NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|392919428|ref|NP_001256080|]
View 

putative phospholipase D F09G2.8 [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PHA02820 super family cl33698
phospholipase-D-like protein; Provisional
 121-516 1.00e-94

phospholipase-D-like protein; Provisional


The actual alignment was detected with superfamily member PHA02820:

Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 294.21  E-value: 1.00e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 121 CSVDCKTFLVESIPIGLPF-KTNNHTAEAWINIIDNSKQYLDISVMYWNLntSDYKSSVYGRRVYEAIIRAGKRGVKIRI 199
Cdd:PHA02820   2 NPDNTIAVITETIPIGMQFdKVYLSTFNFWREILSNTTKTLDISSFYWSL--SDEVGTNFGTMILNEIIQLPKRGVRVRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 200 AQDGASNLSDNKEsayLVQEGLAEVREINVTRLIGsGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQECPCVA 279
Cdd:PHA02820  80 AVNKSNKPLKDVE---LLQMAGVEVRYIDITNILG-GVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 280 SDLYKIFAAYWKLGENDsvIPEKWPISYRTPFNFSSMAKLTMDGEPAEYFISSSPGPFNPKGREHDLAAIQKIMKDARKS 359
Cdd:PHA02820 156 ADLTQIFEVYWYLGVNN--LPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 360 VCISVMDYIPSTLYMKKSNRFWPEIDDSIRDAAY-RGVNVRMLISHWDHSRKEMIPFLKSLQTItdglprynRTEHGQVQ 438
Cdd:PHA02820 234 VYVSVMNFIPIIYSKAGKILFWPYIEDELRRAAIdRKVSVKLLISCWQRSSFIMRNFLRSIAML--------KSKNINIE 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 439 VRIFTVPPNgKEKIPFTRVNHAKYMVTEDIAYIGTSNWSGDYFISTAGVAMVV---RQPSATKRLQNVFDRDWNSEYSKD 515
Cdd:PHA02820 306 VKLFIVPDA-DPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINItpdDGLGLRQQLEDIFIRDWNSKYSYE 384


                 .
gi 392919428 516 L 516
Cdd:PHA02820 385 L 385
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 121-516 1.00e-94

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 294.21  E-value: 1.00e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 121 CSVDCKTFLVESIPIGLPF-KTNNHTAEAWINIIDNSKQYLDISVMYWNLntSDYKSSVYGRRVYEAIIRAGKRGVKIRI 199
Cdd:PHA02820   2 NPDNTIAVITETIPIGMQFdKVYLSTFNFWREILSNTTKTLDISSFYWSL--SDEVGTNFGTMILNEIIQLPKRGVRVRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 200 AQDGASNLSDNKEsayLVQEGLAEVREINVTRLIGsGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQECPCVA 279
Cdd:PHA02820  80 AVNKSNKPLKDVE---LLQMAGVEVRYIDITNILG-GVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 280 SDLYKIFAAYWKLGENDsvIPEKWPISYRTPFNFSSMAKLTMDGEPAEYFISSSPGPFNPKGREHDLAAIQKIMKDARKS 359
Cdd:PHA02820 156 ADLTQIFEVYWYLGVNN--LPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 360 VCISVMDYIPSTLYMKKSNRFWPEIDDSIRDAAY-RGVNVRMLISHWDHSRKEMIPFLKSLQTItdglprynRTEHGQVQ 438
Cdd:PHA02820 234 VYVSVMNFIPIIYSKAGKILFWPYIEDELRRAAIdRKVSVKLLISCWQRSSFIMRNFLRSIAML--------KSKNINIE 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 439 VRIFTVPPNgKEKIPFTRVNHAKYMVTEDIAYIGTSNWSGDYFISTAGVAMVV---RQPSATKRLQNVFDRDWNSEYSKD 515
Cdd:PHA02820 306 VKLFIVPDA-DPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINItpdDGLGLRQQLEDIFIRDWNSKYSYE 384


                 .
gi 392919428 516 L 516
Cdd:PHA02820 385 L 385
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 329-509 1.05e-89

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: 272.20  E-value: 1.05e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 329 FISSSPGPFNPKGREHDLAAIQKIMKDARKSVCISVMDYIPSTLYMKKsNRFWPEIDDSIRDAAY-RGVNVRMLISHWDH 407
Cdd:cd09107    1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADP-RKYWPVIDNALRRAAVdRGVKVRLLVSNWKH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 408 SRKEMIPFLKSLQTITDGlprynrTEHGQVQVRIFTVPPNGKEKIPFTRVNHAKYMVTEDIAYIGTSNWSGDYFISTAGV 487
Cdd:cd09107   80 TDPSMDAFLKSLQLLKSG------VGNGDIEVKIFTVPGDQSTKIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGV 153

                        170       180
                 ....*....|....*....|..
gi 392919428 488 AMVVRQPSATKRLQNVFDRDWN 509
Cdd:cd09107  154 SLVINDPAIVQQLKDVFERDWN 175
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 147-509 1.22e-26

