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Conserved domains on  [gi|90111207|ref|NP_415564|]
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cardiolipin synthase C [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

phospholipase D family protein( domain architecture ID 10173503)

phospholipase D (PLD) family protein similar to Escherichia coli cardiolipin synthase C that catalyzes the synthesis of cardiolipin from phosphatidylglycerol and phosphatidylethanolamine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 250-469 5.60e-102

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: 303.76  E-value: 5.60e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 250 LSDDPAKGEGKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYA 329
Cdd:cd09113   1 LSDPPEKALKEAGPEPVLAYQLAELLKNAKREVLIVSPYFVPGDEGVALLAELARRGVRVRILTNSLAATDVPAVHSGYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 330 RWRKKLLRYGVELYELKPTREQSSTLhdRGITGNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQ 409
Cdd:cd09113  81 RYRKRLLKAGVELYELKPDAAKRKRL--RGLFGSSRASLHAKSFVIDDRLVFVGSFNLDPRSAYLNTEMGLVIDSPELAA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 410 LIDKRFIQSQYDAAWQLRLDRWGRINWVDRHAKKEIILKKEPATSFWKRVMVRLASILPV 469
Cdd:cd09113 159 QLRAAMEEDLAPSAYWVLLLDDGGLVWETEEDGKEKEYDSEPETSFWRRLGAWLLSLLPI 218
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 24-184 3.74e-85

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: 258.62  E-value: 3.74e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  24 LEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVR 103
Cdd:cd09111   1 LEDGLDALAARLALIRSAERSIDLQYYIWHDDESGRLLLGELLEAADRGVRVRLLLDDLGTSGRDRLLAALDAHPNIEVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 104 LFNPFSFRLLRPLGYITDFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPLFSDLDVMAIGPVVEDVADDFARY 183
Cdd:cd09111  81 LFNPFRNRGGRLLEFLTDFSRLNRRMHNKLFIVDGAVAIVGGRNIGDEYFGASPEVNFRDLDVLAVGPVVRQLSESFDTY 160


                .
gi 90111207 184 W 184
Cdd:cd09111 161 W 161
 
Name Accession Description Interval E-value
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 250-469 5.60e-102

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: 303.76  E-value: 5.60e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 250 LSDDPAKGEGKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYA 329
Cdd:cd09113   1 LSDPPEKALKEAGPEPVLAYQLAELLKNAKREVLIVSPYFVPGDEGVALLAELARRGVRVRILTNSLAATDVPAVHSGYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 330 RWRKKLLRYGVELYELKPTREQSSTLhdRGITGNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQ 409
Cdd:cd09113  81 RYRKRLLKAGVELYELKPDAAKRKRL--RGLFGSSRASLHAKSFVIDDRLVFVGSFNLDPRSAYLNTEMGLVIDSPELAA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 410 LIDKRFIQSQYDAAWQLRLDRWGRINWVDRHAKKEIILKKEPATSFWKRVMVRLASILPV 469
Cdd:cd09113 159 QLRAAMEEDLAPSAYWVLLLDDGGLVWETEEDGKEKEYDSEPETSFWRRLGAWLLSLLPI 218
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 24-184 3.74e-85

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: 258.62  E-value: 3.74e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  24 LEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVR 103
Cdd:cd09111   1 LEDGLDALAARLALIRSAERSIDLQYYIWHDDESGRLLLGELLEAADRGVRVRLLLDDLGTSGRDRLLAALDAHPNIEVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 104 LFNPFSFRLLRPLGYITDFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPLFSDLDVMAIGPVVEDVADDFARY 183
Cdd:cd09111  81 LFNPFRNRGGRLLEFLTDFSRLNRRMHNKLFIVDGAVAIVGGRNIGDEYFGASPEVNFRDLDVLAVGPVVRQLSESFDTY 160


                .
gi 90111207 184 W 184
Cdd:cd09111 161 W 161
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 10-436 1.48e-83

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: 262.19  E-value: 1.48e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  10 PLCSQHPGQCG--LFPLEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGL 87
Cdd:COG1502   4 PLAAGLPLVGGnrVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAARRGVKVRVLLDGIGSRAL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  88 D-DILRLLDShPRIEVRLFNPFSFRllrplgyitdFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPL-FSDLD 165
Cdd:COG1502  84 NrDFLRRLRA-AGVEVRLFNPVRLL----------FRRLNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpWRDTH 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 166 VMAIGPVVEDVADDFARYWYCKSvsplqqvldvpegemADRIELPAswhndamthrylrkmesspfinhlvdgtlPLIWA 245
Cdd:COG1502 153 VRIEGPAVADLQAVFAEDWNFAT---------------GEALPFPE-----------------------------PAGDV 188

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 246 KTRLLSDDPakgegkAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNslAANDVAVVH 325
Cdd:COG1502 189 RVQVVPSGP------DSPRETIERALLAAIASARRRIYIETPYFVPDRSLLRALIAAARRGVDVRILLP--AKSDHPLVH 260

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 326 AGYARWRKKLLRYGVELYELKPtreqsstlhdrgitgnsgASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESE 405
Cdd:COG1502 261 WASRSYYEELLEAGVRIYEYEP------------------GFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDP 322

                       410       420       430
                ....*....|....*....|....*....|.
gi 90111207 406 TLAQLIDKRFiQSQYDAAWQLRLDRWGRINW 436
Cdd:COG1502 323 EFAAQLRARF-EEDLAHSREVTLEEWRKRPL 352
PLDc_2 pfam13091
PLD-like domain;
271-415 1.60e-29

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 112.00  E-value: 1.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   271 LFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYARWRKkLLRYGVELYELKPTRE 350
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPDREIIDALIAAAKRGVDVRIILDSNKDDAGGPKKASLKELRS-LLRAGVEIREYQSFLR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111207   351 qsstlhdrgitgnsgaSLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRF 415
Cdd:pfam13091  80 ----------------SMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKDPELAQELEKEF 128
cls PRK01642
cardiolipin synthetase; Reviewed
 29-464 1.05e-21

