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Conserved domains on  [gi|17861816|gb|AAL39385|]
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GM01519p [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA02820 super family cl33698
phospholipase-D-like protein; Provisional
 89-493 2.92e-108

phospholipase-D-like protein; Provisional


The actual alignment was detected with superfamily member PHA02820:

Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 328.49  E-value: 2.92e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   89 LVESIPIGLtypDGSPRFLSTYEAWLELLESATTSLDIASFYWTLKAEDtpgvsdnSTRPGEDVFARLLangNGGSRSPR 168
Cdd:PHA02820  10 ITETIPIGM---QFDKVYLSTFNFWREILSNTTKTLDISSFYWSLSDEV-------GTNFGTMILNEII---QLPKRGVR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  169 IKIRIAQSEpssgTPNLNTKLLASAGAaEVVSISFPKYFGsGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQN 248
Cdd:PHA02820  77 VRIAVNKSN----KPLKDVELLQMAGV-EVRYIDITNILG-GVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  249 CPELTHDVAKIFGEYWYLGnseSSRIP-DWDWRYATSYNLKHPMQLsVNKNTSIEGFLSSSPPPLSPSGRTDDLNAILNT 327
Cdd:PHA02820 151 NSNLAADLTQIFEVYWYLG---VNNLPyNWKNFYPLYYNTDHPLSL-NVSGVPHSVFIASAPQQLCTMERTNDLTALLSC 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  328 INTAITYVNIAVMDYYPlIIYEKNHH--YWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQDLASKedKID 405
Cdd:PHA02820 227 IRNASKFVYVSVMNFIP-IIYSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NIN 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  406 IQIRRFIVPtdSSQEKIPFGRVNHNKYMVTDRVAYIGTSNWSGDYFTDTAGIGLVLSetfeTETTNTLRSDLRNVFERDW 485
Cdd:PHA02820 304 IEVKLFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINIT----PDDGLGLRQQLEDIFIRDW 377


                 ....*...
gi 17861816  486 NSKYATPL 493
Cdd:PHA02820 378 NSKYSYEL 385
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 89-493 2.92e-108

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 328.49  E-value: 2.92e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   89 LVESIPIGLtypDGSPRFLSTYEAWLELLESATTSLDIASFYWTLKAEDtpgvsdnSTRPGEDVFARLLangNGGSRSPR 168
Cdd:PHA02820  10 ITETIPIGM---QFDKVYLSTFNFWREILSNTTKTLDISSFYWSLSDEV-------GTNFGTMILNEII---QLPKRGVR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  169 IKIRIAQSEpssgTPNLNTKLLASAGAaEVVSISFPKYFGsGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQN 248
Cdd:PHA02820  77 VRIAVNKSN----KPLKDVELLQMAGV-EVRYIDITNILG-GVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  249 CPELTHDVAKIFGEYWYLGnseSSRIP-DWDWRYATSYNLKHPMQLsVNKNTSIEGFLSSSPPPLSPSGRTDDLNAILNT 327
Cdd:PHA02820 151 NSNLAADLTQIFEVYWYLG---VNNLPyNWKNFYPLYYNTDHPLSL-NVSGVPHSVFIASAPQQLCTMERTNDLTALLSC 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  328 INTAITYVNIAVMDYYPlIIYEKNHH--YWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQDLASKedKID 405
Cdd:PHA02820 227 IRNASKFVYVSVMNFIP-IIYSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NIN 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  406 IQIRRFIVPtdSSQEKIPFGRVNHNKYMVTDRVAYIGTSNWSGDYFTDTAGIGLVLSetfeTETTNTLRSDLRNVFERDW 485
Cdd:PHA02820 304 IEVKLFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINIT----PDDGLGLRQQLEDIFIRDW 377


                 ....*...
gi 17861816  486 NSKYATPL 493
Cdd:PHA02820 378 NSKYSYEL 385
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 316-486 1.67e-83

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: 255.64  E-value: 1.67e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 316 GRTDDLNAILNTINTAITYVNIAVMDYYPLIIYEKNHHYWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQ 395
Cdd:cd09107  13 GRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHTDPSMDAFLKSLQ 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 396 DLASKEDKIDIQIRRFIVPTDSSQeKIPFGRVNHNKYMVTDRVAYIGTSNWSGDYFTDTAGIGLVLsetfeteTTNTLRS 475
Cdd:cd09107  93 LLKSGVGNGDIEVKIFTVPGDQST-KIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVSLVI-------NDPAIVQ 164

                       170
                ....*....|.
gi 17861816 476 DLRNVFERDWN 486
Cdd:cd09107 165 QLKDVFERDWN 175
PLDc_3 pfam13918
PLD-like domain;
235-414 8.61e-28

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 109.33  E-value: 8.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   235 ALTQVKEMGVLVQNCPELTHDVAKIFGEYWYLgnSESSRIP-DWDWRYATSYNLKHPMQLSVNKNTSiEGFLSSSPPPLS 313
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSL--IFENKVPfTWSKRLCCAVDNEKALNFHLNESGG-GAFFSDSPELFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   314 PSGRTDDLNAILNTINTAITYVNIAVMDYYPLIIYEKNHHYWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRS 393
Cdd:pfam13918  78 GFNRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARS 157

