin synthase C and Neisseria gonorrhoeae phospholipase D; hydrolyzes phospholipid phosphodiester bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 101-294 9.47e-123

Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative catalytic domain, repeat 2, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD.


:

Pssm-ID: 197247  Cd Length: 188  Bit Score: 349.92  E-value: 9.47e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 101 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 180
Cdd:cd09149   1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 181 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknqTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 260
Cdd:cd09149  81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74205305 261 LVINQADV--RDNRSIIKQLKDVFERDWYSPYAKSI 294
Cdd:cd09149 153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_SF super family cl15239
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 1-65 1.12e-42

Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D (PLD) superfamily proteins. The PLD superfamily is composed of a large and diverse group of proteins including plant, mammalian and bacterial PLDs, bacterial cardiolipin (CL) synthases, bacterial phosphatidylserine synthases (PSS), eukaryotic phosphatidylglycerophosphate (PGP) synthase, eukaryotic tyrosyl-DNA phosphodiesterase 1 (Tdp1), and some bacterial endonucleases (Nuc and BfiI), among others. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze the transphosphatidylation of phospholipids to acceptor alcohols. The majority of members in this superfamily contain a short conserved sequence motif (H-x-K-x(4)-D, where x represents any amino acid residue), called the HKD signature motif. There are varying expanded forms of this motif in different family members. Some members contain variant HKD motifs. Most PLD enzymes are monomeric proteins with two HKD motif-containing domains. Two HKD motifs from two domains form a single active site. Some PLD enzymes have only one copy of the HKD motif per subunit but form a functionally active dimer, which has a single active site at the dimer interface containing the two HKD motifs from both subunits. Different PLD enzymes may have evolved through domain fusion of a common catalytic core with separate substrate recognition domains. Despite their various catalytic functions and a very broad range of substrate specificities, the diverse group of PLD enzymes can bind to a phosphodiester moiety. Most of them are active as bi-lobed monomers or dimers, and may possess similar core structures for catalytic activity. They are generally thought to utilize a common two-step ping-pong catalytic mechanism, involving an enzyme-substrate intermediate, to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


The actual alignment was detected with superfamily member cd09146:

Pssm-ID: 472788 [Multi-domain]  Cd Length: 163  Bit Score: 145.01  E-value: 1.12e-42
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74205305   1 MNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALYSSL 65
Cdd:cd09146  99 VNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALYWSL 163
 
Name Accession Description Interval E-value
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 101-294 9.47e-123

Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative catalytic domain, repeat 2, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD.


Pssm-ID: 197247  Cd Length: 188  Bit Score: 349.92  E-value: 9.47e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 101 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 180
Cdd:cd09149   1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 181 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknqTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 260
Cdd:cd09149  81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74205305 261 LVINQADV--RDNRSIIKQLKDVFERDWYSPYAKSI 294
Cdd:cd09149 153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_3 pfam13918
PLD-like domain;
34-213 3.35e-109

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 315.41  E-value: 3.35e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305    34 SLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKN 113
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305   114 RSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKETDPLTFNFISSLKA 193
Cdd:pfam13918  81 RSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLDA 160

                         170       180
                  ....*....|....*....|
gi 74205305   194 ICTEIANCSLKVKFFDLERE 213
Cdd:pfam13918 161 FCTEIANCDLKVKFFDLEGE 180
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 9-299 3.64e-64

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 208.70  E-value: 3.64e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305    9 GRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFkSRVPQTWSKRLYGVYDNEKK 88
Cdd:PHA02820 112 GVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLAADLTQIFEVYWYLGV-NNLPYNWKNFYPLYYNTDHP 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305   89 LQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLP-ISSTSSKRTYWPDLDGKIREALVLRS 167
Cdd:PHA02820 191 LSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKFVYVSVMNFIPiIYSKAGKILFWPYIEDELRRAAIDRK 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305  168 VKVRLLISFWKETDPLTFNFISSLKAICTEiaNCSLKVKFFdlerenaCATKEQKNQTFPKLNRNKYMVTDGAAYIGNFD 247
Cdd:PHA02820 271 VSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NINIEVKLF-------IVPDADPPIPYSRVNHAKYMVTDKTAYIGTSN 341

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74205305  248 WVGNDFTQNAGTGLVINQADVRDNRSiikQLKDVFERDWYSPYAKSI---QPTKQ 299
Cdd:PHA02820 342 WTGNYFTDTCGVSINITPDDGLGLRQ---QLEDIFIRDWNSKYSYELydtSPTKR 393
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 1-65 1.12e-42

Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative catalytic domain, repeat 1, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD.


