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Conserved domains on  [gi|1370452221|ref|XP_024309635|]
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inactive phospholipase D5 isoform X1 [Homo sapiens]

Protein Classification

PLDc_vPLD5_1 and PLDc_vPLD5_2 domain-containing protein( domain architecture ID 10173695)

PLDc_vPLD5_1 and PLDc_vPLD5_2 domain-containing protein

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 ...
 266-459 7.06e-124

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: 359.17  E-value: 7.06e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 266 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKET 345
Cdd:cd09149     1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 346 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknhTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 425
Cdd:cd09149    81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370452221 426 LVINQADV--RNNRSIIKQLKDVFERDWYSPYAKTL 459
Cdd:cd09149   153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 68-230 7.40e-108

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: 7.40e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  68 ALVENIPEGLNYSENAPFHLSLFQGWMNLLNMAKKSVDIVSSHWDLNHTHPSACQGQRLFEKLLQLTSQNIEIKLVSDVT 147
Cdd:cd09146     1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDLNASHPSACQGQRLFERLLGLASRGVELKIVSGIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 148 ADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCSCLVLDLQRIFALY 227
Cdd:cd09146    81 DSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALY 160


                  ...
gi 1370452221 228 SSL 230
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 ...
 266-459 7.06e-124

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: 359.17  E-value: 7.06e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 266 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKET 345
Cdd:cd09149     1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 346 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknhTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 425
Cdd:cd09149    81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370452221 426 LVINQADV--RNNRSIIKQLKDVFERDWYSPYAKTL 459
Cdd:cd09149   153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 68-230 7.40e-108

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: 7.40e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  68 ALVENIPEGLNYSENAPFHLSLFQGWMNLLNMAKKSVDIVSSHWDLNHTHPSACQGQRLFEKLLQLTSQNIEIKLVSDVT 147
Cdd:cd09146     1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDLNASHPSACQGQRLFERLLGLASRGVELKIVSGIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 148 ADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCSCLVLDLQRIFALY 227
Cdd:cd09146    81 DSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALY 160


                  ...
gi 1370452221 228 SSL 230
Cdd:cd09146   161 WSL 163
PLDc_3 pfam13918
PLD-like domain;
199-378 1.78e-106

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 314.64  E-value: 1.78e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 199 SLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKN 278
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 279 RSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKETDPLTFNFISSLKA 358
Cdd:pfam13918  81 RSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLDA 160

                         170       180
                  ....*....|....*....|
gi 1370452221 359 ICTEIANCSLKVKFFDLERE 378
Cdd:pfam13918 161 FCTEIANCDLKVKFFDLEGE 180
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 61-484 4.42e-83

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 263.40  E-value: 4.42e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  61 CQNKCRIALVENIPEGLNYSEnapFHLSLFQGWMNLLNMAKKSVDIVSSHWDLNhTHPSACQGQRLFEKLLQLTSQNIEI 140
Cdd:PHA02820    2 NPDNTIAVITETIPIGMQFDK---VYLSTFNFWREILSNTTKTLDISSFYWSLS-DEVGTNFGTMILNEIIQLPKRGVRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 141 KL-VSDVTADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCSCLVLD 219
Cdd:PHA02820   78 RIaVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLAAD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 220 LQRIFALYSSLKFkSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYI 299
Cdd:PHA02820  158 LTQIFEVYWYLGV-NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKFVYV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 300 AVMDYLP-ISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKETDPLTFNFISSLKAICTEiaNCSLKVKFFdlere 378
Cdd:PHA02820  237 SVMNFIPiIYSKAGKILFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NINIEVKLF----- 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 379 naCATKEQKNHTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTGLVINQADVRNNRSiikQLKDVFERDWYSPYAKT 458
Cdd:PHA02820  310 --IVPDADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQ---QLEDIFIRDWNSKYSYE 384

                         410       420
                  ....*....|....*....|....*....
gi 1370452221 459 L---QPTKqpNCSSLFKLKPLSNKTATDD 484
Cdd:PHA02820  385 LydtSPTK--RCRLLKNMKQCTNDIYCDE 411
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 89-451 2.07e-12