                         170       180
                  ....*....|....*....|.
gi 17861816   394 LQDLASKEDKIDIQIRRFIVP 414
Cdd:pfam13918 158 LDAFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 109-447 1.00e-15

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: 78.45  E-value: 1.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 109 TYEAWLELLESATTSLDIASFYWTlkaedtpgvsdnSTRPGEDVFARLLAngnggSRSPRIKIRI-AQSEPSSGTPNLNT 187
Cdd:COG1502  26 AFAALLEAIEAARRSIDLEYYIFD------------DDEVGRRLADALIA-----AARRGVKVRVlLDGIGSRALNRDFL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 188 KLLASAGAaEV---VSISFPKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKE------MGVLVQNcpELTHDVAK 258
Cdd:COG1502  89 RRLRAAGV-EVrlfNPVRLLFRRLNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGfgpwrdTHVRIEG--PAVADLQA 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 259 IFGEYWYLGNSESSRIPDwdwryatsYNLKHPMQLSVNKNTSiegflsssppplspsgRTDDLN-AILNTINTAITYVNI 337
Cdd:COG1502 166 VFAEDWNFATGEALPFPE--------PAGDVRVQVVPSGPDS----------------PRETIErALLAAIASARRRIYI 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 338 AVMDYYPliiyeknhhywpfiDDALRKA---AVERGVAVKLLISwWKHSNPSEDRYLRS-LQDLAskedKIDIQIRRFIv 413
Cdd:COG1502 222 ETPYFVP--------------DRSLLRAliaAARRGVDVRILLP-AKSDHPLVHWASRSyYEELL----EAGVRIYEYE- 281

                       330       340       350
                ....*....|....*....|....*....|....*
gi 17861816 414 ptdssqekipfGRVNHNKYMVTD-RVAYIGTSNWS 447
Cdd:COG1502 282 -----------PGFLHAKVMVVDdEWALVGSANLD 305
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 210-235 3.23e-09

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: 52.01  E-value: 3.23e-09
                           10        20
                   ....*....|....*....|....*.
gi 17861816    210 GVLHTKLWVVDNKHFYLGSANMDWRA 235
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
DISARM_DrmC_I NF038319
DISARM system phospholipase D-like protein DrmC; DrmC, a phospholipase D (PLD) ...
 114-257 4.93e-06

DISARM system phospholipase D-like protein DrmC; DrmC, a phospholipase D (PLD) domain-containing protein, is a component of DISARM (Defence Island System Associated with Restriction Modification). This HMM represents most but not all DrmC of class I DISARM systems, which contain a DNA adenine N6 methyltransferase. DrmC appears to be an auxiliary rather than core component of DISARM, required for resistance to some phage but not others.


Pssm-ID: 468473 [Multi-domain]  Cd Length: 234  Bit Score: 47.57  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  114 LELLESATTSLDIASFywtlkaedtpgvsdnSTRPGEDVFARLL-ANGNGgsrsprIKIRIA--QSEPSSGTPNLNTKLL 190
Cdd:NF038319  99 LELIRAARQSLLLVTF---------------AAYKVSPLVEALAaAAARG------VAVRVLleTSEGAGGALSGDEPAR 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  191 ASAGAAEV---VSISFPKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQNcPELTHDVA 257
Cdd:NF038319 158 AFAGVPGArvwHWPVDPRALRGGSLHAKVAVADRRVLLVTSANLTESALERNIEAGVLIRG-GALPERLA 226
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 89-493 2.92e-108

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 328.49  E-value: 2.92e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   89 LVESIPIGLtypDGSPRFLSTYEAWLELLESATTSLDIASFYWTLKAEDtpgvsdnSTRPGEDVFARLLangNGGSRSPR 168
Cdd:PHA02820  10 ITETIPIGM---QFDKVYLSTFNFWREILSNTTKTLDISSFYWSLSDEV-------GTNFGTMILNEII---QLPKRGVR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  169 IKIRIAQSEpssgTPNLNTKLLASAGAaEVVSISFPKYFGsGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQN 248
Cdd:PHA02820  77 VRIAVNKSN----KPLKDVELLQMAGV-EVRYIDITNILG-GVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  249 CPELTHDVAKIFGEYWYLGnseSSRIP-DWDWRYATSYNLKHPMQLsVNKNTSIEGFLSSSPPPLSPSGRTDDLNAILNT 327
Cdd:PHA02820 151 NSNLAADLTQIFEVYWYLG---VNNLPyNWKNFYPLYYNTDHPLSL-NVSGVPHSVFIASAPQQLCTMERTNDLTALLSC 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  328 INTAITYVNIAVMDYYPlIIYEKNHH--YWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQDLASKedKID 405
Cdd:PHA02820 227 IRNASKFVYVSVMNFIP-IIYSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLKSK--NIN 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  406 IQIRRFIVPtdSSQEKIPFGRVNHNKYMVTDRVAYIGTSNWSGDYFTDTAGIGLVLSetfeTETTNTLRSDLRNVFERDW 485
Cdd:PHA02820 304 IEVKLFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINIT----PDDGLGLRQQLEDIFIRDW 377