Pssm-ID: 197244 [Multi-domain]  Cd Length: 163  Bit Score: 145.01  E-value: 1.12e-42
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74205305   1 MNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALYSSL 65
Cdd:cd09146  99 VNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALYWSL 163
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 7-34 1.02e-04

Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homologue of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, aspartic acid, and/or asparagine residues which may contribute to the active site. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved.


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 38.91  E-value: 1.02e-04
                           10        20
                   ....*....|....*....|....*...
gi 74205305      7 NKGRLQSSFWIVDKQHVYIGSAGLDWRS 34
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 7-34 1.31e-03

Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homolog of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, and/or asparagine residues which may contribute to the active site. aspartic acid. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologs but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved.


Pssm-ID: 395489 [Multi-domain]  Cd Length: 28  Bit Score: 35.47  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....*...
gi 74205305     7 NKGRLQSSFWIVDKQHVYIGSAGLDWRS 34
Cdd:pfam00614   1 YDGRLHRKIVVVDDELAYIGGANLDGRS 28
 
Name Accession Description Interval E-value
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 101-294 9.47e-123

Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative catalytic domain, repeat 2, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD.


Pssm-ID: 197247  Cd Length: 188  Bit Score: 349.92  E-value: 9.47e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 101 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 180
Cdd:cd09149   1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 181 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknqTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 260
Cdd:cd09149  81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74205305 261 LVINQADV--RDNRSIIKQLKDVFERDWYSPYAKSI 294
Cdd:cd09149 153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_3 pfam13918
PLD-like domain;
34-213 3.35e-109

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 315.41  E-value: 3.35e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305    34 SLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKN 113
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305   114 RSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKETDPLTFNFISSLKA 193
Cdd:pfam13918  81 RSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLDA 160

                         170       180
                  ....*....|....*....|
gi 74205305   194 ICTEIANCSLKVKFFDLERE 213
Cdd:pfam13918 161 FCTEIANCDLKVKFFDLEGE 180
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 101-287 7.67e-75

Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral envelope proteins K4 and p37, and similar proteins; Putative catalytic domain, repeat 2, of vertebrate phospholipases D, PLD3, PLD4, and PLD5 (EC 3.1.4.4), viral envelope proteins (vaccinia virus proteins K4 and p37), and similar proteins. Most family members contain two copies of the HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue), and have been classified into the phospholipase D (PLD) superfamily. Proteins in this subfamily are associated with Golgi membranes, altering their lipid content by the conversion of phospholipids into phosphatidic acid, which is thought to be involved in the regulation of lipid movement. ADP ribosylation factor (ARF), a small guanosine triphosphate binding protein, might be required activity. The vaccinia virus p37 protein, encoded by the F13L gene, is also associated with Golgi membranes and is required for the envelopment and spread of the extracellular enveloped virus (EEV). The vaccinia virus protein K4, encoded by the HindIII K4L gene, remains to be characterized. Sequence analysis indicates that the vaccinia virus proteins K4 and p37 might have evolved from one or more captured eukaryotic genes involved in cellular lipid metabolism. Up to date, no catalytic activity of PLD3 has been shown. Furthermore, due to the lack of functional important histidine and lysine residues in the HKD motif, mammalian PLD5 has been characterized as an inactive PLD. The poxvirus p37 proteins may also lack PLD enzymatic activity, since they contain only one partially conserved HKD motif (N-x-K-x(4)-D).