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: 68.43  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  89 LFQGWMNLLNMAKKSVDIVSSHWDLNHThpsacqGQRLFEKLLQLTSQNIEIKLVSD----VTADSKVLEALKLKGAEVT 164
Cdd:COG1502    26 AFAALLEAIEAARRSIDLEYYIFDDDEV------GRRLADALIAAARRGVKVRVLLDgigsRALNRDFLRRLRAAGVEVR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 165 YMNMTAYNKGRLQSS----FWIVDKQHVYIGSAGLDWQSLGQMKELGViFYNCSCL-----VLDLQRIFALYsslkfksr 235
Cdd:COG1502   100 LFNPVRLLFRRLNGRnhrkIVVIDGRVAFVGGANITDEYLGRDPGFGP-WRDTHVRiegpaVADLQAVFAED-------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 236 vpqtWskrlYGVYDNEKKLQLQLNETKSQaFVSNSPKlfcpKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPisststkrt 315
Cdd:COG1502   171 ----W----NFATGEALPFPEPAGDVRVQ-VVPSGPD----SPRETIERALLAAIASARRRIYIETPYFVP--------- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 316 ywpdlDAKIREALV---LRSVRVRLLLSfwKETD-PLTFnfiSSLKAICTEIANCSLKVKFFDlerenacatkeqknhtf 391
Cdd:COG1502   229 -----DRSLLRALIaaaRRGVDVRILLP--AKSDhPLVH---WASRSYYEELLEAGVRIYEYE----------------- 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370452221 392 PRLNRNKYMVTDGA-AYIG--NFDWVGndFTQNAGTGLVInqadvrNNRSIIKQLKDVFERDW 451
Cdd:COG1502   282 PGFLHAKVMVVDDEwALVGsaNLDPRS--LRLNFEVNLVI------YDPEFAAQLRARFEEDL 336
PLDc_2 pfam13091
PLD-like domain;
95-224 1.16e-05

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 44.98  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  95 NLLNMAKKSVDIVSSHWDLNhthpsacqgQRLFEKLLQLTSQNIEIKLVSDVTADS---------KVLEALKLKGAEVTY 165
Cdd:pfam13091   3 DLINSAKKSIDIATYYFVPD---------REIIDALIAAAKRGVDVRIILDSNKDDaggpkkaslKELRSLLRAGVEIRE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370452221 166 MNMTAynkGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNcSCLVLDLQRIF 224
Cdd:pfam13091  74 YQSFL---RSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEF 128
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 172-197 2.37e-03

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: 35.44  E-value: 2.37e-03
                           10        20
                   ....*....|....*....|....*.
gi 1370452221  172 NKGRLQSSFWIVDKQHVYIGSAGLDW 197
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDG 26
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 88-225 2.42e-03

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: 40.31  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  88 SLFQGWMNLLNMAKKSVDIVSSHWDLnhthpsacqGQRLFEKLLQLTSQNIEIKLVSDVTADSKV--------LEALKLK 159
Cdd:COG1502   203 TIERALLAAIASARRRIYIETPYFVP---------DRSLLRALIAAARRGVDVRILLPAKSDHPLvhwasrsyYEELLEA 273

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370452221 160 GAEVTYmnmtaYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCScLVLDLQRIFA 225
Cdd:COG1502   274 GVRIYE-----YEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDPE-FAAQLRARFE 333
 
Name Accession Description Interval E-value
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 266-459 7.06e-124

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: 359.17  E-value: 7.06e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 266 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKET 345
Cdd:cd09149     1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 346 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqknhTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 425
Cdd:cd09149    81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDC--------TSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVG 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370452221 426 LVINQADV--RNNRSIIKQLKDVFERDWYSPYAKTL 459
Cdd:cd09149   153 LVINQADGveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 68-230 7.40e-108

