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Conserved domains on  [gi|137828|sp|P25392|]
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RecName: Full=Envelope protein F13 homolog; AltName: Full=43 kDa protein; AltName: Full=p43K

Protein Classification

PHA03003 family protein( domain architecture ID 11476127)

PHA03003 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 1-374 0e+00

palmytilated EEV membrane glycoprotein; Provisional


:

Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 560.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828      1 MGNLTSAQPAGCKIVETLPATLplALPAGSMLTYDCFDTLISQTQSELCIASYCCNLRSTPEGGHVLLRLLELARANVRV 80
Cdd:PHA03003   2 WPFSKPPPGAGCRIVETLPKSL--GIATQHMSTYECFDEIISQAKKYIYIASFCCNLRSTPEGRLILDKLKEAAESGVKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     81 TIIVDEQSRDADATQLAGVpNLRYLKMDVGELPGgkPGSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLGVYSECAPLA 160
Cdd:PHA03003  80 TILVDEQSGDKDEEELQSS-NINYIKVDIGKLNN--VGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLGVYSTYPPLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    161 RDLRRRFRDYERLCARRCL-------RCLSLSTRFHLRRRCGDAFFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMEL 233
Cdd:PHA03003 157 TDLRRRFDTFKAFNKNKSVfnrlccaCCLPVSTKYHINNPIGGVFFSDSPEHLLGYSRTLDADVVLHKIKSAKKSIDLEL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    234 LSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRSDVFSLAAVKGLHELGVGHaDISVRVFAIPgakgdai 313
Cdd:PHA03003 237 LSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCVGN-DLSVKVFRIP------- 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 137828    314 NNTKLLVVDDEYVHVSNADIDGTHYARHAFVSFNCAERTFARALGALFERDWQSSFSSPLP 374
Cdd:PHA03003 309 NNTKLLIVDDEFAHITSANFDGTHYLHHAFVSFNTIDKELVKELSAIFERDWTSSYSKPLK 369
 
Name Accession Description Interval E-value
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 1-374 0e+00

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 560.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828      1 MGNLTSAQPAGCKIVETLPATLplALPAGSMLTYDCFDTLISQTQSELCIASYCCNLRSTPEGGHVLLRLLELARANVRV 80
Cdd:PHA03003   2 WPFSKPPPGAGCRIVETLPKSL--GIATQHMSTYECFDEIISQAKKYIYIASFCCNLRSTPEGRLILDKLKEAAESGVKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     81 TIIVDEQSRDADATQLAGVpNLRYLKMDVGELPGgkPGSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLGVYSECAPLA 160
Cdd:PHA03003  80 TILVDEQSGDKDEEELQSS-NINYIKVDIGKLNN--VGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLGVYSTYPPLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    161 RDLRRRFRDYERLCARRCL-------RCLSLSTRFHLRRRCGDAFFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMEL 233
Cdd:PHA03003 157 TDLRRRFDTFKAFNKNKSVfnrlccaCCLPVSTKYHINNPIGGVFFSDSPEHLLGYSRTLDADVVLHKIKSAKKSIDLEL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    234 LSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRSDVFSLAAVKGLHELGVGHaDISVRVFAIPgakgdai 313
Cdd:PHA03003 237 LSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCVGN-DLSVKVFRIP------- 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 137828    314 NNTKLLVVDDEYVHVSNADIDGTHYARHAFVSFNCAERTFARALGALFERDWQSSFSSPLP 374
Cdd:PHA03003 309 NNTKLLIVDDEFAHITSANFDGTHYLHHAFVSFNTIDKELVKELSAIFERDWTSSYSKPLK 369
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 198-365 7.04e-66

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: 207.11  E-value: 7.04e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   198 FFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRS 277
Cdd:cd09107   1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   278 DVFSLAAVKGL--HELGVGHADISVRVFAIPGAKG-----DAINNTKLLVVdDEYVHVSNADIDGTHYARHAFVSFNCAE 350
Cdd:cd09107  81 DPSMDAFLKSLqlLKSGVGNGDIEVKIFTVPGDQStkipfARVNHAKYMVT-DERAYIGTSNWSGDYFYNTAGVSLVIND 159

