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Conserved domains on  [gi|489932033|ref|WP_003835350|]
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MULTISPECIES: CDP-diacylglycerol--serine O-phosphatidyltransferase [Citrobacter]

Protein Classification

CDP-diacylglycerol--serine O-phosphatidyltransferase( domain architecture ID 11484158)

CDP-diacylglycerol--serine O-phosphatidyltransferase catalyzes de novo synthesis of phosphatidylserine from CDP-diacylglycerol and L-serine which leads eventually to the production of phosphatidylethanolamine; binds to the ribosome

EC:  2.7.8.8
Gene Symbol:  pssA
Gene Ontology:  GO:0003882|GO:0008654
PubMed:  1323044

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
1-431 0e+00

CDP-diacylglycerol--serine O-phosphatidyltransferase;


:

Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 869.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033   1 MLSKFKRNKHQQHLAQLPKISQSVDDVDFFYAPANFRETLLEKIASATRRICIIALYLEQDDGGKGILDALYAAKRQRPE 80
Cdd:PRK09428   1 MLSKFKRNKHQQHLAQLPKIPQSPDDVETLYSPADFRETLLEKIASAKKRIYIVALYLEDDEAGREILDALYQAKQQNPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  81 LDVRVLVDWHRAQRGRIGAAASNTNADWYCRMAQENPGIDIPVYGVPINTREALGVLHFKGFIIDDSVLYSGASLNDVYL 160
Cdd:PRK09428  81 LDIKVLVDWHRAQRGLIGAAASNTNADWYCEMAQEYPGVDIPVYGVPVNTREALGVLHLKGFIIDDTVLYSGASLNNVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 161 HQHDKYRYDRYQLIRNAQMADIMFDWVTQNLMNGRGVNRLDDINRPKSPEIKNDIRLYRQELRDASFHFQGDADNEQLSV 240
Cdd:PRK09428 161 HQHDKYRYDRYHLIRNAELADSMVNFIQQNLLNSPAVNRLDQPNRPKTKEIKNDIRQFRQRLRDAAYQFQGQANNDELSV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 241 TPLVGLGKSSLLNKTIFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFFIPEDEPFKIIGAL 320
Cdd:PRK09428 241 TPLVGLGKKNLLNKTIFHLMASAEQKLTICTPYFNLPAILVRNIIRLLRRGKKVEIIVGDKTANDFYIPPDEPFKIIGAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 321 PYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPKQELTPQ 400
Cdd:PRK09428 321 PYLYEINLRRFAKRLQYYIDNGQLNVRLWKDGDNSYHLKGIWVDDRWMLLTGNNLNPRAWRLDLENALLIHDPKQELAEQ 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 489932033 401 RDKELELIRTHTTVVKHYRDLQSIADYPVKV 431
Cdd:PRK09428 401 REKELELIRTHTTRVKHYSQLESIADYPVKV 431
 
Name Accession Description Interval E-value
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
1-431 0e+00

CDP-diacylglycerol--serine O-phosphatidyltransferase;


Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 869.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033   1 MLSKFKRNKHQQHLAQLPKISQSVDDVDFFYAPANFRETLLEKIASATRRICIIALYLEQDDGGKGILDALYAAKRQRPE 80
Cdd:PRK09428   1 MLSKFKRNKHQQHLAQLPKIPQSPDDVETLYSPADFRETLLEKIASAKKRIYIVALYLEDDEAGREILDALYQAKQQNPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  81 LDVRVLVDWHRAQRGRIGAAASNTNADWYCRMAQENPGIDIPVYGVPINTREALGVLHFKGFIIDDSVLYSGASLNDVYL 160
Cdd:PRK09428  81 LDIKVLVDWHRAQRGLIGAAASNTNADWYCEMAQEYPGVDIPVYGVPVNTREALGVLHLKGFIIDDTVLYSGASLNNVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 161 HQHDKYRYDRYQLIRNAQMADIMFDWVTQNLMNGRGVNRLDDINRPKSPEIKNDIRLYRQELRDASFHFQGDADNEQLSV 240
Cdd:PRK09428 161 HQHDKYRYDRYHLIRNAELADSMVNFIQQNLLNSPAVNRLDQPNRPKTKEIKNDIRQFRQRLRDAAYQFQGQANNDELSV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 241 TPLVGLGKSSLLNKTIFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFFIPEDEPFKIIGAL 320
Cdd:PRK09428 241 TPLVGLGKKNLLNKTIFHLMASAEQKLTICTPYFNLPAILVRNIIRLLRRGKKVEIIVGDKTANDFYIPPDEPFKIIGAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 321 PYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPKQELTPQ 400
Cdd:PRK09428 321 PYLYEINLRRFAKRLQYYIDNGQLNVRLWKDGDNSYHLKGIWVDDRWMLLTGNNLNPRAWRLDLENALLIHDPKQELAEQ 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 489932033 401 RDKELELIRTHTTVVKHYRDLQSIADYPVKV 431
Cdd:PRK09428 401 REKELELIRTHTTRVKHYSQLESIADYPVKV 431
PLDc_PSS_G_neg_2 cd09136
Catalytic domain, repeat 2, of phosphatidylserine synthases from gram-negative bacteria; ...
 238-431 2.74e-125

Catalytic domain, repeat 2, of phosphatidylserine synthases from gram-negative bacteria; Catalytic domain, repeat 2, of phosphatidylserine synthases (PSSs) from gram-negative bacteria. There are two subclasses of PSS enzymes in bacteria: subclass I of gram-negative bacteria and subclass II of gram-positive bacteria. It is common that PSSs in gram-positive bacteria and yeast are tight membrane-associated enzymes. By contrast, the gram-negative bacterial PSSs, such as Escherichia coli PSS, are commonly bound to the ribosomes. They are peripheral membrane proteins that can interact with the surface of the inner membrane by binding to the lipid substrate (CDP-diacylglycerol) and the lipid product (phosphatidylserine). The prototypical member of this subfamily is Escherichia coli PSS (also called CDP-diacylglycerol-L-serine O-phosphatidyltransferase, EC 2.7.8.8), which catalyzes the exchange reactions between CMP and CDP-diacylglycerol, and between serine and phosphatidylserine. The phosphatidylserine is then decarboxylated by phosphatidylserine decarboxylase to yield phosphatidylethanolamine, the major phospholipid in Escherichia coli. It also catalyzes the hydrolysis of CDP-diacylglycerol to form phosphatidic acid with the release of CMP. PSS may utilize a ping-pong mechanism involving a phosphatidyl-enzyme intermediate, which is distinct from those of gram-positive bacterial phosphatidylserine synthases. Moreover, all members in this subfamily have 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 constitute an active site for the formation of a covalent substrate-enzyme intermediate.


Pssm-ID: 197234  Cd Length: 215  Bit Score: 362.30  E-value: 2.74e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 238 LSVTPLVGLGKS-SLLNKTIFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFFIPEDEPFKI 316
Cdd:cd09136    1 LSITPLVGLGKRgNQLNRTIRQLIQSAESELIICTPYFNLPRSLVRDIARLLKRGVKVEIIVGDKTANDFYIPPEEPFKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 317 IGALPYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPKQE 396
Cdd:cd09136   81 IGALPYLYEINLRRFAKRLQKYIDNGQLNVRLWKDGNNSFHLKGIWVDDRYHLLTGNNLNPRAWRLDLENGLLIHDPQGQ 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489932033 397 LTPQRDKELELIRTHTTVVKHYRDLQSIADYPVKV 431
Cdd:cd09136  161 LKAQFEKELEQILAHTTRIKHYSQLESIADYPEKV 195
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 9-406 3.33e-55