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: 7.40e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  68 ALVENIPEGLNYSENAPFHLSLFQGWMNLLNMAKKSVDIVSSHWDLNHTHPSACQGQRLFEKLLQLTSQNIEIKLVSDVT 147
Cdd:cd09146     1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDLNASHPSACQGQRLFERLLGLASRGVELKIVSGIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 148 ADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCSCLVLDLQRIFALY 227
Cdd:cd09146    81 DSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHRVFALY 160


                  ...
gi 1370452221 228 SSL 230
Cdd:cd09146   161 WSL 163
PLDc_3 pfam13918
PLD-like domain;
199-378 1.78e-106

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 314.64  E-value: 1.78e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 199 SLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKN 278
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 279 RSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKETDPLTFNFISSLKA 358
Cdd:pfam13918  81 RSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLDA 160

                         170       180
                  ....*....|....*....|
gi 1370452221 359 ICTEIANCSLKVKFFDLERE 378
Cdd:pfam13918 161 FCTEIANCDLKVKFFDLEGE 180
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 61-484 4.42e-83

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 263.40  E-value: 4.42e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  61 CQNKCRIALVENIPEGLNYSEnapFHLSLFQGWMNLLNMAKKSVDIVSSHWDLNhTHPSACQGQRLFEKLLQLTSQNIEI 140
Cdd:PHA02820    2 NPDNTIAVITETIPIGMQFDK---VYLSTFNFWREILSNTTKTLDISSFYWSLS-DEVGTNFGTMILNEIIQLPKRGVRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 141 KL-VSDVTADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCSCLVLD 219
Cdd:PHA02820   78 RIaVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLAAD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 220 LQRIFALYSSLKFkSRVPQTWSKRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYI 299
Cdd:PHA02820  158 LTQIFEVYWYLGV-NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKFVYV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 300 AVMDYLP-ISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKETDPLTFNFISSLKAICTEiaNCSLKVKFFdlere 378
Cdd:PHA02820  237 SVMNFIPiIYSKAGKILFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NINIEVKLF----- 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 379 naCATKEQKNHTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTGLVINQADVRNNRSiikQLKDVFERDWYSPYAKT 458
Cdd:PHA02820  310 --IVPDADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQ---QLEDIFIRDWNSKYSYE 384

                         410       420
                  ....*....|....*....|....*....
gi 1370452221 459 L---QPTKqpNCSSLFKLKPLSNKTATDD 484
Cdd:PHA02820  385 LydtSPTK--RCRLLKNMKQCTNDIYCDE 411
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 266-452 2.21e-77

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: 239.85  E-value: 2.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 266 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKET 345
Cdd:cd09107     1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 346 DPLTFNFISSLKAICTEIANCSLKVKFFDLERENACatkeqkNHTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 425
Cdd:cd09107    81 DPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQST------KIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVS 154

                         170       180
                  ....*....|....*....|....*..
gi 1370452221 426 LVINQADVRNnrsiikQLKDVFERDWY 452
Cdd:cd09107   155 LVINDPAIVQ------QLKDVFERDWN 175
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 266-456 4.16e-59

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: 192.88  E-value: 4.16e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 266 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKET 345
Cdd:cd09147     1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 346 DPLTFNFISSLKAICTEIANCSLKVKFFDLErenacATKEQKNHTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 425
Cdd:cd09147    81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVP-----ADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSA 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370452221 426 LVINQADVRNNRSIIKQLKDVFERDWYSPYA 456
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 ...
 69-213 2.06e-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: 184.76  E-value: 2.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  69 LVENIPEGLNYSENApFHLSLFQGWMNLLNMAKKSVDIVSSHWDLNHTH----PSACQGQRLFEKLLQLTSQNIEIKLVS 144
Cdd:cd09106     1 LVESIPEGLTFLSSS-SHLSTFEAWMELISSAKKSIDIASFYWNLRGTDtnpdSSAQEGEDIFNALLEAAKRGVKIRILQ 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370452221 145 DVTADSK----VLEALKLKGAEVTYMNMT-AYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNC 213
Cdd:cd09106    80 DKPSKDKpdedDLELAALGGAEVRSLDFTkLIGGGVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 266-456 2.35e-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: 180.81  E-value: 2.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 266 FVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKET 345
Cdd:cd09148     1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 346 DPLTFNFISSLKAICTEIANCSLKVKFFdlerenACATKEQKNHTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTG 425
Cdd:cd09148    81 DPDMFPFLRSLNALSNPPLSISVHVKLF------IVPVGNQTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVG 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370452221 426 LVINQADVRNNR--SIIKQLKDVFERDWYSPYA 456
Cdd:cd09148   155 LVILQSPGANEEmlPVQEQLRSLFERDWSSPYA 187
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 69-227 5.66e-50