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: 111.19  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 147 EAWINIIDNSKQYLDISVMYWNLNTSdykssvyGRRVYEAIIRAGKRGVKIRIAQDGASNLSDNKESAYLVQEGLAEVRE 226
Cdd:COG1502   28 AALLEAIEAARRSIDLEYYIFDDDEV-------GRRLADALIAAARRGVKVRVLLDGIGSRALNRDFLRRLRAAGVEVRL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 227 ---INVTRLIGSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVG------VVFqECPCVAsDLYKIFAAYWKLGENDS 297
Cdd:COG1502  101 fnpVRLLFRRLNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpwrdthVRI-EGPAVA-DLQAVFAEDWNFATGEA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 298 vipEKWPIsyrtpfnfssmaklTMDGEPAEyFISSSPGPFNPKGREHDLAAIQKimkdARKSVCISVMDYIPStlymkks 377
Cdd:COG1502  179 ---LPFPE--------------PAGDVRVQ-VVPSGPDSPRETIERALLAAIAS----ARRRIYIETPYFVPD------- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 378 nrfwPEIDDSIRDAAYRGVNVRMLISHW-DHS--RKEMIPFLKSLQtitdglprynrtEHGqvqVRIFTVPPngkekipf 454
Cdd:COG1502  230 ----RSLLRALIAAARRGVDVRILLPAKsDHPlvHWASRSYYEELL------------EAG---VRIYEYEP-------- 282

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392919428 455 tRVNHAKYMVT-EDIAYIGTSNWSGDYFISTAGVAMVVRQPSATKRLQNVFDRDWN 509
Cdd:COG1502  283 -GFLHAKVMVVdDEWALVGSANLDPRSLRLNFEVNLVIYDPEFAAQLRARFEEDLA 337
PLDc_3 pfam13918
PLD-like domain;
261-445 1.59e-23

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 97.39  E-value: 1.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428  261 SLSEVKEVGVVFQECPCVASDLYKIFAAYWKLGENDSViPEKWPISYRTPFNFSSMAKLTMDGEPAEYFISSSPGPFNPK 340
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKV-PFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428  341 GREHDLAAIQKIMKDARKSVCISVMDYIPSTLYMKKSNrFWPEIDDSIRDAAY-RGVNVRMLISHWDHSRKEMIPFLKSL 419
Cdd:pfam13918  80 NRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGARE-YWPDIDDAILEAAIlRGVKVRLIISEWKEADPLSFNAARSL 158

                         170       180
                  ....*....|....*....|....*...
gi 392919428  420 QTITdglprynrTEHGQV--QVRIFTVP 445
Cdd:pfam13918 159 DAFC--------TEIANCdlKVKFFDLE 178
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 456-480 2.64e-04

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 38.14  E-value: 2.64e-04
                           10        20
                   ....*....|....*....|....*.
gi 392919428   456 RVNHAKYMVTED-IAYIGTSNWSGDY 480
Cdd:smart00155   3 GVLHTKLMIVDDeIAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 121-516 1.00e-94

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 294.21  E-value: 1.00e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 121 CSVDCKTFLVESIPIGLPF-KTNNHTAEAWINIIDNSKQYLDISVMYWNLntSDYKSSVYGRRVYEAIIRAGKRGVKIRI 199
Cdd:PHA02820   2 NPDNTIAVITETIPIGMQFdKVYLSTFNFWREILSNTTKTLDISSFYWSL--SDEVGTNFGTMILNEIIQLPKRGVRVRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 200 AQDGASNLSDNKEsayLVQEGLAEVREINVTRLIGsGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQECPCVA 279
Cdd:PHA02820  80 AVNKSNKPLKDVE---LLQMAGVEVRYIDITNILG-GVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 280 SDLYKIFAAYWKLGENDsvIPEKWPISYRTPFNFSSMAKLTMDGEPAEYFISSSPGPFNPKGREHDLAAIQKIMKDARKS 359
Cdd:PHA02820 156 ADLTQIFEVYWYLGVNN--LPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNASKF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 360 VCISVMDYIPSTLYMKKSNRFWPEIDDSIRDAAY-RGVNVRMLISHWDHSRKEMIPFLKSLQTItdglprynRTEHGQVQ 438
Cdd:PHA02820 234 VYVSVMNFIPIIYSKAGKILFWPYIEDELRRAAIdRKVSVKLLISCWQRSSFIMRNFLRSIAML--------KSKNINIE 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 439 VRIFTVPPNgKEKIPFTRVNHAKYMVTEDIAYIGTSNWSGDYFISTAGVAMVV---RQPSATKRLQNVFDRDWNSEYSKD 515
Cdd:PHA02820 306 VKLFIVPDA-DPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINItpdDGLGLRQQLEDIFIRDWNSKYSYE 384


                 .
gi 392919428 516 L 516
Cdd:PHA02820 385 L 385
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 329-509 1.05e-89

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: 272.20  E-value: 1.05e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 329 FISSSPGPFNPKGREHDLAAIQKIMKDARKSVCISVMDYIPSTLYMKKsNRFWPEIDDSIRDAAY-RGVNVRMLISHWDH 407
Cdd:cd09107    1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADP-RKYWPVIDNALRRAAVdRGVKVRLLVSNWKH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 408 SRKEMIPFLKSLQTITDGlprynrTEHGQVQVRIFTVPPNGKEKIPFTRVNHAKYMVTEDIAYIGTSNWSGDYFISTAGV 487
Cdd:cd09107   80 TDPSMDAFLKSLQLLKSG------VGNGDIEVKIFTVPGDQSTKIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGV 153

                        170       180
                 ....*....|....*....|..
gi 392919428 488 AMVVRQPSATKRLQNVFDRDWN 509
Cdd:cd09107  154 SLVINDPAIVQQLKDVFERDWN 175
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 329-513 7.32e-72

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: 226.77  E-value: 7.32e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 329 FISSSPGPFNPKGREHDLAAIQKIMKDARKSVCISVMDYIPsTLYMKKSNRFWPEIDDSIRDAAY-RGVNVRMLISHWDH 407
Cdd:cd09147    1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLP-TLEFSHPHRYWPAIDDGLRRATYeRGVKVRLLISCWGH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 408 SRKEMIPFLKSLQTITDGlprynrTEHGQVQVRIFTVPPN-GKEKIPFTRVNHAKYMVTEDIAYIGTSNWSGDYFISTAG 486
Cdd:cd09147   80 SEPSMFAFLRSLAALRDN------TTHSDIQVKIFVVPADeAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAG 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 392919428 487 VAMVVRQPSAT------KRLQNVFDRDWNSEYS 513
Cdd:cd09147  154 SALVVNQTGRSasgtlqSQLQAVFERDWDSPYS 186
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 129-275 6.64e-64