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 97.54  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   29 DAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDD---NNTPGLDDILRLLDSHprIEVRLF 105
Cdd:PRK01642 126 ETFQAIIRDIELARHYILMEFYIWRPDGLGDQVAEALIAAAKRGVRVRLLYDSigsFAFFRSPYPEELRNAG--VEVVEF 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  106 NPFS-FRLLRplgyitdfSRLNRRMHNKSFTVDGVVTLVGGRNIGD-AYFgaGEEPLFS---DLDVMAIGPVVEDVADDF 180
Cdd:PRK01642 204 LKVNlGRVFR--------RRLDLRNHRKIVVIDGYIAYTGSMNVVDpEYF--KQDPGVGqwrDTHVRIEGPVVTALQLIF 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  181 ARYWYCksvsplqqvldvpegeMADRIELPASWHNDAMTHRYLRkmesspfiNHLVdgtlpliwaktRLLSDDPAKGEGK 260
Cdd:PRK01642 274 AEDWEW----------------ETGERILPPPPDVLIMPFEEAS--------GHTV-----------QVIASGPGDPEET 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  261 AKrhsllpQRLFDIMGSPSERIDIISSYFVPTRAgVAQLLRM-VRKGVKIAILTNSLaaNDVAVV-HAGYARWRkKLLRY 338
Cdd:PRK01642 319 IH------QFLLTAIYSARERLWITTPYFVPDED-LLAALKTaALRGVDVRIIIPSK--NDSLLVfWASRAFFT-ELLEA 388

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  339 GVELYELKPtreqsstlhdrGItgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESET----LAQLIDKR 414
Cdd:PRK01642 389 GVKIYRYEG-----------GL-------LHTKSVLVDDELALVGTVNLDMRSFWLNFEITLVIDDTGfaadLAAMQEDY 450

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 90111207  415 FIQSQydaawQLRLDRWGRinwvdrhakkeiilkkepaTSFWKRVMVRLA 464
Cdd:PRK01642 451 FARSR-----ELDLEEWRK-------------------RPLWQRIAERVA 476
bac_cardiolipin TIGR04265
cardiolipin synthase; This model is based on experimentally characterized bacterial ...
 29-408 1.67e-19

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: 91.01  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207    29 DAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLD----DILRLLDshprIEVRL 104
Cdd:TIGR04265 129 DVYDALIQDIKNARHYIHLEYYIWQPDGLGDQILESLMAKAKQGVHVRILYDDVGSVALFkswpELFRNAG----GEVVA 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   105 FNPFSFRLLrplgyitdFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGageeplfsdldvmaigpvvedvADDFARYW 184
Cdd:TIGR04265 205 FFPVKLPLL--------NLRMNNRNHRKIIVIDGQIGYVGGFNIGDEYLG----------------------KDAKFGYW 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   185 ycksvspLQQVLDVpEGEMADRIELPAS--WHNDamTHRylRKMESSPFINHLVDGTlpliwaktrlLSDDPAK--GEGK 260
Cdd:TIGR04265 255 -------RDTHLRI-EGDAVTALQLIFIldWNSQ--TGR--RIIPYDPDYFPMPNEQ----------AGGHGIQiiASGP 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   261 AKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSlaANDVAVVHAGYARWRKKLLRYGV 340
Cdd:TIGR04265 313 DFPWEQIKYGYLKMIYSAKKSIYIQSPYFIPDDDLLHAIKIAALSGVDVSIMIPN--KPDHPLVFWASRSNFTELLAAGV 390

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111207   341 ELYElkptreqsstlHDRGItgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLA 408
Cdd:TIGR04265 391 KIYQ-----------YENGF-------LHSKSVLVDDEIASVGTANMDMRSFWLNFEVNAFIYDKGFA 440
PLDc_2 pfam13091
PLD-like domain;
36-184 8.91e-08

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 50.75  E-value: 8.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207    36 RLAEMAEHTLDVQYYIWQDDmsgRLLFSALLAAAKRGVRVRLLLDDNNT-------PGLDDILRLLDSHprIEVRLFNPF 108
Cdd:pfam13091   3 DLINSAKKSIDIATYYFVPD---REIIDALIAAAKRGVDVRIILDSNKDdaggpkkASLKELRSLLRAG--VEIREYQSF 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111207   109 sfrllrplgyitdfsrlNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEplfsdLDVMAIGP-VVEDVADDFARYW 184
Cdd:pfam13091  78 -----------------LRSMHAKFYIIDGKTVIVGSANLTRRALRLNLE-----NNVVIKDPeLAQELEKEFDRLW 132
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 364-391 2.95e-06

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: 43.53  E-value: 2.95e-06
                           10        20
                   ....*....|....*....|....*...
gi 90111207    364 SGASLHAKTFSIDGKTVFIGSFNFDPRS 391
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 250-469 5.60e-102

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: 303.76  E-value: 5.60e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 250 LSDDPAKGEGKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYA 329
Cdd:cd09113   1 LSDPPEKALKEAGPEPVLAYQLAELLKNAKREVLIVSPYFVPGDEGVALLAELARRGVRVRILTNSLAATDVPAVHSGYA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 330 RWRKKLLRYGVELYELKPTREQSSTLhdRGITGNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQ 409
Cdd:cd09113  81 RYRKRLLKAGVELYELKPDAAKRKRL--RGLFGSSRASLHAKSFVIDDRLVFVGSFNLDPRSAYLNTEMGLVIDSPELAA 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 410 LIDKRFIQSQYDAAWQLRLDRWGRINWVDRHAKKEIILKKEPATSFWKRVMVRLASILPV 469
Cdd:cd09113 159 QLRAAMEEDLAPSAYWVLLLDDGGLVWETEEDGKEKEYDSEPETSFWRRLGAWLLSLLPI 218
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 24-184 3.74e-85