Pssm-ID: 197206 [Multi-domain]  Cd Length: 175  Bit Score: 227.91  E-value: 7.67e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 101 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 180
Cdd:cd09107   1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 181 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqkNQTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 260
Cdd:cd09107  81 DPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQST------KIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVS 154

                       170       180
                ....*....|....*....|....*..
gi 74205305 261 LVINQADVRdnrsiiKQLKDVFERDWY 287
Cdd:cd09107 155 LVINDPAIV------QQLKDVFERDWN 175
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 9-299 3.64e-64

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 208.70  E-value: 3.64e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305    9 GRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFkSRVPQTWSKRLYGVYDNEKK 88
Cdd:PHA02820 112 GVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLAADLTQIFEVYWYLGV-NNLPYNWKNFYPLYYNTDHP 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305   89 LQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLP-ISSTSSKRTYWPDLDGKIREALVLRS 167
Cdd:PHA02820 191 LSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKFVYVSVMNFIPiIYSKAGKILFWPYIEDELRRAAIDRK 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305  168 VKVRLLISFWKETDPLTFNFISSLKAICTEiaNCSLKVKFFdlerenaCATKEQKNQTFPKLNRNKYMVTDGAAYIGNFD 247
Cdd:PHA02820 271 VSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NINIEVKLF-------IVPDADPPIPYSRVNHAKYMVTDKTAYIGTSN 341

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74205305  248 WVGNDFTQNAGTGLVINQADVRDNRSiikQLKDVFERDWYSPYAKSI---QPTKQ 299
Cdd:PHA02820 342 WTGNYFTDTCGVSINITPDDGLGLRQ---QLEDIFIRDWNSKYSYELydtSPTKR 393
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 101-291 1.28e-58

Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic domain, repeat 2, of phospholipase D3 (PLD3, EC 3.1.4.4). The human protein is also known as Hu-K4 or HUK4 and it was identified as a human homolog of the vaccinia virus protein K4, which is encoded by the HindIII K4L gene. PLD3 is found in many human organs with highest expression levels found in the central nervous system. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD3 has been assigned to the PLD superfamily although no catalytic activity has been detected experimentally. PLD3 is a membrane-bound protein that colocalizes with protein disulfide isomerase, an endoplasmic reticulum (ER) protein. Like other homologs of protein K4, PLD3 might alter the lipid content of associated membranes by selectively hydrolyzing phosphatidylcholine (PC) into the corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement.


Pssm-ID: 197245  Cd Length: 186  Bit Score: 186.71  E-value: 1.28e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 101 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 180
Cdd:cd09147   1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 181 DPLTFNFISSLKAICTEIANCSLKVKFFDLErenacATKEQKNQTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 260
Cdd:cd09147  81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVP-----ADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSA 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 74205305 261 LVINQADVRDNRSIIKQLKDVFERDWYSPYA 291
Cdd:cd09147 156 LVVNQTGRSASGTLQSQLQAVFERDWDSPYS 186
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 101-291 6.56e-54

Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic domain, repeat 2, of vertebrate phospholipases D4 (PLD4, EC 3.1.4.4), homologs of the vaccinia virus protein K4 which is encoded by the HindIII K4L gene. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD4 has been assigned to PLD superfamily although no catalytic activity has been detected to date. Unlike PLD1 and PLD2, PLD4 does not contain Phox (PX) and Pleckstrin homology (PH) domains but has a putative transmembrane domain. Like other vertebrate homologs of protein K4, PLD4 might be associated with Golgi membranes and alter their lipid content by selectively hydrolyze phosphatidylcholine (PC) into corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement.


Pssm-ID: 197246  Cd Length: 187  Bit Score: 174.65  E-value: 6.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 101 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 180
Cdd:cd09148   1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 181 DPLTFNFISSLKAICTEIANCSLKVKFFdlerenACATKEQKNQTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 260
Cdd:cd09148  81 DPDMFPFLRSLNALSNPPLSISVHVKLF------IVPVGNQTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVG 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 74205305 261 LVINQA--DVRDNRSIIKQLKDVFERDWYSPYA 291
Cdd:cd09148 155 LVILQSpgANEEMLPVQEQLRSLFERDWSSPYA 187
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 1-65 1.12e-42

Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative catalytic domain, repeat 1, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD.