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: 204.79  E-value: 6.64e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 129 LVESIPIGLPFKT---NNHTAEAWINIIDNSKQYLDISVMYWNLNTSDYK---SSVYGRRVYEAIIRAGKRGVKIRIAQD 202
Cdd:cd09106    1 LVESIPEGLTFLSsssHLSTFEAWMELISSAKKSIDIASFYWNLRGTDTNpdsSAQEGEDIFNALLEAAKRGVKIRILQD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392919428 203 GASNLSDNKESAYLVQEGLAEVREINVTRLIGSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQEC 275
Cdd:cd09106   81 KPSKDKPDEDDLELAALGGAEVRSLDFTKLIGGGVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 329-513 1.69e-62

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: 202.38  E-value: 1.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 329 FISSSPGPFNPKGREHDLAAIQKIMKDARKSVCISVMDYIPsTLYMKKSNRFWPEIDDSIRDAAY-RGVNVRMLISHWDH 407
Cdd:cd09148    1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFP-TCRFCHPKRYWSVLDNALRAAAFdRRVLIRLLISCGRH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 408 SRKEMIPFLKSLQTITdglpryNRTEHGQVQVRIFTVPPNGKEKIPFTRVNHAKYMVTEDIAYIGTSNWSGDYFISTAGV 487
Cdd:cd09148   80 SDPDMFPFLRSLNALS------NPPLSISVHVKLFIVPVGNQTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGV 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 392919428 488 AMVVRQPSATKR--------LQNVFDRDWNSEYS 513
Cdd:cd09148  154 GLVILQSPGANEemlpvqeqLRSLFERDWSSPYA 187
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 123-516 1.36e-43

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 158.29  E-value: 1.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 123 VDCKtfLVESIPIGLPFKTNN-HTAEAWINIIDNSKQYLDISVMYWNLNTSDYkssvyGRRVYEAIIRAGKRGVKIRIAQ 201
Cdd:PHA03003  11 AGCR--IVETLPKSLGIATQHmSTYECFDEIISQAKKYIYIASFCCNLRSTPE-----GRLILDKLKEAAESGVKVTILV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 202 DGASNLSDNKEsaylVQEGLAEVREINVTRLIGSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGvVFQECPCVASD 281
Cdd:PHA03003  84 DEQSGDKDEEE----LQSSNINYIKVDIGKLNNVGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLG-VYSTYPPLATD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 282 LYKIFAAYWKLGENDSVipekwpisyrtpFNFSSMAKLT-------MDGEPAEYFISSSPGPFNPKGREHDLAAIQKIMK 354
Cdd:PHA03003 159 LRRRFDTFKAFNKNKSV------------FNRLCCACCLpvstkyhINNPIGGVFFSDSPEHLLGYSRTLDADVVLHKIK 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 355 DARKSVCISVMDYIPsTLYMKKSNRFWPEIDDS-IRDAAYRGVNVRMLISHWDHSRKEMIPFLKSLQTITDGlprynrte 433
Cdd:PHA03003 227 SAKKSIDLELLSLVP-VIREDDKTTYWPDIYNAlIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCVG-------- 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 434 hGQVQVRIFTVPpngkekipftrvNHAKYMVTED-IAYIGTSNWSGDYFISTAGVAMVVRQPSATKRLQNVFDRDWNSEY 512
Cdd:PHA03003 298 -NDLSVKVFRIP------------NNTKLLIVDDeFAHITSANFDGTHYLHHAFVSFNTIDKELVKELSAIFERDWTSSY 364


                 ....
gi 392919428 513 SKDL 516
Cdd:PHA03003 365 SKPL 368
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 129-293 8.80e-42

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: 147.40  E-value: 8.80e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 129 LVESIPIGLPFKT----NNHTAEAWINIIDNSKQYLDISVMYWNLNTSDYK----SSVYGRRVYEAIIRAGKRGVKIRIA 200
Cdd:cd09144    2 LVESIPEGLVFNSsstiNPSIYQAWLNLISAAQSSLDIASFYWTLTNSDTHtqepSANQGEQILKKLGQLSQSGVYVRIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 201 QDGASNLSDNKESAYLVQEGlAEVREINVTRLIgSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQECPCVAS 280
Cdd:cd09144   82 VDKPADPKPMEDINALSSYG-ADVRMVDMRKLT-TGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVYNCSCLAE 159

                        170
                 ....*....|...
gi 392919428 281 DLYKIFAAYWKLG 293
Cdd:cd09144  160 DLGKIFEAYWYLG 172
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 329-516 7.01e-38

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: 137.29  E-value: 7.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 329 FISSSPGPFNPKGREHDLAAIQKIMKDARKSVCISVMDYIP--STLYMKksnRFWPEIDDSIRDAA-YRGVNVRMLISHW 405
Cdd:cd09149    1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPllSRSYAR---RYWSRIDSKIREALvLRSVRVRLLISFW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 406 DHSRKEMIPFLKSLQTITDGLPrynrteHGQVQVRIFTVPPNGKEKIPftRVNHAKYMVTEDIAYIGTSNWSGDYFISTA 485
Cdd:cd09149   78 RKTDPLTFNFVSSLKSLCTEQA------NCSLEVKFFDLEEESDCTSP--RLNRNKYMVTDGAAYIGNFDWVGNDFTQNA 149