                 ....*...
gi 17861816  486 NSKYATPL 493
Cdd:PHA02820 378 NSKYSYEL 385
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 316-486 1.67e-83

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: 255.64  E-value: 1.67e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 316 GRTDDLNAILNTINTAITYVNIAVMDYYPLIIYEKNHHYWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQ 395
Cdd:cd09107  13 GRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHTDPSMDAFLKSLQ 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 396 DLASKEDKIDIQIRRFIVPTDSSQeKIPFGRVNHNKYMVTDRVAYIGTSNWSGDYFTDTAGIGLVLsetfeteTTNTLRS 475
Cdd:cd09107  93 LLKSGVGNGDIEVKIFTVPGDQST-KIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVSLVI-------NDPAIVQ 164

                       170
                ....*....|.
gi 17861816 476 DLRNVFERDWN 486
Cdd:cd09107 165 QLKDVFERDWN 175
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 89-249 1.28e-74

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: 231.75  E-value: 1.28e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  89 LVESIPIGLTYPDGSpRFLSTYEAWLELLESATTSLDIASFYWTLKAEDTPGvsDNSTRPGEDVFARLLANGNGGsrspr 168
Cdd:cd09106   1 LVESIPEGLTFLSSS-SHLSTFEAWMELISSAKKSIDIASFYWNLRGTDTNP--DSSAQEGEDIFNALLEAAKRG----- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 169 IKIRIAQSEPSSGTPNLNTKLLASAGAAEVVSISFPKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQN 248
Cdd:cd09106  73 VKIRILQDKPSKDKPDEDDLELAALGGAEVRSLDFTKLIGGGVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYN 152


                .
gi 17861816 249 C 249
Cdd:cd09106 153 C 153
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 316-490 7.94e-74

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: 231.01  E-value: 7.94e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 316 GRTDDLNAILNTINTAITYVNIAVMDYYPLIIYEKNHHYWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQ 395
Cdd:cd09147  13 GRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHSEPSMFAFLRSLA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 396 DLASKEDKIDIQIRRFIVPTDSSQEKIPFGRVNHNKYMVTDRVAYIGTSNWSGDYFTDTAGIGLVLSeTFETETTNTLRS 475
Cdd:cd09147  93 ALRDNTTHSDIQVKIFVVPADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSALVVN-QTGRSASGTLQS 171

                       170
                ....*....|....*
gi 17861816 476 DLRNVFERDWNSKYA 490
Cdd:cd09147 172 QLQAVFERDWDSPYS 186
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 316-490 2.84e-67

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: 214.32  E-value: 2.84e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 316 GRTDDLNAILNTINTAITYVNIAVMDYYPLIIYEKNHHYWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQ 395
Cdd:cd09148  13 GRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHSDPDMFPFLRSLN 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 396 DLASKEDKIDIQIRRFIVPTdSSQEKIPFGRVNHNKYMVTDRVAYIGTSNWSGDYFTDTAGIGLVLSETF-ETETTNTLR 474
Cdd:cd09148  93 ALSNPPLSISVHVKLFIVPV-GNQTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVGLVILQSPgANEEMLPVQ 171

                       170
                ....*....|....*.
gi 17861816 475 SDLRNVFERDWNSKYA 490
Cdd:cd09148 172 EQLRSLFERDWSSPYA 187
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 89-267 7.07e-55

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: 181.69  E-value: 7.07e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  89 LVESIPIGLTYPDGSPRFLSTYEAWLELLESATTSLDIASFYWTLKAEDTPgVSDNSTRPGEDVFARLlangngGSRSPR 168
Cdd:cd09144   2 LVESIPEGLVFNSSSTINPSIYQAWLNLISAAQSSLDIASFYWTLTNSDTH-TQEPSANQGEQILKKL------GQLSQS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 169 -IKIRIAQSEPSSGTPNLNTKLLASAGAaEVVSISFPKyFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQ 247
Cdd:cd09144  75 gVYVRIAVDKPADPKPMEDINALSSYGA-DVRMVDMRK-LTTGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVY 152

                       170       180
                ....*....|....*....|
gi 17861816 248 NCPELTHDVAKIFGEYWYLG 267
Cdd:cd09144 153 NCSCLAEDLGKIFEAYWYLG 172
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 89-266 8.44e-49

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: 165.47  E-value: 8.44e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  89 LVESIPIGLTYPDGSPRFLSTYEAWLELLESATTSLDIASFYWTLKAEDTpGVSDNSTRPGEDV---FARLLANGnggsr 165
Cdd:cd09145   1 LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWSLTGEDI-GVNDSSSLPGEDIlkeLAELLSRN----- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 166 sprIKIRIAQSEPSSGTPNLNTKLLASAGAaEVVSISFPKYFGsGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVL 245
Cdd:cd09145  75 ---VSVRAAASIPTLAANSTDLKILRQKGA-HVRKVNFGRLTG-GVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAV 149