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: 258.62  E-value: 3.74e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  24 LEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVR 103
Cdd:cd09111   1 LEDGLDALAARLALIRSAERSIDLQYYIWHDDESGRLLLGELLEAADRGVRVRLLLDDLGTSGRDRLLAALDAHPNIEVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 104 LFNPFSFRLLRPLGYITDFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPLFSDLDVMAIGPVVEDVADDFARY 183
Cdd:cd09111  81 LFNPFRNRGGRLLEFLTDFSRLNRRMHNKLFIVDGAVAIVGGRNIGDEYFGASPEVNFRDLDVLAVGPVVRQLSESFDTY 160


                .
gi 90111207 184 W 184
Cdd:cd09111 161 W 161
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 10-436 1.48e-83

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: 262.19  E-value: 1.48e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  10 PLCSQHPGQCG--LFPLEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGL 87
Cdd:COG1502   4 PLAAGLPLVGGnrVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAARRGVKVRVLLDGIGSRAL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  88 D-DILRLLDShPRIEVRLFNPFSFRllrplgyitdFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPL-FSDLD 165
Cdd:COG1502  84 NrDFLRRLRA-AGVEVRLFNPVRLL----------FRRLNGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpWRDTH 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 166 VMAIGPVVEDVADDFARYWYCKSvsplqqvldvpegemADRIELPAswhndamthrylrkmesspfinhlvdgtlPLIWA 245
Cdd:COG1502 153 VRIEGPAVADLQAVFAEDWNFAT---------------GEALPFPE-----------------------------PAGDV 188

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 246 KTRLLSDDPakgegkAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNslAANDVAVVH 325
Cdd:COG1502 189 RVQVVPSGP------DSPRETIERALLAAIASARRRIYIETPYFVPDRSLLRALIAAARRGVDVRILLP--AKSDHPLVH 260

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 326 AGYARWRKKLLRYGVELYELKPtreqsstlhdrgitgnsgASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESE 405
Cdd:COG1502 261 WASRSYYEELLEAGVRIYEYEP------------------GFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYDP 322

                       410       420       430
                ....*....|....*....|....*....|.
gi 90111207 406 TLAQLIDKRFiQSQYDAAWQLRLDRWGRINW 436
Cdd:COG1502 323 EFAAQLRARF-EEDLAHSREVTLEEWRKRPL 352
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
 264-467 1.51e-34

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: 127.21  E-value: 1.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 264 HSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVaVVHAGYARWrKKLLRYGVELY 343
Cdd:cd09112   9 WSSIEQAYLKAINSAKKSIYIQTPYFIPDESLLEALKTAALSGVDVRIMIPGKPDHKL-VYWASRSYF-EELLKAGVKIY 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 344 ELKptreqsstlhdrgitgnsGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRFIQSQYDAa 423
Cdd:cd09112  87 EYN------------------KGFLHSKTLIVDDEIASVGTANLDIRSFELNFEVNAVIYDKEVAKKLEEIFEEDLKDS- 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 90111207 424 wqlrldrwgrinwvdrhakKEIILKKEPATSFWKRVMVRLASIL 467
Cdd:cd09112 148 -------------------ELLTLEEWRKRSLWKRFKESLARLL 172
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
 29-185 1.03e-33

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: 124.13  E-value: 1.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  29 DAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGL-DDILRLLDSHpRIEVRLFNP 107
Cdd:cd09110   5 EFFPALLEAIRAARHSIHLEYYIFRDDEIGRRFRDALIEKARRGVEVRLLYDGFGSLGLsRRFLRELREA-GVEVRAFNP 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111207 108 FSFRLLrplgyitdFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPL-FSDLDVMAIGPVVEDVADDFARYWY 185
Cdd:cd09110  84 LSFPLF--------LLRLNYRNHRKILVIDGKIAFVGGFNIGDEYLGKDPGFGpWRDTHVRIEGPAVADLQAAFLEDWY 154
PLDc_2 pfam13091
PLD-like domain;
271-415 1.60e-29

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 112.00  E-value: 1.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   271 LFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYARWRKkLLRYGVELYELKPTRE 350
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPDREIIDALIAAAKRGVDVRIILDSNKDDAGGPKKASLKELRS-LLRAGVEIREYQSFLR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111207   351 qsstlhdrgitgnsgaSLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRF 415
Cdd:pfam13091  80 ----------------SMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKDPELAQELEKEF 128
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 275-439 5.11e-26

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: 103.77  E-value: 5.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 275 MGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILtnsLAAN--DVAVVHAGYARWRKkLLRYGVELYELKPTReqs 352
Cdd:cd09159  20 IAAARRRIWIANAYFVPDRRLRRALIEAARRGVDVRLL---LPGKsdDPLTVAASRALYGK-LLRAGVRIFEYQPSM--- 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 353 stlhdrgitgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRFIQSQYDAAwQLRLDRWG 432
Cdd:cd09159  93 ---------------LHAKTAVIDGDWATVGSSNLDPRSLRLNLEANLVVEDPAFAAQLEELFEEDLARSR-EITLEEWR 156


                ....*..
gi 90111207 433 RINWVDR 439
Cdd:cd09159 157 RRPLWQR 163
cls PRK01642
cardiolipin synthetase; Reviewed
 29-464 1.05e-21

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 97.54  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   29 DAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDD---NNTPGLDDILRLLDSHprIEVRLF 105
Cdd:PRK01642 126 ETFQAIIRDIELARHYILMEFYIWRPDGLGDQVAEALIAAAKRGVRVRLLYDSigsFAFFRSPYPEELRNAG--VEVVEF 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  106 NPFS-FRLLRplgyitdfSRLNRRMHNKSFTVDGVVTLVGGRNIGD-AYFgaGEEPLFS---DLDVMAIGPVVEDVADDF 180
Cdd:PRK01642 204 LKVNlGRVFR--------RRLDLRNHRKIVVIDGYIAYTGSMNVVDpEYF--KQDPGVGqwrDTHVRIEGPVVTALQLIF 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  181 ARYWYCksvsplqqvldvpegeMADRIELPASWHNDAMTHRYLRkmesspfiNHLVdgtlpliwaktRLLSDDPAKGEGK 260
Cdd:PRK01642 274 AEDWEW----------------ETGERILPPPPDVLIMPFEEAS--------GHTV-----------QVIASGPGDPEET 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  261 AKrhsllpQRLFDIMGSPSERIDIISSYFVPTRAgVAQLLRM-VRKGVKIAILTNSLaaNDVAVV-HAGYARWRkKLLRY 338
Cdd:PRK01642 319 IH------QFLLTAIYSARERLWITTPYFVPDED-LLAALKTaALRGVDVRIIIPSK--NDSLLVfWASRAFFT-ELLEA 388

