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Conserved domains on  [gi|83627695|ref|NP_795890|]
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inactive phospholipase D5 isoform 1 [Mus musculus]

Protein Classification

phospholipase D-like domain-containing protein; phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase family protein( domain architecture ID 10173695)

phospholipase D-like domain-containing protein may hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group, and may also catalyze the transphosphatidylation of phospholipids to acceptor alcohols| phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase family protein similar to cardiolipin synthase B, which catalyzes the formation of cardiolipin and whose substrates have not been definitively established

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 ...
 309-502 8.53e-122

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: 355.32  E-value: 8.53e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 309 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 388
Cdd:cd09149   1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 389 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknqTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 468
Cdd:cd09149  81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 83627695 469 LVINQADV--RDNRSIIKQLKDVFERDWYSPYAKSI 502
Cdd:cd09149 153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 111-273 2.16e-107

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: 317.57  E-value: 2.16e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 111 ALVENIPEGLNYSEDAPFHLPLFQGWMNLLNMAKKSVDIVSSHWDLNHTHPAACQGQRLFEKLLQLTSQNIEVKLVSDVT 190
Cdd:cd09146   1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDLNASHPSACQGQRLFERLLGLASRGVELKIVSGIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 191 ADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALY 270
Cdd:cd09146  81 DSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALY 160


                ...
gi 83627695 271 SSL 273
Cdd:cd09146 161 WSL 163
 
Name Accession Description Interval E-value
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 309-502 8.53e-122

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: 355.32  E-value: 8.53e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 309 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 388
Cdd:cd09149   1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 389 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknqTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 468
Cdd:cd09149  81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 83627695 469 LVINQADV--RDNRSIIKQLKDVFERDWYSPYAKSI 502
Cdd:cd09149 153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_3 pfam13918
PLD-like domain;
242-421 7.16e-108

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 319.65  E-value: 7.16e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695   242 SLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKN 321
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695   322 RSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKETDPLTFNFISSLKA 401
Cdd:pfam13918  81 RSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLDA 160

                         170       180
                  ....*....|....*....|
gi 83627695   402 ICTEIANCSLKVKFFDLERE 421
Cdd:pfam13918 161 FCTEIANCDLKVKFFDLEGE 180
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 111-273 2.16e-107

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: 317.57  E-value: 2.16e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 111 ALVENIPEGLNYSEDAPFHLPLFQGWMNLLNMAKKSVDIVSSHWDLNHTHPAACQGQRLFEKLLQLTSQNIEVKLVSDVT 190
Cdd:cd09146   1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDLNASHPSACQGQRLFERLLGLASRGVELKIVSGIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 191 ADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALY 270
Cdd:cd09146  81 DSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALY 160


                ...
gi 83627695 271 SSL 273
Cdd:cd09146 161 WSL 163
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 104-507 3.62e-81

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 259.93  E-value: 3.62e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  104 CQNKCRIALVENIPEGLNYSEdapFHLPLFQGWMNLLNMAKKSVDIVSSHWDLNhTHPAACQGQRLFEKLLQLTSQNIEV 183
Cdd:PHA02820   2 NPDNTIAVITETIPIGMQFDK---VYLSTFNFWREILSNTTKTLDISSFYWSLS-DEVGTNFGTMILNEIIQLPKRGVRV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  184 KL-VSDVTADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLD 262
Cdd:PHA02820  78 RIaVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLAAD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  263 LQRIFALYSSLKFkSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYI 342
Cdd:PHA02820 158 LTQIFEVYWYLGV-NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKFVYV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  343 AVTDYLP-ISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKETDPLTFNFISSLKAICTEiaNCSLKVKFFdlere 421
Cdd:PHA02820 237 SVMNFIPiIYSKAGKILFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NINIEVKLF----- 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  422 naCATKEQKNQTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTGLVINQADVRDNRSiikQLKDVFERDWYSPYAKS 501
Cdd:PHA02820 310 --IVPDADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQ---QLEDIFIRDWNSKYSYE 384


                 ....*....
gi 83627695  502 I---QPTKQ 507
Cdd:PHA02820 385 LydtSPTKR 393
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 132-494 1.61e-11

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 65.73  E-value: 1.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 132 LFQGWMNLLNMAKKSVDIVSSHWDLNHThpaacqGQRLFEKLLQLTSQNIEVKLVSD----VTADSKVLEALKLKGAEVT 207
Cdd:COG1502  26 AFAALLEAIEAARRSIDLEYYIFDDDEV------GRRLADALIAAARRGVKVRVLLDgigsRALNRDFLRRLRAAGVEVR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 208 YMNMTAYNKGRLQSS----FWIVDKQHVYIGSAGLDWRSLGQMKELGViFYNCSCL-----VLDLQRIFALYsslkfksr 278
Cdd:COG1502 100 LFNPVRLLFRRLNGRnhrkIVVIDGRVAFVGGANITDEYLGRDPGFGP-WRDTHVRiegpaVADLQAVFAED-------- 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 279 vpqtWskrlYGVYDNEKKLQLQLNETKSQaFVSNSPKlfcpKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPisstsskrt 358
Cdd:COG1502 171 ----W----NFATGEALPFPEPAGDVRVQ-VVPSGPD----SPRETIERALLAAIASARRRIYIETPYFVP--------- 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 359 ywpdlDGKIREALV---LRSVKVRLLISfwKETD-PLTFnfiSSLKAICTEIANCSLKVKFFDlerenacatkeqknqtf 434
Cdd:COG1502 229 -----DRSLLRALIaaaRRGVDVRILLP--AKSDhPLVH---WASRSYYEELLEAGVRIYEYE----------------- 281

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83627695 435 PKLNRNKYMVTDGA-AYIG--NFDWVGndFTQNAGTGLVInqadvrDNRSIIKQLKDVFERDW 494
Cdd:COG1502 282 PGFLHAKVMVVDDEwALVGsaNLDPRS--LRLNFEVNLVI------YDPEFAAQLRARFEEDL 336
PLDc_2 pfam13091
PLD-like domain;
138-267 1.85e-06

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 47.29  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695   138 NLLNMAKKSVDIVSSHWDLNhthpaacqgQRLFEKLLQLTSQNIEVKLVSDVTADS---------KVLEALKLKGAEVTY 208
Cdd:pfam13091   3 DLINSAKKSIDIATYYFVPD---------REIIDALIAAAKRGVDVRIILDSNKDDaggpkkaslKELRSLLRAGVEIRE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 83627695   209 MNMTAynkGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNcSCLVLDLQRIF 267
Cdd:pfam13091  74 YQSFL---RSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEF 128
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 131-268 2.37e-05

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 46.47  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 131 PLFQGWMNLLNMAKKSVDIVSSHWDLnhthpaacqGQRLFEKLLQLTSQNIEVKLVSDVTADSKV--------LEALKLK 202
Cdd:COG1502 203 TIERALLAAIASARRRIYIETPYFVP---------DRSLLRALIAAARRGVDVRILLPAKSDHPLvhwasrsyYEELLEA 273

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83627695 203 GAEVTYmnmtaYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCScLVLDLQRIFA 268
Cdd:COG1502 274 GVRIYE-----YEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDPE-FAAQLRARFE 333
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 215-242 1.12e-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: 39.30  E-value: 1.12e-04
                           10        20
                   ....*....|....*....|....*...
gi 83627695    215 NKGRLQSSFWIVDKQHVYIGSAGLDWRS 242
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 309-502 8.53e-122

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: 355.32  E-value: 8.53e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 309 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 388
Cdd:cd09149   1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 389 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknqTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 468
Cdd:cd09149  81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 83627695 469 LVINQADV--RDNRSIIKQLKDVFERDWYSPYAKSI 502
Cdd:cd09149 153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_3 pfam13918
PLD-like domain;
242-421 7.16e-108

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 319.65  E-value: 7.16e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695   242 SLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKN 321
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695   322 RSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKETDPLTFNFISSLKA 401
Cdd:pfam13918  81 RSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLDA 160

                         170       180
                  ....*....|....*....|
gi 83627695   402 ICTEIANCSLKVKFFDLERE 421
Cdd:pfam13918 161 FCTEIANCDLKVKFFDLEGE 180
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 111-273 2.16e-107

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: 317.57  E-value: 2.16e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 111 ALVENIPEGLNYSEDAPFHLPLFQGWMNLLNMAKKSVDIVSSHWDLNHTHPAACQGQRLFEKLLQLTSQNIEVKLVSDVT 190
Cdd:cd09146   1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDLNASHPSACQGQRLFERLLGLASRGVELKIVSGIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 191 ADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDLQRIFALY 270
Cdd:cd09146  81 DSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALY 160


                ...
gi 83627695 271 SSL 273
Cdd:cd09146 161 WSL 163
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 104-507 3.62e-81

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 259.93  E-value: 3.62e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  104 CQNKCRIALVENIPEGLNYSEdapFHLPLFQGWMNLLNMAKKSVDIVSSHWDLNhTHPAACQGQRLFEKLLQLTSQNIEV 183
Cdd:PHA02820   2 NPDNTIAVITETIPIGMQFDK---VYLSTFNFWREILSNTTKTLDISSFYWSLS-DEVGTNFGTMILNEIIQLPKRGVRV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  184 KL-VSDVTADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLD 262
Cdd:PHA02820  78 RIaVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLAAD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  263 LQRIFALYSSLKFkSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYI 342
Cdd:PHA02820 158 LTQIFEVYWYLGV-NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKFVYV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  343 AVTDYLP-ISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKETDPLTFNFISSLKAICTEiaNCSLKVKFFdlere 421
Cdd:PHA02820 237 SVMNFIPiIYSKAGKILFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NINIEVKLF----- 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  422 naCATKEQKNQTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTGLVINQADVRDNRSiikQLKDVFERDWYSPYAKS 501
Cdd:PHA02820 310 --IVPDADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQ---QLEDIFIRDWNSKYSYE 384


                 ....*....
gi 83627695  502 I---QPTKQ 507
Cdd:PHA02820 385 LydtSPTKR 393
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 309-495 4.28e-74

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: 232.53  E-value: 4.28e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 309 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 388
Cdd:cd09107   1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 389 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqkNQTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 468
Cdd:cd09107  81 DPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQST------KIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVS 154

                       170       180
                ....*....|....*....|....*..
gi 83627695 469 LVINQADVRdnrsiiKQLKDVFERDWY 495
Cdd:cd09107 155 LVINDPAIV------QQLKDVFERDWN 175
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 309-499 3.03e-57

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: 189.02  E-value: 3.03e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 309 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 388
Cdd:cd09147   1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 389 DPLTFNFISSLKAICTEIANCSLKVKFFDLErenacATKEQKNQTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 468
Cdd:cd09147  81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVP-----ADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSA 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 83627695 469 LVINQADVRDNRSIIKQLKDVFERDWYSPYA 499
Cdd:cd09147 156 LVVNQTGRSASGTLQSQLQAVFERDWDSPYS 186
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 112-256 6.35e-56

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: 184.37  E-value: 6.35e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 112 LVENIPEGLNYSEDApFHLPLFQGWMNLLNMAKKSVDIVSSHWDLNHTH----PAACQGQRLFEKLLQLTSQNIEVKLVS 187
Cdd:cd09106   1 LVESIPEGLTFLSSS-SHLSTFEAWMELISSAKKSIDIASFYWNLRGTDtnpdSSAQEGEDIFNALLEAAKRGVKIRILQ 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83627695 188 DVTADSK----VLEALKLKGAEVTYMNMT-AYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNC 256
Cdd:cd09106  80 DKPSKDKpdedDLELAALGGAEVRSLDFTkLIGGGVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 309-499 6.23e-52

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: 175.42  E-value: 6.23e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 309 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKET 388
Cdd:cd09148   1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 389 DPLTFNFISSLKAICTEIANCSLKVKFFdlerenACATKEQKNQTFPKLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 468
Cdd:cd09148  81 DPDMFPFLRSLNALSNPPLSISVHVKLF------IVPVGNQTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVG 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 83627695 469 LVINQA--DVRDNRSIIKQLKDVFERDWYSPYA 499
Cdd:cd09148 155 LVILQSpgANEEMLPVQEQLRSLFERDWSSPYA 187
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 107-502 1.69e-50

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 177.16  E-value: 1.69e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  107 KCRIalVENIPEGLNYSEDapfHLPLFQGWMNLLNMAKKSVDIVSSHWDLNHTHpaacQGQRLFEKLLQLTSQNIEVKLV 186
Cdd:PHA03003  12 GCRI--VETLPKSLGIATQ---HMSTYECFDEIISQAKKYIYIASFCCNLRSTP----EGRLILDKLKEAAESGVKVTIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  187 SDVTADSKVLEalKLKGAEVTYMNM---TAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGvIFYNCSCLVLDL 263
Cdd:PHA03003  83 VDEQSGDKDEE--ELQSSNINYIKVdigKLNNVGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLG-VYSTYPPLATDL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  264 QRIFALYSSLkfkSRVPQTWSkRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIA 343
Cdd:PHA03003 160 RRRFDTFKAF---NKNKSVFN-RLCCACCLPVSTKYHINNPIGGVFFSDSPEHLLGYSRTLDADVVLHKIKSAKKSIDLE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  344 VTDYLPISSTSSKRTYWPDLDGKIREALVLRSVKVRLLISFWKETDPLTFNFISSLKAICTeiaNCSLKVKFFdlerena 423
Cdd:PHA03003 236 LLSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCV---GNDLSVKVF------- 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695  424 catkeqknqTFPklNRNKYMVTDGA-AYI--GNFDwvGNDFTQNAGTGLviNQADvrdnRSIIKQLKDVFERDWYSPYAK 500
Cdd:PHA03003 306 ---------RIP--NNTKLLIVDDEfAHItsANFD--GTHYLHHAFVSF--NTID----KELVKELSAIFERDWTSSYSK 366