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392919428 486 GVAMVVRQPSAT--------KRLQNVFDRDWNSEYSKDL 516
Cdd:cd09149  150 GVGLVINQADGVeennatiiEQLRAAFERDWYSNYAKSL 188
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 129-292 2.08e-35

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: 130.03  E-value: 2.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 129 LVESIPIGLPFKTNNHTA----EAWINIIDNSKQYLDISVMYWNLNTSDY----KSSVYGRRVYEAIIRAGKRGVKIRIA 200
Cdd:cd09145    1 LVESIPEDLTYEGNSTFAlplqKAWTKLLDMAQEQVHVASYYWSLTGEDIgvndSSSLPGEDILKELAELLSRNVSVRAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 201 QDGASNLSDNKESAYLVQEGlAEVREINVTRLIGsGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQECPCVAS 280
Cdd:cd09145   81 ASIPTLAANSTDLKILRQKG-AHVRKVNFGRLTG-GVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAK 158

                        170
                 ....*....|..
gi 392919428 281 DLYKIFAAYWKL 292
Cdd:cd09145  159 DLHKTFQTYWVL 170
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 129-292 8.93e-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: 114.57  E-value: 8.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 129 LVESIPIGLPFKTNNHT----AEAWINIIDNSKQYLDISVMYWNLNTSDyKSSVYGRRVYEAIIRAGKRGVKIRIAqdga 204
Cdd:cd09146    2 LVENIPDGINFSEHAPPhlplSQGWMNLLDMAVKSVEIVSPLWDLNASH-PSACQGQRLFERLLGLASRGVELKIV---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 205 SNLSDNKESAYLVQEGLAEVREINVTRLiGSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQECPCVASDLYK 284
Cdd:cd09146   77 SGITDSTEVLVLLKKKGAEVHYVNMTAL-TKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLHR 155


                 ....*...
gi 392919428 285 IFAAYWKL 292
Cdd:cd09146  156 VFALYWSL 163
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 147-509 1.22e-26

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: 111.19  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 147 EAWINIIDNSKQYLDISVMYWNLNTSdykssvyGRRVYEAIIRAGKRGVKIRIAQDGASNLSDNKESAYLVQEGLAEVRE 226
Cdd:COG1502   28 AALLEAIEAARRSIDLEYYIFDDDEV-------GRRLADALIAAARRGVKVRVLLDGIGSRALNRDFLRRLRAAGVEVRL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 227 ---INVTRLIGSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVG------VVFqECPCVAsDLYKIFAAYWKLGENDS 297
Cdd:COG1502  101 fnpVRLLFRRLNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpwrdthVRI-EGPAVA-DLQAVFAEDWNFATGEA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 298 vipEKWPIsyrtpfnfssmaklTMDGEPAEyFISSSPGPFNPKGREHDLAAIQKimkdARKSVCISVMDYIPStlymkks 377
Cdd:COG1502  179 ---LPFPE--------------PAGDVRVQ-VVPSGPDSPRETIERALLAAIAS----ARRRIYIETPYFVPD------- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 378 nrfwPEIDDSIRDAAYRGVNVRMLISHW-DHS--RKEMIPFLKSLQtitdglprynrtEHGqvqVRIFTVPPngkekipf 454
Cdd:COG1502  230 ----RSLLRALIAAARRGVDVRILLPAKsDHPlvHWASRSYYEELL------------EAG---VRIYEYEP-------- 282

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392919428 455 tRVNHAKYMVT-EDIAYIGTSNWSGDYFISTAGVAMVVRQPSATKRLQNVFDRDWN 509
Cdd:COG1502  283 -GFLHAKVMVVdDEWALVGSANLDPRSLRLNFEVNLVIYDPEFAAQLRARFEEDLA 337
PLDc_3 pfam13918
PLD-like domain;
261-445 1.59e-23

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 97.39  E-value: 1.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428  261 SLSEVKEVGVVFQECPCVASDLYKIFAAYWKLGENDSViPEKWPISYRTPFNFSSMAKLTMDGEPAEYFISSSPGPFNPK 340
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKV-PFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428  341 GREHDLAAIQKIMKDARKSVCISVMDYIPSTLYMKKSNrFWPEIDDSIRDAAY-RGVNVRMLISHWDHSRKEMIPFLKSL 419
Cdd:pfam13918  80 NRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGARE-YWPDIDDAILEAAIlRGVKVRLIISEWKEADPLSFNAARSL 158

                         170       180
                  ....*....|....*....|....*...
gi 392919428  420 QTITdglprynrTEHGQV--QVRIFTVP 445
Cdd:pfam13918 159 DAFC--------TEIANCdlKVKFFDLE 178
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 147-272 1.56e-15

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: 72.93  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 147 EAWINIIDNSKQYLDISVMYWNLNTSDykssvygrRVYEAIIRAGKRGVKIRIAQDGASNLSDNKESAYLVQ--EGLAEV 224
Cdd:cd00138    1 EALLELLKNAKESIFIATPNFSFNSAD--------RLLKALLAAAERGVDVRLIIDKPPNAAGSLSAALLEAllRAGVNV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 392919428 225 REINvTRLIGSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVF 272
Cdd:cd00138   73 RSYV-TPPHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 138-304 4.21e-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: 76.90  E-value: 4.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 138 PFKTNNHTAEAWINIIDNSKQYLDISVMYWnlntsdykssVYGRRVYEAIIRAGKRGVKIRIaqdgasnLSDNKESAYLV 217
Cdd:COG1502  197 PDSPRETIERALLAAIASARRRIYIETPYF----------VPDRSLLRALIAAARRGVDVRI-------LLPAKSDHPLV 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 218 QEG----LAEVREINVT-RLIGSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFqECPCVASDLYKIFAAYWKL 292
Cdd:COG1502  260 HWAsrsyYEELLEAGVRiYEYEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVI-YDPEFAAQLRARFEEDLAH 338