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  339 GVELYELKPtreqsstlhdrGItgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESET----LAQLIDKR 414
Cdd:PRK01642 389 GVKIYRYEG-----------GL-------LHTKSVLVDDELALVGTVNLDMRSFWLNFEITLVIDDTGfaadLAAMQEDY 450

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 90111207  415 FIQSQydaawQLRLDRWGRinwvdrhakkeiilkkepaTSFWKRVMVRLA 464
Cdd:PRK01642 451 FARSR-----ELDLEEWRK-------------------RPLWQRIAERVA 476
bac_cardiolipin TIGR04265
cardiolipin synthase; This model is based on experimentally characterized bacterial ...
 29-408 1.67e-19

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: 91.01  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207    29 DAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLD----DILRLLDshprIEVRL 104
Cdd:TIGR04265 129 DVYDALIQDIKNARHYIHLEYYIWQPDGLGDQILESLMAKAKQGVHVRILYDDVGSVALFkswpELFRNAG----GEVVA 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   105 FNPFSFRLLrplgyitdFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGageeplfsdldvmaigpvvedvADDFARYW 184
Cdd:TIGR04265 205 FFPVKLPLL--------NLRMNNRNHRKIIVIDGQIGYVGGFNIGDEYLG----------------------KDAKFGYW 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   185 ycksvspLQQVLDVpEGEMADRIELPAS--WHNDamTHRylRKMESSPFINHLVDGTlpliwaktrlLSDDPAK--GEGK 260
Cdd:TIGR04265 255 -------RDTHLRI-EGDAVTALQLIFIldWNSQ--TGR--RIIPYDPDYFPMPNEQ----------AGGHGIQiiASGP 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   261 AKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSlaANDVAVVHAGYARWRKKLLRYGV 340
Cdd:TIGR04265 313 DFPWEQIKYGYLKMIYSAKKSIYIQSPYFIPDDDLLHAIKIAALSGVDVSIMIPN--KPDHPLVFWASRSNFTELLAAGV 390

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111207   341 ELYElkptreqsstlHDRGItgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLA 408
Cdd:TIGR04265 391 KIYQ-----------YENGF-------LHSKSVLVDDEIASVGTANMDMRSFWLNFEVNAFIYDKGFA 440
PRK12452 PRK12452
cardiolipin synthase;
29-446 5.32e-19

cardiolipin synthase;


Pssm-ID: 171510 [Multi-domain]  Cd Length: 509  Bit Score: 89.59  E-value: 5.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   29 DAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVRLFNPF 108
Cdd:PRK12452 150 QTFSEILQAIEQAKHHIHIQYYIYKSDEIGTKVRDALIKKAKDGVIVRFLYDGLGSNTLRRRFLQPMKEAGIEIVEFDPI 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  109 SFRLLrplgyitdFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEE-PLFSDLDVMAIGPVVEDVADDFARYWYCK 187
Cdd:PRK12452 230 FSAWL--------LETVNYRNHRKIVIVDGEIGFTGGLNVGDEYLGRSKKfPVWRDSHLKVEGKALYKLQAIFLEDWLYA 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  188 SvsplqqvldvpegemadrIELPASWHNDAMTHRYLRKMESSPfinhlVDGTLPLIWAKTRllSDDPakgegkAKRHSLL 267
Cdd:PRK12452 302 S------------------SGLNTYSWDPFMNRQYFPGKEISN-----AEGAVQIVASGPS--SDDK------SIRNTLL 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  268 PqrlfdIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNslAANDVAVVHAGYARWRKKLLRYGVELYELKp 347
Cdd:PRK12452 351 A-----VMGSAKKSIWIATPYFIPDQETLTLLRLSAISGIDVRILYP--GKSDSIISDQASQSYFTPLLKAGASIYSYK- 422

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  348 treqsstlhdRGItgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTE-MGFVIESETLAQLidKRFIQSQYDAAWQL 426
Cdd:PRK12452 423 ----------DGF-------MHAKIVLVDDKIATIGTANMDVRSFELNYEiISVLYESETVHDI--KRDFEDDFKHSTEI 483

                        410       420
                 ....*....|....*....|
gi 90111207  427 rldRWGriNWVDRHAKKEII 446
Cdd:PRK12452 484 ---KWN--AFQKRSIKKRIL 498
PLDc_EcCLS_like_2 cd09158
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins; ...
 259-431 5.22e-17

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: 78.39  E-value: 5.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 259 GKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTrAGVAQLLRM-VRKGVKIAILTNslAANDVAVVHAGYARWRKKLLR 337
Cdd:cd09158   4 GPDYPTENIPQLLLSAIHAARRRVVITTPYFVPD-ESLLQALCTaALRGVEVTLILP--AKNDSFLVGAASRSYYEELLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 338 YGVELYELKPtreqsstlhdrGItgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKrfIQ 417
Cdd:cd09158  81 AGVKIYLYRG-----------GL-------LHAKTVTVDDEVALVGSSNFDIRSFALNFEISLILYDKEFTAQLRA--IQ 140

                       170
                ....*....|....*
gi 90111207 418 SQY-DAAWQLRLDRW 431
Cdd:cd09158 141 ERYlARSDPLTLEEW 155
PLDc_CLS_unchar1_1 cd09156
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 29-184 1.59e-16

Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin synthase; Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197253 [Multi-domain]  Cd Length: 154  Bit Score: 76.53  E-value: 1.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  29 DAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVRLFNPF 108
Cdd:cd09156   5 EAYQALIQLIESAKHSIDVCTFILGDDATGRRVIDALARKAREGVEVRLLLDALGSFFLSRRALKKLRAAGGKVAFFMPV 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111207 109 sFRLLRPlgyitdfSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGE-EPLFSDLDVMAIGPVVEDVADDFARYW 184
Cdd:cd09156  85 -FRLPFR-------GRTNLRNHRKIAIADGSTAISGGMNLANEYMGPEPdDGRWVDLSFLIEGPAVAQYQEVFRSDW 153
PLDc_PaCLS_like_1 cd09155
Putative catalytic domain, repeat 1, of Pseudomonas aeruginosa cardiolipin synthase and ...
 29-185 2.28e-15

Putative catalytic domain, repeat 1, of Pseudomonas aeruginosa cardiolipin synthase and similar proteins; Putative catalytic domain, repeat 1, of Pseudomonas aeruginosa cardiolipin (CL) synthase (PaCLS) and similar proteins. Although PaCLS and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, PaCLS and other members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197252 [Multi-domain]  Cd Length: 156  Bit Score: 73.43  E-value: 2.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  29 DAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDD--ILRLLDSHprIEVRLFN 106
Cdd:cd09155   5 ATFAAIFEAIASAEEYILVQFYIIRDDDLGRELKDALIARAQAGVRVYLLYDEIGSHSLSRsyIERLRKAG--VEVSAFN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 107 PFSFRLLRplgyitdFsRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFgaGEEPLFS---DLDVMAIGPVVEDVADDFARY 183
Cdd:cd09155  83 TTRGWGNR-------F-QLNFRNHRKIVVVDGQTAFVGGHNVGDEYL--GRDPRLGpwrDTHVKLEGPAVQQLQLSFAED 152


                ..
gi 90111207 184 WY 185
Cdd:cd09155 153 WY 154
PLDc_EcCLS_like_1 cd09152
Catalytic domain, repeat 1, of Escherichia coli cardiolipin synthase and similar proteins; ...
 41-185 1.69e-12

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


Pssm-ID: 197250 [Multi-domain]  Cd Length: 163  Bit Score: 65.31  E-value: 1.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  41 AEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDD--NNTPGLDDILRLLdSHPRIEVRLFNPFSFRLLRplgy 118
Cdd:cd09152  24 AKHHVHLLFYIWADDGTGDRVAEALERAAKRGVTCRLLLDAvgSRAFFRSSLWKRL-REAGVEVVEALPLRLFRRR---- 98

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111207 119 itdFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAgEEPLFSDLDVMA--IGPVVEDVADDFARYWY 185
Cdd:cd09152  99 ---LARFDLRNHRKIAVIDGRIAYTGSQNIIDPEFFK-KAGGGPWVDLMVrvEGPVVSQLQAVFASDWY 163
PLDc_CLS_unchar2_1 cd09157
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 41-185 3.38e-12

Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin synthase; Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197254 [Multi-domain]  Cd Length: 155  Bit Score: 64.12  E-value: 3.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  41 AEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTP-GLDDILRLLDSHPrIEVRLFNPfsFRLLRPLGYI 119
Cdd:cd09157  17 ARHSIALSSYIFDNDGVGREFVDALAEAVARGVDVRVLIDGVGARySRPSIRRRLRRAG-VPVARFLP--PRLPPRLPFI 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111207 120 tdfsrlNRRMHNKSFTVDGVVTLVGGRNIGDAYF--GAGEEPlFSDLDVMAIGPVVEDVADDFARYWY 185
Cdd:cd09157  94 ------NLRNHRKILVVDGRTGFTGGMNIRDGHLvaDDPKNP-VQDLHFRVEGPVVAQLQEVFAEDWY 154
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 270-424 1.05e-10

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 59.60  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 270 RLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDvavvhAGYARWRKKLLRYGVELYELKPTR 349
Cdd:cd09128  14 ALLALIDSAEESLLIQNEEMGDDAPILDALVDAAKRGVDVRVLLPSAWSAE-----DERQARLRALEGAGVPVRLLKDKF 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111207 350 EQsstlhdrgitgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQlidkrFIQSQYDAAW 424
Cdd:cd09128  89 LK----------------IHAKGIVVDGKTALVGSENWSANSLDRNREVGLIFDDPEVAA-----YLQAVFESDW 142
PLDc_CLS_unchar2_2 cd09163
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 280-465 1.70e-10

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


Pssm-ID: 197260 [Multi-domain]  Cd Length: 176  Bit Score: 59.88  E-value: 1.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 280 ERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNslAANDVAVVHagYAR----WRkkLLRYGVELYElkptreqsstl 355
Cdd:cd09163  25 HSIRIMTPYFLPDRTLITALQAAALRGVEVDIVLP--ERNNLPLVD--WAMranlWE--LLEHGVRIYL----------- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 356 hdrgitgNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRFIQSqydaawqlrldrwgrin 435
Cdd:cd09163  88 -------QPPPFDHSKLMVVDGAWALIGSANWDPRSLRLNFELNLEVYDTALAGQLDALFDSK----------------- 143

                       170       180       190
                ....*....|....*....|....*....|...
gi 90111207 436 wvdRHAKKEIILKKEPATSFWKRV---MVRLAS 465
Cdd:cd09163 144 ---IAKSREVTLEELDARPLPIRLrdaAARLFS 173
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 280-423 2.36e-10

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


Pssm-ID: 197259 [Multi-domain]  Cd Length: 172  Bit Score: 59.20  E-value: 2.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 280 ERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILT----NSLAANdvavvhagYARWR--KKLLRYGVELYELKPtreqss 353
Cdd:cd09162  25 HRIWIVTPYFVPDEVLLRALRLAARRGVDVRLIVpkrsNHRIAD--------LARGSylRDLQEAGAEIYLYQP------ 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 354 tlhdrgitgnsgASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKrFIQSQYDAA 423
Cdd:cd09162  91 ------------GMLHAKAVVVDDKLALVGSANLDMRSLFLNYEVAVFFYSPADIKELSD-WIESLISQC 147
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 269-402 7.05e-10

