NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|58865906|ref|NP_001012167|]
View 

5'-3' exonuclease PLD3 [Rattus norvegicus]

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
 77-488 1.54e-146

phospholipase-D-like protein; Provisional


The actual alignment was detected with superfamily member PHA02820:

Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 425.95  E-value: 1.54e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   77 CYDPCEAVLVESIPEGLEFPNAttsNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDthtqepSAQQGEEVLQQLQALAP 156
Cdd:PHA02820   2 NPDNTIAVITETIPIGMQFDKV---YLSTFNFWREILSNTTKTLDISSFYWSLSDEV------GTNFGTMILNEIIQLPK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  157 RGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCS 236
Cdd:PHA02820  73 RGVRVRIAVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  237 CLARDLTKIFEAYWFLGQagSSIPSTWPRPFDTRYNQETPMEICLNGTPALAYLASAPPPLCPGGRTPDLKALLSVVDNA 316
Cdd:PHA02820 153 NLAADLTQIFEVYWYLGV--NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  317 RSFIYIAVMNYLPTMeFSHPRR--FWPAIDDGLRRAAYERGVKVRLLISCWGHSEPSMRSFLLSLAALrdNHTHSDIQVK 394
Cdd:PHA02820 231 SKFVYVSVMNFIPII-YSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAML--KSKNINIEVK 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  395 LFVVPadEAQARIPYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTSLLVTQNGHGGLRSQLEAVFLRDWESPYSHNL 474
Cdd:PHA02820 308 LFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQQLEDIFIRDWNSKYSYEL 385

                        410
                 ....*....|....
gi 58865906  475 dtSADSVGNACRLL 488
Cdd:PHA02820 386 --YDTSPTKRCRLL 397
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 77-488 1.54e-146

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 425.95  E-value: 1.54e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   77 CYDPCEAVLVESIPEGLEFPNAttsNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDthtqepSAQQGEEVLQQLQALAP 156
Cdd:PHA02820   2 NPDNTIAVITETIPIGMQFDKV---YLSTFNFWREILSNTTKTLDISSFYWSLSDEV------GTNFGTMILNEIIQLPK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  157 RGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCS 236
Cdd:PHA02820  73 RGVRVRIAVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  237 CLARDLTKIFEAYWFLGQagSSIPSTWPRPFDTRYNQETPMEICLNGTPALAYLASAPPPLCPGGRTPDLKALLSVVDNA 316
Cdd:PHA02820 153 NLAADLTQIFEVYWYLGV--NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  317 RSFIYIAVMNYLPTMeFSHPRR--FWPAIDDGLRRAAYERGVKVRLLISCWGHSEPSMRSFLLSLAALrdNHTHSDIQVK 394
Cdd:PHA02820 231 SKFVYVSVMNFIPII-YSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAML--KSKNINIEVK 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  395 LFVVPadEAQARIPYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTSLLVTQNGHGGLRSQLEAVFLRDWESPYSHNL 474
Cdd:PHA02820 308 LFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQQLEDIFIRDWNSKYSYEL 385

                        410
                 ....*....|....
gi 58865906  475 dtSADSVGNACRLL 488
Cdd:PHA02820 386 --YDTSPTKRCRLL 397
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 289-471 4.57e-131

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: 377.39  E-value: 4.57e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 289 YLASAPPPLCPGGRTPDLKALLSVVDNARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 368
Cdd:cd09147   1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 369 EPSMRSFLLSLAALRDNHTHSDIQVKLFVVPADEAQARIPYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTSLLVTQ 448
Cdd:cd09147  81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVPADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSALVVNQ 160

                       170       180
                ....*....|....*....|....*.
gi 58865906 449 NG---HGGLRSQLEAVFLRDWESPYS 471
Cdd:cd09147 161 TGrsaSGTLQSQLQAVFERDWDSPYS 186
PLDc_3 pfam13918
PLD-like domain;
221-399 3.76e-42

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 148.24  E-value: 3.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   221 SLTQVKELGVVMYNCSCLARDLTKIFEAYWFLgQAGSSIPSTWPRPFDTRYNQETPMEICLNGTPALAYLASAPPPLCPG 300
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSL-IFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   301 GRTPDLKALLSVVDNARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHSEPSMRSFLLSLA 380
Cdd:pfam13918  80 NRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLD 159

                         170
                  ....*....|....*....
gi 58865906   381 ALRDNHTHSDIQVKLFVVP 399
Cdd:pfam13918 160 AFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 107-470 5.41e-24

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: 103.10  E-value: 5.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 107 QAWLGLLAGAHSSLDIASFYWTltnNDthtqepsaQQGEEVLQQLQALAPRGVKVRI---AVSKPNGPLADLQSLLQSGA 183
Cdd:COG1502  28 AALLEAIEAARRSIDLEYYIFD---DD--------EVGRRLADALIAAARRGVKVRVlldGIGSRALNRDFLRRLRAAGV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 184 QVRMVDMQKLT----HGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELG-----VVMYNCSCLArDLTKIFEAYWFLgQ 254
Cdd:COG1502  97 EVRLFNPVRLLfrrlNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpwrdtHVRIEGPAVA-DLQAVFAEDWNF-A 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 255 AGSSIPstWPRPFDTrynqeTPMEICLNGtpalaylasappplcPGGRTPDL-KALLSVVDNARSFIYIAvmnylpTMEF 333
Cdd:COG1502 175 TGEALP--FPEPAGD-----VRVQVVPSG---------------PDSPRETIeRALLAAIASARRRIYIE------TPYF 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 334 SHPRRfwpaIDDGLRRAAyERGVKVRLLISCWGHSEPSMRSFLLSLAALRdnhthsdiqvklfvvpadEAQARI--PYAR 411
Cdd:COG1502 227 VPDRS----LLRALIAAA-RRGVDVRILLPAKSDHPLVHWASRSYYEELL------------------EAGVRIyeYEPG 283

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865906 412 VNHNKYMVT-ERTTYIGTSNWSGSYF---TETAgtsLLVTqngHGGLRSQLEAVFLRDWESPY 470
Cdd:COG1502 284 FLHAKVMVVdDEWALVGSANLDPRSLrlnFEVN---LVIY---DPEFAAQLRARFEEDLAHSR 340
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 196-221 7.37e-10

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: 53.93  E-value: 7.37e-10
                           10        20
                   ....*....|....*....|....*.
gi 58865906    196 GVLHTKFWVVDQTHFYLGSANMDWRS 221
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
bac_cardiolipin TIGR04265
cardiolipin synthase; This model is based on experimentally characterized bacterial ...
 107-249 2.72e-06

cardiolipin synthase; This model is based on experimentally characterized bacterial cardiolipin synthases (cls) from E. coli, Staphylococcus aureus (two), and Bacillus pseudofirmus OF4. This model describes just one of several homologous but non-orthologous forms of cls. The cutoff score is set arbitrarily high to avoid false-positives. Note that there are two enzymatic activites called cardiolipin synthase. This model represents type 1, which does not rely on a CDP-linked donor, but instead does a reversible transfer of a phosphatidyl group from one phosphatidylglycerol molecule to another.


Pssm-ID: 211988 [Multi-domain]  Cd Length: 483  Bit Score: 49.79  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   107 QAWLGLLAGAHSSLDIASFYWTltnndthtqePSaqqgEEVLQQLQALAPRGVKVRIAV-SKPNGPL------ADLQSLL 179
Cdd:TIGR04265 321 YGYLKMIYSAKKSIYIQSPYFI----------PD----DDLLHAIKIAALSGVDVSIMIpNKPDHPLvfwasrSNFTELL 386

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   180 QSGAQVRMVDmqkltHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCScLARDLTKIFEAY 249
Cdd:TIGR04265 387 AAGVKIYQYE-----NGFLHSKSVLVDDEIASVGTANMDMRSFWLNFEVNAFIYDKG-FAKDLAAAYDDD 450
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 77-488 1.54e-146

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 425.95  E-value: 1.54e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   77 CYDPCEAVLVESIPEGLEFPNAttsNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDthtqepSAQQGEEVLQQLQALAP 156
Cdd:PHA02820   2 NPDNTIAVITETIPIGMQFDKV---YLSTFNFWREILSNTTKTLDISSFYWSLSDEV------GTNFGTMILNEIIQLPK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  157 RGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCS 236
Cdd:PHA02820  73 RGVRVRIAVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  237 CLARDLTKIFEAYWFLGQagSSIPSTWPRPFDTRYNQETPMEICLNGTPALAYLASAPPPLCPGGRTPDLKALLSVVDNA 316
Cdd:PHA02820 153 NLAADLTQIFEVYWYLGV--NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  317 RSFIYIAVMNYLPTMeFSHPRR--FWPAIDDGLRRAAYERGVKVRLLISCWGHSEPSMRSFLLSLAALrdNHTHSDIQVK 394
Cdd:PHA02820 231 SKFVYVSVMNFIPII-YSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAML--KSKNINIEVK 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  395 LFVVPadEAQARIPYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTSLLVTQNGHGGLRSQLEAVFLRDWESPYSHNL 474
Cdd:PHA02820 308 LFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQQLEDIFIRDWNSKYSYEL 385

                        410
                 ....*....|....
gi 58865906  475 dtSADSVGNACRLL 488
Cdd:PHA02820 386 --YDTSPTKRCRLL 397
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 289-471 4.57e-131

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: 377.39  E-value: 4.57e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 289 YLASAPPPLCPGGRTPDLKALLSVVDNARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 368
Cdd:cd09147   1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 369 EPSMRSFLLSLAALRDNHTHSDIQVKLFVVPADEAQARIPYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTSLLVTQ 448
Cdd:cd09147  81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVPADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSALVVNQ 160

                       170       180
                ....*....|....*....|....*.
gi 58865906 449 NG---HGGLRSQLEAVFLRDWESPYS 471
Cdd:cd09147 161 TGrsaSGTLQSQLQAVFERDWDSPYS 186
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 84-253 1.20e-116

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: 340.00  E-value: 1.20e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  84 VLVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLQQLQALAPRGVKVRI 163
Cdd:cd09144   1 VLVESIPEGLVFNSSSTINPSIYQAWLNLISAAQSSLDIASFYWTLTNSDTHTQEPSANQGEQILKKLGQLSQSGVYVRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 164 AVSKPNG--PLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARD 241
Cdd:cd09144  81 AVDKPADpkPMEDINALSSYGADVRMVDMRKLTTGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVYNCSCLAED 160

                       170
                ....*....|..
gi 58865906 242 LTKIFEAYWFLG 253
Cdd:cd09144 161 LGKIFEAYWYLG 172
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 289-466 7.76e-96

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: 286.84  E-value: 7.76e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 289 YLASAPPPLCPGGRTPDLKALLSVVDNARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 368
Cdd:cd09107   1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 369 EPSMRSFLLSLAALRDNHTHSDIQVKLFVVPADEAQaRIPYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTSLLVTQ 448
Cdd:cd09107  81 DPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQST-KIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVSLVIND 159

                       170
                ....*....|....*...
gi 58865906 449 NghgGLRSQLEAVFLRDW 466
Cdd:cd09107 160 P---AIVQQLKDVFERDW 174
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 289-471 7.18e-82

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: 251.69  E-value: 7.18e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 289 YLASAPPPLCPGGRTPDLKALLSVVDNARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 368
Cdd:cd09148   1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 369 EPSMRSFLLSLAALRDNHTHSDIQVKLFVVPADEaQARIPYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTSLLVTQ 448
Cdd:cd09148  81 DPDMFPFLRSLNALSNPPLSISVHVKLFIVPVGN-QTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVGLVILQ 159

                       170       180
                ....*....|....*....|....*...
gi 58865906 449 N-GHGG----LRSQLEAVFLRDWESPYS 471
Cdd:cd09148 160 SpGANEemlpVQEQLRSLFERDWSSPYA 187
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 85-235 2.81e-72

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: 225.59  E-value: 2.81e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  85 LVESIPEGLEFPNaTTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTqEPSAQQGEEVLQQLQALAPRGVKVRIA 164
Cdd:cd09106   1 LVESIPEGLTFLS-SSSHLSTFEAWMELISSAKKSIDIASFYWNLRGTDTNP-DSSAQEGEDIFNALLEAAKRGVKIRIL 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58865906 165 VSKPNGPLA---DLQSLLQSGAQVRMVDMQKL-THGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNC 235
Cdd:cd09106  79 QDKPSKDKPdedDLELAALGGAEVRSLDFTKLiGGGVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 85-252 5.56e-65

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: 207.45  E-value: 5.56e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  85 LVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLQQLQALAPRGVKVRIA 164
Cdd:cd09145   1 LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWSLTGEDIGVNDSSSLPGEDILKELAELLSRNVSVRAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 165 VSKPNGPL--ADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDL 242
Cdd:cd09145  81 ASIPTLAAnsTDLKILRQKGAHVRKVNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAKDL 160

                       170
                ....*....|
gi 58865906 243 TKIFEAYWFL 252
Cdd:cd09145 161 HKTFQTYWVL 170
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 85-475 8.20e-52

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 179.86  E-value: 8.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   85 LVESIPEGLEFpnaTTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDthtqepsaqQGEEVLQQLQALAPRGVKVRIA 164
Cdd:PHA03003  15 IVETLPKSLGI---ATQHMSTYECFDEIISQAKKYIYIASFCCNLRSTP---------EGRLILDKLKEAAESGVKVTIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  165 VSKPNGPlADLQSLLQSGAQVRMVDMQKLTH-GVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVvmYN-CSCLARDL 242
Cdd:PHA03003  83 VDEQSGD-KDEEELQSSNINYIKVDIGKLNNvGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLGV--YStYPPLATDL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  243 TKIFEAYWFLGQAGSSIPSTWPR---PFDTRYNQETPMEIClngtpalaYLASAPPPLCPGGRTPDLKALLSVVDNARSF 319
Cdd:PHA03003 160 RRRFDTFKAFNKNKSVFNRLCCAcclPVSTKYHINNPIGGV--------FFSDSPEHLLGYSRTLDADVVLHKIKSAKKS 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  320 IYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHSEPSMRSFLLSLAALRDNHthsDIQVKLFVVP 399
Cdd:PHA03003 232 IDLELLSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCVGN---DLSVKVFRIP 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58865906  400 adeaqaripyarvNHNKYM-VTERTTYIGTSNWSGSYFTETAGTSLlvtQNGHGGLRSQLEAVFLRDWESPYSHNLD 475
Cdd:PHA03003 309 -------------NNTKLLiVDDEFAHITSANFDGTHYLHHAFVSF---NTIDKELVKELSAIFERDWTSSYSKPLK 369
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 289-474 3.13e-50

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: 169.65  E-value: 3.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 289 YLASAPPPLCPGGRTPDLKALLSVVDNARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 368
Cdd:cd09149   1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 369 EPSMRSFLLSLAALRDNHTHSDIQVKLFVVPADEAQAripYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTSLLVTQ 448
Cdd:cd09149  81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEEESDCT---SPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVGLVINQ 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 58865906 449 -----NGHGGLRSQLEAVFLRDWESPYSHNL 474
Cdd:cd09149 158 adgveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 84-252 2.32e-46

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: 158.49  E-value: 2.32e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  84 VLVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLtnNDTHtqePSAQQGEEVLQQLQALAPRGVKVRI 163
Cdd:cd09146   1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDL--NASH---PSACQGQRLFERLLGLASRGVELKI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 164 aVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDLT 243
Cdd:cd09146  76 -VSGITDSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLH 154


                ....*....
gi 58865906 244 KIFEAYWFL 252
Cdd:cd09146 155 RVFALYWSL 163
PLDc_3 pfam13918
PLD-like domain;
221-399 3.76e-42

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 148.24  E-value: 3.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   221 SLTQVKELGVVMYNCSCLARDLTKIFEAYWFLgQAGSSIPSTWPRPFDTRYNQETPMEICLNGTPALAYLASAPPPLCPG 300
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSL-IFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   301 GRTPDLKALLSVVDNARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHSEPSMRSFLLSLA 380
Cdd:pfam13918  80 NRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLD 159

                         170
                  ....*....|....*....
gi 58865906   381 ALRDNHTHSDIQVKLFVVP 399
Cdd:pfam13918 160 AFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 107-470 5.41e-24

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: 103.10  E-value: 5.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 107 QAWLGLLAGAHSSLDIASFYWTltnNDthtqepsaQQGEEVLQQLQALAPRGVKVRI---AVSKPNGPLADLQSLLQSGA 183
Cdd:COG1502  28 AALLEAIEAARRSIDLEYYIFD---DD--------EVGRRLADALIAAARRGVKVRVlldGIGSRALNRDFLRRLRAAGV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 184 QVRMVDMQKLT----HGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELG-----VVMYNCSCLArDLTKIFEAYWFLgQ 254
Cdd:COG1502  97 EVRLFNPVRLLfrrlNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpwrdtHVRIEGPAVA-DLQAVFAEDWNF-A 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 255 AGSSIPstWPRPFDTrynqeTPMEICLNGtpalaylasappplcPGGRTPDL-KALLSVVDNARSFIYIAvmnylpTMEF 333
Cdd:COG1502 175 TGEALP--FPEPAGD-----VRVQVVPSG---------------PDSPRETIeRALLAAIASARRRIYIE------TPYF 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 334 SHPRRfwpaIDDGLRRAAyERGVKVRLLISCWGHSEPSMRSFLLSLAALRdnhthsdiqvklfvvpadEAQARI--PYAR 411
Cdd:COG1502 227 VPDRS----LLRALIAAA-RRGVDVRILLPAKSDHPLVHWASRSYYEELL------------------EAGVRIyeYEPG 283

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865906 412 VNHNKYMVT-ERTTYIGTSNWSGSYF---TETAgtsLLVTqngHGGLRSQLEAVFLRDWESPY 470
Cdd:COG1502 284 FLHAKVMVVdDEWALVGSANLDPRSLrlnFEVN---LVIY---DPEFAAQLRARFEEDLAHSR 340
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 107-232 1.36e-21

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: 89.88  E-value: 1.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 107 QAWLGLLAGAHSSLDIASFYWtltnndthtqepSAQQGEEVLQQLQALAPRGVKVRIAVSKPNGPL-----ADLQSLLQS 181
Cdd:cd00138   1 EALLELLKNAKESIFIATPNF------------SFNSADRLLKALLAAAERGVDVRLIIDKPPNAAgslsaALLEALLRA 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 58865906 182 GAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVM 232
Cdd:cd00138  69 GVNVRSYVTPPHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
PLDc_2 pfam13091
PLD-like domain;
112-250 1.63e-18

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 81.57  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   112 LLAGAHSSLDIASFYWTLtnndthtqepsaqqGEEVLQQLQALAPRGVKVRIAVSKPNG--------PLADLQSLLQSGA 183
Cdd:pfam13091   4 LINSAKKSIDIATYYFVP--------------DREIIDALIAAAKRGVDVRIILDSNKDdaggpkkaSLKELRSLLRAGV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58865906   184 QVRMVDMQkltHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFEAYW 250
Cdd:pfam13091  70 EIREYQSF---LRSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEFDRLW 132
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 307-436 2.78e-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: 72.16  E-value: 2.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 307 KALLSVVDNARSFIYIAvmnylpTMEFSHprRFWPAIDDGLRRAAyERGVKVRLLISCWGHSEPSMRsfllslAALRDNH 386
Cdd:cd00138   1 EALLELLKNAKESIFIA------TPNFSF--NSADRLLKALLAAA-ERGVDVRLIIDKPPNAAGSLS------AALLEAL 65

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 58865906 387 THSDIQVKLFVVPADeaqaripYARVNHNKYMVTE-RTTYIGTSNWSGSYF 436
Cdd:cd00138  66 LRAGVNVRSYVTPPH-------FFERLHAKVVVIDgEVAYVGSANLSTASA 109
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
 100-247 1.26e-13

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: 69.04  E-value: 1.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 100 TSNPSTSQAWLGLLAGAHSSLDIASFYWTLTnndthtqepsaqqgEEVLQQLQALAPRGVKVRIAVS-KPNGPLADLQS- 177
Cdd:cd09112   7 SDWSSIEQAYLKAINSAKKSIYIQTPYFIPD--------------ESLLEALKTAALSGVDVRIMIPgKPDHKLVYWASr 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58865906 178 -----LLQSGAQVRMvdMQKlthGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFE 247
Cdd:cd09112  73 syfeeLLKAGVKIYE--YNK---GFLHSKTLIVDDEIASVGTANLDIRSFELNFEVNAVIYD-KEVAKKLEEIFE 141
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 306-488 3.96e-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: 64.58  E-value: 3.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 306 LKALLSVVDNARSFIYIAvmnylpTMEFsHPRRFWPAIDDGLRRAAyERGVKVRLLISCWGHSEPSmRSFLLSLAALRdn 385
Cdd:COG1502  27 FAALLEAIEAARRSIDLE------YYIF-DDDEVGRRLADALIAAA-RRGVKVRVLLDGIGSRALN-RDFLRRLRAAG-- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 386 hthsdIQVKLFVvPADEAQARIPyaRVNHNKYMVT-ERTTYIGTSNWSGSYFTETAG------TSLLVTqnghGGLRSQL 458
Cdd:COG1502  96 -----VEVRLFN-PVRLLFRRLN--GRNHRKIVVIdGRVAFVGGANITDEYLGRDPGfgpwrdTHVRIE----GPAVADL 163

                       170       180       190
                ....*....|....*....|....*....|
gi 58865906 459 EAVFLRDWESPYSHNLDTSADSVGNACRLL 488
Cdd:COG1502 164 QAVFAEDWNFATGEALPFPEPAGDVRVQVV 193
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 96-250 9.74e-11

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: 59.60  E-value: 9.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  96 PNATTSNPSTSQAWLGLLAGAHSSLDIasfywtltnndthtQEPSAQQGEEVLQQLQALAPRGVKVRI----AVSKPNGP 171
Cdd:cd09128   2 VQLLLSPDNAREALLALIDSAEESLLI--------------QNEEMGDDAPILDALVDAAKRGVDVRVllpsAWSAEDER 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58865906 172 LADLQSLLQSGAQVRMVDMQKLThgvLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARdLTKIFEAYW 250
Cdd:cd09128  68 QARLRALEGAGVPVRLLKDKFLK---IHAKGIVVDGKTALVGSENWSANSLDRNREVGLIFDDPEVAAY-LQAVFESDW 142
PLDc_2 pfam13091
PLD-like domain;
309-466 6.70e-10

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 56.92  E-value: 6.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   309 LLSVVDNARSFIYIAVMnYLPTMefshprrfwPAIDDGLRRAAyERGVKVRLLISCWGHSEPSM----RSFLLSLAAlrd 384
Cdd:pfam13091   1 LIDLINSAKKSIDIATY-YFVPD---------REIIDALIAAA-KRGVDVRIILDSNKDDAGGPkkasLKELRSLLR--- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   385 nhthSDIQVKLFVvpadeaqariPYARVNHNKYMVT-ERTTYIGTSNWSGSYFTETAGTSLLVTqngHGGLRSQLEAVFL 463
Cdd:pfam13091  67 ----AGVEIREYQ----------SFLRSMHAKFYIIdGKTVIVGSANLTRRALRLNLENNVVIK---DPELAQELEKEFD 129


                  ...
gi 58865906   464 RDW 466
Cdd:pfam13091 130 RLW 132
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 196-221 7.37e-10

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: 53.93  E-value: 7.37e-10
                           10        20
                   ....*....|....*....|....*.
gi 58865906    196 GVLHTKFWVVDQTHFYLGSANMDWRS 221
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 110-247 8.41e-10

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: 57.55  E-value: 8.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 110 LGLLAGAHSSLDIASFYWTltnndthtqePsaqqGEEVLQQLQALAPRGVKVRIAV-SKPNGPLADL------QSLLQSG 182
Cdd:cd09159  17 LVAIAAARRRIWIANAYFV----------P----DRRLRRALIEAARRGVDVRLLLpGKSDDPLTVAasralyGKLLRAG 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58865906 183 AQVRMvdmqkLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYnCSCLARDLTKIFE 247
Cdd:cd09159  83 VRIFE-----YQPSMLHAKTAVIDGDWATVGSSNLDPRSLRLNLEANLVVE-DPAFAAQLEELFE 141
PLDc_Nuc_like_unchar1_1 cd09172
Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, ...
 146-250 2.50e-09

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: 55.82  E-value: 2.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 146 EVLQQLQALAPRGVKVRI------AVSKPNGPLADLQSLLQSGAQVRmvdmQKLTHGVLHTKFWVVDQ----THFYLGSA 215
Cdd:cd09172  36 EIIDALKAAKDRGVRVRIilddssVTGDPTEESAAATLSKGPGALVK----RRHSSGLMHNKFLVVDRkdgpNRVLTGST 111

                        90       100       110
                ....*....|....*....|....*....|....*
gi 58865906 216 NMDWRSLTQVKELGVVMYNcsclaRDLTKIFEAYW 250
Cdd:cd09172 112 NFTTSGLYGQSNNVLIFRN-----PAFAAAYLAYW 141
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 151-265 3.29e-09

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: 56.12  E-value: 3.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 151 LQAL---APRGVKVRIAVSKP-NGPLAD------LQSLLQSGAQVRMvdmqkLTHGVLHTKFWVVDQTHFYLGSANMDWR 220
Cdd:cd09162  41 LRALrlaARRGVDVRLIVPKRsNHRIADlargsyLRDLQEAGAEIYL-----YQPGMLHAKAVVVDDKLALVGSANLDMR 115

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 58865906 221 SLTQVKELGVVMYNcsclARDLTKIFEayWFLGQAGSSIPSTWPR 265
Cdd:cd09162 116 SLFLNYEVAVFFYS----PADIKELSD--WIESLISQCTEGAPPP 154
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 110-250 5.36e-09

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: 54.61  E-value: 5.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 110 LGLLAGAHSSLDIASFywTLTNNdthtqepsaqqgeEVLQQLQALAPRGVKVRIAV----SKPNGPLADLQSLLQSGAQV 185
Cdd:cd09116  15 VALIANAKSSIDVAMY--ALTDP-------------EIAEALKRAAKRGVRVRIILdkdsLADNLSITLLALLSNLGIPV 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58865906 186 RmVDMQKlthGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcsclaRDLTKIFEAYW 250
Cdd:cd09116  80 R-TDSGS---KLMHHKFIIIDGKIVITGSANWTKSGFHRNDENLLIIDD-----PKLAASFEEEF 135
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 112-249 6.76e-09

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: 56.07  E-value: 6.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 112 LLAGAHSSLDIASFYWTLtnndthtqepsaqqGEEVLQQLQALAPRGVKVRI-----------AVSkpngplADLQS--- 177
Cdd:cd09113  25 LLKNAKREVLIVSPYFVP--------------GDEGVALLAELARRGVRVRIltnslaatdvpAVH------SGYARyrk 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 178 -LLQSGAQV-----------RMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVmYNCSCLARDLTKI 245
Cdd:cd09113  85 rLLKAGVELyelkpdaakrkRLRGLFGSSRASLHAKSFVIDDRLVFVGSFNLDPRSAYLNTEMGLV-IDSPELAAQLRAA 163


                ....
gi 58865906 246 FEAY 249
Cdd:cd09113 164 MEED 167
PLDc_SMU_988_like_2 cd09160
Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 ...
 144-247 6.82e-09

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: 55.20  E-value: 6.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 144 GEEVLQQLQALAPRGVKVRI------------AVSKPNGPladlqSLLQSGaqvrmVDMQKLTHGVLHTKFWVVDQTHFY 211
Cdd:cd09160  37 DDEMLDALCLAAKRGVDVRIitphipdkkyvfLVTRSNYP-----ELLEAG-----VKIYEYTPGFIHAKTFVSDDKAAV 106

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 58865906 212 LGSANMDWRSLTQVKELGVVMYNCSCLA---RDLTKIFE 247
Cdd:cd09160 107 VGTINLDYRSLYLHFECGVYMYDTPVISdikEDFEETLA 145
cls PRK01642
cardiolipin synthetase; Reviewed
 60-249 1.49e-08

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 56.71  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   60 WEYGDLHLFGPNQHPAPCYDPCEAVLVESIPEGLEFPNATTSnpstsQAWLGLLAGAHSSLDIASFYWTltnndthtqeP 139
Cdd:PRK01642 279 WETGERILPPPPDVLIMPFEEASGHTVQVIASGPGDPEETIH-----QFLLTAIYSARERLWITTPYFV----------P 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  140 SaqqgEEVLQQLQALAPRGVKVRIAV-SKPNGPLADLQS------LLQSGaqVRMVDMQKlthGVLHTKFWVVDQTHFYL 212
Cdd:PRK01642 344 D----EDLLAALKTAALRGVDVRIIIpSKNDSLLVFWASraffteLLEAG--VKIYRYEG---GLLHTKSVLVDDELALV 414

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 58865906  213 GSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFEAY 249
Cdd:PRK01642 415 GTVNLDMRSFWLNFEITLVIDD-TGFAADLAAMQEDY 450
PLDc_EcCLS_like_2 cd09158
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins; ...
 145-222 3.43e-08

Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins; Catalytic domain, repeat 2, of Escherichia coli cardiolipin (CL) synthase and similar proteins. Escherichia coli CL synthase (EcCLS), specified by the cls gene, is the prototype of this family. EcCLS is a multi-pass membrane protein that catalyzes reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form cardiolipin (CL) and glycerol. The monomer of EcCLS 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. EcCLS 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, EcCLS utilizes 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: 197255 [Multi-domain]  Cd Length: 174  Bit Score: 52.96  E-value: 3.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 145 EEVLQQLQALAPRGVKVRIAVSKPN-GPLADLQS------LLQSGAQVRMvdmqkLTHGVLHTKFWVVDQTHFYLGSANM 217
Cdd:cd09158  38 ESLLQALCTAALRGVEVTLILPAKNdSFLVGAASrsyyeeLLEAGVKIYL-----YRGGLLHAKTVTVDDEVALVGSSNF 112


                ....*
gi 58865906 218 DWRSL 222
Cdd:cd09158 113 DIRSF 117
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 196-221 5.12e-08

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: 48.57  E-value: 5.12e-08
                          10        20
                  ....*....|....*....|....*.
gi 58865906   196 GVLHTKFWVVDQTHFYLGSANMDWRS 221
Cdd:pfam00614   3 GRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_vPLD6_like cd09171
Catalytic domain of vertebrate phospholipase D6 and similar proteins; Catalytic domain of ...
 113-250 1.22e-07

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: 50.69  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 113 LAGAHSSLDIASFywTLTNNDthtqepsaqqgeeVLQQLQALAPRGVKVRIAVS--KPNGPLADLQSLLQSGAQVRMvdm 190
Cdd:cd09171  17 LLSARKSLDVCVF--TITCDD-------------LADAILDLHRRGVRVRIITDddQMEDKGSDIGKLRKAGIPVRT--- 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58865906 191 qKLTHGVLHTKFWVVDQTHFYLGSANmdW-RSLTQV-KELGVVMYNcSCLARDLTKIFEAYW 250
Cdd:cd09171  79 -DLSSGHMHHKFAVIDGKILITGSFN--WtRQAVTGnQENVLITND-PKLVKPFTEEFEKLW 136
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 304-465 1.27e-07

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: 50.72  E-value: 1.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 304 PD--LKALLSVVDNARSFIYIAVmnYlptmEFSHPrrfwpAIDDGLRrAAYERGVKVRLLIscwghsEPSMRSFLLSLAA 381
Cdd:cd09127   6 PDdgVAPVVDAIASAKRSILLKM--Y----EFTDP-----ALEKALA-AAAKRGVRVRVLL------EGGPVGGISRAEK 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 382 LRDNHTHSDIQVKLfvvpaDEAQARIPYarvNHNKYMVT-ERTTYIGTSNWSGSYFTETAGTsLLVTQNGHggLRSQLEA 460
Cdd:cd09127  68 LLDYLNEAGVEVRW-----TNGTARYRY---THAKYIVVdDERALVLTENFKPSGFTGTRGF-GVVTDDPA--VVAEIAD 136


                ....*
gi 58865906 461 VFLRD 465
Cdd:cd09127 137 VFDAD 141
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 110-248 2.33e-07

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: 49.95  E-value: 2.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 110 LGLLAGAHSSLDIASFYWTltnndthtqepsaqqGEEVLQQLQALAPRGVKVRIAV-SKPNGPLADLQS----LLQSGAQ 184
Cdd:cd09127  14 VDAIASAKRSILLKMYEFT---------------DPALEKALAAAAKRGVRVRVLLeGGPVGGISRAEKlldyLNEAGVE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58865906 185 VR-MVDMQKLTHgvLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFEA 248
Cdd:cd09127  79 VRwTNGTARYRY--THAKYIVVDDERALVLTENFKPSGFTGTRGFGVVTDD-PAVVAEIADVFDA 140
PLDc_CLS_unchar2_1 cd09157
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 308-467 1.26e-06

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: 48.33  E-value: 1.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 308 ALLSVVDNARSFIYIA--VMNYLPT-MEFShprrfwpaidDGLRRAAyERGVKVRLLI----SCWghSEPSMRSFLlsla 380
Cdd:cd09157   9 AMLEAIDAARHSIALSsyIFDNDGVgREFV----------DALAEAV-ARGVDVRVLIdgvgARY--SRPSIRRRL---- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 381 alrdnhTHSDIQVKLFVVPAdeAQARIPYARV-NHNKYMVTE-RTTYIGTSNWSGSYFTETAGTSllVTQNGH----GGL 454
Cdd:cd09157  72 ------RRAGVPVARFLPPR--LPPRLPFINLrNHRKILVVDgRTGFTGGMNIRDGHLVADDPKN--PVQDLHfrveGPV 141

                       170
                ....*....|...
gi 58865906 455 RSQLEAVFLRDWE 467
Cdd:cd09157 142 VAQLQEVFAEDWY 154
PLDc_CLS_unchar2_2 cd09163
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 145-248 1.95e-06

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: 197260 [Multi-domain]  Cd Length: 176  Bit Score: 47.93  E-value: 1.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 145 EEVLQQLQALAPRGVKVRIAV-SKPNGPLAD------LQSLLQSGAQVRmvdmqkLTHGVL-HTKFWVVDQTHFYLGSAN 216
Cdd:cd09163  38 RTLITALQAAALRGVEVDIVLpERNNLPLVDwamranLWELLEHGVRIY------LQPPPFdHSKLMVVDGAWALIGSAN 111

                        90       100       110
                ....*....|....*....|....*....|..
gi 58865906 217 MDWRSLTQVKELGVVMYNCScLARDLTKIFEA 248
Cdd:cd09163 112 WDPRSLRLNFELNLEVYDTA-LAGQLDALFDS 142
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 303-466 1.95e-06

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 47.27  E-value: 1.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 303 TPD--LKALLSVVDNARSFIYIavmnYLPTMEFShprrfwPAIDDGLRRAAyERGVKVRLLIScwghSEPSMRSFLLSLA 380
Cdd:cd09128   7 SPDnaREALLALIDSAEESLLI----QNEEMGDD------APILDALVDAA-KRGVDVRVLLP----SAWSAEDERQARL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 381 ALRDNHthsDIQVKLFVVPAdeaqariPYarvNHNKYMV-TERTTYIGTSNWSGSYFTETAGTSLLVTqngHGGLRSQLE 459
Cdd:cd09128  72 RALEGA---GVPVRLLKDKF-------LK---IHAKGIVvDGKTALVGSENWSANSLDRNREVGLIFD---DPEVAAYLQ 135


                ....*..
gi 58865906 460 AVFLRDW 466
Cdd:cd09128 136 AVFESDW 142
bac_cardiolipin TIGR04265
cardiolipin synthase; This model is based on experimentally characterized bacterial ...
 107-249 2.72e-06

cardiolipin synthase; This model is based on experimentally characterized bacterial cardiolipin synthases (cls) from E. coli, Staphylococcus aureus (two), and Bacillus pseudofirmus OF4. This model describes just one of several homologous but non-orthologous forms of cls. The cutoff score is set arbitrarily high to avoid false-positives. Note that there are two enzymatic activites called cardiolipin synthase. This model represents type 1, which does not rely on a CDP-linked donor, but instead does a reversible transfer of a phosphatidyl group from one phosphatidylglycerol molecule to another.


Pssm-ID: 211988 [Multi-domain]  Cd Length: 483  Bit Score: 49.79  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   107 QAWLGLLAGAHSSLDIASFYWTltnndthtqePSaqqgEEVLQQLQALAPRGVKVRIAV-SKPNGPL------ADLQSLL 179
Cdd:TIGR04265 321 YGYLKMIYSAKKSIYIQSPYFI----------PD----DDLLHAIKIAALSGVDVSIMIpNKPDHPLvfwasrSNFTELL 386

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   180 QSGAQVRMVDmqkltHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCScLARDLTKIFEAY 249
Cdd:TIGR04265 387 AAGVKIYQYE-----NGFLHSKSVLVDDEIASVGTANMDMRSFWLNFEVNAFIYDKG-FAKDLAAAYDDD 450
PLDc_PaCLS_like_2 cd09161
Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin synthase and ...
 144-222 3.48e-06

Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin synthase and similar proteins; Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin (CL) synthase (PaCLS) and similar proteins. Although PaCLS and similar proteins have not been functionally characterized, members in 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, PaCLS and other 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: 197258 [Multi-domain]  Cd Length: 176  Bit Score: 47.28  E-value: 3.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 144 GEEVLQQLQALAPRGVKVRIAV-SKPNGPLADLQS------LLQSGAQVrmvdmQKLTHGVLHTKFWVVDQTHFYLGSAN 216
Cdd:cd09161  37 DEGVLAALQLAALRGVDVRILIpERPDHLLVYLASfsylpeLIRAGVKV-----YRYQPGFLHQKVVLVDDELAAVGTAN 111


                ....*.
gi 58865906 217 MDWRSL 222
Cdd:cd09161 112 LDNRSF 117
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 306-434 8.23e-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: 45.36  E-value: 8.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 306 LKALLSVVDNARSFIYIAVmnYlptmEFSHPRrfwpaIDDGLRRAAyERGVKVRLLISCWGHSEPSMRSFLLSLAALRdn 385
Cdd:cd09116  11 ERLIVALIANAKSSIDVAM--Y----ALTDPE-----IAEALKRAA-KRGVRVRIILDKDSLADNLSITLLALLSNLG-- 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 58865906 386 hthsdIQVKLfvvpaDEAQARIpyarvnHNK-YMVTERTTYIGTSNWSGS 434
Cdd:cd09116  77 -----IPVRT-----DSGSKLM------HHKfIIIDGKIVITGSANWTKS 110
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 307-446 3.93e-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: 197229 [Multi-domain]  Cd Length: 143  Bit Score: 43.48  E-value: 3.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 307 KALLSVVDNARSFIYIA--VMNYLPtmefshPRRFWPA-IDDGLRRAAyERGVKVRLL----ISCWGHSEPSMRSFllsl 379
Cdd:cd09131   6 PALLDLINNAKRSIYIAmyMFKYYE------NPGNGVNtLLEALIDAH-KRGVDVKVVledsIDDDEVTEENDNTY---- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58865906 380 AALRDNHthsdIQVKLfvvpaDEAQARIpyarvnHNKYMVT-ERTTYIGTSNWSGSYFTETAGTSLLV 446
Cdd:cd09131  75 RYLKDNG----VEVRF-----DSPSVTT------HTKLVVIdGRTVYVGSHNWTYSALDYNHEASVLI 127
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 347-436 5.80e-05

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: 43.29  E-value: 5.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 347 LRRAAyERGVKVRLLISCWGHSepSMRSFLLSLAAlrdnhtHSDIQVKLF------VVPADEAQARIPyaRVN---HNKY 417
Cdd:cd09111  42 LLEAA-DRGVRVRLLLDDLGTS--GRDRLLAALDA------HPNIEVRLFnpfrnrGGRLLEFLTDFS--RLNrrmHNKL 110

                        90       100
                ....*....|....*....|
gi 58865906 418 MVTERTTYI-GTSNWSGSYF 436
Cdd:cd09111 111 FIVDGAVAIvGGRNIGDEYF 130
PLDc_Nuc cd09170
Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar ...
 303-472 1.40e-04

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: 42.12  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 303 TPD---LKALLSVVDNARSFIYIAVmnYlptmEFSHPRrfwpaIDDGLrRAAYERGVKVRLLIscwghSEPSMRSFLLSL 379
Cdd:cd09170   7 SPEggaRELILDVIDSARRSIDVAA--Y----SFTSPP-----IARAL-IAAKKRGVDVRVVL-----DKSQAGGKYSAL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 380 AALRDNHthsdIQVKLFVVPAdeaqaripyarVNHNKYMVTERTTYIgtsnwSGSY-FTETAGTS----LLVTQNghggl 454
Cdd:cd09170  70 NYLANAG----IPVRIDDNYA-----------IMHNKVMVIDGKTVI-----TGSFnFTASAEKRnaenLLVIRN----- 124

                       170
                ....*....|....*...
gi 58865906 455 RSQLEAVFLRDWESPYSH 472
Cdd:cd09170 125 PPELAQQYLQEWQRRWAQ 142
PLDc_Nuc cd09170
Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar ...
 113-216 2.97e-04

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: 40.96  E-value: 2.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 113 LAGAHSSLDIASFYwtLTNNDthtqepsaqqgeeVLQQLQALAPRGVKVRIAVSKPN--GPLADLQSLLQSGAQVRMVDm 190
Cdd:cd09170  20 IDSARRSIDVAAYS--FTSPP-------------IARALIAAKKRGVDVRVVLDKSQagGKYSALNYLANAGIPVRIDD- 83

                        90       100
                ....*....|....*....|....*.
gi 58865906 191 qklTHGVLHTKFWVVDQTHFYLGSAN 216
Cdd:cd09170  84 ---NYAIMHNKVMVIDGKTVITGSFN 106
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 409-435 4.05e-04

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 37.75  E-value: 4.05e-04
                           10        20
                   ....*....|....*....|....*...
gi 58865906    409 YARVNHNKYMVTE-RTTYIGTSNWSGSY 435
Cdd:smart00155   1 YDGVLHTKLMIVDdEIAYIGSANLDGRS 28
PRK13912 PRK13912
nuclease NucT; Provisional
 306-449 4.11e-04

nuclease NucT; Provisional


Pssm-ID: 184389 [Multi-domain]  Cd Length: 177  Bit Score: 41.30  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906  306 LKALLSVVDNARSFIYIAVMNylptmeFSHPRrfwpaIDDGLRRAAyERGVKVRlLISCWGHSEPSMRSFLLSLAALRDn 385
Cdd:PRK13912  35 LNKLVSLISNARSSIKIAIYS------FTHKD-----IAKALKSAA-KRGVKIS-IIYDYESNHNNDQSTIGYLDKYPN- 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58865906  386 hthsdiqVKLFVVPADEAQARIPYARVNHNKYMVTERTTYIGTSNWSGSYFTETAGTsLLVTQN 449
Cdd:PRK13912 101 -------IKVCLLKGLKAKNGKYYGIMHQKVAIIDDKIVVLGSANWSKNAFENNYEV-LLITDD 156
PLDc_EcCLS_like_1 cd09152
Catalytic domain, repeat 1, of Escherichia coli cardiolipin synthase and similar proteins; ...
 306-467 4.71e-04

Catalytic domain, repeat 1, of Escherichia coli cardiolipin synthase and similar proteins; Catalytic domain, repeat 1, of Escherichia coli cardiolipin (CL) synthase and similar proteins. Escherichia coli CL synthase (EcCLS), specified by the cls gene, is the prototype of this family. EcCLS is a multi-pass membrane protein that catalyzes reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form cardiolipin (CL) and glycerol. The monomer of EcCLS 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. EcCLS 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, EcCLS utilizes 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: 197250 [Multi-domain]  Cd Length: 163  Bit Score: 40.65  E-value: 4.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 306 LKALLSVVDNARSFIYiavmnylptMEFS--HPRRFWPAIDDGLRRAAyERGVKVRLLISCWGhsepSMRSFLLSLAALR 383
Cdd:cd09152  14 IDRLIADIDAAKHHVH---------LLFYiwADDGTGDRVAEALERAA-KRGVTCRLLLDAVG----SRAFFRSSLWKRL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 384 dnhTHSDIQVklfvVPADEAQ-ARIPYARV---NHNKYMVTE-RTTYIGTSN-WSGSYFTETAGT-----SLLVTqnghG 452
Cdd:cd09152  80 ---REAGVEV----VEALPLRlFRRRLARFdlrNHRKIAVIDgRIAYTGSQNiIDPEFFKKAGGGpwvdlMVRVE----G 148

                       170
                ....*....|....*
gi 58865906 453 GLRSQLEAVFLRDWE 467
Cdd:cd09152 149 PVVSQLQAVFASDWY 163
PRK12452 PRK12452
cardiolipin synthase;
99-247 9.21e-04

cardiolipin synthase;


Pssm-ID: 171510 [Multi-domain]  Cd Length: 509  Bit Score: 41.83  E-value: 9.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906   99 TTSNPSTSQAWLGLLAGAHSSLDIASFYWtLTNNDTHTqepsaqqgeevLQQLQALAprGVKVRI-------AVSKPNGP 171
Cdd:PRK12452 339 SSDDKSIRNTLLAVMGSAKKSIWIATPYF-IPDQETLT-----------LLRLSAIS--GIDVRIlypgksdSIISDQAS 404

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865906  172 LADLQSLLQSGAQVrmvdmQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFE 247
Cdd:PRK12452 405 QSYFTPLLKAGASI-----YSYKDGFMHAKIVLVDDKIATIGTANMDVRSFELNYEIISVLYE-SETVHDIKRDFE 474
PLDc_CLS_unchar1_1 cd09156
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 107-251 2.29e-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: 197253 [Multi-domain]  Cd Length: 154  Bit Score: 38.78  E-value: 2.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 107 QAWLGLLAGAHSSLDIASFywTLTNNDThtqepsaqqGEEVLQQLQALAPRGVKVRI---AVSKPNGPLADLQSLLQSGA 183
Cdd:cd09156   8 QALIQLIESAKHSIDVCTF--ILGDDAT---------GRRVIDALARKAREGVEVRLlldALGSFFLSRRALKKLRAAGG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 184 QVR--MVDMQKLTHGVL----HTKFWVVDQTHFYLGSANMD------------WRSLTQVKElgvvmyncSCLARDLTKI 245
Cdd:cd09156  77 KVAffMPVFRLPFRGRTnlrnHRKIAIADGSTAISGGMNLAneymgpepddgrWVDLSFLIE--------GPAVAQYQEV 148


                ....*.
gi 58865906 246 FEAYWF 251
Cdd:cd09156 149 FRSDWA 154
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 108-246 2.70e-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: 38.09  E-value: 2.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 108 AWLGLLAGAHSSLDIASFYWTLTNNDTHtqepsaqQGEEVLQQLQALAPRGVKVRIAVSKPNGPLADLQS-------LLQ 180
Cdd:cd09131   7 ALLDLINNAKRSIYIAMYMFKYYENPGN-------GVNTLLEALIDAHKRGVDVKVVLEDSIDDDEVTEEndntyryLKD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865906 181 SGAQVRmVDMQKLThgvLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMyNCSCLARDLTKIF 246
Cdd:cd09131  80 NGVEVR-FDSPSVT---THTKLVVIDGRTVYVGSHNWTYSALDYNHEASVLI-ESPEVADFAINYF 140
COG3886 COG3886
HKD family nuclease [Replication, recombination and repair];
148-250 2.99e-03

HKD family nuclease [Replication, recombination and repair];


Pssm-ID: 443094 [Multi-domain]  Cd Length: 941  Bit Score: 40.35  E-value: 2.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 148 LQQLQALAPRGVKVRIAVSKPNG---PLAdLQSLLQ-SGAQVRMVDMQKlthGVLHTKFWVVDQTHF---YLGSANMDWR 220
Cdd:COG3886  61 LDALKELLERGVKGRILTSTYLGftePKA-LRELLDlPNIEVRVSYDRK---TRFHAKAYIFERTGYgtaIIGSSNLTRS 136

                        90       100       110
                ....*....|....*....|....*....|..
gi 58865906 221 SLTQVKELGV-VMYNCS-CLARDLTKIFEAYW 250
Cdd:COG3886 137 ALTDNLEWNVkLSSAEDpDLIEKFRAEFESLW 168
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 300-431 3.15e-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: 38.29  E-value: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 300 GGRTPDLKALLSVVDNARSFIYIAvMNYlptmeFSHPRRFwpaiDDGLRRAAyERGVKVRLLIScwGHSEPSM-----RS 374
Cdd:cd09159   7 RRRSSIRRAYLVAIAAARRRIWIA-NAY-----FVPDRRL----RRALIEAA-RRGVDVRLLLP--GKSDDPLtvaasRA 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 58865906 375 FLLSLaaLRDNhthsdiqVKLFvvpadEAQARIPyarvnHNKYMVTERT-TYIGTSNW 431
Cdd:cd09159  74 LYGKL--LRAG-------VRIF-----EYQPSML-----HAKTAVIDGDwATVGSSNL 112
PLDc_unchar4 cd09132
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 107-216 3.27e-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: 197230 [Multi-domain]  Cd Length: 122  Bit Score: 37.64  E-value: 3.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 107 QAWLGLLAGAHSSLDIASFYWTLTnndthtqepsaqqgEEVLQQLQALAPRGVKVRIAV--SKPNGPLADLQSLLQSGAQ 184
Cdd:cd09132   2 QVLLELIEGAERSLLIVGYSAYKV--------------SELLQALAAALERGVQVRVVVesSEKAGSVLSLDEDELMWPK 67

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 58865906 185 VRMVD-------MQKLTHGVLHTKFWVVDQTHFYLGSAN 216
Cdd:cd09132  68 LAGATlyvwpekKRPGKRASLHAKVIVADRRRLLVTSAN 106
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
 199-233 4.58e-03

Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; Catalytic domain, repeat 2, of phospholipase D (PLD, EC 3.1.4.4) found in yeast, plants, and vertebrates, and their bacterial homologs. PLDs are involved in signal transduction, vesicle formation, protein transport, and mitosis by participating in phospholipid metabolism. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both prokaryotic and eukaryotic PLDs have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. PLDs are active as bi-lobed monomers. Each monomer contains two domains, each of which carries one copy of the HKD motif. Two HKD motifs from two domains form a single active site. PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197204 [Multi-domain]  Cd Length: 146  Bit Score: 37.67  E-value: 4.58e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 58865906 199 HTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMY 233
Cdd:cd09105 111 HSKVVIVDDEWATVGSANLNRRSMTWDTELNLAVV 145
PLDc_CLS_unchar1_1 cd09156
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 306-467 8.11e-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: 197253 [Multi-domain]  Cd Length: 154  Bit Score: 36.85  E-value: 8.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 306 LKALLSVVDNARSFIYIAvmnylpTMEFSHpRRFWPAIDDGLRRAAyERGVKVRLLISCWGhsepSMRSFLLSLAALRDN 385
Cdd:cd09156   7 YQALIQLIESAKHSIDVC------TFILGD-DATGRRVIDALARKA-REGVEVRLLLDALG----SFFLSRRALKKLRAA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865906 386 HTHSDIQVKLFVVPadeAQARIPYaRvNHNK-YMVTERTTYIGTSNWSGSYFTETAG----TSLLVTQngHGGLRSQLEA 460
Cdd:cd09156  75 GGKVAFFMPVFRLP---FRGRTNL-R-NHRKiAIADGSTAISGGMNLANEYMGPEPDdgrwVDLSFLI--EGPAVAQYQE 147


                ....*..
gi 58865906 461 VFLRDWE 467
Cdd:cd09156 148 VFRSDWA 154
 
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