                       170       180
                ....*....|....*....|.
gi 17861816 246 VQNCPELTHDVAKIFGEYWYL 266
Cdd:cd09145 150 IYNCSSLAKDLHKTFQTYWVL 170
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 84-493 4.45e-45

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 161.76  E-value: 4.45e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   84 DCniQLVESIPIGLTYPDGSprfLSTYEAWLELLESATTSLDIASFYWTLKaedtpgvsdnSTRPGEDVFARLLANGNGG 163
Cdd:PHA03003  12 GC--RIVETLPKSLGIATQH---MSTYECFDEIISQAKKYIYIASFCCNLR----------STPEGRLILDKLKEAAESG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  164 srsprIKIRIAQSEPSsgtPNLNTKLLASAGAaEVVSISFPKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMG 243
Cdd:PHA03003  77 -----VKVTILVDEQS---GDKDEEELQSSNI-NYIKVDIGKLNNVGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  244 VLVQNCPeLTHDVAKIFGEYWYLGNSESS---RIPDWDWRYATSYNLKHPmqlsvnkntsIEG-FLSSSPPPLSPSGRTD 319
Cdd:PHA03003 148 VYSTYPP-LATDLRRRFDTFKAFNKNKSVfnrLCCACCLPVSTKYHINNP----------IGGvFFSDSPEHLLGYSRTL 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  320 DLNAILNTINTAITYVNIAVMDYYPLIIYEKNHHYWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQDLAS 399
Cdd:PHA03003 217 DADVVLHKIKSAKKSIDLELLSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCV 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  400 KEdkiDIQIRRFIVPtdssqekipfgrvNHNKYMVTD-RVAYIGTSNWSGDYFTDTAGIGLvlsetfeTETTNTLRSDLR 478
Cdd:PHA03003 297 GN---DLSVKVFRIP-------------NNTKLLIVDdEFAHITSANFDGTHYLHHAFVSF-------NTIDKELVKELS 353

                        410
                 ....*....|....*
gi 17861816  479 NVFERDWNSKYATPL 493
Cdd:PHA03003 354 AIFERDWTSSYSKPL 368
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 317-493 7.97e-43

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: 150.39  E-value: 7.97e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 317 RTDDLNAILNTINTAITYVNIAVMDYYPLIIYEKNHHYWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRSLQD 396
Cdd:cd09149  14 RSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKTDPLTFNFVSSLKS 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 397 LASKEDKIDIQIRRFivptDSSQEKI-PFGRVNHNKYMVTDRVAYIGTSNWSGDYFTDTAGIGLVLSET-FETETTNTLR 474
Cdd:cd09149  94 LCTEQANCSLEVKFF----DLEEESDcTSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVGLVINQAdGVEENNATII 169

                       170
                ....*....|....*....
gi 17861816 475 SDLRNVFERDWNSKYATPL 493
Cdd:cd09149 170 EQLRAAFERDWYSNYAKSL 188
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 89-266 5.42e-30

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: 114.96  E-value: 5.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  89 LVESIPIGLTYPDGSPRFLSTYEAWLELLESATTSLDIASFYWTLKAedtpgvSDNSTRPGEDVFARLLangngGSRSPR 168
Cdd:cd09146   2 LVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDLNA------SHPSACQGQRLFERLL-----GLASRG 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 169 IKIRIAqSEPSSGTPNLNTklLASAGAaEVVSISFPKYfGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQN 248
Cdd:cd09146  71 VELKIV-SGITDSTEVLVL--LKKKGA-EVHYVNMTAL-TKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYN 145

                       170
                ....*....|....*...
gi 17861816 249 CPELTHDVAKIFGEYWYL 266
Cdd:cd09146 146 CSCLALDLHRVFALYWSL 163
PLDc_3 pfam13918
PLD-like domain;
235-414 8.61e-28

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 109.33  E-value: 8.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   235 ALTQVKEMGVLVQNCPELTHDVAKIFGEYWYLgnSESSRIP-DWDWRYATSYNLKHPMQLSVNKNTSiEGFLSSSPPPLS 313
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSL--IFENKVPfTWSKRLCCAVDNEKALNFHLNESGG-GAFFSDSPELFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   314 PSGRTDDLNAILNTINTAITYVNIAVMDYYPLIIYEKNHHYWPFIDDALRKAAVERGVAVKLLISWWKHSNPSEDRYLRS 393
Cdd:pfam13918  78 GFNRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARS 157

                         170       180
                  ....*....|....*....|.
gi 17861816   394 LQDLASKEDKIDIQIRRFIVP 414
Cdd:pfam13918 158 LDAFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 109-447 1.00e-15

