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Conserved domains on  [gi|815890872|ref|NP_001295103|]
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5'-3' exonuclease PLD4 isoform 1 [Homo sapiens]

Protein Classification

phospholipase D-like domain-containing protein; phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase family protein( domain architecture ID 10173693)

phospholipase D-like domain-containing protein may hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group, and may also catalyze the transphosphatidylation of phospholipids to acceptor alcohols| phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase family protein similar to cardiolipin synthase B, which catalyzes the formation of cardiolipin and whose substrates have not been definitively established

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 311-497 1.13e-124

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: 361.86  E-value: 1.13e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 311 YFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNT 390
Cdd:cd09148    1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 391 DPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQS 470
Cdd:cd09148   81 DPDMFPFLRSLNALSNPPLSISVHVKLFIVPVGNQTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVGLVILQS 160

                        170       180
                 ....*....|....*....|....*..
gi 815890872 471 PGAQPAGATVQEQLRQLFERDWSSRYA 497
Cdd:cd09148  161 PGANEEMLPVQEQLRSLFERDWSSPYA 187
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 105-274 5.27e-108

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: 318.78  E-value: 5.27e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 105 LVESIPQDLPSAAGSPSAQPLGQAWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAVA 184
Cdd:cd09145    1 LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWSLTGEDIGVNDSSSLPGEDILKELAELLSRNVSVRAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 185 TSSPTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCSHLAQDL 264
Cdd:cd09145   81 ASIPTLAANSTDLKILRQKGAHVRKVNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAKDL 160

                        170
                 ....*....|
gi 815890872 265 EKTFQTYWVL 274
Cdd:cd09145  161 HKTFQTYWVL 170
 
Name Accession Description Interval E-value
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 311-497 1.13e-124

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: 361.86  E-value: 1.13e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 311 YFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNT 390
Cdd:cd09148    1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 391 DPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQS 470
Cdd:cd09148   81 DPDMFPFLRSLNALSNPPLSISVHVKLFIVPVGNQTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVGLVILQS 160

                        170       180
                 ....*....|....*....|....*..
gi 815890872 471 PGAQPAGATVQEQLRQLFERDWSSRYA 497
Cdd:cd09148  161 PGANEEMLPVQEQLRSLFERDWSSPYA 187
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 105-274 5.27e-108

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: 318.78  E-value: 5.27e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 105 LVESIPQDLPSAAGSPSAQPLGQAWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAVA 184
Cdd:cd09145    1 LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWSLTGEDIGVNDSSSLPGEDILKELAELLSRNVSVRAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 185 TSSPTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCSHLAQDL 264
Cdd:cd09145   81 ASIPTLAANSTDLKILRQKGAHVRKVNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAKDL 160

                        170
                 ....*....|
gi 815890872 265 EKTFQTYWVL 274
Cdd:cd09145  161 HKTFQTYWVL 170
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 99-509 7.94e-97

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 299.60  E-value: 7.94e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  99 DSCQLVLVESIPQDLPSAAGSPSAQPLgqaWLQLLDTAQESVHVASYYWSLTGPDiGVNDSSSQLGEallQKLQQLLGRN 178
Cdd:PHA02820   4 DNTIAVITETIPIGMQFDKVYLSTFNF---WREILSNTTKTLDISSFYWSLSDEV-GTNFGTMILNE---IIQLPKRGVR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 179 ISLAVATSSptlaRTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCS 258
Cdd:PHA02820  77 VRIAVNKSN----KPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 259 HLAQDLEKTFQTYWVLGVPKavLPKTWPQNFSSHFNRFQPFHGLFDGVPTTAYFSASPPALCPQGRTRDLEALLAVMGSA 338
Cdd:PHA02820 153 NLAADLTQIFEVYWYLGVNN--LPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 339 QEFIYASVMEYFPTTrFSHPPR--YWPVLDNALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQALSnpAANVSVDVK 416
Cdd:PHA02820 231 SKFVYVSVMNFIPII-YSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLK--SKNINIEVK 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 417 VFIVPvGNHSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQSpgaqpAGATVQEQLRQLFERDWSSRY 496
Cdd:PHA02820 308 LFIVP-DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPD-----DGLGLRQQLEDIFIRDWNSKY 381

                        410
                 ....*....|...
gi 815890872 497 AVGLDGQAPGQDC 509
Cdd:PHA02820 382 SYELYDTSPTKRC 394
PLDc_3 pfam13918
PLD-like domain;
243-421 6.16e-36

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 131.67  E-value: 6.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  243 SLTQVKELGAVIYNCSHLAQDLEKTFQTYWVLGVPKAVlPKTWPQNFSSHFNRFQPFHGLFDGVPTTAYFSASPPALCPQ 322
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKV-PFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  323 GRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQ 402
Cdd:pfam13918  80 NRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLD 159