                       170
                ....*....|....*
gi 137828   351 RTFARALGALFERDW 365
Cdd:cd09107 160 PAIVQQLKDVFERDW 174
PLDc_3 pfam13918
PLD-like domain;
143-307 7.14e-36

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 129.36  E-value: 7.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     143 SISTIKSLGVYS-ECAPLARDLRRRFRDY--------------ERLCarrCLRCLSLSTRFHLRRRCGDAFFSDAPESLI 207
Cdd:pfam13918   1 SLGQIKELGLVFtNCKCLALDLMNIFALFsslifenkvpftwsKRLC---CAVDNEKALNFHLNESGGGAFFSDSPELFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     208 GSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRSDVFSLAAVKG 287
Cdd:pfam13918  78 GFNRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARS 157

                         170       180
                  ....*....|....*....|..
gi 137828     288 LHELG--VGHADISVRVFAIPG 307
Cdd:pfam13918 158 LDAFCteIANCDLKVKFFDLEG 179
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 124-368 1.61e-07

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: 52.64  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   124 FWVSDKRRFYLGSASLTGGSISTIKSLGVYSECA-----PLARDLRRRFRDYERLCARRclrclslstRFHLRRRCGDA- 197
Cdd:COG1502 119 IVVIDGRVAFVGGANITDEYLGRDPGFGPWRDTHvriegPAVADLQAVFAEDWNFATGE---------ALPFPEPAGDVr 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   198 --FFSDAPESLIGSTRtfdaDAVLAHVQAARSTIDMELLSLVPlvrDEdsvkywpRMHDALVRAAlERNVRLRLLVGlwH 275
Cdd:COG1502 190 vqVVPSGPDSPRETIE----RALLAAIASARRRIYIETPYFVP---DR-------SLLRALIAAA-RRGVDVRILLP--A 252

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   276 RSDVF-----SLAAVKGLHELGVghadisvRVFAIPGAkgdaINNTKLLVVDDEYVHV--SNADIdgtHYARHAF-VSFN 347
Cdd:COG1502 253 KSDHPlvhwaSRSYYEELLEAGV-------RIYEYEPG----FLHAKVMVVDDEWALVgsANLDP---RSLRLNFeVNLV 318

                       250       260
                ....*....|....*....|.
gi 137828   348 CAERTFARALGALFERDWQSS 368
Cdd:COG1502 319 IYDPEFAAQLRARFEEDLAHS 339
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 117-143 3.86e-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: 37.37  E-value: 3.86e-04
                           10        20
                   ....*....|....*....|....*..
gi 137828      117 PGSLLSSFWVSDKRRFYLGSASLTGGS 143
Cdd:smart00155   2 DGVLHTKLMIVDDEIAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 1-374 0e+00

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 560.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828      1 MGNLTSAQPAGCKIVETLPATLplALPAGSMLTYDCFDTLISQTQSELCIASYCCNLRSTPEGGHVLLRLLELARANVRV 80
Cdd:PHA03003   2 WPFSKPPPGAGCRIVETLPKSL--GIATQHMSTYECFDEIISQAKKYIYIASFCCNLRSTPEGRLILDKLKEAAESGVKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     81 TIIVDEQSRDADATQLAGVpNLRYLKMDVGELPGgkPGSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLGVYSECAPLA 160
Cdd:PHA03003  80 TILVDEQSGDKDEEELQSS-NINYIKVDIGKLNN--VGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLGVYSTYPPLA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    161 RDLRRRFRDYERLCARRCL-------RCLSLSTRFHLRRRCGDAFFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMEL 233
Cdd:PHA03003 157 TDLRRRFDTFKAFNKNKSVfnrlccaCCLPVSTKYHINNPIGGVFFSDSPEHLLGYSRTLDADVVLHKIKSAKKSIDLEL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    234 LSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRSDVFSLAAVKGLHELGVGHaDISVRVFAIPgakgdai 313
Cdd:PHA03003 237 LSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCVGN-DLSVKVFRIP------- 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 137828    314 NNTKLLVVDDEYVHVSNADIDGTHYARHAFVSFNCAERTFARALGALFERDWQSSFSSPLP 374
Cdd:PHA03003 309 NNTKLLIVDDEFAHITSANFDGTHYLHHAFVSFNTIDKELVKELSAIFERDWTSSYSKPLK 369
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 198-365 7.04e-66