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: 78.45  E-value: 1.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 109 TYEAWLELLESATTSLDIASFYWTlkaedtpgvsdnSTRPGEDVFARLLAngnggSRSPRIKIRI-AQSEPSSGTPNLNT 187
Cdd:COG1502  26 AFAALLEAIEAARRSIDLEYYIFD------------DDEVGRRLADALIA-----AARRGVKVRVlLDGIGSRALNRDFL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 188 KLLASAGAaEV---VSISFPKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKE------MGVLVQNcpELTHDVAK 258
Cdd:COG1502  89 RRLRAAGV-EVrlfNPVRLLFRRLNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGfgpwrdTHVRIEG--PAVADLQA 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 259 IFGEYWYLGNSESSRIPDwdwryatsYNLKHPMQLSVNKNTSiegflsssppplspsgRTDDLN-AILNTINTAITYVNI 337
Cdd:COG1502 166 VFAEDWNFATGEALPFPE--------PAGDVRVQVVPSGPDS----------------PRETIErALLAAIASARRRIYI 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 338 AVMDYYPliiyeknhhywpfiDDALRKA---AVERGVAVKLLISwWKHSNPSEDRYLRS-LQDLAskedKIDIQIRRFIv 413
Cdd:COG1502 222 ETPYFVP--------------DRSLLRAliaAARRGVDVRILLP-AKSDHPLVHWASRSyYEELL----EAGVRIYEYE- 281

                       330       340       350
                ....*....|....*....|....*....|....*
gi 17861816 414 ptdssqekipfGRVNHNKYMVTD-RVAYIGTSNWS 447
Cdd:COG1502 282 -----------PGFLHAKVMVVDdEWALVGSANLD 305
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 111-246 9.26e-14

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: 67.54  E-value: 9.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 111 EAWLELLESATTSLDIASFYWtlkaedtpgvsdnSTRPGEDVFARLLANGNGGsrsprIKIRIAQSEPSSGTPNLNTKLL 190
Cdd:cd00138   1 EALLELLKNAKESIFIATPNF-------------SFNSADRLLKALLAAAERG-----VDVRLIIDKPPNAAGSLSAALL 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17861816 191 ASAGA--AEVVSISFPKYFgSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLV 246
Cdd:cd00138  63 EALLRagVNVRSYVTPPHF-FERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
PLDc_2 pfam13091
PLD-like domain;
114-264 1.26e-12

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 65.01  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   114 LELLESATTSLDIASFYWtlkaedtpgvsdNSTRPGEDVFARLLANGnggsrsprIKIRI--AQSEPSSGTPNL-NTKLL 190
Cdd:pfam13091   2 IDLINSAKKSIDIATYYF------------VPDREIIDALIAAAKRG--------VDVRIilDSNKDDAGGPKKaSLKEL 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17861816   191 ASAGAAEVVSISFPKYFGSgvLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQNcPELTHDVAKIFGEYW 264
Cdd:pfam13091  62 RSLLRAGVEIREYQSFLRS--MHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEFDRLW 132
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 323-493 7.59e-11

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


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 63.81  E-value: 7.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 323 AILNTINTAITYVNIAvmdYYpliIYEKNHHYWPFIDdALRKAAvERGVAVKLLISWWkHSNPSEDRYLRSLQDLasked 402
Cdd:COG1502  29 ALLEAIEAARRSIDLE---YY---IFDDDEVGRRLAD-ALIAAA-RRGVKVRVLLDGI-GSRALNRDFLRRLRAA----- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 403 kiDIQIRRFiVPTDSSQEKIpfGRVNHNKYMVTD-RVAYIGTSNWSGDYFTDTAGIG-----LVLsetfetettntLRS- 475
Cdd:COG1502  95 --GVEVRLF-NPVRLLFRRL--NGRNHRKIVVIDgRVAFVGGANITDEYLGRDPGFGpwrdtHVR-----------IEGp 158

                       170       180
                ....*....|....*....|.
gi 17861816 476 ---DLRNVFERDWNSKYATPL 493
Cdd:COG1502 159 avaDLQAVFAEDWNFATGEAL 179
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 110-280 5.11e-10

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: 61.11  E-value: 5.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 110 YEAWLELLESATTSLDIASFYWTLkaedtpgvsdnsTRPGEDVFARLLANGnggsrsPRIKIrIAQSEPSSGTPNLNT-- 187
Cdd:COG1502 205 ERALLAAIASARRRIYIETPYFVP------------DRSLLRALIAAARRG------VDVRI-LLPAKSDHPLVHWASrs 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 188 --KLLASAGaaevVSIsfpKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQNcPELTHDVAKIFGEYWy 265
Cdd:COG1502 266 yyEELLEAG----VRI---YEYEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYD-PEFAAQLRARFEEDL- 336

                       170
                ....*....|....*
gi 17861816 266 lgnSESSRIPDWDWR 280
Cdd:COG1502 337 ---AHSREVTLEEWR 348
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 346-448 1.17e-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: 55.99  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 346 IIYEKNHHYWPFIDDALRKAAvERGVAVKLLISWWKHSNPSedrylrSLQDLASKEDKIDIQIRRFIVPTDSSqekipfg 425
Cdd:cd00138  17 ATPNFSFNSADRLLKALLAAA-ERGVDVRLIIDKPPNAAGS------LSAALLEALLRAGVNVRSYVTPPHFF------- 82

                        90       100
                ....*....|....*....|....
gi 17861816 426 RVNHNKYMVTD-RVAYIGTSNWSG 448
Cdd:cd00138  83 ERLHAKVVVIDgEVAYVGSANLST 106
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 210-235 3.23e-09