                         170
                  ....*....|....*....
gi 815890872  403 ALSNPAANVSVDVKVFIVP 421
Cdd:pfam13918 160 AFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 107-501 1.18e-19

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: 90.39  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 107 ESIPQDLPSAAGSpSAQPLG------QAWLQLLDTAQESVHVASYYWSLtgPDIGvndssSQLGEAllqklqqllgrnis 180
Cdd:COG1502    3 APLAAGLPLVGGN-RVTLLVdgdeafAALLEAIEAARRSIDLEYYIFDD--DEVG-----RRLADA-------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 181 LAVAT-----------SSPTLARTSTDLQVLAARGAHVRQ-VPMGRLTR---GVLHSKFWVVDGRHIYMGSANMDWRSLT 245
Cdd:COG1502   61 LIAAArrgvkvrvlldGIGSRALNRDFLRRLRAAGVEVRLfNPVRLLFRrlnGRNHRKIVVIDGRVAFVGGANITDEYLG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 246 QVKELGAvIYNCSHL-----AQDLEKTFQTYWvlgvpkavlpktwpqNFSSHFNRFQPFHglfdGVPTTAYFSASPPAlc 320
Cdd:COG1502  141 RDPGFGP-WRDTHVRiegpaVADLQAVFAEDW---------------NFATGEALPFPEP----AGDVRVQVVPSGPD-- 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 321 pqGRTRDLE-ALLAVMGSAQEFIYAsVMEYFPTTRfshpprywpVLDNALRAAAfGKGVRVRLLVGcGLNTDPTMFPYLR 399
Cdd:COG1502  199 --SPRETIErALLAAIASARRRIYI-ETPYFVPDR---------SLLRALIAAA-RRGVDVRILLP-AKSDHPLVHWASR 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 400 S-LQALsnpaanVSVDVKVFIVPVGnhsnipfsrVNHSKFMVT-EKAAYIGTSNWseDYFSSTAG--VGLVVTqspgaqp 475
Cdd:COG1502  265 SyYEEL------LEAGVRIYEYEPG---------FLHAKVMVVdDEWALVGSANL--DPRSLRLNfeVNLVIY------- 320

                        410       420
                 ....*....|....*....|....*.
gi 815890872 476 aGATVQEQLRQLFERDWSSRYAVGLD 501
Cdd:COG1502  321 -DPEFAAQLRARFEEDLAHSREVTLE 345
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 200-287 1.59e-11

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


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 65.73  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 200 LAARGAHVRqvpmgRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQTYWvlGVPKA 279
Cdd:COG1502  270 LLEAGVRIY-----EYEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYD-PEFAAQLRARFEEDL--AHSRE 341


                 ....*...
gi 815890872 280 VLPKTWPQ 287
Cdd:COG1502  342 VTLEEWRK 349
PLDc_2 pfam13091
PLD-like domain;
130-272 2.48e-11

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 61.15  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  130 LQLLDTAQESVHVASYYWsLTGPDIGvndssSQLGEALLQklqqllGRNISL---AVATSSPTLA-RTSTDLQVLAARGA 205
Cdd:pfam13091   2 IDLINSAKKSIDIATYYF-VPDREII-----DALIAAAKR------GVDVRIildSNKDDAGGPKkASLKELRSLLRAGV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815890872  206 HVRqVPMGRLTRgvLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQTYW 272
Cdd:pfam13091  70 EIR-EYQSFLRS--MHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEFDRLW 132
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 218-243 7.92e-09

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 50.85  E-value: 7.92e-09
                           10        20
                   ....*....|....*....|....*.
gi 815890872   218 GVLHSKFWVVDGRHIYMGSANMDWRS 243
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
cls PRK01642
cardiolipin synthetase; Reviewed
 214-271 6.32e-05

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 45.54  E-value: 6.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 815890872 214 RLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQTY 271
Cdd:PRK01642 394 RYEGGLLHTKSVLVDDELALVGTVNLDMRSFWLNFEITLVIDD-TGFAADLAAMQEDY 450
bac_cardiolipin TIGR04265
cardiolipin synthase; This model is based on experimentally characterized bacterial ...
 217-271 3.33e-04

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: 43.24  E-value: 3.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 815890872  217 RGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCShLAQDLEKTFQTY 271
Cdd:TIGR04265 397 NGFLHSKSVLVDDEIASVGTANMDMRSFWLNFEVNAFIYDKG-FAKDLAAAYDDD 450
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 430-456 1.34e-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: 36.21  E-value: 1.34e-03
                           10        20
                   ....*....|....*....|....*...
gi 815890872   430 FSRVNHSKFMVTE-KAAYIGTSNWSEDY 456
Cdd:smart00155   1 YDGVLHTKLMIVDdEIAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 311-497 1.13e-124