Pssm-ID: 197244 [Multi-domain]  Cd Length: 163  Bit Score: 145.01  E-value: 1.12e-42
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74205305   1 MNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALYSSL 65
Cdd:cd09146  99 VNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALYWSL 163
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 6-294 4.16e-42

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 149.43  E-value: 4.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305    6 YNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGvIFYNCSCLVLDLQRIFALYSSLkfkSRVPQTWSkRLYGVYDN 85
Cdd:PHA03003 111 NNVGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLG-VYSTYPPLATDLRRRFDTFKAF---NKNKSVFN-RLCCACCL 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305   86 EKKLQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVL 165
Cdd:PHA03003 186 PVSTKYHINNPIGGVFFSDSPEHLLGYSRTLDADVVLHKIKSAKKSIDLELLSLVPVIREDDKTTYWPDIYNALIRAAIN 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305  166 RSVKVRLLISFWKETDPLTFNFISSLKAICTeiaNCSLKVKFFdlerenacatkeqknqTFPklNRNKYMVTDGA-AYI- 243
Cdd:PHA03003 266 RGVKVRLLVGSWKKNDVYSMASVKSLQALCV---GNDLSVKVF----------------RIP--NNTKLLIVDDEfAHIt 324

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 74205305  244 -GNFDwvGNDFTQNAGTGLviNQADvrdnRSIIKQLKDVFERDWYSPYAKSI 294
Cdd:PHA03003 325 sANFD--GTHYLHHAFVSF--NTID----KELVKELSAIFERDWTSSYSKPL 368
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 1-62 1.10e-22

Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic domain, repeat 1, of phospholipase D3 (PLD3, EC 3.1.4.4). The human protein is also known as Hu-K4 or HUK4 and it was identified as a human homolog of the vaccinia virus protein K4, which is encoded by the HindIII K4L gene. PLD3 is found in many human organs with highest expression levels found in the central nervous system. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD3 has been assigned to the PLD superfamily although no catalytic activity has been detected experimentally. PLD3 is a membrane-bound protein that colocalizes with protein disulfide isomerase, an endoplasmic reticulum (ER) protein. Like other homologs of protein K4, PLD3 might alter the lipid content of associated membranes by selectively hydrolyzing phosphatidylcholine (PC) into the corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement.


Pssm-ID: 197242 [Multi-domain]  Cd Length: 172  Bit Score: 92.70  E-value: 1.10e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74205305   1 MNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALY 62
Cdd:cd09144 107 VDMRKLTTGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVYNCSCLAEDLGKIFEAY 168
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 1-62 1.62e-21

Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic domain, repeat 1, of vertebrate phospholipases D4 (PLD4, EC 3.1.4.4), homologs of the vaccinia virus protein K4 which is encoded by the HindIII K4L gene. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD4 has been assigned to PLD superfamily although no catalytic activity has been detected to date. Unlike PLD1 and PLD2, PLD4 does not contain Phox (PX) and Pleckstrin homology (PH) domains but has a putative transmembrane domain. Like other vertebrate homologs of protein K4, PLD4 might be associated with Golgi membranes and alter their lipid content by selectively hydrolyze phosphatidylcholine (PC) into corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement.


Pssm-ID: 197243 [Multi-domain]  Cd Length: 170  Bit Score: 89.58  E-value: 1.62e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74205305   1 MNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALY 62
Cdd:cd09145 106 VNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAKDLHKTFQTY 167
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 1-48 2.78e-21

Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral envelope proteins K4 and p37, and similar proteins; Putative catalytic domain, repeat 1, of vertebrate phospholipases D, PLD3, PLD4, and PLD5 (EC 3.1.4.4), viral envelope proteins (vaccinia virus proteins K4 and p37), and similar proteins. Most family members contain two copies of the HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue), and have been classified into the phospholipase D (PLD) superfamily. Proteins in this subfamily are associated with Golgi membranes, altering their lipid content by the conversion of phospholipids into phosphatidic acid, which is thought to be involved in the regulation of lipid movement. ADP ribosylation factor (ARF), a small guanosine triphosphate binding protein, might be required activity. The vaccinia virus p37 protein, encoded by the F13L gene, is also associated with Golgi membranes and is required for the envelopment and spread of the extracellular enveloped virus (EEV). The vaccinia virus protein K4, encoded by the HindIII K4L gene, remains to be characterized. Sequence analysis indicates that the vaccinia virus proteins K4 and p37 might have evolved from one or more captured eukaryotic genes involved in cellular lipid metabolism. Up to date, no catalytic activity of PLD3 has been shown. Furthermore, due to the lack of functional important histidine and lysine residues in the HKD motif, mammalian PLD5 has been characterized as an inactive PLD. The poxvirus p37 proteins may also lack PLD enzymatic activity, since they contain only one partially conserved HKD motif (N-x-K-x(4)-D).