                        170
                 ....*....|..
gi 392919428 293 GEndSVIPEKWP 304
Cdd:COG1502  339 SR--EVTLEEWR 348
PLDc_2 pfam13091
PLD-like domain;
150-290 9.77e-15

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 70.78  E-value: 9.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428  150 INIIDNSKQYLDISVMYWNLNtsdykssvygRRVYEAIIRAGKRGVKIRI------AQDGASNLSDNKESAYLVQEGlAE 223
Cdd:pfam13091   2 IDLINSAKKSIDIATYYFVPD----------REIIDALIAAAKRGVDVRIildsnkDDAGGPKKASLKELRSLLRAG-VE 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392919428  224 VREINVTrligSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQEcPCVASDLYKIFAAYW 290
Cdd:pfam13091  71 IREYQSF----LRSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEFDRLW 132
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 150-263 2.89e-11

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: 61.16  E-value: 2.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 150 INIIDNSKQYLDISvMYWnLNTsdykssvygRRVYEAIIRAGKRGVKIRIAQDGaSNLSDNKESAYLvqeGLAEVREINV 229
Cdd:cd09116   15 VALIANAKSSIDVA-MYA-LTD---------PEIAEALKRAAKRGVRVRIILDK-DSLADNLSITLL---ALLSNLGIPV 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 392919428 230 TRLIGSGIIHTKFILSDIATLYIGSANMDWKSLS 263
Cdd:cd09116   80 RTDSGSKLMHHKFIIIDGKIVITGSANWTKSGFH 113
PLDc_2 pfam13091
PLD-like domain;
349-508 4.96e-11

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 60.38  E-value: 4.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428  349 IQKIMKdARKSVCISVMDYIPStlymkksnrfwPEIDDSIRDAAYRGVNVRMLIShwdhSRKEMIPFLKSlqtitDGLPR 428
Cdd:pfam13091   2 IDLINS-AKKSIDIATYYFVPD-----------REIIDALIAAAKRGVDVRIILD----SNKDDAGGPKK-----ASLKE 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428  429 YNRTEHGQVQVRIFTvppngkekiPFTRVNHAKYMVTED-IAYIGTSNWSGDYFISTAGVAMVVRQPSATKRLQNVFDRD 507
Cdd:pfam13091  61 LRSLLRAGVEIREYQ---------SFLRSMHAKFYIIDGkTVIVGSANLTRRALRLNLENNVVIKDPELAQELEKEFDRL 131


                  .
gi 392919428  508 W 508
Cdd:pfam13091 132 W 132
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 347-478 6.19e-11

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: 59.84  E-value: 6.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 347 AAIQKIMKDARKSVCIsVMDYIpstlymkkSNRFWPEIDDSIRDAAYRGVNVRMLISHWDHSRKEMIPflkslqtitdgl 426
Cdd:cd00138    1 EALLELLKNAKESIFI-ATPNF--------SFNSADRLLKALLAAAERGVDVRLIIDKPPNAAGSLSA------------ 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392919428 427 PRYNRTEHGQVQVRIFTVPPNgkekipFTRVNHAKYMVTED-IAYIGTSNWSG 478
Cdd:cd00138   60 ALLEALLRAGVNVRSYVTPPH------FFERLHAKVVVIDGeVAYVGSANLST 106
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 181-290 1.62e-10

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: 59.21  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 181 RRVYEAIIRAGKRGVKIRIAQDGA-SNLSDNKESAYLVQEGLAEVReinvTRLIGSGIIHTKFILSDIATLYIGSANMDW 259
Cdd:cd09128   37 APILDALVDAAKRGVDVRVLLPSAwSAEDERQARLRALEGAGVPVR----LLKDKFLKIHAKGIVVDGKTALVGSENWSA 112

                         90       100       110
                 ....*....|....*....|....*....|.
gi 392919428 260 KSLSEVKEVGVVFQEcPCVASDLYKIFAAYW 290
Cdd:cd09128  113 NSLDRNREVGLIFDD-PEVAAYLQAVFESDW 142
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 346-516 2.58e-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: 62.27  E-value: 2.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 346 LAAIQKimkdARKSVCISVmdyipstlYMKKSNRFWPEIDDSIRDAAYRGVNVRMLISHWDhSRKEMIPFLKSLQtitdg 425
Cdd:COG1502   31 LEAIEA----ARRSIDLEY--------YIFDDDEVGRRLADALIAAARRGVKVRVLLDGIG-SRALNRDFLRRLR----- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 426 lprynrtEHGqVQVRIFtVPPNGKEKIPFtRVNHAKYMVTED-IAYIGTSNWSGDYFISTAG------VAMVVRQPSATK 498
Cdd:COG1502   93 -------AAG-VEVRLF-NPVRLLFRRLN-GRNHRKIVVIDGrVAFVGGANITDEYLGRDPGfgpwrdTHVRIEGPAVAD 162

                        170
                 ....*....|....*...
gi 392919428 499 rLQNVFDRDWNSEYSKDL 516
Cdd:COG1502  163 -LQAVFAEDWNFATGEAL 179
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 347-507 1.37e-09