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: 52.01  E-value: 3.23e-09
                           10        20
                   ....*....|....*....|....*.
gi 17861816    210 GVLHTKLWVVDNKHFYLGSANMDWRA 235
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_2 pfam13091
PLD-like domain;
324-485 5.87e-09

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 54.22  E-value: 5.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   324 ILNTINTAITYVNIAVMDYYPLiiyeknhhywPFIDDALRKAAvERGVAVKLLISWWKHSNP-SEDRYLRSLQDLAsked 402
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPD----------REIIDALIAAA-KRGVDVRIILDSNKDDAGgPKKASLKELRSLL---- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816   403 KIDIQIRRFIvptdssqekiPFGRVNHNKYMVTD-RVAYIGTSNWSGDYFTDTAGIGLVLSetfetetTNTLRSDLRNVF 481
Cdd:pfam13091  66 RAGVEIREYQ----------SFLRSMHAKFYIIDgKTVIVGSANLTRRALRLNLENNVVIK-------DPELAQELEKEF 128


                  ....
gi 17861816   482 ERDW 485
Cdd:pfam13091 129 DRLW 132
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 210-235 2.10e-07

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: 47.03  E-value: 2.10e-07
                          10        20
                  ....*....|....*....|....*.
gi 17861816   210 GVLHTKLWVVDNKHFYLGSANMDWRA 235
Cdd:pfam00614   3 GRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 360-485 4.03e-07

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: 49.20  E-value: 4.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 360 DALRKAAvERGVAVKLLISwwkhSNPSEDRYLRSLQDLAskeDKIDIQIRRFIVPtdssQEKIpfgrvnHNKYMVTD-RV 438
Cdd:cd09128  41 DALVDAA-KRGVDVRVLLP----SAWSAEDERQARLRAL---EGAGVPVRLLKDK----FLKI------HAKGIVVDgKT 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17861816 439 AYIGTSNWSGDYFTDTAGIGLVLsetfeteTTNTLRSDLRNVFERDW 485
Cdd:cd09128 103 ALVGSENWSANSLDRNREVGLIF-------DDPEVAAYLQAVFESDW 142
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 205-290 3.04e-06

Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and similar proteins; Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli cardiolipin (CL) synthase. The prototype of this subfamily is an uncharacterized protein ymdC specified by the o493 (ymdC) gene. Although the functional characterization of ymdC and similar proteins remains unknown, members of this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, ymdC and its similar proteins contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characteriszes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197212 [Multi-domain]  Cd Length: 218  Bit Score: 47.98  E-value: 3.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 205 KYFGSGV--LHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQNcPELTHDVAKIFGE------YWYLGNSESSRIPD 276
Cdd:cd09113 108 GLFGSSRasLHAKSFVIDDRLVFVGSFNLDPRSAYLNTEMGLVIDS-PELAAQLRAAMEEdlapsaYWVLLLDDGGLVWE 186

                        90
                ....*....|....
gi 17861816 277 WDWRYATSYNLKHP 290
Cdd:cd09113 187 TEEDGKEKEYDSEP 200
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 324-462 3.84e-06

Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; Putative catalytic domain, repeat 1, 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: 197225 [Multi-domain]  Cd Length: 141  Bit Score: 46.49  E-value: 3.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 324 ILNTINTAITYVNIAVmdyypliiYEKNHhywPFIDDALRkAAVERGVAVKLLISwwkhSNPSedrylrslqdlaSKEDK 403
Cdd:cd09127  13 VVDAIASAKRSILLKM--------YEFTD---PALEKALA-AAAKRGVRVRVLLE----GGPV------------GGISR 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17861816 404 IDIQIRRFI---VPTDSSQEKIPFgRVNHNKYMVTDR-VAYIGTSNWSGDYFTDTAGIGLVLS 462
Cdd:cd09127  65 AEKLLDYLNeagVEVRWTNGTARY-RYTHAKYIVVDDeRALVLTENFKPSGFTGTRGFGVVTD 126
DISARM_DrmC_I NF038319
DISARM system phospholipase D-like protein DrmC; DrmC, a phospholipase D (PLD) ...
 114-257 4.93e-06

DISARM system phospholipase D-like protein DrmC; DrmC, a phospholipase D (PLD) domain-containing protein, is a component of DISARM (Defence Island System Associated with Restriction Modification). This HMM represents most but not all DrmC of class I DISARM systems, which contain a DNA adenine N6 methyltransferase. DrmC appears to be an auxiliary rather than core component of DISARM, required for resistance to some phage but not others.