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: 207.11  E-value: 7.04e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   198 FFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRS 277
Cdd:cd09107   1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   278 DVFSLAAVKGL--HELGVGHADISVRVFAIPGAKG-----DAINNTKLLVVdDEYVHVSNADIDGTHYARHAFVSFNCAE 350
Cdd:cd09107  81 DPSMDAFLKSLqlLKSGVGNGDIEVKIFTVPGDQStkipfARVNHAKYMVT-DERAYIGTSNWSGDYFYNTAGVSLVIND 159

                       170
                ....*....|....*
gi 137828   351 RTFARALGALFERDW 365
Cdd:cd09107 160 PAIVQQLKDVFERDW 174
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 14-157 9.82e-47

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: 156.64  E-value: 9.82e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    14 IVETLPATLPLALPAGSMLTYDCFDTLISQTQSELCIASYCCNLR--------STPEGGHVLLRLLELARANVRVTIIVD 85
Cdd:cd09106   1 LVESIPEGLTFLSSSSHLSTFEAWMELISSAKKSIDIASFYWNLRgtdtnpdsSAQEGEDIFNALLEAAKRGVKIRILQD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 137828    86 EQSR---DADATQLAGVPNLRYLKMDVGELPGGkpGSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLGVYSECA 157
Cdd:cd09106  81 KPSKdkpDEDDLELAALGGAEVRSLDFTKLIGG--GVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PLDc_3 pfam13918
PLD-like domain;
143-307 7.14e-36

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 129.36  E-value: 7.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     143 SISTIKSLGVYS-ECAPLARDLRRRFRDY--------------ERLCarrCLRCLSLSTRFHLRRRCGDAFFSDAPESLI 207
Cdd:pfam13918   1 SLGQIKELGLVFtNCKCLALDLMNIFALFsslifenkvpftwsKRLC---CAVDNEKALNFHLNESGGGAFFSDSPELFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     208 GSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRSDVFSLAAVKG 287
Cdd:pfam13918  78 GFNRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARS 157

                         170       180
                  ....*....|....*....|..
gi 137828     288 LHELG--VGHADISVRVFAIPG 307
Cdd:pfam13918 158 LDAFCteIANCDLKVKFFDLEG 179
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 14-385 7.43e-32

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 124.72  E-value: 7.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     14 IVETLPATLPLALPAGSmlTYDCFDTLISQTQSELCIASY---CCNLRSTPEGGHVLLRLLELARANVRVTIIVDEQ--- 87
Cdd:PHA02820  10 ITETIPIGMQFDKVYLS--TFNFWREILSNTTKTLDISSFywsLSDEVGTNFGTMILNEIIQLPKRGVRVRIAVNKSnkp 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     88 SRDADATQLAGVpNLRYLkmDVGELPGGkpgSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLGV---YSECapLARDLR 164
Cdd:PHA02820  88 LKDVELLQMAGV-EVRYI--DITNILGG---VLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIaifNNSN--LAADLT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    165 RRFRDYERLCARRcLRC---------------LSL--STRFHlrrrcgDAFFSDAPESLIGSTRTFDADAVLAHVQAARS 227
Cdd:PHA02820 160 QIFEVYWYLGVNN-LPYnwknfyplyyntdhpLSLnvSGVPH------SVFIASAPQQLCTMERTNDLTALLSCIRNASK 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    228 TIDMELLSLVPLVRDE-DSVKYWPRMHDALVRAALERNVRLRLLVGLWHRSDVFSLAAVKGLHELGVGHADISVRVFAIP 306
Cdd:PHA02820 233 FVYVSVMNFIPIIYSKaGKILFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLKSKNINIEVKLFIVP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    307 GAKGDA----INNTKLLVVDD-EYVHVSNAdiDGTHYARHAFVSFNCA---ERTFARALGALFERDWQSSFSSPLPRALP 378
Cdd:PHA02820 313 DADPPIpysrVNHAKYMVTDKtAYIGTSNW--TGNYFTDTCGVSINITpddGLGLRQQLEDIFIRDWNSKYSYELYDTSP 390