                 ..
gi 83627695  501 SI 502
Cdd:PHA03003 367 PL 368
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 112-270 1.14e-48

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: 165.89  E-value: 1.14e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 112 LVENIPEGLNYSEDAPFHLPLFQGWMNLLNMAKKSVDIVSSHWDL--NHTH---PAACQGQRLFEKLLQLTSQNIEVKLV 186
Cdd:cd09144   2 LVESIPEGLVFNSSSTINPSIYQAWLNLISAAQSSLDIASFYWTLtnSDTHtqePSANQGEQILKKLGQLSQSGVYVRIA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 187 SDVTAD---SKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDL 263
Cdd:cd09144  82 VDKPADpkpMEDINALSSYGADVRMVDMRKLTTGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVYNCSCLAEDL 161


                ....*..
gi 83627695 264 QRIFALY 270
Cdd:cd09144 162 GKIFEAY 168
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 112-270 1.77e-45

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: 157.38  E-value: 1.77e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 112 LVENIPEGLNYSEDAPFHLPLFQGWMNLLNMAKKSVDIVSSHW-----DLNHTHPAACQGQRLFEKLLQLTSQNIEVKL- 185
Cdd:cd09145   1 LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWsltgeDIGVNDSSSLPGEDILKELAELLSRNVSVRAa 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 186 --VSDVTADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCSCLVLDL 263
Cdd:cd09145  81 asIPTLAANSTDLKILRQKGAHVRKVNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAKDL 160


                ....*..
gi 83627695 264 QRIFALY 270
Cdd:cd09145 161 HKTFQTY 167
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 132-494 1.61e-11

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 65.73  E-value: 1.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 132 LFQGWMNLLNMAKKSVDIVSSHWDLNHThpaacqGQRLFEKLLQLTSQNIEVKLVSD----VTADSKVLEALKLKGAEVT 207
Cdd:COG1502  26 AFAALLEAIEAARRSIDLEYYIFDDDEV------GRRLADALIAAARRGVKVRVLLDgigsRALNRDFLRRLRAAGVEVR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 208 YMNMTAYNKGRLQSS----FWIVDKQHVYIGSAGLDWRSLGQMKELGViFYNCSCL-----VLDLQRIFALYsslkfksr 278
Cdd:COG1502 100 LFNPVRLLFRRLNGRnhrkIVVIDGRVAFVGGANITDEYLGRDPGFGP-WRDTHVRiegpaVADLQAVFAED-------- 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 279 vpqtWskrlYGVYDNEKKLQLQLNETKSQaFVSNSPKlfcpKNRSFDIDAIYSVIDDAKQYVYIAVTDYLPisstsskrt 358
Cdd:COG1502 171 ----W----NFATGEALPFPEPAGDVRVQ-VVPSGPD----SPRETIERALLAAIASARRRIYIETPYFVP--------- 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 359 ywpdlDGKIREALV---LRSVKVRLLISfwKETD-PLTFnfiSSLKAICTEIANCSLKVKFFDlerenacatkeqknqtf 434
Cdd:COG1502 229 -----DRSLLRALIaaaRRGVDVRILLP--AKSDhPLVH---WASRSYYEELLEAGVRIYEYE----------------- 281

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 83627695 435 PKLNRNKYMVTDGA-AYIG--NFDWVGndFTQNAGTGLVInqadvrDNRSIIKQLKDVFERDW 494
Cdd:COG1502 282 PGFLHAKVMVVDDEwALVGsaNLDPRS--LRLNFEVNLVI------YDPEFAAQLRARFEEDL 336
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 136-253 8.79e-10

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: 56.37  E-value: 8.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 136 WMNLLNMAKKSVDIVSSHWDLNHthpaacqGQRLFEKLLQLTSQNIEVKLVSD------VTADSKVLEALKLKGAEVTYM 209
Cdd:cd00138   3 LLELLKNAKESIFIATPNFSFNS-------ADRLLKALLAAAERGVDVRLIIDkppnaaGSLSAALLEALLRAGVNVRSY 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 83627695 210 NMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIF 253
Cdd:cd00138  76 VTPPHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
PLDc_2 pfam13091
PLD-like domain;
138-267 1.85e-06

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 47.29  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695   138 NLLNMAKKSVDIVSSHWDLNhthpaacqgQRLFEKLLQLTSQNIEVKLVSDVTADS---------KVLEALKLKGAEVTY 208
Cdd:pfam13091   3 DLINSAKKSIDIATYYFVPD---------REIIDALIAAAKRGVDVRIILDSNKDDaggpkkaslKELRSLLRAGVEIRE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 83627695   209 MNMTAynkGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNcSCLVLDLQRIF 267
Cdd:pfam13091  74 YQSFL---RSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEF 128
PLDc_2 pfam13091
PLD-like domain;
333-494 1.33e-05

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 44.98  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695   333 IDDAKQYVYIAVtdylPISSTSskrtywPDLDGKIREALvLRSVKVRLLISFWKETDPL----TFNFISSLKAicteiAN 408
Cdd:pfam13091   5 INSAKKSIDIAT----YYFVPD------REIIDALIAAA-KRGVDVRIILDSNKDDAGGpkkaSLKELRSLLR-----AG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695   409 CslKVKFFdlerenacatkeqknQTFPKLNRNKYMVTDGA-AYIGNFDWVGNDFTQNAGTGLVInqadvrDNRSIIKQLK 487
Cdd:pfam13091  69 V--EIREY---------------QSFLRSMHAKFYIIDGKtVIVGSANLTRRALRLNLENNVVI------KDPELAQELE 125


                  ....*..
gi 83627695   488 DVFERDW 494
Cdd:pfam13091 126 KEFDRLW 132
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 131-268 2.37e-05

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 46.47  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 131 PLFQGWMNLLNMAKKSVDIVSSHWDLnhthpaacqGQRLFEKLLQLTSQNIEVKLVSDVTADSKV--------LEALKLK 202
Cdd:COG1502 203 TIERALLAAIASARRRIYIETPYFVP---------DRSLLRALIAAARRGVDVRILLPAKSDHPLvhwasrsyYEELLEA 273

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83627695 203 GAEVTYmnmtaYNKGRLQSSFWIVDKQHVYIGSAGLDWRSLGQMKELGVIFYNCScLVLDLQRIFA 268
Cdd:COG1502 274 GVRIYE-----YEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDPE-FAAQLRARFE 333
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 327-471 4.62e-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: 42.89  E-value: 4.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 327 DAIYSVIDDAKQYVYIAvTDYLpisstsSKRTYWPDLDGKIreALVLRSVKVRLLIsfwketDPLTFNFISSLKAICTEI 406
Cdd:cd00138   1 EALLELLKNAKESIFIA-TPNF------SFNSADRLLKALL--AAAERGVDVRLII------DKPPNAAGSLSAALLEAL 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 83627695 407 ANCSLKVKFFDLEREnacatkeqknqtFPKLNRNKYMVTDGA-AYIGNFDWVGNDFTQNAGTGLVI 471
Cdd:cd00138  66 LRAGVNVRSYVTPPH------------FFERLHAKVVVIDGEvAYVGSANLSTASAAQNREAGVLV 119
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 215-242 1.12e-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: 39.30  E-value: 1.12e-04
                           10        20
                   ....*....|....*....|....*...
gi 83627695    215 NKGRLQSSFWIVDKQHVYIGSAGLDWRS 242
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 326-494 1.40e-04

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: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 326 IDAIYSVIDDAKQYVYIAVTDYLPisstsskrtywpdlDGKIREALV---LRSVKVRLLI-SFWKETDPlTFNFISSLKA 401
Cdd:cd09128  12 REALLALIDSAEESLLIQNEEMGD--------------DAPILDALVdaaKRGVDVRVLLpSAWSAEDE-RQARLRALEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83627695 402 IcteiancSLKVKFFDlerenacatkeqknQTFPKLNrNKYMVTDG-AAYIGNFDWVGNDFTQNAGTGLVInqadvrDNR 480
Cdd:cd09128  77 A-------GVPVRLLK--------------DKFLKIH-AKGIVVDGkTALVGSENWSANSLDRNREVGLIF------DDP 128

                       170
                ....*....|....
gi 83627695 481 SIIKQLKDVFERDW 494
Cdd:cd09128 129 EVAAYLQAVFESDW 142
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 215-242 1.62e-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: 35.86  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|....*...
gi 83627695   215 NKGRLQSSFWIVDKQHVYIGSAGLDWRS 242
Cdd:pfam00614   1 YDGRLHRKIVVVDDELAYIGGANLDGRS 28
 
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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