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: 361.86  E-value: 1.13e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 311 YFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNT 390
Cdd:cd09148    1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 391 DPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQS 470
Cdd:cd09148   81 DPDMFPFLRSLNALSNPPLSISVHVKLFIVPVGNQTNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVGLVILQS 160

                        170       180
                 ....*....|....*....|....*..
gi 815890872 471 PGAQPAGATVQEQLRQLFERDWSSRYA 497
Cdd:cd09148  161 PGANEEMLPVQEQLRSLFERDWSSPYA 187
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 105-274 5.27e-108

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: 318.78  E-value: 5.27e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 105 LVESIPQDLPSAAGSPSAQPLGQAWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAVA 184
Cdd:cd09145    1 LVESIPEDLTYEGNSTFALPLQKAWTKLLDMAQEQVHVASYYWSLTGEDIGVNDSSSLPGEDILKELAELLSRNVSVRAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 185 TSSPTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCSHLAQDL 264
Cdd:cd09145   81 ASIPTLAANSTDLKILRQKGAHVRKVNFGRLTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIYNCSSLAKDL 160

                        170
                 ....*....|
gi 815890872 265 EKTFQTYWVL 274
Cdd:cd09145  161 HKTFQTYWVL 170
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 99-509 7.94e-97

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 299.60  E-value: 7.94e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  99 DSCQLVLVESIPQDLPSAAGSPSAQPLgqaWLQLLDTAQESVHVASYYWSLTGPDiGVNDSSSQLGEallQKLQQLLGRN 178
Cdd:PHA02820   4 DNTIAVITETIPIGMQFDKVYLSTFNF---WREILSNTTKTLDISSFYWSLSDEV-GTNFGTMILNE---IIQLPKRGVR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 179 ISLAVATSSptlaRTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCS 258
Cdd:PHA02820  77 VRIAVNKSN----KPLKDVELLQMAGVEVRYIDITNILGGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 259 HLAQDLEKTFQTYWVLGVPKavLPKTWPQNFSSHFNRFQPFHGLFDGVPTTAYFSASPPALCPQGRTRDLEALLAVMGSA 338
Cdd:PHA02820 153 NLAADLTQIFEVYWYLGVNN--LPYNWKNFYPLYYNTDHPLSLNVSGVPHSVFIASAPQQLCTMERTNDLTALLSCIRNA 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 339 QEFIYASVMEYFPTTrFSHPPR--YWPVLDNALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQALSnpAANVSVDVK 416
Cdd:PHA02820 231 SKFVYVSVMNFIPII-YSKAGKilFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLK--SKNINIEVK 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 417 VFIVPvGNHSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQSpgaqpAGATVQEQLRQLFERDWSSRY 496
Cdd:PHA02820 308 LFIVP-DADPPIPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITPD-----DGLGLRQQLEDIFIRDWNSKY 381

                        410
                 ....*....|...
gi 815890872 497 AVGLDGQAPGQDC 509
Cdd:PHA02820 382 SYELYDTSPTKRC 394
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 311-493 2.52e-93

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: 281.45  E-value: 2.52e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 311 YFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNT 390
Cdd:cd09107    1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 391 DPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQS 470
Cdd:cd09107   81 DPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQSTKIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVSLVINDP 160

                        170       180
                 ....*....|....*....|...
gi 815890872 471 pgaqpagaTVQEQLRQLFERDWS 493
Cdd:cd09107  161 --------AIVQQLKDVFERDWN 175
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 311-497 2.61e-79

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: 246.03  E-value: 2.61e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 311 YFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNT 390
Cdd:cd09147    1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 391 DPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGN-HSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQ 469
Cdd:cd09147   81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVPADEaQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSALVVNQ 160

                        170       180
                 ....*....|....*....|....*...
gi 815890872 470 SPGAqpAGATVQEQLRQLFERDWSSRYA 497
Cdd:cd09147  161 TGRS--ASGTLQSQLQAVFERDWDSPYS 186
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 104-275 1.10e-61

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: 199.79  E-value: 1.10e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 104 VLVESIPQDLPSAAGSPSAQPLGQAWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAV 183
Cdd:cd09144    1 VLVESIPEGLVFNSSSTINPSIYQAWLNLISAAQSSLDIASFYWTLTNSDTHTQEPSANQGEQILKKLGQLSQSGVYVRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 184 ATSSPTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCSHLAQD 263
Cdd:cd09144   81 AVDKPADPKPMEDINALSSYGADVRMVDMRKLTTGVLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVYNCSCLAED 160

                        170
                 ....*....|..
gi 815890872 264 LEKTFQTYWVLG 275
Cdd:cd09144  161 LGKIFEAYWYLG 172
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 105-257 1.18e-57