                 ....*..
gi 137828    379 PEPATLL 385
Cdd:PHA02820 391 TKRCRLL 397
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 198-370 8.55e-22

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: 91.57  E-value: 8.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   198 FFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRS 277
Cdd:cd09147   1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   278 D------VFSLAAVKGLHElgvgHADISVRVFAIPGAKGDA------INNTKLLVVDD-EYVHVSNADIDG-THYARHAF 343
Cdd:cd09147  81 EpsmfafLRSLAALRDNTT----HSDIQVKIFVVPADEAQKkipyarVNHNKYMVTDRvAYIGTSNWSGDYfTNTAGSAL 156

                       170       180       190
                ....*....|....*....|....*....|
gi 137828   344 V---SFNCAERTFARALGALFERDWQSSFS 370
Cdd:cd09147 157 VvnqTGRSASGTLQSQLQAVFERDWDSPYS 186
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 198-370 1.81e-19

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: 85.28  E-value: 1.81e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   198 FFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVKYWPRMHDALVRAALERNVRLRLLVGLWHRS 277
Cdd:cd09148   1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   278 DVFSLAAVKGLHELGVGHADIS--VRVFAIPGAKGDAI-----NNTKLLVVDD-EYVHVSNADIDgtHYARHAFVSF--- 346
Cdd:cd09148  81 DPDMFPFLRSLNALSNPPLSISvhVKLFIVPVGNQTNIpysrvNHNKFMVTDKaAYIGTSNWSED--YFLNTAGVGLvil 158

                       170       180
                ....*....|....*....|....*....
gi 137828   347 -----NCAERTFARALGALFERDWQSSFS 370
Cdd:cd09148 159 qspgaNEEMLPVQEQLRSLFERDWSSPYA 187
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 198-373 8.79e-17

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: 77.97  E-value: 8.79e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   198 FFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVKYWPRMhDALVRAALE-RNVRLRLLVGLWHR 276
Cdd:cd09149   1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRI-DSKIREALVlRSVRVRLLISFWRK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   277 SDVFSLAAVKGLHELGVGHADIS--VRVFAIPGAKGDA---INNTKLLVVDDEyVHVSNADIDGTHYARHAFVSF--NCA 349
Cdd:cd09149  80 TDPLTFNFVSSLKSLCTEQANCSleVKFFDLEEESDCTsprLNRNKYMVTDGA-AYIGNFDWVGNDFTQNAGVGLviNQA 158

                       170       180       190
                ....*....|....*....|....*....|
gi 137828   350 E------RTFARALGALFERDWQSSFSSPL 373
Cdd:cd09149 159 DgveennATIIEQLRAAFERDWYSNYAKSL 188
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 14-170 1.98e-11

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: 62.23  E-value: 1.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    14 IVETLPATLPLAL--PAGSMLtYDCFDTLISQTQSELCIASY---------CCNLRSTPEGGHVLLRLLELARANVRVTI 82
Cdd:cd09145   1 LVESIPEDLTYEGnsTFALPL-QKAWTKLLDMAQEQVHVASYywsltgediGVNDSSSLPGEDILKELAELLSRNVSVRA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    83 IVDEQSRDADATQLA-----GVpNLRylKMDVGELPGGkpgSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLG-VYSEC 156
Cdd:cd09145  80 AASIPTLAANSTDLKilrqkGA-HVR--KVNFGRLTGG---VLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGaVIYNC 153