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: 187.46  E-value: 3.33e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033   9 KHQQHLAQLPKisQSVDDVDFFYAPANFRETLLEKIASATRRICIIALYLEQDDGGKGILDALYAAKRqrPELDVRVLVD 88
Cdd:COG1502    1 KAAPLAAGLPL--VGGNRVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAAR--RGVKVRVLLD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  89 WhraqrgrIGAAAsnTNADWYCRMaqENPGIDIPVYG-VPINTREALGVLHFKGFIIDDSVLY-SGASLNDVYLHQHDK- 165
Cdd:COG1502   77 G-------IGSRA--LNRDFLRRL--RAAGVEVRLFNpVRLLFRRLNGRNHRKIVVIDGRVAFvGGANITDEYLGRDPGf 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 166 -YRYDRYQLIRNAQMADImfdwvtQNLMNgrgvnrlDDINRPKSPEIKNDirlyrqelrdasfHFQGDADNEQLSVTPLv 244
Cdd:COG1502  146 gPWRDTHVRIEGPAVADL------QAVFA-------EDWNFATGEALPFP-------------EPAGDVRVQVVPSGPD- 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 245 glGKSSLLNKTIFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTandffipeDEPFKIIGALPYLY 324
Cdd:COG1502  199 --SPRETIERALLAAIASARRRIYIETPYFVPDRSLLRALIAAARRGVDVRILLPAKS--------DHPLVHWASRSYYE 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 325 EINLRRflsrlqyyvntdqlvVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPK--QELTPQRD 402
Cdd:COG1502  269 ELLEAG---------------VRIYEYEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDPEfaAQLRARFE 333


                 ....
gi 489932033 403 KELE 406
Cdd:COG1502  334 EDLA 337
PLDc_2 pfam13091
PLD-like domain;
256-394 1.70e-21

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 89.66  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  256 IFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTAnDFFIPEDEPFKIIGALpYLYEINLRRFLSRL 335
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPDREIIDALIAAAKRGVDVRIILDSNKD-DAGGPKKASLKELRSL-LRAGVEIREYQSFL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489932033  336 qyyvntdqlvvrlwkdddNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPK 394
Cdd:pfam13091  79 ------------------RSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKDPE 119
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 353-379 1.87e-04

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 38.52  E-value: 1.87e-04
                           10        20
                   ....*....|....*....|....*..
gi 489932033   353 DNTYHLKGMWVDDKWMLLTGNNLNPRA 379
Cdd:smart00155   2 DGVLHTKLMIVDDEIAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
1-431 0e+00

CDP-diacylglycerol--serine O-phosphatidyltransferase;


Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 869.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033   1 MLSKFKRNKHQQHLAQLPKISQSVDDVDFFYAPANFRETLLEKIASATRRICIIALYLEQDDGGKGILDALYAAKRQRPE 80
Cdd:PRK09428   1 MLSKFKRNKHQQHLAQLPKIPQSPDDVETLYSPADFRETLLEKIASAKKRIYIVALYLEDDEAGREILDALYQAKQQNPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  81 LDVRVLVDWHRAQRGRIGAAASNTNADWYCRMAQENPGIDIPVYGVPINTREALGVLHFKGFIIDDSVLYSGASLNDVYL 160
Cdd:PRK09428  81 LDIKVLVDWHRAQRGLIGAAASNTNADWYCEMAQEYPGVDIPVYGVPVNTREALGVLHLKGFIIDDTVLYSGASLNNVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 161 HQHDKYRYDRYQLIRNAQMADIMFDWVTQNLMNGRGVNRLDDINRPKSPEIKNDIRLYRQELRDASFHFQGDADNEQLSV 240
Cdd:PRK09428 161 HQHDKYRYDRYHLIRNAELADSMVNFIQQNLLNSPAVNRLDQPNRPKTKEIKNDIRQFRQRLRDAAYQFQGQANNDELSV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 241 TPLVGLGKSSLLNKTIFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFFIPEDEPFKIIGAL 320
Cdd:PRK09428 241 TPLVGLGKKNLLNKTIFHLMASAEQKLTICTPYFNLPAILVRNIIRLLRRGKKVEIIVGDKTANDFYIPPDEPFKIIGAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 321 PYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPKQELTPQ 400
Cdd:PRK09428 321 PYLYEINLRRFAKRLQYYIDNGQLNVRLWKDGDNSYHLKGIWVDDRWMLLTGNNLNPRAWRLDLENALLIHDPKQELAEQ 400