Pssm-ID: 468473 [Multi-domain]  Cd Length: 234  Bit Score: 47.57  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  114 LELLESATTSLDIASFywtlkaedtpgvsdnSTRPGEDVFARLL-ANGNGgsrsprIKIRIA--QSEPSSGTPNLNTKLL 190
Cdd:NF038319  99 LELIRAARQSLLLVTF---------------AAYKVSPLVEALAaAAARG------VAVRVLleTSEGAGGALSGDEPAR 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816  191 ASAGAAEV---VSISFPKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQNcPELTHDVA 257
Cdd:NF038319 158 AFAGVPGArvwHWPVDPRALRGGSLHAKVAVADRRVLLVTSANLTESALERNIEAGVLIRG-GALPERLA 226
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 114-264 5.91e-06

Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar proteins; Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), and similar proteins. Nuc is an endonuclease from Salmonella typhimurium and the smallest known member of the PLD superfamily. It cleaves both single- and double-stranded DNA. PLD6 selectively hydrolyzes the terminal phosphodiester bond of phosphatidylcholine (PC), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLD6 also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which is essential for catalysis. PLDs utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. This subfamily also includes some uncharacterized hypothetical proteins, which have two HKD motifs in a single polypeptide chain.


Pssm-ID: 197215 [Multi-domain]  Cd Length: 138  Bit Score: 45.75  E-value: 5.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 114 LELLESATTSLDIASFYWTLKaedtpgvsdnstrpgeDVFARLlanGNGGSRSPRIKIrIAQSEPSSGTPNLNTKLLASA 193
Cdd:cd09116  15 VALIANAKSSIDVAMYALTDP----------------EIAEAL---KRAAKRGVRVRI-ILDKDSLADNLSITLLALLSN 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17861816 194 GAAEVVsisfpKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQNcpeltHDVAKIFGEYW 264
Cdd:cd09116  75 LGIPVR-----TDSGSKLMHHKFIIIDGKIVITGSANWTKSGFHRNDENLLIIDD-----PKLAASFEEEF 135
PLDc_unchar4 cd09132
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 114-246 2.16e-05

Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic domain of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. Members of this subfamily contain one copy of HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily.


Pssm-ID: 197230 [Multi-domain]  Cd Length: 122  Bit Score: 43.80  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 114 LELLESATTSLDIASFYWTLKAEDTPGVSDNSTRpgeDVFARLLANGnggsrsprikiriaqSEPSSGTPNLNTKLLASA 193
Cdd:cd09132   5 LELIEGAERSLLIVGYSAYKVSELLQALAAALER---GVQVRVVVES---------------SEKAGSVLSLDEDELMWP 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17861816 194 GAAEV---VSISFPKYFGSGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLV 246
Cdd:cd09132  67 KLAGAtlyVWPEKKRPGKRASLHAKVIVADRRRLLVTSANLTGAGMERNIEAGVLV 122
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 424-450 5.76e-05

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: 40.07  E-value: 5.76e-05
                           10        20
                   ....*....|....*....|....*...
gi 17861816    424 FGRVNHNKYMVTD-RVAYIGTSNWSGDY 450
Cdd:smart00155   1 YDGVLHTKLMIVDdEIAYIGSANLDGRS 28
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
 323-486 7.02e-05

Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic domain, repeat 1, of bacterial cardiolipin (CL) synthase and a few homologs found in eukaryotes and archaea. Bacterial CL synthases catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. The monomer of bacterial CL synthase consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. Bacterial CL synthases can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily. Like other PLD enzymes, bacterial CL synthases 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: 197209 [Multi-domain]  Cd Length: 154  Bit Score: 43.23  E-value: 7.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 323 AILNTINTAITYVNiavMDYYpliIYEKNHHYWPFIDdALRKAAvERGVAVKLLISWWkHSNPSEDRYLRSLQDLAsked 402
Cdd:cd09110   9 ALLEAIRAARHSIH---LEYY---IFRDDEIGRRFRD-ALIEKA-RRGVEVRLLYDGF-GSLGLSRRFLRELREAG---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 403 kidIQIRRFIvPTDSSQEKIPFGRVNHNKYMVTD-RVAYIGTSNWSGDYFTDTAGIG------------LVlsetfetet 469
Cdd:cd09110  76 ---VEVRAFN-PLSFPLFLLRLNYRNHRKILVIDgKIAFVGGFNIGDEYLGKDPGFGpwrdthvriegpAV--------- 142

                       170
                ....*....|....*..
gi 17861816 470 tntlrSDLRNVFERDWN 486
Cdd:cd09110 143 -----ADLQAAFLEDWY 154
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 111-264 1.16e-04

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 42.26  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 111 EAWLELLESATTSLDIASfywtlkaedtPGVSDNstrpgEDVFARLLANGNGGsrsprIKIRIAQSEPSSGTPNLNTKLL 190
Cdd:cd09128  13 EALLALIDSAEESLLIQN----------EEMGDD-----APILDALVDAAKRG-----VDVRVLLPSAWSAEDERQARLR 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17861816 191 ASAGAAEVVSISFPKYfgsGVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQNcPELTHDVAKIFGEYW 264
Cdd:cd09128  73 ALEGAGVPVRLLKDKF---LKIHAKGIVVDGKTALVGSENWSANSLDRNREVGLIFDD-PEVAAYLQAVFESDW 142
PLDc_Nuc_like_unchar1_1 cd09172
Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, ...
 316-447 2.16e-04

Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, an endonuclease from Salmonella typhimurium; Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins, which show high sequence homology to the endonuclease from Salmonella typhimurium and vertebrate phospholipase D6. Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which characterizes the PLD superfamily and is essential for catalysis. Nuc and PLD6 utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. However, proteins in this subfamily have two HKD motifs in a single polypeptide chain.