                       170
                ....*....|....
gi 137828   157 APLARDLRRRFRDY 170
Cdd:cd09145 154 SSLAKDLHKTFQTY 167
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 14-170 1.10e-10

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: 59.96  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    14 IVETLPATLplALPAGSML---TYDCFDTLISQTQSELCIASYCCNLR---------STPEGGHVLLRLLELARANVRVT 81
Cdd:cd09144   2 LVESIPEGL--VFNSSSTInpsIYQAWLNLISAAQSSLDIASFYWTLTnsdthtqepSANQGEQILKKLGQLSQSGVYVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828    82 IIVD-----EQSRDADATQLAGVpNLRYLKMdvgelPGGKPGSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLG-VYSE 155
Cdd:cd09144  80 IAVDkpadpKPMEDINALSSYGA-DVRMVDM-----RKLTTGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGaVVYN 153

                       170
                ....*....|....*
gi 137828   156 CAPLARDLRRRFRDY 170
Cdd:cd09144 154 CSCLAEDLGKIFEAY 168
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 118-173 5.70e-10

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: 57.56  E-value: 5.70e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 137828   118 GSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLGV-YSECAPLARDLRRRFRDYERL 173
Cdd:cd09146 107 GRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGViVYNCSCLALDLHRVFALYWSL 163
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 124-368 1.61e-07

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: 52.64  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   124 FWVSDKRRFYLGSASLTGGSISTIKSLGVYSECA-----PLARDLRRRFRDYERLCARRclrclslstRFHLRRRCGDA- 197
Cdd:COG1502 119 IVVIDGRVAFVGGANITDEYLGRDPGFGPWRDTHvriegPAVADLQAVFAEDWNFATGE---------ALPFPEPAGDVr 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   198 --FFSDAPESLIGSTRtfdaDAVLAHVQAARSTIDMELLSLVPlvrDEdsvkywpRMHDALVRAAlERNVRLRLLVGlwH 275
Cdd:COG1502 190 vqVVPSGPDSPRETIE----RALLAAIASARRRIYIETPYFVP---DR-------SLLRALIAAA-RRGVDVRILLP--A 252

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   276 RSDVF-----SLAAVKGLHELGVghadisvRVFAIPGAkgdaINNTKLLVVDDEYVHV--SNADIdgtHYARHAF-VSFN 347
Cdd:COG1502 253 KSDHPlvhwaSRSYYEELLEAGV-------RIYEYEPG----FLHAKVMVVDDEWALVgsANLDP---RSLRLNFeVNLV 318

                       250       260
                ....*....|....*....|.
gi 137828   348 CAERTFARALGALFERDWQSS 368
Cdd:COG1502 319 IYDPEFAAQLRARFEEDLAHS 339
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 216-384 1.79e-07

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: 52.64  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   216 DAVLAHVQAARSTIDMELLSLvplvrDEDSVkyWPRMHDALVRAAlERNVRLRLLVGlWHRSDVFSLAAVKGLHELGvgh 295
Cdd:COG1502  28 AALLEAIEAARRSIDLEYYIF-----DDDEV--GRRLADALIAAA-RRGVKVRVLLD-GIGSRALNRDFLRRLRAAG--- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   296 adISVRVF---AIPGAKGDAINNTKLLVVDDEYVHVSNADIDGTHYARHAFVSFNcAERTF------ARALGALFERDWQ 366
Cdd:COG1502  96 --VEVRLFnpvRLLFRRLNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGPW-RDTHVriegpaVADLQAVFAEDWN 172

                       170
                ....*....|....*...
gi 137828   367 SSFSSPLPRALPPEPATL 384
Cdd:COG1502 173 FATGEALPFPEPAGDVRV 190
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 215-365 5.83e-06