                        410       420       430
                 ....*....|....*....|....*....|.
gi 489932033 401 RDKELELIRTHTTVVKHYRDLQSIADYPVKV 431
Cdd:PRK09428 401 REKELELIRTHTTRVKHYSQLESIADYPVKV 431
PLDc_PSS_G_neg_2 cd09136
Catalytic domain, repeat 2, of phosphatidylserine synthases from gram-negative bacteria; ...
 238-431 2.74e-125

Catalytic domain, repeat 2, of phosphatidylserine synthases from gram-negative bacteria; Catalytic domain, repeat 2, of phosphatidylserine synthases (PSSs) from gram-negative bacteria. There are two subclasses of PSS enzymes in bacteria: subclass I of gram-negative bacteria and subclass II of gram-positive bacteria. It is common that PSSs in gram-positive bacteria and yeast are tight membrane-associated enzymes. By contrast, the gram-negative bacterial PSSs, such as Escherichia coli PSS, are commonly bound to the ribosomes. They are peripheral membrane proteins that can interact with the surface of the inner membrane by binding to the lipid substrate (CDP-diacylglycerol) and the lipid product (phosphatidylserine). The prototypical member of this subfamily is Escherichia coli PSS (also called CDP-diacylglycerol-L-serine O-phosphatidyltransferase, EC 2.7.8.8), which catalyzes the exchange reactions between CMP and CDP-diacylglycerol, and between serine and phosphatidylserine. The phosphatidylserine is then decarboxylated by phosphatidylserine decarboxylase to yield phosphatidylethanolamine, the major phospholipid in Escherichia coli. It also catalyzes the hydrolysis of CDP-diacylglycerol to form phosphatidic acid with the release of CMP. PSS may utilize a ping-pong mechanism involving a phosphatidyl-enzyme intermediate, which is distinct from those of gram-positive bacterial phosphatidylserine synthases. Moreover, all members in this subfamily have 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 constitute an active site for the formation of a covalent substrate-enzyme intermediate.


Pssm-ID: 197234  Cd Length: 215  Bit Score: 362.30  E-value: 2.74e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 238 LSVTPLVGLGKS-SLLNKTIFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFFIPEDEPFKI 316
Cdd:cd09136    1 LSITPLVGLGKRgNQLNRTIRQLIQSAESELIICTPYFNLPRSLVRDIARLLKRGVKVEIIVGDKTANDFYIPPEEPFKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 317 IGALPYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPKQE 396
Cdd:cd09136   81 IGALPYLYEINLRRFAKRLQKYIDNGQLNVRLWKDGNNSFHLKGIWVDDRYHLLTGNNLNPRAWRLDLENGLLIHDPQGQ 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489932033 397 LTPQRDKELELIRTHTTVVKHYRDLQSIADYPVKV 431
Cdd:cd09136  161 LKAQFEKELEQILAHTTRIKHYSQLESIADYPEKV 195
PLDc_CDP-OH_P_transf_II_2 cd09103
Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members; ...
 238-420 2.10e-116

Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members; Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily.


Pssm-ID: 197202 [Multi-domain]  Cd Length: 184  Bit Score: 338.43  E-value: 2.10e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 238 LSVTPLVGLGKS-SLLNKTIFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTANDFFIPEDEPFKI 316
Cdd:cd09103    1 LSITPLVGLGKRgNILNRTIEQLITSAESKIILCTPYFNLPQALMRDILRLLKRGVKVEIIVGDKTANDFYIPPEEPFKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 317 IGALPYLYEINLRRFLSRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPKQE 396
Cdd:cd09103   81 IGALPYLYEINLRRFAKRLQKYIDQGQLNVRLWKDGDNSFHLKGIWVDDRYTLLTGNNLNPRAWRLDLENGLLIHDPQKQ 160