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


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 56.76  E-value: 7.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 269 QRLFDIMGSPSERIDIISSYFVPTRAG--VAQLLRMVRKGVKIAILTNSlaANDVAVVHAgyARWRKKLLRYGVELYELK 346
Cdd:cd00138   1 EALLELLKNAKESIFIATPNFSFNSADrlLKALLAAAERGVDVRLIIDK--PPNAAGSLS--AALLEALLRAGVNVRSYV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111207 347 PTREQSSTLHdrgitgnsgaslhAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVI 402
Cdd:cd00138  77 TPPHFFERLH-------------AKVVVIDGEVAYVGSANLSTASAAQNREAGVLV 119
PRK11263 PRK11263
cardiolipin synthase ClsB;
41-410 3.40e-08

cardiolipin synthase ClsB;


Pssm-ID: 236888 [Multi-domain]  Cd Length: 411  Bit Score: 55.34  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   41 AEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDD--ILRLLDSHPRieVRLFNPFSfrllRPLGY 118
Cdd:PRK11263  30 AQEEILLETFILFEDKVGKQLHAALLAAAQRGVKVEVLVDGYGSPDLSDefVNELTAAGVR--FRYFDPRP----RLLGM 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  119 itdfsRLN--RRMHNKSFTVDGVVTLVGGRNI-GDAYFGAGEEPLfSDLDVMAIGPVVEDVAdDFARywycksvsplqqv 195
Cdd:PRK11263 104 -----RTNlfRRMHRKIVVIDGRIAFVGGINYsADHLSDYGPEAK-QDYAVEVEGPVVADIH-QFEL------------- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  196 ldvpegemadrielpASWHNDAMTHRYLRKMESSPFINHLVDGTLPLIWAKTRLLSDDpakgegkAKRHSLLPQRlfdim 275
Cdd:PRK11263 164 ---------------EALPGQSAARRWWRRHHRAEENRQPGEAQALLVWRDNEEHRDD-------IERHYLKALR----- 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  276 gSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIA-ILTnslAANDVAVVHAGYARWRKKLLRYGVELYELKptreqsst 354
Cdd:PRK11263 217 -QARREVIIANAYFFPGYRLLRALRNAARRGVRVRlILQ---GEPDMPIVRVGARLLYNYLLKGGVQIYEYC-------- 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 90111207  355 lhDRgitgnsgaSLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQL 410
Cdd:PRK11263 285 --RR--------PLHGKVALMDDHWATVGSSNLDPLSLSLNLEANLIIRDRAFNQT 330
PLDc_2 pfam13091
PLD-like domain;
36-184 8.91e-08

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 50.75  E-value: 8.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207    36 RLAEMAEHTLDVQYYIWQDDmsgRLLFSALLAAAKRGVRVRLLLDDNNT-------PGLDDILRLLDSHprIEVRLFNPF 108
Cdd:pfam13091   3 DLINSAKKSIDIATYYFVPD---REIIDALIAAAKRGVDVRIILDSNKDdaggpkkASLKELRSLLRAG--VEIREYQSF 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111207   109 sfrllrplgyitdfsrlNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEplfsdLDVMAIGP-VVEDVADDFARYW 184
Cdd:pfam13091  78 -----------------LRSMHAKFYIIDGKTVIVGSANLTRRALRLNLE-----NNVVIKDPeLAQELEKEFDRLW 132
PLDc_PaCLS_like_2 cd09161
Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin synthase and ...
 280-469 7.93e-07

Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin synthase and similar proteins; Putative catalytic domain, repeat 2, of Pseudomonas aeruginosa cardiolipin (CL) synthase (PaCLS) and similar proteins. Although PaCLS and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, PaCLS and other members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197258 [Multi-domain]  Cd Length: 176  Bit Score: 49.21  E-value: 7.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 280 ERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVaVVHAGYArWRKKLLRYGVELYELKPtreqsstlhdrg 359
Cdd:cd09161  25 KRLWIASPYFVPDEGVLAALQLAALRGVDVRILIPERPDHLL-VYLASFS-YLPELIRAGVKVYRYQP------------ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 360 itgnsgASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRFiQSQYDAAWQLRLDrwgrinwvDR 439
Cdd:cd09161  91 ------GFLHQKVVLVDDELAAVGTANLDNRSFRLNFEITALVADPGFAQEVEAML-EADFAASREVTAA--------EL 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 90111207 440 HAKkeiilkkepatSFWKRVMVRLASIL-PV 469
Cdd:cd09161 156 ANR-----------PLWFRLGARVARLFaPI 175
PLDc_SMU_988_like_2 cd09160
Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 ...
 251-439 1.48e-06

Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins; Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins. Although SMU_988 and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197257 [Multi-domain]  Cd Length: 176  Bit Score: 48.26  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 251 SDDPAKGEGKAKRHSLlpqrlfDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAanDVAVVHAGYAR 330
Cdd:cd09160   2 GDSPLDNEPVGENVYL------DLINQAKDYVYITTPYLILDDEMLDALCLAAKRGVDVRIITPHIP--DKKYVFLVTRS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 331 WRKKLLRYGVELYELKPtreqsstlhdrGItgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMG-FVIESETLAQ 409
Cdd:cd09160  74 NYPELLEAGVKIYEYTP-----------GF-------IHAKTFVSDDKAAVVGTINLDYRSLYLHFECGvYMYDTPVISD 135

                       170       180       190
                ....*....|....*....|....*....|...
gi 90111207 410 L---IDKRFIQSQydaawQLRLDRWGRINWVDR 439
Cdd:cd09160 136 IkedFEETLAQSQ-----EITLEECRKRSLVTR 163
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 269-415 1.79e-06

Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar proteins; Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), and similar proteins. Nuc is an endonuclease from Salmonella typhimurium and the smallest known member of the PLD superfamily. It cleaves both single- and double-stranded DNA. PLD6 selectively hydrolyzes the terminal phosphodiester bond of phosphatidylcholine (PC), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLD6 also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which is essential for catalysis. PLDs utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. This subfamily also includes some uncharacterized hypothetical proteins, which have two HKD motifs in a single polypeptide chain.