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: 56.50  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 347 AAIQKIMKDARKSVCISV--MDYipstlymkksnrfwPEIDDSIRDAAYRGVNVRMLIshwDHSRKemipflkslQTITD 424
Cdd:cd09127   11 APVVDAIASAKRSILLKMyeFTD--------------PALEKALAAAAKRGVRVRVLL---EGGPV---------GGISR 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 425 GLPRYNRTEHGQVQVRIftvpPNGKEKIPFTrvnHAKYMVTED-IAYIGTSNWSGDYFISTAGVAMVVRQPSATKRLQNV 503
Cdd:cd09127   65 AEKLLDYLNEAGVEVRW----TNGTARYRYT---HAKYIVVDDeRALVLTENFKPSGFTGTRGFGVVTDDPAVVAEIADV 137


                 ....
gi 392919428 504 FDRD 507
Cdd:cd09127  138 FDAD 141
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 382-508 1.93e-09

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: 56.13  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 382 PEIDDSIRDAAYRGVNVRMLishwdhsrkemipfLKSLQTITDGLPRYNRT-EHGQVQVRIFTVPPngkEKIpftrvnHA 460
Cdd:cd09128   37 APILDALVDAAKRGVDVRVL--------------LPSAWSAEDERQARLRAlEGAGVPVRLLKDKF---LKI------HA 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 392919428 461 KYMVTED-IAYIGTSNWSGDYFISTAGVAMVVRQPSATKRLQNVFDRDW 508
Cdd:cd09128   94 KGIVVDGkTALVGSENWSANSLDRNREVGLIFDDPEVAAYLQAVFESDW 142
PRK13912 PRK13912
nuclease NucT; Provisional
 137-256 1.44e-07

nuclease NucT; Provisional


Pssm-ID: 184389 [Multi-domain]  Cd Length: 177  Bit Score: 51.32  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 137 LPFKtNNHTAEAWINIIDNSKQYLDISvMYwnlntsdyksSVYGRRVYEAIIRAGKRGVKIRIAQDGASNLSDNkesaYL 216
Cdd:PRK13912  27 LPYE-QKDALNKLVSLISNARSSIKIA-IY----------SFTHKDIAKALKSAAKRGVKISIIYDYESNHNND----QS 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 392919428 217 VQEGLAEVREINVTRLIG--------SGIIHTKFILSDIATLYIGSAN 256
Cdd:PRK13912  91 TIGYLDKYPNIKVCLLKGlkakngkyYGIMHQKVAIIDDKIVVLGSAN 138
PLDc_Nuc_like_unchar1_1 cd09172
Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, ...
 147-290 3.90e-07

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: 49.66  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 147 EAWINIIDNSKQYLDISVmywnlntsdYksSVYGRRVYEAIIRAGKRGVKIRIAQDGASNLSDNKESAYlvQEGLAEVRE 226
Cdd:cd09172   12 LAFLDEARSAGSSIRLAI---------Y--ELDDPEIIDALKAAKDRGVRVRIILDDSSVTGDPTEESA--AATLSKGPG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392919428 227 INVTRLIGSGIIHTKFILSD----IATLYIGSANMDWKSLSEVKEVGVVFqecpcVASDLYKIFAAYW 290
Cdd:cd09172   79 ALVKRRHSSGLMHNKFLVVDrkdgPNRVLTGSTNFTTSGLYGQSNNVLIF-----RNPAFAAAYLAYW 141
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 142-286 2.01e-06

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: 47.34  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 142 NNHTAEAWINIIDNSKQYLDISvMYWNLNTSDYKSSVYgrRVYEAIIRAGKRGVKIRIAQDGASNLSD----NKESAYLV 217
Cdd:cd09131    1 DQEYYPALLDLINNAKRSIYIA-MYMFKYYENPGNGVN--TLLEALIDAHKRGVDVKVVLEDSIDDDEvteeNDNTYRYL 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392919428 218 QEGLAEVR--EINVTrligsgiIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFqECPCVASDLYKIF 286
Cdd:cd09131   78 KDNGVEVRfdSPSVT-------THTKLVVIDGRTVYVGSHNWTYSALDYNHEASVLI-ESPEVADFAINYF 140
PLDc_SMU_988_like_2 cd09160
Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 ...
 142-287 3.24e-06

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: 47.49  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 142 NNHTAE-AWINIIDNSKQYLDISVMYWNLntsdykssvyGRRVYEAIIRAGKRGVKIRIAQDGasnLSDnKESAYLVQEG 220
Cdd:cd09160    8 NEPVGEnVYLDLINQAKDYVYITTPYLIL----------DDEMLDALCLAAKRGVDVRIITPH---IPD-KKYVFLVTRS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 221 laevreiNVTRLIGSGI---------IHTKFILSD--IATlyIGSANMDWKSLSEVKEVGVVFQECPCVAS---DLYKIF 286
Cdd:cd09160   74 -------NYPELLEAGVkiyeytpgfIHAKTFVSDdkAAV--VGTINLDYRSLYLHFECGVYMYDTPVISDikeDFEETL 144


                 .
gi 392919428 287 A 287
Cdd:cd09160  145 A 145
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 153-303 2.41e-05

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: 44.84  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 153 IDNSKQYLDISVMYWnlntsdykssVYGRRVYEAIIRAGKRGVKIRIAQDGASNLSDNKESAY-----LVQEGlAEVREI 227
Cdd:cd09159   20 IAAARRRIWIANAYF----------VPDRRLRRALIEAARRGVDVRLLLPGKSDDPLTVAASRalygkLLRAG-VRIFEY 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392919428 228 NvtrligSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFqECPCVASDLYKIFAAywKLGENDSVIPEKW 303
Cdd:cd09159   89 Q------PSMLHAKTAVIDGDWATVGSSNLDPRSLRLNLEANLVV-EDPAFAAQLEELFEE--DLARSREITLEEW 155
PLDc_Nuc cd09170
Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar ...
 181-256 6.67e-05

Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar proteins; Catalytic domain of an EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar proteins. Nuc is an endonuclease cleaving both single- and double-stranded DNA. It is the smallest known member of the phospholipase D (PLD, EC 3.1.4.4) superfamily that includes a diverse group of proteins with various catalytic functions. Most members of this superfamily have two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in a single polypeptide chain and both are required for catalytic activity. However, Nuc only has one copy of the HKD motif per subunit but form a functionally active homodimer (it is most likely also active in solution as a multimeric protein), which has a single active site at the dimer interface containing the HKD motifs from both subunits. Due to the lack of a distinct domain for DNA binding, Nuc cuts DNA non-specifically. It utilizes 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.