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: 188.61  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 105 LVESIPQDLPSAAGSpSAQPLGQAWLQLLDTAQESVHVASYYWSLTGPDIGvNDSSSQLGEALLQKLQQLLGRNISLAVA 184
Cdd:cd09106    1 LVESIPEGLTFLSSS-SHLSTFEAWMELISSAKKSIDIASFYWNLRGTDTN-PDSSAQEGEDIFNALLEAAKRGVKIRIL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815890872 185 TSSPTLARTSTDLQVLAARG-AHVRQVPMGRL-TRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNC 257
Cdd:cd09106   79 QDKPSKDKPDEDDLELAALGgAEVRSLDFTKLiGGGVLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 311-500 1.41e-55

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: 184.29  E-value: 1.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 311 YFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNT 390
Cdd:cd09149    1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 391 DPTMFPYLRSLQALSNPAANVSVDVKVFIVPVgnHSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQS 470
Cdd:cd09149   81 DPLTFNFVSSLKSLCTEQANCSLEVKFFDLEE--ESDCTSPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVGLVINQA 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 815890872 471 PGAQPAGATVQEQLRQLFERDWSSRYAVGL 500
Cdd:cd09149  159 DGVEENNATIIEQLRAAFERDWYSNYAKSL 188
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 105-501 6.00e-43

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 156.36  E-value: 6.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 105 LVESIPQDLPSAAGSPSAQplgQAWLQLLDTAQESVHVASYYWSLTGPDIGVnDSSSQLGEALLQklqqllGRNISLAVA 184
Cdd:PHA03003  15 IVETLPKSLGIATQHMSTY---ECFDEIISQAKKYIYIASFCCNLRSTPEGR-LILDKLKEAAES------GVKVTILVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 185 TSSPTlaRTSTDLqvlaaRGAHVR--QVPMGRLTR-GVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGavIYN-CSHL 260
Cdd:PHA03003  85 EQSGD--KDEEEL-----QSSNINyiKVDIGKLNNvGVLLGSFWVSDDRRCYIGNASLTGGSISTIKTLG--VYStYPPL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 261 AQDLEKTFQTYWVLGVPKAVLPKTWPQ---NFSSHFNRFQPFHGLFdgvpttayFSASPPALCPQGRTRDLEALLAVMGS 337
Cdd:PHA03003 156 ATDLRRRFDTFKAFNKNKSVFNRLCCAcclPVSTKYHINNPIGGVF--------FSDSPEHLLGYSRTLDADVVLHKIKS 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 338 AQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQAL-SNPAanvsVDVK 416
Cdd:PHA03003 228 AKKSIDLELLSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQALcVGND----LSVK 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 417 VFIVPvgnhsnipfsrvNHSKFM-VTEKAAYIGTSNWSEDYFSSTAGVGLvvtqspgaqpagATVQEQL----RQLFERD 491
Cdd:PHA03003 304 VFRIP------------NNTKLLiVDDEFAHITSANFDGTHYLHHAFVSF------------NTIDKELvkelSAIFERD 359

                        410
                 ....*....|
gi 815890872 492 WSSRYAVGLD 501
Cdd:PHA03003 360 WTSSYSKPLK 369
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 104-274 3.67e-38

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: 137.30  E-value: 3.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 104 VLVESIPQDLPSAAGSPSAQPLGQAWLQLLDTAQESVHVASYYWsltgpDIGVNDSSSQLGEALLQKLQQLLGRNISLAV 183
Cdd:cd09146    1 ALVENIPDGINFSEHAPPHLPLSQGWMNLLDMAVKSVEIVSPLW-----DLNASHPSACQGQRLFERLLGLASRGVELKI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 184 ATSsptLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCSHLAQD 263
Cdd:cd09146   76 VSG---ITDSTEVLVLLKKKGAEVHYVNMTALTKGRLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSCLALD 152

                        170
                 ....*....|.
gi 815890872 264 LEKTFQTYWVL 274
Cdd:cd09146  153 LHRVFALYWSL 163
PLDc_3 pfam13918
PLD-like domain;
243-421 6.16e-36

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 131.67  E-value: 6.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  243 SLTQVKELGAVIYNCSHLAQDLEKTFQTYWVLGVPKAVlPKTWPQNFSSHFNRFQPFHGLFDGVPTTAYFSASPPALCPQ 322
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIFENKV-PFTWSKRLCCAVDNEKALNFHLNESGGGAFFSDSPELFCGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  323 GRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQ 402
Cdd:pfam13918  80 NRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARSLD 159

                         170
                  ....*....|....*....
gi 815890872  403 ALSNPAANVSVDVKVFIVP 421
Cdd:pfam13918 160 AFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 107-501 1.18e-19