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: 168.59  E-value: 5.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  69 LVENIPEGLNYSENAPFHLSLFQGWMNLLNMAKKSVDIVSSHWDL--NHTH---PSACQGQRLFEKLLQLTSQNIEIKLV 143
Cdd:cd09144     2 LVESIPEGLVFNSSSTINPSIYQAWLNLISAAQSSLDIASFYWTLtnSDTHtqePSANQGEQILKKLGQLSQSGVYVRIA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 144 SDVTAD---SKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCSCLVLDL 220
Cdd:cd09144    82 VDKPADpkpMEDINALSSYGADVRMVDMRKLTTGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVYNCSCLAEDL 161


                  ....*..
gi 1370452221 221 QRIFALY 227
Cdd:cd09144   162 GKIFEAY 168
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 64-459 6.95e-50

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 174.85  E-value: 6.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  64 KCRIalVENIPEGLNYSENapfHLSLFQGWMNLLNMAKKSVDIVSSHWDLNHTHpsacQGQRLFEKLLQLTSQNIEIKLV 143
Cdd:PHA03003   12 GCRI--VETLPKSLGIATQ---HMSTYECFDEIISQAKKYIYIASFCCNLRSTP----EGRLILDKLKEAAESGVKVTIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 144 SDVTADSKVLEalKLKGAEVTYMNM---TAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGvIFYNCSCLVLDL 220
Cdd:PHA03003   83 VDEQSGDKDEE--ELQSSNINYIKVdigKLNNVGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLG-VYSTYPPLATDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 221 QRIFALYSSLkfkSRVPQTWSkRLYGVYDNEKKLQLQLNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIA 300
Cdd:PHA03003  160 RRRFDTFKAF---NKNKSVFN-RLCCACCLPVSTKYHINNPIGGVFFSDSPEHLLGYSRTLDADVVLHKIKSAKKSIDLE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 301 VMDYLPISSTSTKRTYWPDLDAKIREALVLRSVRVRLLLSFWKETDPLTFNFISSLKAICTeiaNCSLKVKFFdlerena 380
Cdd:PHA03003  236 LLSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCV---GNDLSVKVF------- 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 381 catkeqknhTFPrlNRNKYMVTDGA-AYI--GNFDwvGNDFTQNAGTGLviNQADvrnnRSIIKQLKDVFERDWYSPYAK 457
Cdd:PHA03003  306 ---------RIP--NNTKLLIVDDEfAHItsANFD--GTHYLHHAFVSF--NTID----KELVKELSAIFERDWTSSYSK 366


                  ..
gi 1370452221 458 TL 459
Cdd:PHA03003  367 PL 368
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 69-227 8.22e-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: 155.07  E-value: 8.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  69 LVENIPEGLNYSENAPFHLSLFQGWMNLLNMAKKSVDIVSSHW-----DLNHTHPSACQGQRLFEKLLQLTSQNIEIKL- 142
Cdd:cd09145     1 LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWsltgeDIGVNDSSSLPGEDILKELAELLSRNVSVRAa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 143 --VSDVTADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCSCLVLDL 220
Cdd:cd09145    81 asIPTLAANSTDLKILRQKGAHVRKVNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAKDL 160