Pssm-ID: 197267 [Multi-domain]  Cd Length: 142  Bit Score: 42.89  E-value: 6.67e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392919428 181 RRVYEAIIRAGKRGVKIRIAQDGASNLSDNKESAYLVQEGlAEVREINVtrligSGIIHTKFILSDIATLYIGSAN 256
Cdd:cd09170   37 PPIARALIAAKKRGVDVRVVLDKSQAGGKYSALNYLANAG-IPVRIDDN-----YAIMHNKVMVIDGKTVITGSFN 106
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 386-507 7.49e-05

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: 43.30  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 386 DSIRDAAYRGVNVRMLIshwdhSRKEMIPFLKSLqtitdGLPRYNR-TEHGqvqVRIFTVPPngkekipftRVNHAKYMV 464
Cdd:cd09159   42 RALIEAARRGVDVRLLL-----PGKSDDPLTVAA-----SRALYGKlLRAG---VRIFEYQP---------SMLHAKTAV 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 392919428 465 TEDI-AYIGTSNWsgDYFiSTAG---VAMVVRQPSATKRLQNVFDRD 507
Cdd:cd09159  100 IDGDwATVGSSNL--DPR-SLRLnleANLVVEDPAFAAQLEELFEED 143
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 150-288 1.04e-04

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: 42.25  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 150 INIIDNSKQYLDISVMYWnlnTSdykssvygRRVYEAIIRAGKRGVKIRIAQDGA--SNLSDN-KESAYLVQEGlAEVRE 226
Cdd:cd09127   14 VDAIASAKRSILLKMYEF---TD--------PALEKALAAAAKRGVRVRVLLEGGpvGGISRAeKLLDYLNEAG-VEVRW 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392919428 227 IN----VTRLigsgiiHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFQEcPCVASDLYKIFAA 288
Cdd:cd09127   82 TNgtarYRYT------HAKYIVVDDERALVLTENFKPSGFTGTRGFGVVTDD-PAVVAEIADVFDA 140
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
 346-509 1.97e-04

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: 41.69  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 346 LAAIQKimkdARKSVCISVmdYIpstlymkksnrFWP-EIDDSIRDA----AYRGVNVRMLIshwDH--SRKEMIPFLKS 418
Cdd:cd09110   11 LEAIRA----ARHSIHLEY--YI-----------FRDdEIGRRFRDAliekARRGVEVRLLY---DGfgSLGLSRRFLRE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 419 LqtitdglprynrTEHGqVQVRIFTVPPNGKEKIPFTRVNHAKyMVTED--IAYIGTSNWSGDYFISTAG------VAMV 490
Cdd:cd09110   71 L------------REAG-VEVRAFNPLSFPLFLLRLNYRNHRK-ILVIDgkIAFVGGFNIGDEYLGKDPGfgpwrdTHVR 136

                        170
                 ....*....|....*....
gi 392919428 491 VRQPsATKRLQNVFDRDWN 509
Cdd:cd09110  137 IEGP-AVADLQAAFLEDWY 154
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 180-296 2.62e-04

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: 42.59  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 180 GRRVYEAIIRAGKRGVKIRIAQDG-ASNlsDNKE--SAY------LVQEG--LAEVR-----EINVTRLIGSGI--IHTK 241
Cdd:cd09113   43 GDEGVALLAELARRGVRVRILTNSlAAT--DVPAvhSGYaryrkrLLKAGveLYELKpdaakRKRLRGLFGSSRasLHAK 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392919428 242 FILSDIATLYIGSANMDWKSLSEVKEVGVVFqECPCVASDLYKIF------AAYWKLGEND 296
Cdd:cd09113  121 SFVIDDRLVFVGSFNLDPRSAYLNTEMGLVI-DSPELAAQLRAAMeedlapSAYWVLLLDD 180
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 456-480 2.64e-04

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 38.14  E-value: 2.64e-04
                           10        20
                   ....*....|....*....|....*.
gi 392919428   456 RVNHAKYMVTED-IAYIGTSNWSGDY 480
Cdd:smart00155   3 GVLHTKLMIVDDeIAYIGSANLDGRS 28
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
 147-286 3.19e-04

catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD corresponds to the catalytic domain repeat 2 of bacterial cardiolipin synthase (CL synthase, EC 2.7.8.-) and a few homologs found in eukaryotes and archea. Bacterial CL synthases catalyze reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form cardiolipin (CL) and glycerol. The monomer of bacterial CL synthase consists of two catalytic domains. Each catalytic domain contains one copy of conserved HKD motifs (H-X-K-X(4)-D, X represents any amino acid residue) that are the characteristic of the phospholipase D (PLD) superfamily. Two HKD motifs from two domains together form a single active site involving 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 in PLD superfamily. Like other PLD enzymes, bacterial CL synthase 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: 197211 [Multi-domain]  Cd Length: 174  Bit Score: 41.69  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 147 EAWINIIDNSKQYLDISVMYWnlntsdykssVYGRRVYEAIIRAGKRGVKIRIAqdgASNLSDNK------ES--AYLVQ 218
Cdd:cd09112   14 QAYLKAINSAKKSIYIQTPYF----------IPDESLLEALKTAALSGVDVRIM---IPGKPDHKlvywasRSyfEELLK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392919428 219 EGlAEVREINvtrligSGIIHTKFILSDIATLYIGSANMDWKSLSEVKEVGVVFqECPCVASDLYKIF 286
Cdd:cd09112   81 AG-VKIYEYN------KGFLHSKTLIVDDEIASVGTANLDIRSFELNFEVNAVI-YDKEVAKKLEEIF 140
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 185-272 3.50e-04

Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial cardiolipin synthase; Putative catalytic domain, repeat 2, 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: 197259 [Multi-domain]  Cd Length: 172  Bit Score: 41.48  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 185 EAIIRAGKRGVKIRIAQDGASN--LSDNKESAYL--VQEGLAEVReinvtrLIGSGIIHTKFILSDIATLYIGSANMDWK 260
Cdd:cd09162   42 RALRLAARRGVDVRLIVPKRSNhrIADLARGSYLrdLQEAGAEIY------LYQPGMLHAKAVVVDDKLALVGSANLDMR 115

                         90
                 ....*....|..
gi 392919428 261 SLSEVKEVGVVF 272
Cdd:cd09162  116 SLFLNYEVAVFF 127
PLDc_vPLD6_like cd09171
Catalytic domain of vertebrate phospholipase D6 and similar proteins; Catalytic domain of ...
 150-256 4.26e-04

Catalytic domain of vertebrate phospholipase D6 and similar proteins; Catalytic domain of vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), a homolog of the EDTA-resistant nuclease Nuc from Salmonella typhimurium, and similar proteins. PLD6 can selectively hydrolyze 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. It also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. PLD6 belongs to the phospholipase D (PLD) superfamily. Its monomer contains a short conserved sequence motif, H-x-K-x(4)-D (where x represents any amino acid residue), termed the HKD motif, which is essential in catalysis. PLD6 is more closely related to the nuclease Nuc than to other vertebrate phospholipases, which have two copies of the HKD motif in a single polypeptide chain. Like Nuc, PLD6 may utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from the HKD motif of one subunit 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.


Pssm-ID: 197268 [Multi-domain]  Cd Length: 136  Bit Score: 40.67  E-value: 4.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 150 INIIDNSKQYLDIsVMYwnLNTSDykssvygrRVYEAIIRAGKRGVKIRIAQDgaSNLSDNKES--AYLVQEGLaEVREI 227
Cdd:cd09171   14 LRYLLSARKSLDV-CVF--TITCD--------DLADAILDLHRRGVRVRIITD--DDQMEDKGSdiGKLRKAGI-PVRTD 79

                         90       100
                 ....*....|....*....|....*....
gi 392919428 228 NVtrligSGIIHTKFILSDIATLYIGSAN 256
Cdd:cd09171   80 LS-----SGHMHHKFAVIDGKILITGSFN 103
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 236-261 1.85e-03

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 35.83  E-value: 1.85e-03
                           10        20
                   ....*....|....*....|....*.
gi 392919428   236 GIIHTKFILSDIATLYIGSANMDWKS 261
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_unchar2_2 cd09130
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 383-511 5.68e-03

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: 197228 [Multi-domain]  Cd Length: 157  Bit Score: 37.61  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 383 EIDDSIRDAAYRGVNVRMLIshwDHSRKemiPFLKSlqtiTDGLPryNRT--------EHGQVQVRIFTvppNGKEKipf 454
Cdd:cd09130   34 DVIKALIDAANRGVDVRLIL---DPNKD---AFGRE----KNGIP--NRPvaaelmkkTKGKIQIRWYN---TGGEQ--- 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392919428 455 trvNHAKYMV----TEDIAYIGTSNWS----GDYFIST-AGVAMVVRQPsATKRLQNVFDRDWNSE 511
Cdd:cd09130   96 ---FHTKLLLikkkGQAIIIGGSANFTrrnlRDYNLETdLKILAPNDSP-VSKDVDAYFDRLWNNE 157
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
 180-291 6.43e-03

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: 37.46  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 180 GRRVYEAIIRAGKRGVKIRIAQD--GASNLSDNKESAyLVQEGlAEVREINVT--RLIGSGII---HTKFILSDIATLYI 252
Cdd:cd09110   34 GRRFRDALIEKARRGVEVRLLYDgfGSLGLSRRFLRE-LREAG-VEVRAFNPLsfPLFLLRLNyrnHRKILVIDGKIAFV 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 392919428 253 GSANM--DWKSLSEVKE----VGVVFqECPCVAsDLYKIFAAYWK 291
Cdd:cd09110  112 GGFNIgdEYLGKDPGFGpwrdTHVRI-EGPAVA-DLQAAFLEDWY 154
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 388-509 9.31e-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: 37.13  E-value: 9.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392919428 388 IRDAAYRGVNVRMLISHWDHSRKEmiPFLKSLqtitdglprynrTEHGQVQVRIFTVPPNGKEKIP-----FTRVN---H 459
Cdd:cd09111   42 LLEAADRGVRVRLLLDDLGTSGRD--RLLAAL------------DAHPNIEVRLFNPFRNRGGRLLefltdFSRLNrrmH 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392919428 460 AKYMVTEDIAYI-GTSNWSGDYFISTAGVA-----MVVRQPSAtKRLQNVFDRDWN 509
Cdd:cd09111  108 NKLFIVDGAVAIvGGRNIGDEYFGASPEVNfrdldVLAVGPVV-RQLSESFDTYWN 162
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH