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Conserved domains on  [gi|1039777590|ref|XP_017177531|]
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5'-3' exonuclease PLD3 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA02820 super family cl33698
phospholipase-D-like protein; Provisional
 24-435 1.49e-145

phospholipase-D-like protein; Provisional


The actual alignment was detected with superfamily member PHA02820:

Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 421.33  E-value: 1.49e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  24 CYDPCEAVLVESIPEGLEFPNAttsNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDthtqepSAQQGEEVLQQLQALAP 103
Cdd:PHA02820    2 NPDNTIAVITETIPIGMQFDKV---YLSTFNFWREILSNTTKTLDISSFYWSLSDEV------GTNFGTMILNEIIQLPK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 104 RGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCS 183
Cdd:PHA02820   73 RGVRVRIAVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 184 CLARDLTKIFEAYWFLGQagSSIPSTWPRSFDTRYNQETPMEICLNGTPALAYLASAPPPLCPSGRTPDLKALLNVVDSA 263
Cdd:PHA02820  153 NLAADLTQIFEVYWYLGV--NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 264 RSFIYIAVMNYLPTMeFSHPRR--FWPAIDDGLRRAAYERGVKVRLLISCWGHSDPSMRSFLLSLAALhdNHTHSDIQVK 341
Cdd:PHA02820  231 SKFVYVSVMNFIPII-YSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAML--KSKNINIEVK 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 342 LFVVPtdESQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQNGHGGLRSQLEAVFLRDWESPYSHDL 421
Cdd:PHA02820  308 LFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQQLEDIFIRDWNSKYSYEL 385

                         410
                  ....*....|....
gi 1039777590 422 dtSANSVGNACRLL 435
Cdd:PHA02820  386 --YDTSPTKRCRLL 397
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 24-435 1.49e-145

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 421.33  E-value: 1.49e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  24 CYDPCEAVLVESIPEGLEFPNAttsNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDthtqepSAQQGEEVLQQLQALAP 103
Cdd:PHA02820    2 NPDNTIAVITETIPIGMQFDKV---YLSTFNFWREILSNTTKTLDISSFYWSLSDEV------GTNFGTMILNEIIQLPK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 104 RGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCS 183
Cdd:PHA02820   73 RGVRVRIAVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 184 CLARDLTKIFEAYWFLGQagSSIPSTWPRSFDTRYNQETPMEICLNGTPALAYLASAPPPLCPSGRTPDLKALLNVVDSA 263
Cdd:PHA02820  153 NLAADLTQIFEVYWYLGV--NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 264 RSFIYIAVMNYLPTMeFSHPRR--FWPAIDDGLRRAAYERGVKVRLLISCWGHSDPSMRSFLLSLAALhdNHTHSDIQVK 341
Cdd:PHA02820  231 SKFVYVSVMNFIPII-YSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAML--KSKNINIEVK 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 342 LFVVPtdESQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQNGHGGLRSQLEAVFLRDWESPYSHDL 421
Cdd:PHA02820  308 LFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQQLEDIFIRDWNSKYSYEL 385

                         410
                  ....*....|....
gi 1039777590 422 dtSANSVGNACRLL 435
Cdd:PHA02820  386 --YDTSPTKRCRLL 397
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 236-418 7.89e-130

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: 371.99  E-value: 7.89e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 236 YLASAPPPLCPSGRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 315
Cdd:cd09147     1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 316 DPSMRSFLLSLAALHDNHTHSDIQVKLFVVPTDESQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQ 395
Cdd:cd09147    81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVPADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSALVVNQ 160

                         170       180
                  ....*....|....*....|....*.
gi 1039777590 396 NG---HGGLRSQLEAVFLRDWESPYS 418
Cdd:cd09147   161 TGrsaSGTLQSQLQAVFERDWDSPYS 186
PLDc_3 pfam13918
PLD-like domain;
168-346 2.99e-42

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 147.47  E-value: 2.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 168 SLTQVKELGVVMYNCSCLARDLTKIFEAYWFLgQAGSSIPSTWPRSFDTRYNQETPMEICLNGTPALAYLASAPPPLCPS 247
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSL-IFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 248 GRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHSDPSMRSFLLSLA 327
Cdd:pfam13918  80 NRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLD 159

                         170
                  ....*....|....*....
gi 1039777590 328 ALHDNHTHSDIQVKLFVVP 346
Cdd:pfam13918 160 AFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 54-422 7.34e-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: 101.94  E-value: 7.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  54 QAWLGLLAGAHSSLDIASFYWTltnNDthtqepsaQQGEEVLQQLQALAPRGVKVRI---AVSKPNGPLADLQSLLQSGA 130
Cdd:COG1502    28 AALLEAIEAARRSIDLEYYIFD---DD--------EVGRRLADALIAAARRGVKVRVlldGIGSRALNRDFLRRLRAAGV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 131 QVRMVDMQKLT----HGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELG-----VVMYNCSCLArDLTKIFEAYWFLgQ 201
Cdd:COG1502    97 EVRLFNPVRLLfrrlNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpwrdtHVRIEGPAVA-DLQAVFAEDWNF-A 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 202 AGSSIPstWPRSFdtrynqetpmeiclnGTPALAYLASAPpplcPSGRTPDLKALLNVVDSARSFIYIAvmnylpTMEFS 281
Cdd:COG1502   175 TGEALP--FPEPA---------------GDVRVQVVPSGP----DSPRETIERALLAAIASARRRIYIE------TPYFV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 282 HPRRfwpaIDDGLRRAAyERGVKVRLLISCWGHS---DPSMRSFLLSLAALHdnhthsdiqVKLFVvptdesqariPYAR 358
Cdd:COG1502   228 PDRS----LLRALIAAA-RRGVDVRILLPAKSDHplvHWASRSYYEELLEAG---------VRIYE----------YEPG 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777590 359 VNHNKYMVT-ERASYIGTSNWSGSYF---TETAgtsLLVTqngHGGLRSQLEAVFLRDWESPYSHDLD 422
Cdd:COG1502   284 FLHAKVMVVdDEWALVGSANLDPRSLrlnFEVN---LVIY---DPEFAAQLRARFEEDLAHSREVTLE 345
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 143-168 6.59e-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: 6.59e-10
                           10        20
                   ....*....|....*....|....*.
gi 1039777590  143 GVLHTKFWVVDQTHFYLGSANMDWRS 168
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
bac_cardiolipin TIGR04265
cardiolipin synthase; This model is based on experimentally characterized bacterial ...
 54-196 2.24e-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: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  54 QAWLGLLAGAHSSLDIASFYWTltnndthtqePSaqqgEEVLQQLQALAPRGVKVRIAV-SKPNGPL------ADLQSLL 126
Cdd:TIGR04265 321 YGYLKMIYSAKKSIYIQSPYFI----------PD----DDLLHAIKIAALSGVDVSIMIpNKPDHPLvfwasrSNFTELL 386

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 127 QSGAQVRMVDmqkltHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCScLARDLTKIFEAY 196
Cdd:TIGR04265 387 AAGVKIYQYE-----NGFLHSKSVLVDDEIASVGTANMDMRSFWLNFEVNAFIYDKG-FAKDLAAAYDDD 450
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 24-435 1.49e-145

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 421.33  E-value: 1.49e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  24 CYDPCEAVLVESIPEGLEFPNAttsNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDthtqepSAQQGEEVLQQLQALAP 103
Cdd:PHA02820    2 NPDNTIAVITETIPIGMQFDKV---YLSTFNFWREILSNTTKTLDISSFYWSLSDEV------GTNFGTMILNEIIQLPK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 104 RGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCS 183
Cdd:PHA02820   73 RGVRVRIAVNKSNKPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 184 CLARDLTKIFEAYWFLGQagSSIPSTWPRSFDTRYNQETPMEICLNGTPALAYLASAPPPLCPSGRTPDLKALLNVVDSA 263
Cdd:PHA02820  153 NLAADLTQIFEVYWYLGV--NNLPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 264 RSFIYIAVMNYLPTMeFSHPRR--FWPAIDDGLRRAAYERGVKVRLLISCWGHSDPSMRSFLLSLAALhdNHTHSDIQVK 341
Cdd:PHA02820  231 SKFVYVSVMNFIPII-YSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAML--KSKNINIEVK 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 342 LFVVPtdESQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQNGHGGLRSQLEAVFLRDWESPYSHDL 421
Cdd:PHA02820  308 LFIVP--DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPDDGLGLRQQLEDIFIRDWNSKYSYEL 385

                         410
                  ....*....|....
gi 1039777590 422 dtSANSVGNACRLL 435
Cdd:PHA02820  386 --YDTSPTKRCRLL 397
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 236-418 7.89e-130

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: 371.99  E-value: 7.89e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 236 YLASAPPPLCPSGRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 315
Cdd:cd09147     1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 316 DPSMRSFLLSLAALHDNHTHSDIQVKLFVVPTDESQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQ 395
Cdd:cd09147    81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVPADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSALVVNQ 160

                         170       180
                  ....*....|....*....|....*.
gi 1039777590 396 NG---HGGLRSQLEAVFLRDWESPYS 418
Cdd:cd09147   161 TGrsaSGTLQSQLQAVFERDWDSPYS 186
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 31-200 7.28e-117

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: 338.85  E-value: 7.28e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  31 VLVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLQQLQALAPRGVKVRI 110
Cdd:cd09144     1 VLVESIPEGLVFNSSSTINPSIYQAWLNLISAAQSSLDIASFYWTLTNSDTHTQEPSANQGEQILKKLGQLSQSGVYVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 111 AVSKPNGP--LADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARD 188
Cdd:cd09144    81 AVDKPADPkpMEDINALSSYGADVRMVDMRKLTTGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVYNCSCLAED 160

                         170
                  ....*....|..
gi 1039777590 189 LTKIFEAYWFLG 200
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 ...
 236-413 2.32e-97

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: 289.15  E-value: 2.32e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 236 YLASAPPPLCPSGRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 315
Cdd:cd09107     1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 316 DPSMRSFLLSLAALHDNHTHSDIQVKLFVVPTDESQaRIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQ 395
Cdd:cd09107    81 DPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQST-KIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVSLVIND 159

                         170
                  ....*....|....*...
gi 1039777590 396 NghgGLRSQLEAVFLRDW 413
Cdd:cd09107   160 P---AIVQQLKDVFERDW 174
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 236-418 9.15e-84

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: 254.77  E-value: 9.15e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 236 YLASAPPPLCPSGRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 315
Cdd:cd09148     1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 316 DPSMRSFLLSLAALHDNHTHSDIQVKLFVVPTDEsQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQ 395
Cdd:cd09148    81 DPDMFPFLRSLNALSNPPLSISVHVKLFIVPVGN-QTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVGLVILQ 159

                         170       180
                  ....*....|....*....|....*...
gi 1039777590 396 N-GHGG----LRSQLEAVFLRDWESPYS 418
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 ...
 32-182 2.14e-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: 224.43  E-value: 2.14e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  32 LVESIPEGLEFPNaTTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTqEPSAQQGEEVLQQLQALAPRGVKVRIA 111
Cdd:cd09106     1 LVESIPEGLTFLS-SSSHLSTFEAWMELISSAKKSIDIASFYWNLRGTDTNP-DSSAQEGEDIFNALLEAAKRGVKIRIL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777590 112 VSKPNGPLA---DLQSLLQSGAQVRMVDMQKL-THGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNC 182
Cdd:cd09106    79 QDKPSKDKPdedDLELAALGGAEVRSLDFTKLiGGGVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 32-199 2.82e-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: 206.68  E-value: 2.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  32 LVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLQQLQALAPRGVKVRIA 111
Cdd:cd09145     1 LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWSLTGEDIGVNDSSSLPGEDILKELAELLSRNVSVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 112 VSKPNGPL--ADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDL 189
Cdd:cd09145    81 ASIPTLAAnsTDLKILRQKGAHVRKVNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAKDL 160

                         170
                  ....*....|
gi 1039777590 190 TKIFEAYWFL 199
Cdd:cd09145   161 HKTFQTYWVL 170
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 32-422 4.17e-54

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 184.48  E-value: 4.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  32 LVESIPEGLEFpnaTTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDthtqepsaqQGEEVLQQLQALAPRGVKVRIA 111
Cdd:PHA03003   15 IVETLPKSLGI---ATQHMSTYECFDEIISQAKKYIYIASFCCNLRSTP---------EGRLILDKLKEAAESGVKVTIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 112 VSKPNGPlADLQSLLQSGAQVRMVDMQKLTH-GVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVvmYN-CSCLARDL 189
Cdd:PHA03003   83 VDEQSGD-KDEEELQSSNINYIKVDIGKLNNvGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLGV--YStYPPLATDL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 190 TKIFEAYWFLGQAGS-----SIPSTWPRSfdTRYNQETPMEIClngtpalaYLASAPPPLCPSGRTPDLKALLNVVDSAR 264
Cdd:PHA03003  160 RRRFDTFKAFNKNKSvfnrlCCACCLPVS--TKYHINNPIGGV--------FFSDSPEHLLGYSRTLDADVVLHKIKSAK 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 265 SFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHSDPSMRSFLLSLAALHDNHthsDIQVKLFV 344
Cdd:PHA03003  230 KSIDLELLSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALCVGN---DLSVKVFR 306

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777590 345 VPtdesqaripyarvNHNKYM-VTERASYIGTSNWSGSYFTETAGTSLlvtQNGHGGLRSQLEAVFLRDWESPYSHDLD 422
Cdd:PHA03003  307 IP-------------NNTKLLiVDDEFAHITSANFDGTHYLHHAFVSF---NTIDKELVKELSAIFERDWTSSYSKPLK 369
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 236-421 3.98e-51

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: 170.80  E-value: 3.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 236 YLASAPPPLCPSGRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHS 315
Cdd:cd09149     1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 316 DPSMRSFLLSLAALHDNHTHSDIQVKLFvvpTDESQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQ 395
Cdd:cd09149    81 DPLTFNFVSSLKSLCTEQANCSLEVKFF---DLEEESDCTSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVGLVINQ 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039777590 396 -----NGHGGLRSQLEAVFLRDWESPYSHDL 421
Cdd:cd09149   158 adgveENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 31-199 2.82e-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: 157.33  E-value: 2.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  31 VLVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLtnNDTHtqePSAQQGEEVLQQLQALAPRGVKVRI 110
Cdd:cd09146     1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLWDL--NASH---PSACQGQRLFERLLGLASRGVELKI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 111 aVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDLT 190
Cdd:cd09146    76 -VSGITDSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALDLH 154


                  ....*....
gi 1039777590 191 KIFEAYWFL 199
Cdd:cd09146   155 RVFALYWSL 163
PLDc_3 pfam13918
PLD-like domain;
168-346 2.99e-42

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 147.47  E-value: 2.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 168 SLTQVKELGVVMYNCSCLARDLTKIFEAYWFLgQAGSSIPSTWPRSFDTRYNQETPMEICLNGTPALAYLASAPPPLCPS 247
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSL-IFENKVPFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 248 GRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHSDPSMRSFLLSLA 327
Cdd:pfam13918  80 NRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLD 159

                         170
                  ....*....|....*....
gi 1039777590 328 ALHDNHTHSDIQVKLFVVP 346
Cdd:pfam13918 160 AFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 54-422 7.34e-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: 101.94  E-value: 7.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  54 QAWLGLLAGAHSSLDIASFYWTltnNDthtqepsaQQGEEVLQQLQALAPRGVKVRI---AVSKPNGPLADLQSLLQSGA 130
Cdd:COG1502    28 AALLEAIEAARRSIDLEYYIFD---DD--------EVGRRLADALIAAARRGVKVRVlldGIGSRALNRDFLRRLRAAGV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 131 QVRMVDMQKLT----HGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELG-----VVMYNCSCLArDLTKIFEAYWFLgQ 201
Cdd:COG1502    97 EVRLFNPVRLLfrrlNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpwrdtHVRIEGPAVA-DLQAVFAEDWNF-A 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 202 AGSSIPstWPRSFdtrynqetpmeiclnGTPALAYLASAPpplcPSGRTPDLKALLNVVDSARSFIYIAvmnylpTMEFS 281
Cdd:COG1502   175 TGEALP--FPEPA---------------GDVRVQVVPSGP----DSPRETIERALLAAIASARRRIYIE------TPYFV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 282 HPRRfwpaIDDGLRRAAyERGVKVRLLISCWGHS---DPSMRSFLLSLAALHdnhthsdiqVKLFVvptdesqariPYAR 358
Cdd:COG1502   228 PDRS----LLRALIAAA-RRGVDVRILLPAKSDHplvHWASRSYYEELLEAG---------VRIYE----------YEPG 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777590 359 VNHNKYMVT-ERASYIGTSNWSGSYF---TETAgtsLLVTqngHGGLRSQLEAVFLRDWESPYSHDLD 422
Cdd:COG1502   284 FLHAKVMVVdDEWALVGSANLDPRSLrlnFEVN---LVIY---DPEFAAQLRARFEEDLAHSREVTLE 345
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 54-179 1.00e-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: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  54 QAWLGLLAGAHSSLDIASFYWtltnndthtqepSAQQGEEVLQQLQALAPRGVKVRIAVSKPNGPL-----ADLQSLLQS 128
Cdd:cd00138     1 EALLELLKNAKESIFIATPNF------------SFNSADRLLKALLAAAERGVDVRLIIDKPPNAAgslsaALLEALLRA 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039777590 129 GAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVM 179
Cdd:cd00138    69 GVNVRSYVTPPHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
PLDc_2 pfam13091
PLD-like domain;
59-197 1.30e-18

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 81.57  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  59 LLAGAHSSLDIASFYWTLtnndthtqepsaqqGEEVLQQLQALAPRGVKVRIAVSKPNG--------PLADLQSLLQSGA 130
Cdd:pfam13091   4 LINSAKKSIDIATYYFVP--------------DREIIDALIAAAKRGVDVRIILDSNKDdaggpkkaSLKELRSLLRAGV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039777590 131 QVRMVDMQkltHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFEAYW 197
Cdd:pfam13091  70 EIREYQSF---LRSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEFDRLW 132
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
 47-194 1.07e-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: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  47 TSNPSTSQAWLGLLAGAHSSLDIASFYWTLTnndthtqepsaqqgEEVLQQLQALAPRGVKVRIAVS-KPNGPLADLQS- 124
Cdd:cd09112     7 SDWSSIEQAYLKAINSAKKSIYIQTPYFIPD--------------ESLLEALKTAALSGVDVRIMIPgKPDHKLVYWASr 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777590 125 -----LLQSGAQVRMvdMQKlthGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFE 194
Cdd:cd09112    73 syfeeLLKAGVKIYE--YNK---GFLHSKTLIVDDEIASVGTANLDIRSFELNFEVNAVIYD-KEVAKKLEEIFE 141
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 254-383 1.95e-13

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: 66.77  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 254 KALLNVVDSARSFIYIAvmnylpTMEFSHprRFWPAIDDGLRRAAyERGVKVRLLISCWGHSDPSMRSFLLSLAalhdnh 333
Cdd:cd00138     1 EALLELLKNAKESIFIA------TPNFSF--NSADRLLKALLAAA-ERGVDVRLIIDKPPNAAGSLSAALLEAL------ 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039777590 334 THSDIQVKLFVvptdesqARIPYARVNHNKYMVTERAS-YIGTSNWSGSYF 383
Cdd:cd00138    66 LRAGVNVRSYV-------TPPHFFERLHAKVVVIDGEVaYVGSANLSTASA 109
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 253-435 7.47e-11

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


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 63.42  E-value: 7.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 253 LKALLNVVDSARSFIYIAvmnylpTMEFsHPRRFWPAIDDGLRRAAyERGVKVRLLISCWGHSDPSmRSFLLSLAAlhdn 332
Cdd:COG1502    27 FAALLEAIEAARRSIDLE------YYIF-DDDEVGRRLADALIAAA-RRGVKVRVLLDGIGSRALN-RDFLRRLRA---- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 333 hthSDIQVKLFVvPTDESQARIPyaRVNHNKYMVT-ERASYIGTSNWSGSYFTETAG------TSLLVTqnghGGLRSQL 405
Cdd:COG1502    94 ---AGVEVRLFN-PVRLLFRRLN--GRNHRKIVVIdGRVAFVGGANITDEYLGRDPGfgpwrdTHVRIE----GPAVADL 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039777590 406 EAVFLRDWESPYSHDLDTSANSVGNACRLL 435
Cdd:COG1502   164 QAVFAEDWNFATGEALPFPEPAGDVRVQVV 193
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 43-197 8.45e-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: 8.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  43 PNATTSNPSTSQAWLGLLAGAHSSLDIasfywtltnndthtQEPSAQQGEEVLQQLQALAPRGVKVRI----AVSKPNGP 118
Cdd:cd09128     2 VQLLLSPDNAREALLALIDSAEESLLI--------------QNEEMGDDAPILDALVDAAKRGVDVRVllpsAWSAEDER 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777590 119 LADLQSLLQSGAQVRMVDMQKLThgvLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARdLTKIFEAYW 197
Cdd:cd09128    68 QARLRALEGAGVPVRLLKDKFLK---IHAKGIVVDGKTALVGSENWSANSLDRNREVGLIFDDPEVAAY-LQAVFESDW 142
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 143-168 6.59e-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: 6.59e-10
                           10        20
                   ....*....|....*....|....*.
gi 1039777590  143 GVLHTKFWVVDQTHFYLGSANMDWRS 168
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 98-214 8.05e-10

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: 57.66  E-value: 8.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  98 LQAL---APRGVKVRIAVSKP-NGPLAD------LQSLLQSGAQVRMvdmqkLTHGVLHTKFWVVDQTHFYLGSANMDWR 167
Cdd:cd09162    41 LRALrlaARRGVDVRLIVPKRsNHRIADlargsyLRDLQEAGAEIYL-----YQPGMLHAKAVVVDDKLALVGSANLDMR 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039777590 168 SLTQVKELGVVMYNcsclARDLTKIFEayWFLGQAGSSIPSTWPRSF 214
Cdd:cd09162   116 SLFLNYEVAVFFYS----PADIKELSD--WIESLISQCTEGAPPPSA 156
PLDc_2 pfam13091
PLD-like domain;
256-413 9.47e-10

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 56.53  E-value: 9.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 256 LLNVVDSARSFIYIAVMnYLPTMefshprrfwPAIDDGLRRAAyERGVKVRLLISCWGHSDPSM----RSFLLSLAAlhd 331
Cdd:pfam13091   1 LIDLINSAKKSIDIATY-YFVPD---------REIIDALIAAA-KRGVDVRIILDSNKDDAGGPkkasLKELRSLLR--- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 332 nhthSDIQVKLFVvptdesqariPYARVNHNKYMVT-ERASYIGTSNWSGSYFTETAGTSLLVTqngHGGLRSQLEAVFL 410
Cdd:pfam13091  67 ----AGVEIREYQ----------SFLRSMHAKFYIIdGKTVIVGSANLTRRALRLNLENNVVIK---DPELAQELEKEFD 129


                  ...
gi 1039777590 411 RDW 413
Cdd:pfam13091 130 RLW 132
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 57-194 1.09e-09

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: 57.16  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  57 LGLLAGAHSSLDIASFYWTltnndthtqePsaqqGEEVLQQLQALAPRGVKVRIAV-SKPNGPLADL------QSLLQSG 129
Cdd:cd09159    17 LVAIAAARRRIWIANAYFV----------P----DRRLRRALIEAARRGVDVRLLLpGKSDDPLTVAasralyGKLLRAG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777590 130 AQVRMvdmqkLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYnCSCLARDLTKIFE 194
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, ...
 93-197 2.17e-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: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  93 EVLQQLQALAPRGVKVRI------AVSKPNGPLADLQSLLQSGAQVRmvdmQKLTHGVLHTKFWVVDQ----THFYLGSA 162
Cdd:cd09172    36 EIIDALKAAKDRGVRVRIilddssVTGDPTEESAAATLSKGPGALVK----RRHSSGLMHNKFLVVDRkdgpNRVLTGST 111

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039777590 163 NMDWRSLTQVKELGVVMYNcsclaRDLTKIFEAYW 197
Cdd:cd09172   112 NFTTSGLYGQSNNVLIFRN-----PAFAAAYLAYW 141
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 57-197 4.67e-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: 4.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  57 LGLLAGAHSSLDIASFywTLTNNdthtqepsaqqgeEVLQQLQALAPRGVKVRIAV----SKPNGPLADLQSLLQSGAQV 132
Cdd:cd09116    15 VALIANAKSSIDVAMY--ALTDP-------------EIAEALKRAAKRGVRVRIILdkdsLADNLSITLLALLSNLGIPV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777590 133 RmVDMQKlthGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcsclaRDLTKIFEAYW 197
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 ...
 59-196 5.69e-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: 5.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  59 LLAGAHSSLDIASFYWTLtnndthtqepsaqqGEEVLQQLQALAPRGVKVRI-----------AVSkpngplADLQS--- 124
Cdd:cd09113    25 LLKNAKREVLIVSPYFVP--------------GDEGVALLAELARRGVRVRIltnslaatdvpAVH------SGYARyrk 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 125 -LLQSGAQV-----------RMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVmYNCSCLARDLTKI 192
Cdd:cd09113    85 rLLKAGVELyelkpdaakrkRLRGLFGSSRASLHAKSFVIDDRLVFVGSFNLDPRSAYLNTEMGLV-IDSPELAAQLRAA 163


                  ....
gi 1039777590 193 FEAY 196
Cdd:cd09113   164 MEED 167
PLDc_SMU_988_like_2 cd09160
Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 ...
 91-194 5.87e-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: 5.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  91 GEEVLQQLQALAPRGVKVRI------------AVSKPNGPladlqSLLQSGaqvrmVDMQKLTHGVLHTKFWVVDQTHFY 158
Cdd:cd09160    37 DDEMLDALCLAAKRGVDVRIitphipdkkyvfLVTRSNYP-----ELLEAG-----VKIYEYTPGFIHAKTFVSDDKAAV 106

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1039777590 159 LGSANMDWRSLTQVKELGVVMYNCSCLA---RDLTKIFE 194
Cdd:cd09160   107 VGTINLDYRSLYLHFECGVYMYDTPVISdikEDFEETLA 145
cls PRK01642
cardiolipin synthetase; Reviewed
 7-196 9.05e-09

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 57.10  E-value: 9.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590   7 WEYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLEFPNATTSnpstsQAWLGLLAGAHSSLDIASFYWTltnndthtqeP 86
Cdd:PRK01642  279 WETGERILPPPPDVLIMPFEEASGHTVQVIASGPGDPEETIH-----QFLLTAIYSARERLWITTPYFV----------P 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  87 SaqqgEEVLQQLQALAPRGVKVRIAV-SKPNGPLADLQS------LLQSGaqVRMVDMQKlthGVLHTKFWVVDQTHFYL 159
Cdd:PRK01642  344 D----EDLLAALKTAALRGVDVRIIIpSKNDSLLVFWASraffteLLEAG--VKIYRYEG---GLLHTKSVLVDDELALV 414

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039777590 160 GSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFEAY 196
Cdd:PRK01642  415 GTVNLDMRSFWLNFEITLVIDD-TGFAADLAAMQEDY 450
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 251-412 4.11e-08

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: 51.88  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 251 PD--LKALLNVVDSARSFIYIAVmnYlptmEFSHPrrfwpAIDDGLRrAAYERGVKVRLLIscwghsDPSMRSFLLSLAA 328
Cdd:cd09127     6 PDdgVAPVVDAIASAKRSILLKM--Y----EFTDP-----ALEKALA-AAAKRGVRVRVLL------EGGPVGGISRAEK 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 329 LHDNHTHSDIQVKLfvvptDESQARIPYarvNHNKYMVT-ERASYIGTSNWSGSYFTETAGTsLLVTQNGHggLRSQLEA 407
Cdd:cd09127    68 LLDYLNEAGVEVRW-----TNGTARYRY---THAKYIVVdDERALVLTENFKPSGFTGTRGF-GVVTDDPA--VVAEIAD 136


                  ....*
gi 1039777590 408 VFLRD 412
Cdd:cd09127   137 VFDAD 141
PLDc_EcCLS_like_2 cd09158
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins; ...
 92-169 4.41e-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: 52.58  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  92 EEVLQQLQALAPRGVKVRIAVSKPN-GPLADLQS------LLQSGAQVRMvdmqkLTHGVLHTKFWVVDQTHFYLGSANM 164
Cdd:cd09158    38 ESLLQALCTAALRGVEVTLILPAKNdSFLVGAASrsyyeeLLEAGVKIYL-----YRGGLLHAKTVTVDDEVALVGSSNF 112


                  ....*
gi 1039777590 165 DWRSL 169
Cdd:cd09158   113 DIRSF 117
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 143-168 4.58e-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: 4.58e-08
                          10        20
                  ....*....|....*....|....*.
gi 1039777590 143 GVLHTKFWVVDQTHFYLGSANMDWRS 168
Cdd:pfam00614   3 GRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_vPLD6_like cd09171
Catalytic domain of vertebrate phospholipase D6 and similar proteins; Catalytic domain of ...
 60-197 1.06e-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: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  60 LAGAHSSLDIASFywTLTNNDthtqepsaqqgeeVLQQLQALAPRGVKVRIAVS--KPNGPLADLQSLLQSGAQVRMvdm 137
Cdd:cd09171    17 LLSARKSLDVCVF--TITCDD-------------LADAILDLHRRGVRVRIITDddQMEDKGSDIGKLRKAGIPVRT--- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039777590 138 qKLTHGVLHTKFWVVDQTHFYLGSANmdW-RSLTQV-KELGVVMYNcSCLARDLTKIFEAYW 197
Cdd:cd09171    79 -DLSSGHMHHKFAVIDGKILITGSFN--WtRQAVTGnQENVLITND-PKLVKPFTEEFEKLW 136
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 57-195 2.03e-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: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  57 LGLLAGAHSSLDIASFYWTltnndthtqepsaqqGEEVLQQLQALAPRGVKVRIAV-SKPNGPLADLQS----LLQSGAQ 131
Cdd:cd09127    14 VDAIASAKRSILLKMYEFT---------------DPALEKALAAAAKRGVRVRVLLeGGPVGGISRAEKlldyLNEAGVE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777590 132 VR-MVDMQKLTHgvLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFEA 195
Cdd:cd09127    79 VRwTNGTARYRY--THAKYIVVDDERALVLTENFKPSGFTGTRGFGVVTDD-PAVVAEIADVFDA 140
PLDc_CLS_unchar2_2 cd09163
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 92-195 1.78e-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: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  92 EEVLQQLQALAPRGVKVRIAV-SKPNGPLAD------LQSLLQSGAQVRmvdmqkLTHGVL-HTKFWVVDQTHFYLGSAN 163
Cdd:cd09163    38 RTLITALQAAALRGVEVDIVLpERNNLPLVDwamranLWELLEHGVRIY------LQPPPFdHSKLMVVDGAWALIGSAN 111

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039777590 164 MDWRSLTQVKELGVVMYNCScLARDLTKIFEA 195
Cdd:cd09163   112 WDPRSLRLNFELNLEVYDTA-LAGQLDALFDS 142
bac_cardiolipin TIGR04265
cardiolipin synthase; This model is based on experimentally characterized bacterial ...
 54-196 2.24e-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: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  54 QAWLGLLAGAHSSLDIASFYWTltnndthtqePSaqqgEEVLQQLQALAPRGVKVRIAV-SKPNGPL------ADLQSLL 126
Cdd:TIGR04265 321 YGYLKMIYSAKKSIYIQSPYFI----------PD----DDLLHAIKIAALSGVDVSIMIpNKPDHPLvfwasrSNFTELL 386

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 127 QSGAQVRMVDmqkltHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCScLARDLTKIFEAY 196
Cdd:TIGR04265 387 AAGVKIYQYE-----NGFLHSKSVLVDDEIASVGTANMDMRSFWLNFEVNAFIYDKG-FAKDLAAAYDDD 450
PLDc_PaCLS_like_2 cd09161
Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin synthase and ...
 91-169 3.00e-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: 3.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  91 GEEVLQQLQALAPRGVKVRIAV-SKPNGPLADLQS------LLQSGAQVrmvdmQKLTHGVLHTKFWVVDQTHFYLGSAN 163
Cdd:cd09161    37 DEGVLAALQLAALRGVDVRILIpERPDHLLVYLASfsylpeLIRAGVKV-----YRYQPGFLHQKVVLVDDELAAVGTAN 111


                  ....*.
gi 1039777590 164 MDWRSL 169
Cdd:cd09161   112 LDNRSF 117
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 294-383 7.05e-06

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: 45.99  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 294 LRRAAyERGVKVRLLISCWGHSdpSMRSFLLSLAAlHDNhthsdIQVKLF------VVPTDESQARIPyaRVN---HNKY 364
Cdd:cd09111    42 LLEAA-DRGVRVRLLLDDLGTS--GRDRLLAALDA-HPN-----IEVRLFnpfrnrGGRLLEFLTDFS--RLNrrmHNKL 110

                          90       100
                  ....*....|....*....|
gi 1039777590 365 M-VTERASYIGTSNWSGSYF 383
Cdd:cd09111   111 FiVDGAVAIVGGRNIGDEYF 130
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 250-413 8.21e-06

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 45.34  E-value: 8.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 250 TPD--LKALLNVVDSARSFIYIavmnYLPTMEFShprrfwPAIDDGLRRAAyERGVKVRLLIScwgHSDPSMRSFLLSLA 327
Cdd:cd09128     7 SPDnaREALLALIDSAEESLLI----QNEEMGDD------APILDALVDAA-KRGVDVRVLLP---SAWSAEDERQARLR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 328 ALHDnhthSDIQVKLFVVPTdesqariPYarvNHNKYMV-TERASYIGTSNWSGSYFTETAGTSLLVTqngHGGLRSQLE 406
Cdd:cd09128    73 ALEG----AGVPVRLLKDKF-------LK---IHAKGIVvDGKTALVGSENWSANSLDRNREVGLIFD---DPEVAAYLQ 135


                  ....*..
gi 1039777590 407 AVFLRDW 413
Cdd:cd09128   136 AVFESDW 142
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 253-381 1.07e-05

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: 44.98  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 253 LKALLNVVDSARSFIYIAVmnYlptmEFSHPRrfwpaIDDGLRRAAyERGVKVRLLISCWGHSDPSMRSFLLSLAALHdn 332
Cdd:cd09116    11 ERLIVALIANAKSSIDVAM--Y----ALTDPE-----IAEALKRAA-KRGVRVRIILDKDSLADNLSITLLALLSNLG-- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039777590 333 hthsdIQVKlfvvpTDESQARIpyarvnHNK-YMVTERASYIGTSNWSGS 381
Cdd:cd09116    77 -----IPVR-----TDSGSKLM------HHKfIIIDGKIVITGSANWTKS 110
PLDc_CLS_unchar2_1 cd09157
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 255-414 1.31e-05

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: 44.86  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 255 ALLNVVDSARSFIYIA--VMNYLPT-MEFShprrfwpaidDGLRRAAyERGVKVRLLI----SCWghSDPSMRSFLlsla 327
Cdd:cd09157     9 AMLEAIDAARHSIALSsyIFDNDGVgREFV----------DALAEAV-ARGVDVRVLIdgvgARY--SRPSIRRRL---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 328 alhdnhTHSDIQVKLFVVPTdeSQARIPYARV-NHNKYMVTE-RASYIGTSNWSGSYFTETAGTSllVTQNGH----GGL 401
Cdd:cd09157    72 ------RRAGVPVARFLPPR--LPPRLPFINLrNHRKILVVDgRTGFTGGMNIRDGHLVADDPKN--PVQDLHfrveGPV 141

                         170
                  ....*....|...
gi 1039777590 402 RSQLEAVFLRDWE 414
Cdd:cd09157   142 VAQLQEVFAEDWY 154
PLDc_Nuc cd09170
Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar ...
 250-419 9.39e-05

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


Pssm-ID: 197267 [Multi-domain]  Cd Length: 142  Bit Score: 42.12  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 250 TPD---LKALLNVVDSARSFIYIAVmnYlptmEFSHPRrfwpaIDDGLrRAAYERGVKVRLLIscwghsdpsmrsfllsl 326
Cdd:cd09170     7 SPEggaRELILDVIDSARRSIDVAA--Y----SFTSPP-----IARAL-IAAKKRGVDVRVVL----------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 327 aalhdnhthsdiqvklfvvptDESQARIPYARVN------------------HNKYMVTERASYIgtsnwSGSY-FTETA 387
Cdd:cd09170    58 ---------------------DKSQAGGKYSALNylanagipvriddnyaimHNKVMVIDGKTVI-----TGSFnFTASA 111

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039777590 388 GTS----LLVTQNghgglRSQLEAVFLRDWESPYSH 419
Cdd:cd09170   112 EKRnaenLLVIRN-----PPELAQQYLQEWQRRWAQ 142
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 247-378 1.29e-04

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: 42.53  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 247 SGRTPDLKALLNVVDSARSFIYIAvMNYlptmeFSHPRRFwpaiDDGLRRAAyERGVKVRLLIScwGHSDPSM-----RS 321
Cdd:cd09159     7 RRRSSIRRAYLVAIAAARRRIWIA-NAY-----FVPDRRL----RRALIEAA-RRGVDVRLLLP--GKSDDPLtvaasRA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777590 322 FLLSLaaLHDNhthsdiqVKLFvvptdESQARIPyarvnHNKYMVT-ERASYIGTSNW 378
Cdd:cd09159    74 LYGKL--LRAG-------VRIF-----EYQPSML-----HAKTAVIdGDWATVGSSNL 112
PLDc_Nuc cd09170
Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar ...
 60-163 2.59e-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: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  60 LAGAHSSLDIASFYwtLTNNDthtqepsaqqgeeVLQQLQALAPRGVKVRIAVSKPN--GPLADLQSLLQSGAQVRMVDm 137
Cdd:cd09170    20 IDSARRSIDVAAYS--FTSPP-------------IARALIAAKKRGVDVRVVLDKSQagGKYSALNYLANAGIPVRIDD- 83

                          90       100
                  ....*....|....*....|....*.
gi 1039777590 138 qklTHGVLHTKFWVVDQTHFYLGSAN 163
Cdd:cd09170    84 ---NYAIMHNKVMVIDGKTVITGSFN 106
PRK12452 PRK12452
cardiolipin synthase;
46-194 8.63e-04

cardiolipin synthase;


Pssm-ID: 171510 [Multi-domain]  Cd Length: 509  Bit Score: 41.44  E-value: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  46 TTSNPSTSQAWLGLLAGAHSSLDIASFYWtLTNNDTHTqepsaqqgeevLQQLQALAprGVKVRI-------AVSKPNGP 118
Cdd:PRK12452  339 SSDDKSIRNTLLAVMGSAKKSIWIATPYF-IPDQETLT-----------LLRLSAIS--GIDVRIlypgksdSIISDQAS 404

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777590 119 LADLQSLLQSGAQVrmvdmQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNcSCLARDLTKIFE 194
Cdd:PRK12452  405 QSYFTPLLKAGASI-----YSYKDGFMHAKIVLVDDKIATIGTANMDVRSFELNYEIISVLYE-SETVHDIKRDFE 474
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 356-382 1.46e-03

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 35.83  E-value: 1.46e-03
                           10        20
                   ....*....|....*....|....*...
gi 1039777590  356 YARVNHNKYMVTE-RASYIGTSNWSGSY 382
Cdd:smart00155   1 YDGVLHTKLMIVDdEIAYIGSANLDGRS 28
PLDc_CLS_unchar1_1 cd09156
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 54-198 1.99e-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: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  54 QAWLGLLAGAHSSLDIASFywTLTNNDThtqepsaqqGEEVLQQLQALAPRGVKVRI---AVSKPNGPLADLQSLLQSGA 130
Cdd:cd09156     8 QALIQLIESAKHSIDVCTF--ILGDDAT---------GRRVIDALARKAREGVEVRLlldALGSFFLSRRALKKLRAAGG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 131 QVR--MVDMQKLTHGVL----HTKFWVVDQTHFYLGSANMD------------WRSLTQVKElgvvmyncSCLARDLTKI 192
Cdd:cd09156    77 KVAffMPVFRLPFRGRTnlrnHRKIAIADGSTAISGGMNLAneymgpepddgrWVDLSFLIE--------GPAVAQYQEV 148


                  ....*.
gi 1039777590 193 FEAYWF 198
Cdd:cd09156   149 FRSDWA 154
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 55-193 2.35e-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: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  55 AWLGLLAGAHSSLDIASFYWTLTNNDTHtqepsaqQGEEVLQQLQALAPRGVKVRIAVSKPNGPLADLQS-------LLQ 127
Cdd:cd09131     7 ALLDLINNAKRSIYIAMYMFKYYENPGN-------GVNTLLEALIDAHKRGVDVKVVLEDSIDDDEVTEEndntyryLKD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777590 128 SGAQVRmVDMQKLThgvLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMyNCSCLARDLTKIF 193
Cdd:cd09131    80 NGVEVR-FDSPSVT---THTKLVVIDGRTVYVGSHNWTYSALDYNHEASVLI-ESPEVADFAINYF 140
COG3886 COG3886
HKD family nuclease [Replication, recombination and repair];
95-197 2.52e-03

HKD family nuclease [Replication, recombination and repair];


Pssm-ID: 443094 [Multi-domain]  Cd Length: 941  Bit Score: 40.35  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  95 LQQLQALAPRGVKVRIAVSKPNG---PLAdLQSLLQ-SGAQVRMVDMQKlthGVLHTKFWVVDQTHF---YLGSANMDWR 167
Cdd:COG3886    61 LDALKELLERGVKGRILTSTYLGftePKA-LRELLDlPNIEVRVSYDRK---TRFHAKAYIFERTGYgtaIIGSSNLTRS 136

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039777590 168 SLTQVKELGV-VMYNCS-CLARDLTKIFEAYW 197
Cdd:COG3886   137 ALTDNLEWNVkLSSAEDpDLIEKFRAEFESLW 168
PLDc_unchar4 cd09132
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 54-163 2.87e-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: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590  54 QAWLGLLAGAHSSLDIASFYWTLTnndthtqepsaqqgEEVLQQLQALAPRGVKVRIAV--SKPNGPLADLQSLLQSGAQ 131
Cdd:cd09132     2 QVLLELIEGAERSLLIVGYSAYKV--------------SELLQALAAALERGVQVRVVVesSEKAGSVLSLDEDELMWPK 67

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1039777590 132 VRMVD-------MQKLTHGVLHTKFWVVDQTHFYLGSAN 163
Cdd:cd09132    68 LAGATlyvwpekKRPGKRASLHAKVIVADRRRLLVTSAN 106
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
 146-180 4.14e-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: 4.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1039777590 146 HTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMY 180
Cdd:cd09105   111 HSKVVIVDDEWATVGSANLNRRSMTWDTELNLAVV 145
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 254-393 4.72e-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: 37.32  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777590 254 KALLNVVDSARSFIYIA--VMNYLPtmefshPRRFWPA-IDDGLRRAAyERGVKVRLL----ISCWGHSDPSMRSFllsl 326
Cdd:cd09131     6 PALLDLINNAKRSIYIAmyMFKYYE------NPGNGVNtLLEALIDAH-KRGVDVKVVledsIDDDEVTEENDNTY---- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777590 327 AALHDNHthsdIQVKLfvvptDESQARIpyarvnHNKYMVT-ERASYIGTSNWSGSYFTETAGTSLLV 393
Cdd:cd09131    75 RYLKDNG----VEVRF-----DSPSVTT------HTKLVVIdGRTVYVGSHNWTYSALDYNHEASVLI 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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