Pssm-ID: 197215 [Multi-domain]  Cd Length: 138  Bit Score: 47.29  E-value: 1.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 269 QRLFDIMGSPSERIDIiSSYFVPTRAGVAQLLRMVRKGVKIAILTNslaandvavvhagyaRWRKKLLRYGVELYELKPT 348
Cdd:cd09116  12 RLIVALIANAKSSIDV-AMYALTDPEIAEALKRAAKRGVRVRIILD---------------KDSLADNLSITLLALLSNL 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111207 349 REQSSTLHDRGItgnsgasLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRF 415
Cdd:cd09116  76 GIPVRTDSGSKL-------MHHKFIIIDGKIVITGSANWTKSGFHRNDENLLIIDDPKLAASFEEEF 135
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 364-391 2.95e-06

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: 43.53  E-value: 2.95e-06
                           10        20
                   ....*....|....*....|....*...
gi 90111207    364 SGASLHAKTFSIDGKTVFIGSFNFDPRS 391
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_CDP-OH_P_transf_II_2 cd09103
Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members; ...
 259-414 3.33e-06

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


Pssm-ID: 197202 [Multi-domain]  Cd Length: 184  Bit Score: 47.61  E-value: 3.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 259 GKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAAND--------VAVVHAgyar 330
Cdd:cd09103   8 GLGKRGNILNRTIEQLITSAESKIILCTPYFNLPQALMRDILRLLKRGVKVEIIVGDKTANDfyippeepFKVIGA---- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 331 wrkklLRYgveLYE--LKPTREQSSTLHDRG-----ITGNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIE 403
Cdd:cd09103  84 -----LPY---LYEinLRRFAKRLQKYIDQGqlnvrLWKDGDNSFHLKGIWVDDRYTLLTGNNLNPRAWRLDLENGLLIH 155

                       170
                ....*....|.
gi 90111207 404 SETlAQLIDKR 414
Cdd:cd09103 156 DPQ-KQLQQQL 165
PLDc_Nuc cd09170
Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar ...
 269-430 4.15e-06

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


Pssm-ID: 197267 [Multi-domain]  Cd Length: 142  Bit Score: 46.36  E-value: 4.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 269 QRLFDIMGSPSERIDIISSYFvpTRAGVAQ-LLRMVRKGVKIAILTNSLAANdvavvhAGYARWRKkLLRYGVELYelkp 347
Cdd:cd09170  14 ELILDVIDSARRSIDVAAYSF--TSPPIARaLIAAKKRGVDVRVVLDKSQAG------GKYSALNY-LANAGIPVR---- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 348 treqsstlhdrgITGNSGAsLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESE-TLAQlidkrfiqsQYDAAWQL 426
Cdd:cd09170  81 ------------IDDNYAI-MHNKVMVIDGKTVITGSFNFTASAEKRNAENLLVIRNPpELAQ---------QYLQEWQR 138


                ....
gi 90111207 427 RLDR 430
Cdd:cd09170 139 RWAQ 142
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 355-417 2.05e-05

Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic domain of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. Members of this subfamily contain one copy of HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily.


Pssm-ID: 197229 [Multi-domain]  Cd Length: 143  Bit Score: 44.25  E-value: 2.05e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111207 355 LHDRGIT---GNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRFIQ 417
Cdd:cd09131  77 LKDNGVEvrfDSPSVTTHTKLVVIDGRTVYVGSHNWTYSALDYNHEASVLIESPEVADFAINYFDS 142
PLDc_SMU_988_like_1 cd09154
Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 ...
 70-153 4.72e-05

Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins; Putative catalytic domain, repeat 1, 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: 197251 [Multi-domain]  Cd Length: 155  Bit Score: 43.67  E-value: 4.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  70 KRGVRVRLLLDD-----NNTPGLDDILRLLDshprIEVRLFNPFsfrllRPLgyitDFSRLNRRMHNKSFTVDGVVTLVG 144
Cdd:cd09154  47 KEGVEVRIMYDDfgsitTLPKDYPKELEKIG----IKCRVFNPF-----KPI----LSLYMNNRDHRKITVIDGKVAFTG 113


                ....*....
gi 90111207 145 GRNIGDAYF 153
Cdd:cd09154 114 GINLADEYI 122
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 268-415 6.36e-05

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: 43.02  E-value: 6.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 268 PQRLFDIMGSPSERIDIISSYFVPTRAGVAqLLRMVRKGVKIAILTNSLAandvavvHAGYARWRK---KLLRYGVELYE 344
Cdd:cd09127  10 VAPVVDAIASAKRSILLKMYEFTDPALEKA-LAAAAKRGVRVRVLLEGGP-------VGGISRAEKlldYLNEAGVEVRW 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90111207 345 LKPTreqsstlhdrgitgNSGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVIESETLAQLIDKRF 415
Cdd:cd09127  82 TNGT--------------ARYRYTHAKYIVVDDERALVLTENFKPSGFTGTRGFGVVTDDPAVVAEIADVF 138
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 274-403 8.94e-05

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: 42.62  E-value: 8.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 274 IMGSPSERIDIISSYF------VPTRAGVAQ-------LLRMVRKGVKIAILTNSlAANDVAVVHAGYArwrkkLLRYGV 340
Cdd:cd09106  27 LISSAKKSIDIASFYWnlrgtdTNPDSSAQEgedifnaLLEAAKRGVKIRILQDK-PSKDKPDEDDLEL-----AALGGA 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111207 341 ELYELKPTReqsstlhdrgitGNSGASLHAKTFSIDGKTVFIGSFNFDPRStlLNT--EMGFVIE 403
Cdd:cd09106 101 EVRSLDFTK------------LIGGGVLHTKFWIVDGKHFYLGSANLDWRS--LTQvkELGVYIY 151
PLDc_unchar4 cd09132
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 269-402 9.35e-05

Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic domain of uncharacterized phospholipase D (PLD, EC 3.1.4.4)-like proteins. Members of this subfamily contain one copy of HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily.