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: 45.73  E-value: 5.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   215 ADAVLAHVQAARSTIDMEllslvplvrdEDSVKYWPRMHDALVRAAlERNVRLRLLVGLWHRSDVFSLAAVKGLHELGVG 294
Cdd:cd09128  12 REALLALIDSAEESLLIQ----------NEEMGDDAPILDALVDAA-KRGVDVRVLLPSAWSAEDERQARLRALEGAGVP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 137828   295 hadisVRVFAIPGAKgdaiNNTKLLVVDDEYVHVS--NADIDGTHYARHAFVSFNcAERTFARaLGALFERDW 365
Cdd:cd09128  81 -----VRLLKDKFLK----IHAKGIVVDGKTALVGseNWSANSLDRNREVGLIFD-DPEVAAY-LQAVFESDW 142
PLDc_2 pfam13091
PLD-like domain;
218-365 1.63e-05

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 44.21  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828     218 VLAHVQAARSTIDMELLSLVPLvrdedsvkywPRMHDALVRAALeRNVRLRLLVGLWHrsDVFSLAAVKGLHELG-VGHA 296
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPD----------REIIDALIAAAK-RGVDVRIILDSNK--DDAGGPKKASLKELRsLLRA 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 137828     297 DISVRVFAIPgakgDAINNTKLLVVDDEYVHV--SNADIDGTHYAR-HAFVSFNcaeRTFARALGALFERDW 365
Cdd:pfam13091  68 GVEIREYQSF----LRSMHAKFYIIDGKTVIVgsANLTRRALRLNLeNNVVIKD---PELAQELEKEFDRLW 132
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 117-143 7.50e-05

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: 39.32  E-value: 7.50e-05
                          10        20
                  ....*....|....*....|....*..
gi 137828     117 PGSLLSSFWVSDKRRFYLGSASLTGGS 143
Cdd:pfam00614   2 DGRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 216-344 2.27e-04

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: 40.58  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   216 DAVLAHVQAARSTIDMELLSLvplvrdedSVKYWPRMHDALvRAALERNVRLRLLVGlWHRSDVFSLAAVKGLHELgvgH 295
Cdd:cd00138   1 EALLELLKNAKESIFIATPNF--------SFNSADRLLKAL-LAAAERGVDVRLIID-KPPNAAGSLSAALLEALL---R 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 137828   296 ADISVRVFAIPGAKGDAiNNTKLLVVDDEYVHVS--NADIDGTHYARHAFV 344
Cdd:cd00138  68 AGVNVRSYVTPPHFFER-LHAKVVVIDGEVAYVGsaNLSTASAAQNREAGV 117
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 117-143 3.86e-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: 37.37  E-value: 3.86e-04
                           10        20
                   ....*....|....*....|....*..
gi 137828      117 PGSLLSSFWVSDKRRFYLGSASLTGGS 143
Cdd:smart00155   2 DGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
 215-335 3.74e-03

Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; Catalytic domain, repeat 2, of phospholipase D (PLD, EC 3.1.4.4) found in yeast, plants, and vertebrates, and their bacterial homologs. PLDs are involved in signal transduction, vesicle formation, protein transport, and mitosis by participating in phospholipid metabolism. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both prokaryotic and eukaryotic PLDs have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. PLDs are active as bi-lobed monomers. Each monomer contains two domains, each of which carries one copy of the HKD motif. Two HKD motifs from two domains form a single active site. PLDs 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 residue 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: 197204 [Multi-domain]  Cd Length: 146  Bit Score: 37.67  E-value: 3.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 137828   215 ADAVLAHVQAARSTIDMELLSLVPlvrdedsvkywPRMHDALVRAaLERNVRLRLLVGLWHRSDVFSLAAVKGLHELGVG 294
Cdd:cd09105  10 ADAYLKAIRNARRYIYIEDQYLWS-----------PELLDALAEA-LKANPGLRVVLVLPALPDAVAFGADDGLDALALL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 137828   295 HADISV-----RVFAIPGAKGDAINNT--------KLLVVDDEYVHVSNADIDG 335
Cdd:cd09105  78 ALLLLAdaapdRVAVFSLATHRRGLLGgppiyvhsKVVIVDDEWATVGSANLNR 131
 
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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