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: 90.39  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 107 ESIPQDLPSAAGSpSAQPLG------QAWLQLLDTAQESVHVASYYWSLtgPDIGvndssSQLGEAllqklqqllgrnis 180
Cdd:COG1502    3 APLAAGLPLVGGN-RVTLLVdgdeafAALLEAIEAARRSIDLEYYIFDD--DEVG-----RRLADA-------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 181 LAVAT-----------SSPTLARTSTDLQVLAARGAHVRQ-VPMGRLTR---GVLHSKFWVVDGRHIYMGSANMDWRSLT 245
Cdd:COG1502   61 LIAAArrgvkvrvlldGIGSRALNRDFLRRLRAAGVEVRLfNPVRLLFRrlnGRNHRKIVVIDGRVAFVGGANITDEYLG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 246 QVKELGAvIYNCSHL-----AQDLEKTFQTYWvlgvpkavlpktwpqNFSSHFNRFQPFHglfdGVPTTAYFSASPPAlc 320
Cdd:COG1502  141 RDPGFGP-WRDTHVRiegpaVADLQAVFAEDW---------------NFATGEALPFPEP----AGDVRVQVVPSGPD-- 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 321 pqGRTRDLE-ALLAVMGSAQEFIYAsVMEYFPTTRfshpprywpVLDNALRAAAfGKGVRVRLLVGcGLNTDPTMFPYLR 399
Cdd:COG1502  199 --SPRETIErALLAAIASARRRIYI-ETPYFVPDR---------SLLRALIAAA-RRGVDVRILLP-AKSDHPLVHWASR 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 400 S-LQALsnpaanVSVDVKVFIVPVGnhsnipfsrVNHSKFMVT-EKAAYIGTSNWseDYFSSTAG--VGLVVTqspgaqp 475
Cdd:COG1502  265 SyYEEL------LEAGVRIYEYEPG---------FLHAKVMVVdDEWALVGSANL--DPRSLRLNfeVNLVIY------- 320

                        410       420
                 ....*....|....*....|....*.
gi 815890872 476 aGATVQEQLRQLFERDWSSRYAVGLD 501
Cdd:COG1502  321 -DPEFAAQLRARFEEDLAHSREVTLE 345
PLDc_2 pfam13091
PLD-like domain;
331-492 1.26e-12

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 65.01  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  331 LLAVMGSAQEFIYASVMeYFPTTRFshpprywpvLDNALRAAAfGKGVRVRLLVGcGLNTDPTMFPYLRSLQALSNPAAN 410
Cdd:pfam13091   1 LIDLINSAKKSIDIATY-YFVPDRE---------IIDALIAAA-KRGVDVRIILD-SNKDDAGGPKKASLKELRSLLRAG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  411 vsVDVKVFivpvgnhsnIPFSRVNHSKFMVT-EKAAYIGTSNWSEDYFSSTAGVGLVVTqspgaqpaGATVQEQLRQLFE 489
Cdd:pfam13091  69 --VEIREY---------QSFLRSMHAKFYIIdGKTVIVGSANLTRRALRLNLENNVVIK--------DPELAQELEKEFD 129


                  ...
gi 815890872  490 RDW 492
Cdd:pfam13091 130 RLW 132
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 127-254 6.41e-12

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: 62.53  E-value: 6.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 127 QAWLQLLDTAQESVHVASYYWSLTGPDIGVNDsssqLGEALlqklqqllGRNISLAVATSSPTLARTSTDLQVLAA---R 203
Cdd:cd00138    1 EALLELLKNAKESIFIATPNFSFNSADRLLKA----LLAAA--------ERGVDVRLIIDKPPNAAGSLSAALLEAllrA 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 815890872 204 GAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVI 254
Cdd:cd00138   69 GVNVRSYVTPPHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 200-287 1.59e-11

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


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 65.73  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 200 LAARGAHVRqvpmgRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQTYWvlGVPKA 279
Cdd:COG1502  270 LLEAGVRIY-----EYEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYD-PEFAAQLRARFEEDL--AHSRE 341


                 ....*...
gi 815890872 280 VLPKTWPQ 287
Cdd:COG1502  342 VTLEEWRK 349
PLDc_2 pfam13091
PLD-like domain;
130-272 2.48e-11

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 61.15  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872  130 LQLLDTAQESVHVASYYWsLTGPDIGvndssSQLGEALLQklqqllGRNISL---AVATSSPTLA-RTSTDLQVLAARGA 205
Cdd:pfam13091   2 IDLINSAKKSIDIATYYF-VPDREII-----DALIAAAKR------GVDVRIildSNKDDAGGPKkASLKELRSLLRAGV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815890872  206 HVRqVPMGRLTRgvLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQTYW 272
Cdd:pfam13091  70 EIR-EYQSFLRS--MHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEFDRLW 132
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 329-492 4.31e-09