Pssm-ID: 197269 [Multi-domain]  Cd Length: 144  Bit Score: 41.57  E-value: 2.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 316 GRTDDLNAILNTINTAITYVNIAvmdyypliIYEKNHhywPFIDDALrKAAVERGVAVKLLIswwkHSNPSEDRYLRSLQ 395
Cdd:cd09172   6 ELREALLAFLDEARSAGSSIRLA--------IYELDD---PEIIDAL-KAAKDRGVRVRIIL----DDSSVTGDPTEESA 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17861816 396 DLASKEDKIDIQIRRFivptdssqekipFGRVNHNKYMVTDR-----VAYIGTSNWS 447
Cdd:cd09172  70 AATLSKGPGALVKRRH------------SSGLMHNKFLVVDRkdgpnRVLTGSTNFT 114
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 211-260 1.08e-03

Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; Catalytic domain, repeat 2, of Escherichia coli cardiolipin (CL) synthase ybhO and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli CL synthase. The prototype of this subfamily is Escherichia coli CL synthase ybhO specified by the f413 (ybhO) gene. ybhO is a membrane-bound protein that catalyzes the formation of cardiolipin (CL) by transferring phosphatidyl group between two phosphatidylglycerol molecules. It can also catalyze phosphatidyl group transfer to water to form phosphatidate. In contrast to the Escherichia coli CL synthase encoded by the cls gene (EcCLS), ybhO does not hydrolyze CL. Moreover, ybhO lacks an N-terminal segment encoded by Escherichia coli cls, which makes ybhO easy to denature. The monomer of ybhO consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. ybhO can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily.


Pssm-ID: 197256 [Multi-domain]  Cd Length: 170  Bit Score: 39.83  E-value: 1.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17861816 211 VLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQnCPELTHDVAKIF 260
Cdd:cd09159  92 MLHAKTAVIDGDWATVGSSNLDPRSLRLNLEANLVVE-DPAFAAQLEELF 140
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
 213-247 1.53e-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: 39.21  E-value: 1.53e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 17861816 213 HTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQ 247
Cdd:cd09105 111 HSKVVIVDDEWATVGSANLNRRSMTWDTELNLAVV 145
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 212-260 1.64e-03

Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic domain of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. Members of this subfamily contain one copy of HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily.


Pssm-ID: 197229 [Multi-domain]  Cd Length: 143  Bit Score: 38.86  E-value: 1.64e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17861816 212 LHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVqNCPELTHDVAKIF 260
Cdd:cd09131  93 THTKLVVIDGRTVYVGSHNWTYSALDYNHEASVLI-ESPEVADFAINYF 140
PLDc_CLS_unchar2_1 cd09157
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 360-456 3.06e-03

Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin synthase; Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197254 [Multi-domain]  Cd Length: 155  Bit Score: 38.32  E-value: 3.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 360 DALrKAAVERGVAVKLLI----SWWkhSNPSEDRYLRslqdlaskedKIDIQIRRFIVPtdSSQEKIPFGRV-NHNKYMV 434
Cdd:cd09157  39 DAL-AEAVARGVDVRVLIdgvgARY--SRPSIRRRLR----------RAGVPVARFLPP--RLPPRLPFINLrNHRKILV 103

                        90       100
                ....*....|....*....|...
gi 17861816 435 TD-RVAYIGTSNWSGDYFTDTAG 456
Cdd:cd09157 104 VDgRTGFTGGMNIRDGHLVADDP 126
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 360-451 4.89e-03

Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and similar proteins; Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli cardiolipin (CL) synthase. The prototype of this subfamily is an uncharacterized protein ymdC specified by the o493 (ymdC) gene. Although the functional characterization of ymdC and similar proteins remains unknown, members of this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, ymdC and its similar proteins contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characteriszes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197210 [Multi-domain]  Cd Length: 162  Bit Score: 37.90  E-value: 4.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17861816 360 DALRKAAvERGVAVKLLISWWKHSnpSEDRYlrsLQDLASKEdkiDIQIRRFiVPTDSSQEKIP-----FGRVN---HNK 431
Cdd:cd09111  40 GELLEAA-DRGVRVRLLLDDLGTS--GRDRL---LAALDAHP---NIEVRLF-NPFRNRGGRLLefltdFSRLNrrmHNK 109

                        90       100
                ....*....|....*....|.
gi 17861816 432 YMVTD-RVAYIGTSNWSGDYF 451
Cdd:cd09111 110 LFIVDgAVAIVGGRNIGDEYF 130
PLDc_SMU_988_like_2 cd09160
Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 ...
 210-250 6.76e-03

Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins; Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins. Although SMU_988 and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197257 [Multi-domain]  Cd Length: 176  Bit Score: 37.48  E-value: 6.76e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17861816 210 GVLHTKLWVVDNKHFYLGSANMDWRALTQVKEMGVLVQNCP 250
Cdd:cd09160  91 GFIHAKTFVSDDKAAVVGTINLDYRSLYLHFECGVYMYDTP 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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