                  ....*..
gi 1370452221 221 QRIFALY 227
Cdd:cd09145   161 HKTFQTY 167
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 89-451 2.07e-12

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: 68.43  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  89 LFQGWMNLLNMAKKSVDIVSSHWDLNHThpsacqGQRLFEKLLQLTSQNIEIKLVSD----VTADSKVLEALKLKGAEVT 164
Cdd:COG1502    26 AFAALLEAIEAARRSIDLEYYIFDDDEV------GRRLADALIAAARRGVKVRVLLDgigsRALNRDFLRRLRAAGVEVR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 165 YMNMTAYNKGRLQSS----FWIVDKQHVYIGSAGLDWQSLGQMKELGViFYNCSCL-----VLDLQRIFALYsslkfksr 235
Cdd:COG1502   100 LFNPVRLLFRRLNGRnhrkIVVIDGRVAFVGGANITDEYLGRDPGFGP-WRDTHVRiegpaVADLQAVFAED-------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 236 vpqtWskrlYGVYDNEKKLQLQLNETKSQaFVSNSPKlfcpKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPisststkrt 315
Cdd:COG1502   171 ----W----NFATGEALPFPEPAGDVRVQ-VVPSGPD----SPRETIERALLAAIASARRRIYIETPYFVP--------- 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 316 ywpdlDAKIREALV---LRSVRVRLLLSfwKETD-PLTFnfiSSLKAICTEIANCSLKVKFFDlerenacatkeqknhtf 391
Cdd:COG1502   229 -----DRSLLRALIaaaRRGVDVRILLP--AKSDhPLVH---WASRSYYEELLEAGVRIYEYE----------------- 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370452221 392 PRLNRNKYMVTDGA-AYIG--NFDWVGndFTQNAGTGLVInqadvrNNRSIIKQLKDVFERDW 451
Cdd:COG1502   282 PGFLHAKVMVVDDEwALVGsaNLDPRS--LRLNFEVNLVI------YDPEFAAQLRARFEEDL 336
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 93-210 5.14e-09

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: 54.06  E-value: 5.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  93 WMNLLNMAKKSVDIVSSHWDLNHthpsacqGQRLFEKLLQLTSQNIEIKLVSD------VTADSKVLEALKLKGAEVTYM 166
Cdd:cd00138     3 LLELLKNAKESIFIATPNFSFNS-------ADRLLKALLAAAERGVDVRLIIDkppnaaGSLSAALLEALLRAGVNVRSY 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370452221 167 NMTAYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIF 210
Cdd:cd00138    76 VTPPHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
PLDc_2 pfam13091
PLD-like domain;
290-451 3.45e-06

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 46.52  E-value: 3.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 290 IDDAKQYVYIAVMdYLPISststkrtywPDLDAKIREALvLRSVRVRLLLSFWKETDPltFNFISSLKAIcTEIANCSLK 369
Cdd:pfam13091   5 INSAKKSIDIATY-YFVPD---------REIIDALIAAA-KRGVDVRIILDSNKDDAG--GPKKASLKEL-RSLLRAGVE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 370 VKFFDlerenacatkeqknhTFPRLNRNKYMVTDGA-AYIGNFDWVGNDFTQNAGTGLVINQADvrnnrsIIKQLKDVFE 448
Cdd:pfam13091  71 IREYQ---------------SFLRSMHAKFYIIDGKtVIVGSANLTRRALRLNLENNVVIKDPE------LAQELEKEFD 129


                  ...
gi 1370452221 449 RDW 451
Cdd:pfam13091 130 RLW 132
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 283-466 5.30e-06

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: 48.40  E-value: 5.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 283 IDAIYSVIDDAKQYVYIAVMDYLPisststkrtywPDLDAKIREALVL---RSVRVRLLLSfWKETDPLTFNFISSLKAi 359
Cdd:COG1502    27 FAALLEAIEAARRSIDLEYYIFDD-----------DEVGRRLADALIAaarRGVKVRVLLD-GIGSRALNRDFLRRLRA- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 360 cteiANCslKVKFFDlerenacatkeQKNHTFPRLNR---NKYMVTDGA-AYIGNFDWVGNDFTQNAGTGLVINqADVRN 435
Cdd:COG1502    94 ----AGV--EVRLFN-----------PVRLLFRRLNGrnhRKIVVIDGRvAFVGGANITDEYLGRDPGFGPWRD-THVRI 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370452221 436 NRSIIKQLKDVFERDWYSPYAKTLQPTKQPN 466
Cdd:COG1502   156 EGPAVADLQAVFAEDWNFATGEALPFPEPAG 186
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 284-428 9.39e-06

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: 44.81  E-value: 9.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 284 DAIYSVIDDAKQYVYIAvMDYLpisstsTKRTYWPDLDAKIreALVLRSVRVRLLlsfwkeTDPLTFNFISSLKAICTEI 363
Cdd:cd00138     1 EALLELLKNAKESIFIA-TPNF------SFNSADRLLKALL--AAAERGVDVRLI------IDKPPNAAGSLSAALLEAL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370452221 364 ANCSLKVKFFDLERENAcatkeQKNHTfprlnrnKYMVTDGA-AYIGNFDWVGNDFTQNAGTGLVI 428
Cdd:cd00138    66 LRAGVNVRSYVTPPHFF-----ERLHA-------KVVVIDGEvAYVGSANLSTASAAQNREAGVLV 119
PLDc_2 pfam13091
PLD-like domain;
95-224 1.16e-05

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 44.98  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  95 NLLNMAKKSVDIVSSHWDLNhthpsacqgQRLFEKLLQLTSQNIEIKLVSDVTADS---------KVLEALKLKGAEVTY 165
Cdd:pfam13091   3 DLINSAKKSIDIATYYFVPD---------REIIDALIAAAKRGVDVRIILDSNKDDaggpkkaslKELRSLLRAGVEIRE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370452221 166 MNMTAynkGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNcSCLVLDLQRIF 224
Cdd:pfam13091  74 YQSFL---RSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEF 128
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 283-451 2.87e-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: 43.80  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 283 IDAIYSVIDDAKQYVYIAVMDYLPisststkrtywpdlDAKIREALV---LRSVRVRLLL-SFWKETDPlTFNFISSLKA 358
Cdd:cd09128    12 REALLALIDSAEESLLIQNEEMGD--------------DAPILDALVdaaKRGVDVRVLLpSAWSAEDE-RQARLRALEG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221 359 IcteiancSLKVKFFDLEREnacatkeqKNHtfprlnrNKYMVTDG-AAYIGNFDWVGNDFTQNAGTGLVINQADVrnnr 437
Cdd:cd09128    77 A-------GVPVRLLKDKFL--------KIH-------AKGIVVDGkTALVGSENWSANSLDRNREVGLIFDDPEV---- 130

                         170
                  ....*....|....
gi 1370452221 438 siIKQLKDVFERDW 451
Cdd:cd09128   131 --AAYLQAVFESDW 142
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 172-197 2.37e-03

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: 35.44  E-value: 2.37e-03
                           10        20
                   ....*....|....*....|....*.
gi 1370452221  172 NKGRLQSSFWIVDKQHVYIGSAGLDW 197
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDG 26
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 88-225 2.42e-03

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: 40.31  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370452221  88 SLFQGWMNLLNMAKKSVDIVSSHWDLnhthpsacqGQRLFEKLLQLTSQNIEIKLVSDVTADSKV--------LEALKLK 159
Cdd:COG1502   203 TIERALLAAIASARRRIYIETPYFVP---------DRSLLRALIAAARRGVDVRILLPAKSDHPLvhwasrsyYEELLEA 273

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370452221 160 GAEVTYmnmtaYNKGRLQSSFWIVDKQHVYIGSAGLDWQSLGQMKELGVIFYNCScLVLDLQRIFA 225
Cdd:COG1502   274 GVRIYE-----YEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDPE-FAAQLRARFE 333
 
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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