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 54.97  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 329 EALLAVMGSAQE--FIYASVMEYFPttrfshpprywPVLDnALRAAAfGKGVRVRLLVgcglntdPTMFPYLRSLQALSN 406
Cdd:cd09128   13 EALLALIDSAEEslLIQNEEMGDDA-----------PILD-ALVDAA-KRGVDVRVLL-------PSAWSAEDERQARLR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 407 PAANVSVDVKVFIVPVGNHsnipfsrvnHSKFMV-TEKAAYIGTSNWSEDYFSSTAGVGLVVTQSPGAQpagatvqeQLR 485
Cdd:cd09128   73 ALEGAGVPVRLLKDKFLKI---------HAKGIVvDGKTALVGSENWSANSLDRNREVGLIFDDPEVAA--------YLQ 135


                 ....*..
gi 815890872 486 QLFERDW 492
Cdd:cd09128  136 AVFESDW 142
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 218-243 7.92e-09

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 50.85  E-value: 7.92e-09
                           10        20
                   ....*....|....*....|....*.
gi 815890872   218 GVLHSKFWVVDGRHIYMGSANMDWRS 243
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 329-453 9.63e-09

Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D (PLD) superfamily proteins. The PLD superfamily is composed of a large and diverse group of proteins including plant, mammalian and bacterial PLDs, bacterial cardiolipin (CL) synthases, bacterial phosphatidylserine synthases (PSS), eukaryotic phosphatidylglycerophosphate (PGP) synthase, eukaryotic tyrosyl-DNA phosphodiesterase 1 (Tdp1), and some bacterial endonucleases (Nuc and BfiI), among others. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze the transphosphatidylation of phospholipids to acceptor alcohols. The majority of members in this superfamily contain a short conserved sequence motif (H-x-K-x(4)-D, where x represents any amino acid residue), called the HKD signature motif. There are varying expanded forms of this motif in different family members. Some members contain variant HKD motifs. Most PLD enzymes are monomeric proteins with two HKD motif-containing domains. Two HKD motifs from two domains form a single active site. Some PLD enzymes have only one copy of the HKD motif per subunit but form a functionally active dimer, which has a single active site at the dimer interface containing the two HKD motifs from both subunits. Different PLD enzymes may have evolved through domain fusion of a common catalytic core with separate substrate recognition domains. Despite their various catalytic functions and a very broad range of substrate specificities, the diverse group of PLD enzymes can bind to a phosphodiester moiety. Most of them are active as bi-lobed monomers or dimers, and may possess similar core structures for catalytic activity. They are generally thought to utilize a common two-step ping-pong catalytic mechanism, involving an enzyme-substrate intermediate, to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 53.29  E-value: 9.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 329 EALLAVMGSAQEFIYAsvmeyfptTRFSHPPRYWPVLDNALRAAAfGKGVRVRLLVGCGlntdPTMFPYLRSLQALSNPA 408
Cdd:cd00138    1 EALLELLKNAKESIFI--------ATPNFSFNSADRLLKALLAAA-ERGVDVRLIIDKP----PNAAGSLSAALLEALLR 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 815890872 409 ANVSVdvkVFIVPVGNhsnipFSRVNHSKFMVTEKA-AYIGTSNWS 453
Cdd:cd00138   68 AGVNV---RSYVTPPH-----FFERLHAKVVVIDGEvAYVGSANLS 105
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
 200-268 2.77e-08

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: 53.64  E-value: 2.77e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815890872 200 LAARGAHVRQvpmgrLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTF 268
Cdd:cd09112   78 LLKAGVKIYE-----YNKGFLHSKTLIVDDEIASVGTANLDIRSFELNFEVNAVIYD-KEVAKKLEEIF 140
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 218-243 9.67e-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: 47.80  E-value: 9.67e-08
                          10        20
                  ....*....|....*....|....*.
gi 815890872  218 GVLHSKFWVVDGRHIYMGSANMDWRS 243
Cdd:pfam00614   3 GRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 217-269 2.07e-07

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: 51.00  E-value: 2.07e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 815890872 217 RGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYnCSHLAQDLEKTFQ 269
Cdd:cd09159   90 PSMLHAKTAVIDGDWATVGSSNLDPRSLRLNLEANLVVE-DPAFAAQLEELFE 141
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 201-288 6.36e-07

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: 50.30  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 201 AARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYN---CSHLAQDLEKTFQT--YWVLG 275
Cdd:cd09113   98 PDAAKRKRLRGLFGSSRASLHAKSFVIDDRLVFVGSFNLDPRSAYLNTEMGLVIDSpelAAQLRAAMEEDLAPsaYWVLL 177

                         90
                 ....*....|...
gi 815890872 276 VPKAVLPKTWPQN 288
Cdd:cd09113  178 LDDGGLVWETEED 190
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 329-491 2.24e-06

Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; Putative catalytic domain, repeat 1, of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze transphosphatidylation of phospholipids to acceptor alcohols. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197225 [Multi-domain]  Cd Length: 141  Bit Score: 47.26  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 329 EALLAVMGSAQEFIYASVMEyfpttrFSHPPrywpvLDNALRAAAfGKGVRVRLLVgcglntDPTMFPYLRSLQALSNPA 408
Cdd:cd09127   11 APVVDAIASAKRSILLKMYE------FTDPA-----LEKALAAAA-KRGVRVRVLL------EGGPVGGISRAEKLLDYL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 409 ANVSVDVKVfivpvgNHSNIPFsRVNHSKFMVT-EKAAYIGTSNWSEDYFSSTAGVGLVVTQspgaqpagATVQEQLRQL 487
Cdd:cd09127   73 NEAGVEVRW------TNGTARY-RYTHAKYIVVdDERALVLTENFKPSGFTGTRGFGVVTDD--------PAVVAEIADV 137


                 ....
gi 815890872 488 FERD 491
Cdd:cd09127  138 FDAD 141
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 190-256 9.68e-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: 46.10  E-value: 9.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815890872 190 LARTSTdLQVLAARGAHVRqvpmgRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYN 256
Cdd:cd09162   69 LARGSY-LRDLQEAGAEIY-----LYQPGMLHAKAVVVDDKLALVGSANLDMRSLFLNYEVAVFFYS 129
PLDc_SMU_988_like_2 cd09160
Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 ...
 216-268 1.41e-05

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: 45.57  E-value: 1.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 815890872 216 TRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCSHLA---QDLEKTF 268
Cdd:cd09160   89 TPGFIHAKTFVSDDKAAVVGTINLDYRSLYLHFECGVYMYDTPVISdikEDFEETL 144
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
 221-255 5.31e-05

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: 43.44  E-value: 5.31e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 815890872 221 HSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIY 255
Cdd:cd09105  111 HSKVVIVDDEWATVGSANLNRRSMTWDTELNLAVV 145
PLDc_CLS_unchar2_2 cd09163
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 221-270 6.25e-05

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: 43.70  E-value: 6.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 815890872 221 HSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYnCSHLAQDLEKTFQT 270
Cdd:cd09163   94 HSKLMVVDGAWALIGSANWDPRSLRLNFELNLEVY-DTALAGQLDALFDS 142
cls PRK01642
cardiolipin synthetase; Reviewed
 214-271 6.32e-05

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 45.54  E-value: 6.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 815890872 214 RLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQTY 271
Cdd:PRK01642 394 RYEGGLLHTKSVLVDDELALVGTVNLDMRSFWLNFEITLVIDD-TGFAADLAAMQEDY 450
COG3886 COG3886
HKD family nuclease [Replication, recombination and repair];
364-454 1.84e-04

HKD family nuclease [Replication, recombination and repair];


Pssm-ID: 443094 [Multi-domain]  Cd Length: 941  Bit Score: 44.20  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 364 VLDNALRAAAfGKGVRVRLLVGCGLN-TDPTMfpyLRSLQALSNpaanvsVDVKVFivpvgNHSNIPFsrvnHSK---FM 439
Cdd:COG3886   59 LLLDALKELL-ERGVKGRILTSTYLGfTEPKA---LRELLDLPN------IEVRVS-----YDRKTRF----HAKayiFE 119

                         90
                 ....*....|....*.
gi 815890872 440 VTEKA-AYIGTSNWSE 454
Cdd:COG3886  120 RTGYGtAIIGSSNLTR 135
PRK12452 PRK12452
cardiolipin synthase;
217-269 2.61e-04

cardiolipin synthase;


Pssm-ID: 171510 [Multi-domain]  Cd Length: 509  Bit Score: 43.37  E-value: 2.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 815890872 217 RGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQ 269
Cdd:PRK12452 423 DGFMHAKIVLVDDKIATIGTANMDVRSFELNYEIISVLYE-SETVHDIKRDFE 474
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
 329-492 2.86e-04

Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic domain, repeat 1, of bacterial cardiolipin (CL) synthase and a few homologs found in eukaryotes and archaea. Bacterial CL synthases catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. The monomer of bacterial CL synthase consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. Bacterial CL synthases can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily. Like other PLD enzymes, bacterial CL synthases utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197209 [Multi-domain]  Cd Length: 154  Bit Score: 41.31  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 329 EALLAVMGSAQEFIYasvMEYF------PTTRFShpprywpvldNALRAAAfGKGVRVRLLV---GCgLNTDPTMFPYLR 399
Cdd:cd09110    8 PALLEAIRAARHSIH---LEYYifrddeIGRRFR----------DALIEKA-RRGVEVRLLYdgfGS-LGLSRRFLRELR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 400 slqalsnpAANvsVDVKVFIVPVGNHSNIPFSRVNHSKFMVT-EKAAYIGTSNWSEDYFSSTAG------VGLVVTqspg 472
Cdd:cd09110   73 --------EAG--VEVRAFNPLSFPLFLLRLNYRNHRKILVIdGKIAFVGGFNIGDEYLGKDPGfgpwrdTHVRIE---- 138

                        170       180
                 ....*....|....*....|
gi 815890872 473 aqpaGATVqEQLRQLFERDW 492
Cdd:cd09110  139 ----GPAV-ADLQAAFLEDW 153
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 195-272 3.05e-04

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 41.11  E-value: 3.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815890872 195 TDLQVLAARGAHVRQVPMGRLTrgvLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQTYW 272
Cdd:cd09128   69 ARLRALEGAGVPVRLLKDKFLK---IHAKGIVVDGKTALVGSENWSANSLDRNREVGLIFDD-PEVAAYLQAVFESDW 142
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 130-270 3.12e-04

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: 40.74  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 130 LQLLDTAQESVHVASYywSLTGPDIG--VNDSSSQlgeallqklqqllGRNISLAVATSSPTLARTSTDLQVLAARGAHV 207
Cdd:cd09116   15 VALIANAKSSIDVAMY--ALTDPEIAeaLKRAAKR-------------GVRVRIILDKDSLADNLSITLLALLSNLGIPV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815890872 208 RQVPmgrlTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQT 270
Cdd:cd09116   80 RTDS----GSKLMHHKFIIIDGKIVITGSANWTKSGFHRNDENLLIIDD-PKLAASFEEEFNR 137
bac_cardiolipin TIGR04265
cardiolipin synthase; This model is based on experimentally characterized bacterial ...
 217-271 3.33e-04

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: 43.24  E-value: 3.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 815890872  217 RGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCShLAQDLEKTFQTY 271
Cdd:TIGR04265 397 NGFLHSKSVLVDDEIASVGTANMDMRSFWLNFEVNAFIYDKG-FAKDLAAAYDDD 450
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 430-456 1.34e-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: 36.21  E-value: 1.34e-03
                           10        20
                   ....*....|....*....|....*...
gi 815890872   430 FSRVNHSKFMVTE-KAAYIGTSNWSEDY 456
Cdd:smart00155   1 YDGVLHTKLMIVDdEIAYIGSANLDGRS 28
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 367-457 1.62e-03

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


Pssm-ID: 197210 [Multi-domain]  Cd Length: 162  Bit Score: 39.44  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 367 NALRAAAfGKGVRVRLLVGcGLNTDPtMFPYLRSLQALSNpaanvsVDVKVFiVPVGNHSNIP------FSRVN---HSK 437
Cdd:cd09111   40 GELLEAA-DRGVRVRLLLD-DLGTSG-RDRLLAALDAHPN------IEVRLF-NPFRNRGGRLlefltdFSRLNrrmHNK 109

                         90       100
                 ....*....|....*....|.
gi 815890872 438 -FMVTEKAAYIGTSNWSEDYF 457
Cdd:cd09111  110 lFIVDGAVAIVGGRNIGDEYF 130
PLDc_Nuc_like_unchar1_1 cd09172
Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, ...
 127-245 1.75e-03

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: 38.88  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 127 QAWLQLLDTAQESVHVASYywSLTGPDIgvndsssqlgeALLQKLQQLLGRNISLAVATSSPTLARTSTDlQVLAARGAH 206
Cdd:cd09172   12 LAFLDEARSAGSSIRLAIY--ELDDPEI-----------IDALKAAKDRGVRVRIILDDSSVTGDPTEES-AAATLSKGP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 815890872 207 VRQVpMGRLTRGVLHSKFWVVDG----RHIYMGSANMDWRSLT 245
Cdd:cd09172   78 GALV-KRRHSSGLMHNKFLVVDRkdgpNRVLTGSTNFTTSGLY 119
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 220-268 2.37e-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: 38.48  E-value: 2.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 815890872 220 LHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIyNCSHLAQDLEKTF 268
Cdd:cd09131   93 THTKLVVIDGRTVYVGSHNWTYSALDYNHEASVLI-ESPEVADFAINYF 140
PLDc_EcCLS_like_2 cd09158
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins; ...
 218-271 7.01e-03

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: 37.55  E-value: 7.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 815890872 218 GVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQTY 271
Cdd:cd09158   91 GLLHAKTVTVDDEVALVGSSNFDIRSFALNFEISLILYD-KEFTAQLRAIQERY 143
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 130-269 7.89e-03

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: 36.86  E-value: 7.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890872 130 LQLLDTAQESVHVASYywSLTGPDIgvndsSSQLGEALlqklqqllGRNISLAV-ATSSPT--LARTSTDLQVLAARGAH 206
Cdd:cd09127   14 VDAIASAKRSILLKMY--EFTDPAL-----EKALAAAA--------KRGVRVRVlLEGGPVggISRAEKLLDYLNEAGVE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815890872 207 VRQVPmGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNcSHLAQDLEKTFQ 269
Cdd:cd09127   79 VRWTN-GTARYRYTHAKYIVVDDERALVLTENFKPSGFTGTRGFGVVTDD-PAVVAEIADVFD 139
 
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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