                        170       180
                 ....*....|....*....|....
gi 489932033 397 LTPQRDKELELIRTHTTVVKHYRD 420
Cdd:cd09103  161 LQQQLEKELEQILLHTTRISHYTQ 184
PLDc_PSS_G_neg_1 cd09134
Catalytic domain, repeat 1, of phosphatidylserine synthases from gram-negative bacteria; ...
 17-190 1.40e-106

Catalytic domain, repeat 1, of phosphatidylserine synthases from gram-negative bacteria; Catalytic domain, repeat 1, of phosphatidylserine synthases (PSSs) from gram-negative bacteria. There are two subclasses of PSS enzymes in bacteria: subclass I of gram-negative bacteria and subclass II of gram-positive bacteria. It is common that PSSs in gram-positive bacteria and yeast are tight membrane-associated enzymes. By contrast, the gram-negative bacterial PSSs, such as Escherichia coli PSS, are commonly bound to the ribosomes. They are peripheral membrane proteins that can interact with the surface of the inner membrane by binding to the lipid substrate (CDP-diacylglycerol) and the lipid product (phosphatidylserine). The prototypical member of this subfamily is Escherichia coli PSS (also called CDP-diacylglycerol-L-serine O-phosphatidyltransferase, EC 2.7.8.8), which catalyzes the exchange reactions between CMP and CDP-diacylglycerol, and between serine and phosphatidylserine. The phosphatidylserine is then decarboxylated by phosphatidylserine decarboxylase to yield phosphatidylethanolamine, the major phospholipid in Escherichia coli. It also catalyzes the hydrolysis of CDP-diacylglycerol to form phosphatidic acid with the release of CMP. PSS may utilize a ping-pong mechanism involving a phosphatidyl-enzyme intermediate, which is distinct from those of gram-positive bacterial phosphatidylserine synthases. Moreover, all members in this subfamily have 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 constitute an active site for the formation of a covalent substrate-enzyme intermediate.


Pssm-ID: 197232 [Multi-domain]  Cd Length: 173  Bit Score: 313.03  E-value: 1.40e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  17 LPKISQSVDDVDFFYAPANFRETLLEKIASATRRICIIALYLEQDDGGKGILDALYAAKRQRPELDVRVLVDWHRAQRGR 96
Cdd:cd09134    1 LPKIPQQPEDIDVLYSPKDFRARLLELISNAKKRIYIVALYLEDDEAGREILDALYEAKANNPGLDIKVLVDWHRAQRGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  97 IGAAASNTNADWYCRMAQENPgIDIPVYGVPINTREALGVLHFKGFIIDDSVLYSGASLNDVYLHQHDKYRYDRYQLIRN 176
Cdd:cd09134   81 IGAKKSLGNADWYRKIAQRYG-HDVPIYGVPVKTRELFGVLHLKGFIIDDTVLYSGASLNNVYLHQFDKYRYDRYHLIYN 159

                        170
                 ....*....|....
gi 489932033 177 AQMADIMFDWVTQN 190
Cdd:cd09134  160 PELADSMVNFIQDY 173
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 9-406 3.33e-55

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: 187.46  E-value: 3.33e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033   9 KHQQHLAQLPKisQSVDDVDFFYAPANFRETLLEKIASATRRICIIALYLEQDDGGKGILDALYAAKRqrPELDVRVLVD 88
Cdd:COG1502    1 KAAPLAAGLPL--VGGNRVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAAR--RGVKVRVLLD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  89 WhraqrgrIGAAAsnTNADWYCRMaqENPGIDIPVYG-VPINTREALGVLHFKGFIIDDSVLY-SGASLNDVYLHQHDK- 165
Cdd:COG1502   77 G-------IGSRA--LNRDFLRRL--RAAGVEVRLFNpVRLLFRRLNGRNHRKIVVIDGRVAFvGGANITDEYLGRDPGf 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 166 -YRYDRYQLIRNAQMADImfdwvtQNLMNgrgvnrlDDINRPKSPEIKNDirlyrqelrdasfHFQGDADNEQLSVTPLv 244
Cdd:COG1502  146 gPWRDTHVRIEGPAVADL------QAVFA-------EDWNFATGEALPFP-------------EPAGDVRVQVVPSGPD- 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 245 glGKSSLLNKTIFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTandffipeDEPFKIIGALPYLY 324
Cdd:COG1502  199 --SPRETIERALLAAIASARRRIYIETPYFVPDRSLLRALIAAARRGVDVRILLPAKS--------DHPLVHWASRSYYE 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 325 EINLRRflsrlqyyvntdqlvVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPK--QELTPQRD 402
Cdd:COG1502  269 ELLEAG---------------VRIYEYEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDPEfaAQLRARFE 333