Pssm-ID: 197205 [Multi-domain]  Cd Length: 153  Bit Score: 88.46  E-value: 2.78e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 74205305   1 MNMT-AYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNC 48
Cdd:cd09106 105 LDFTkLIGGGVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PLDc_2 pfam13091
PLD-like domain;
125-286 1.40e-05

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 43.82  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305   125 IDDAKQYVYIAVtdylPISSTSskrtywPDLDGKIREALvLRSVKVRLLISFWKETDPltFNFISSLKAIcTEIANCSLK 204
Cdd:pfam13091   5 INSAKKSIDIAT----YYFVPD------REIIDALIAAA-KRGVDVRIILDSNKDDAG--GPKKASLKEL-RSLLRAGVE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305   205 VKFFdlerenacatkeqknQTFPKLNRNKYMVTDGA-AYIGNFDWVGNDFTQNAGTGLVInqadvrDNRSIIKQLKDVFE 283
Cdd:pfam13091  71 IREY---------------QSFLRSMHAKFYIIDGKtVIVGSANLTRRALRLNLENNVVI------KDPELAQELEKEFD 129


                  ...
gi 74205305   284 RDW 286
Cdd:pfam13091 130 RLW 132
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 119-263 4.14e-05

Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D (PLD) superfamily proteins. The PLD superfamily is composed of a large and diverse group of proteins including plant, mammalian and bacterial PLDs, bacterial cardiolipin (CL) synthases, bacterial phosphatidylserine synthases (PSS), eukaryotic phosphatidylglycerophosphate (PGP) synthase, eukaryotic tyrosyl-DNA phosphodiesterase 1 (Tdp1), and some bacterial endonucleases (Nuc and BfiI), among others. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze the transphosphatidylation of phospholipids to acceptor alcohols. The majority of members in this superfamily contain a short conserved sequence motif (H-x-K-x(4)-D, where x represents any amino acid residue), called the HKD signature motif. There are varying expanded forms of this motif in different family members. Some members contain variant HKD motifs. Most PLD enzymes are monomeric proteins with two HKD motif-containing domains. Two HKD motifs from two domains form a single active site. Some PLD enzymes have only one copy of the HKD motif per subunit but form a functionally active dimer, which has a single active site at the dimer interface containing the two HKD motifs from both subunits. Different PLD enzymes may have evolved through domain fusion of a common catalytic core with separate substrate recognition domains. Despite their various catalytic functions and a very broad range of substrate specificities, the diverse group of PLD enzymes can bind to a phosphodiester moiety. Most of them are active as bi-lobed monomers or dimers, and may possess similar core structures for catalytic activity. They are generally thought to utilize a common two-step ping-pong catalytic mechanism, involving an enzyme-substrate intermediate, to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 42.50  E-value: 4.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 119 DAIYSVIDDAKQYVYIAvTDYLpisstsSKRTYWPDLDGKIreALVLRSVKVRLLIsfwketDPLTFNFISSLKAICTEI 198
Cdd:cd00138   1 EALLELLKNAKESIFIA-TPNF------SFNSADRLLKALL--AAAERGVDVRLII------DKPPNAAGSLSAALLEAL 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74205305 199 ANCSLKVKFFDLEREnacatkeqknqtFPKLNRNKYMVTDGA-AYIGNFDWVGNDFTQNAGTGLVI 263
Cdd:cd00138  66 LRAGVNVRSYVTPPH------------FFERLHAKVVVIDGEvAYVGSANLSTASAAQNREAGVLV 119
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 118-286 7.65e-05

Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; Putative catalytic domain, repeat 2, of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 42.26  E-value: 7.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 118 IDAIYSVIDDAKQYVYIAVTDYLPisstsskrtywpdlDGKIREALV---LRSVKVRLLI-SFWKETDPlTFNFISSLKA 193
Cdd:cd09128  12 REALLALIDSAEESLLIQNEEMGD--------------DAPILDALVdaaKRGVDVRVLLpSAWSAEDE-RQARLRALEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74205305 194 IcteiancSLKVKFFDlerenacatkeqknQTFPKLNrNKYMVTDG-AAYIGNFDWVGNDFTQNAGTGLVInqadvrDNR 272
Cdd:cd09128  77 A-------GVPVRLLK--------------DKFLKIH-AKGIVVDGkTALVGSENWSANSLDRNREVGLIF------DDP 128

                       170
                ....*....|....
gi 74205305 273 SIIKQLKDVFERDW 286
Cdd:cd09128 129 EVAAYLQAVFESDW 142
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 7-34 1.02e-04

Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homologue of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, aspartic acid, and/or asparagine residues which may contribute to the active site. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologues but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved.


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 38.91  E-value: 1.02e-04
                           10        20
                   ....*....|....*....|....*...
gi 74205305      7 NKGRLQSSFWIVDKQHVYIGSAGLDWRS 34
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 7-34 1.31e-03

Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) isoforms are activated by ADP-ribosylation factors (ARFs). PLD produces phosphatidic acid from phosphatidylcholine, which may be essential for the formation of certain types of transport vesicles or may be constitutive vesicular transport to signal transduction pathways. PC-hydrolysing PLD is a homolog of cardiolipin synthase, phosphatidylserine synthase, bacterial PLDs, and viral proteins. Each of these appears to possess a domain duplication which is apparent by the presence of two motifs containing well-conserved histidine, lysine, and/or asparagine residues which may contribute to the active site. aspartic acid. An E. coli endonuclease (nuc) and similar proteins appear to be PLD homologs but possess only one of these motifs. The profile contained here represents only the putative active site regions, since an accurate multiple alignment of the repeat units has not been achieved.


Pssm-ID: 395489 [Multi-domain]  Cd Length: 28  Bit Score: 35.47  E-value: 1.31e-03
                          10        20
                  ....*....|....*....|....*...
gi 74205305     7 NKGRLQSSFWIVDKQHVYIGSAGLDWRS 34
Cdd:pfam00614   1 YDGRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 15-45 1.69e-03

Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D (PLD) superfamily proteins. The PLD superfamily is composed of a large and diverse group of proteins including plant, mammalian and bacterial PLDs, bacterial cardiolipin (CL) synthases, bacterial phosphatidylserine synthases (PSS), eukaryotic phosphatidylglycerophosphate (PGP) synthase, eukaryotic tyrosyl-DNA phosphodiesterase 1 (Tdp1), and some bacterial endonucleases (Nuc and BfiI), among others. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze the transphosphatidylation of phospholipids to acceptor alcohols. The majority of members in this superfamily contain a short conserved sequence motif (H-x-K-x(4)-D, where x represents any amino acid residue), called the HKD signature motif. There are varying expanded forms of this motif in different family members. Some members contain variant HKD motifs. Most PLD enzymes are monomeric proteins with two HKD motif-containing domains. Two HKD motifs from two domains form a single active site. Some PLD enzymes have only one copy of the HKD motif per subunit but form a functionally active dimer, which has a single active site at the dimer interface containing the two HKD motifs from both subunits. Different PLD enzymes may have evolved through domain fusion of a common catalytic core with separate substrate recognition domains. Despite their various catalytic functions and a very broad range of substrate specificities, the diverse group of PLD enzymes can bind to a phosphodiester moiety. Most of them are active as bi-lobed monomers or dimers, and may possess similar core structures for catalytic activity. They are generally thought to utilize a common two-step ping-pong catalytic mechanism, involving an enzyme-substrate intermediate, to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 37.88  E-value: 1.69e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 74205305  15 FWIVDKQHVYIGSAGLDWRSLGQMKELGVIF 45
Cdd:cd00138  89 VVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
 
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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