                 ....
gi 489932033 403 KELE 406
Cdd:COG1502  334 EDLA 337
PLDc_CDP-OH_P_transf_II_1 cd09102
Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members; ...
 27-187 1.10e-41

Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members; Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily.


Pssm-ID: 197201 [Multi-domain]  Cd Length: 168  Bit Score: 145.81  E-value: 1.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  27 VDFFYAPANFRETLLEKIASATRRICIIALYLEQDDGGKGILDALYAAKRQRPELDVRVLVDWHRAQRGRIGAAA-SNTN 105
Cdd:cd09102    2 IRFLGSPAEFKTQIIELIRNAKRRVYVASLYWGKDEAGQEILDEIYSVKQENPNLDVSVLIDWHRAQRNLLGSETkSATN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 106 ADWYCRMAQENPGIDIPV-----YGVPINTREALGVLHFKGFIIDDSVLYSGASLNDVYLHqhdkYRYDRYQLIRN-AQM 179
Cdd:cd09102   82 ADWYCEQRQTSQLHLLPDdgn*fFGVPINTNEVFGVLHVKGYVFDDTVLLSGANLSNVYFH----YRYDRYVKITHgAEL 157


                 ....*...
gi 489932033 180 ADIMFDWV 187
Cdd:cd09102  158 ADS*VNLI 165
PLDc_2 pfam13091
PLD-like domain;
256-394 1.70e-21

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 89.66  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  256 IFHLMPCAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKTAnDFFIPEDEPFKIIGALpYLYEINLRRFLSRL 335
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPDREIIDALIAAAKRGVDVRIILDSNKD-DAGGPKKASLKELRSL-LRAGVEIREYQSFL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489932033  336 qyyvntdqlvvrlwkdddNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPK 394
Cdd:pfam13091  79 ------------------RSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKDPE 119
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
 26-185 1.91e-21

Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic domain, repeat 1, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197233 [Multi-domain]  Cd Length: 170  Bit Score: 90.69  E-value: 1.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  26 DVDFFYAPANFRETLLEKIASATRRICIIALYLeqddgGKGIL-----DALYAAKRQRPELDVRVLVDWHRAQRGRIGAA 100
Cdd:cd09135    1 QIRILRTPSEFYNTLLDKIRNAKRRIVLSSLYI-----GTGPLeqelvDALQEALERNPNLKVSILLDYLRGTRGEPNSR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 101 ASNTNAdwycRMAQE-NPGIDIPVYGVPiNTR------------EALGVLHFKGFIIDDSVLYSGASLNDVYLHQhdkyR 167
Cdd:cd09135   76 TASLLL----PLLKLfPDRVRVSLYHTP-NLRgllkkllperfnEIIGLQHMKLYIFDDDVILSGANLSDDYFTN----R 146

                        170
                 ....*....|....*....
gi 489932033 168 YDRYQLIRNA-QMADIMFD 185
Cdd:cd09135  147 QDRYMLIENCpELADFYHD 165
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
 264-415 7.67e-18

Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197235  Cd Length: 186  Bit Score: 81.08  E-value: 7.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 264 EHKLTICTPYFNLPailvRNIIQLLREGK-KVEIIVGDKTANDFFipedePFKII-GALPYLYEINLRRFLSRLQYYVNT 341
Cdd:cd09137   31 GSSLTLASGYFNLT----PEYLNLLLNSSaNLDVLTASPEANGFY-----GSKGVsGYIPPAYTYIARQFLKRVRKNGKQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 342 DQLVVRLWKDDDNTYHLKGMWVDDK-----WMLLTGN-NLNPRAWRLDLENAILIHDPKQELTPQRDKELELIRTHTTVV 415
Cdd:cd09137  102 PRIKLFEYKRPGWTFHAKGLWIYLPgtdlpSLTLIGSsNYGYRSVHRDLEAQFLIVTNNPKLQQQLKEELENLFEYSKPV 181
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 258-390 5.44e-10

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: 56.76  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 258 HLMPCAEHKLTICTPYFNLPA--ILVRNIIQLLREGKKVEIIVGDKTANDFFIPEDEPFKIIGALpylyeINLRRFLSRL 335
Cdd:cd00138    5 ELLKNAKESIFIATPNFSFNSadRLLKALLAAAERGVDVRLIIDKPPNAAGSLSAALLEALLRAG-----VNVRSYVTPP 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489932033 336 QYyvntdqlvvrlwkddDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILI 390
Cdd:cd00138   80 HF---------------FERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 250-395 1.99e-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: 197259 [Multi-domain]  Cd Length: 172  Bit Score: 47.64  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 250 SLLNKTIFHlmpcAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVgdktandffiPEDEPFKIIgalpylyeiNLR 329
Cdd:cd09162   14 EALLSAIFE----AEHRIWIVTPYFVPDEVLLRALRLAARRGVDVRLIV----------PKRSNHRIA---------DLA 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489932033 330 R--FLSRLQYyvntdqLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPKQ 395
Cdd:cd09162   71 RgsYLRDLQE------AGAEIYLYQPGMLHAKAVVVDDKLALVGSANLDMRSLFLNYEVAVFFYSPAD 132
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 38-162 4.22e-06

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: 45.59  E-value: 4.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  38 ETLLEKIASATRRICIIALYLEQDDGGKgILDALYAAKRQrpELDVRVLVDWHRAQRGRIGAA--ASNTNADWYCRMAQe 115
Cdd:cd00138    1 EALLELLKNAKESIFIATPNFSFNSADR-LLKALLAAAER--GVDVRLIIDKPPNAAGSLSAAllEALLRAGVNVRSYV- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489932033 116 npgidipvygvpiNTREALGVLHFKGFIIDDSVLY-SGASLNDVYLHQ 162
Cdd:cd00138   77 -------------TPPHFFERLHAKVVVIDGEVAYvGSANLSTASAAQ 111
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 353-379 1.58e-05

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


Pssm-ID: 395489 [Multi-domain]  Cd Length: 28  Bit Score: 41.64  E-value: 1.58e-05
                          10        20
                  ....*....|....*....|....*..
gi 489932033  353 DNTYHLKGMWVDDKWMLLTGNNLNPRA 379
Cdd:pfam00614   2 DGRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 26-156 2.56e-05

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: 43.80  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  26 DVDFFYAPANFRETLLEKIASATRRICIIALYLEQDDggkGILDALyaAKRQRPELDVRVLVDwhraqrgriGAAASNTN 105
Cdd:cd09128    1 SVQLLLSPDNAREALLALIDSAEESLLIQNEEMGDDA---PILDAL--VDAAKRGVDVRVLLP---------SAWSAEDE 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489932033 106 ADWYCRMAQENpgidipvyGVPINTRE-ALGVLHFKGFIIDDSVLYSGaSLN 156
Cdd:cd09128   67 RQARLRALEGA--------GVPVRLLKdKFLKIHAKGIVVDGKTALVG-SEN 109
PLDc_CLS_unchar2_2 cd09163
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 262-411 1.36e-04

Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial cardiolipin synthase; Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197260 [Multi-domain]  Cd Length: 176  Bit Score: 42.54  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 262 CAEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKtaNDffipedepfkiigaLPYLyeinlrRFLSRLQYyvnt 341
Cdd:cd09163   22 AARHSIRIMTPYFLPDRTLITALQAAALRGVEVDIVLPER--NN--------------LPLV------DWAMRANL---- 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489932033 342 DQLV---VRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPkqELTPQRDKELELIRTH 411
Cdd:cd09163   76 WELLehgVRIYLQPPPFDHSKLMVVDGAWALIGSANWDPRSLRLNFELNLEVYDT--ALAGQLDALFDSKIAK 146
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 353-379 1.87e-04

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 38.52  E-value: 1.87e-04
                           10        20
                   ....*....|....*....|....*..
gi 489932033   353 DNTYHLKGMWVDDKWMLLTGNNLNPRA 379
Cdd:smart00155   2 DGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_PaCLS_like_2 cd09161
Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin synthase and ...
 255-394 3.33e-04

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: 41.51  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 255 TIFHLMPCAEHKLTICTPYFnLPAILVRNIIQL--LReGKKVEIIVGDKTandffipeDEPfkiigaLPYLyeinlrrfl 332
Cdd:cd09161   15 FFVQAINAAQKRLWIASPYF-VPDEGVLAALQLaaLR-GVDVRILIPERP--------DHL------LVYL--------- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489932033 333 SRLQYYVNTDQLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPK 394
Cdd:cd09161   70 ASFSYLPELIRAGVKVYRYQPGFLHQKVVLVDDELAAVGTANLDNRSFRLNFEITALVADPG 131
PLDc_2 pfam13091
PLD-like domain;
40-156 5.76e-04

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 39.97  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033   40 LLEKIASATRRICIIALYLEQDdggKGILDALYAAKRqRPeLDVRVLVDwhrAQRGRIGAAASNTNADWycrMAQENPGI 119
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPD---REIIDALIAAAK-RG-VDVRIILD---SNKDDAGGPKKASLKEL---RSLLRAGV 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489932033  120 DIPVYGVpintreALGVLHFKGFIIDDSVLYSGaSLN 156
Cdd:pfam13091  70 EIREYQS------FLRSMHAKFYIIDGKTVIVG-SAN 99
PLDc_CLS_unchar1_1 cd09156
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 37-88 8.45e-04

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: 39.94  E-value: 8.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489932033  37 RETLLEKIASATRRICIIALYLEQDDGGKGILDALyaAKRQRPELDVRVLVD 88
Cdd:cd09156    7 YQALIQLIESAKHSIDVCTFILGDDATGRRVIDAL--ARKAREGVEVRLLLD 56
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 29-156 5.45e-03

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: 37.28  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033  29 FFYAPA-NFRETLLEKIASATRRICIIALYLEQddggKGILDAL-YAAKRQrpeLDVRVLVD-WHRAQRGRIGAAASNTN 105
Cdd:cd09116    2 FLPRPQdNLERLIVALIANAKSSIDVAMYALTD----PEIAEALkRAAKRG---VRVRIILDkDSLADNLSITLLALLSN 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489932033 106 AdwycrmaqenpgidipvyGVPINTREALGVLHFKGFIIDDSVLYSGaSLN 156
Cdd:cd09116   75 L------------------GIPVRTDSGSKLMHHKFIIIDGKIVITG-SAN 106
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 263-394 7.09e-03

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 36.87  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489932033 263 AEHKLTICTPYFNLPAILVRNIIQLLREGKKVEIIVGDKtandffIPEDEpfkiigalpylYEINLRRFLSRLqyyvntd 342
Cdd:cd09128   22 AEESLLIQNEEMGDDAPILDALVDAAKRGVDVRVLLPSA------WSAED-----------ERQARLRALEGA------- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489932033 343 QLVVRLWKDDDNTYHLKGMWVDDKWMLLTGNNLNPRAWRLDLENAILIHDPK 394
Cdd:cd09128   78 GVPVRLLKDKFLKIHAKGIVVDGKTALVGSENWSANSLDRNREVGLIFDDPE 129
 
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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