Pssm-ID: 197230 [Multi-domain]  Cd Length: 122  Bit Score: 41.88  E-value: 9.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 269 QRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYARWRKKLLRygVELYELKpt 348
Cdd:cd09132   2 QVLLELIEGAERSLLIVGYSAYKVSELLQALAAALERGVQVRVVVESSEKAGSVLSLDEDELMWPKLAG--ATLYVWP-- 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 90111207 349 REQSSTLHdrgitgnsgASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVI 402
Cdd:cd09132  78 EKKRPGKR---------ASLHAKVIVADRRRLLVTSANLTGAGMERNIEAGVLV 122
PLDc_Bfil_DEXD_like cd09117
Catalytic domain of type II restriction endonucleases BfiI and NgoFVII, and uncharacterized ...
 268-402 1.37e-04

Catalytic domain of type II restriction endonucleases BfiI and NgoFVII, and uncharacterized proteins with a DEAD domain; Catalytic domain of type II restriction endonucleases BfiI and NgoFVII, uncharacterized type III restriction endonuclease Res subunit, and uncharacterized DNA/RNA helicase superfamily II members. Proteins in this family are found mainly in prokaryotes. They contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in a single polypeptide chain, and have been classified as members of the phospholipase D (PLD, EC 3.1.4.4) superfamily. BfiI consists of two discrete domains with distinct functions: an N-terminal catalytic domain with non-specific nuclease activity and dimerization function that is more closely related to Nuc, an EDTA-resistant nuclease from the phospholipase D (PLD) superfamily; and a C-terminal domain that specifically recognizes its target sequences, 5'-ACTGGG-3'. BfiI forms a functionally active homodimer which has two DNA-binding surfaces located at the C-terminal domains but only one active site, located at the dimer interface between the two N-terminal catalytic domains that contain the two HKD motifs from both subunits. BfiI utilizes a single active site to cut both DNA strands, which represents a novel mechanism for the scission of double-stranded DNA. It uses a histidine residue from the HKD motif in one subunit as the nucleophile for the cleavage of the target phosphodiester bond in both of the anti-parallel DNA strands, while the symmetrically-related histidine residue from the HKD motif of the opposite subunit acts as the proton donor/acceptor during both strand-scission events.


Pssm-ID: 197216 [Multi-domain]  Cd Length: 117  Bit Score: 41.23  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 268 PQRLFDIMGSPSERIDIISSYFvpTRAGVAQLLRMVRKGVKIAILTNSLAANDVAVVHAGYARwrKKLLRYGVELYELKP 347
Cdd:cd09117   3 LEELLTRLIERADTIRIAVAFA--SAGGAIKLLDKFREGKKIRLIVGLDFGGTSPADFALKLL--LALGNLNVRIFDAGP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111207 348 TreqsstlhdrgitgnsgasLHAKTFSI---DGKTVFIGSFNFDPRSTLLNTEMGFVI 402
Cdd:cd09117  79 L-------------------LHAKLYLFendDPTRAIVGSANLTQGGLSGNIEAAVVI 117
PLDc_PMFPLD_like_2 cd09109
Catalytic domain, repeat 2, of phospholipase D from Streptomyces Sp. Strain PMF and similar ...
 368-425 1.82e-04

Catalytic domain, repeat 2, of phospholipase D from Streptomyces Sp. Strain PMF and similar proteins; Catalytic domain, repeat 2, of phospholipases D (PLD, EC 3.1.4.4) from Streptomyces Sp. Strain PMF (PMFPLD) and similar proteins, which are generally extracellular and bear N-terminal signal sequences. PMFPLD hydrolyzes the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. It also catalyzes a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. In contrast to eukaryotic PLDs, PMFPLD has a compact structure, which consists of two catalytic domains, but lacks the regulatory domains. Each catalytic domain contains one copy of the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. Two HKD motifs from two domains form a single active site. Like other PLD enzymes, PMFPLD may 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. A calcium-dependent PLD from Streptomyce chromofuscus is excluded from this family, since it displays very little sequence homology with other Streptomyces PLDs. Moreover, it does not contain the conserved HKD motif and hydrolyzes the phospholipids via a different mechanism.


Pssm-ID: 197208  Cd Length: 212  Bit Score: 42.66  E-value: 1.82e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 90111207 368 LHAKTFSIDGKTVFIGSFNFDPRStllNTEMGFVIESETLAQLIDKRFiqsqYDAAWQ 425
Cdd:cd09109 160 LHAKLVIVDGKLFYIGSDNLYPSW---LQEFGYIVEDPDAAKQLEDGY----LDPLWK 210
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 71-153 2.30e-04

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: 41.85  E-value: 2.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  71 RGVRVRLLL-DDNNT-PGLDDILRLLDS------HPRIEVRLFN-PfsfrlLRPLGYItDFSRLNrrmHNKSFTVDGVVt 141
Cdd:cd09107  66 RGVKVRLLVsNWKHTdPSMDAFLKSLQLlksgvgNGDIEVKIFTvP-----GDQSTKI-PFARVN---HAKYMVTDERA- 135

                        90
                ....*....|..
gi 90111207 142 LVGGRNIGDAYF 153
Cdd:cd09107 136 YIGTSNWSGDYF 147
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 36-147 3.67e-04

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: 40.19  E-value: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  36 RLAEMAEHTLDVQYYIWQDDmSGRLLFSALLAAAKRGVRVRLLLDDNNT--PGLDDILRLLDSHPRIEVRLFNpfsfrll 113
Cdd:cd00138   5 ELLKNAKESIFIATPNFSFN-SADRLLKALLAAAERGVDVRLIIDKPPNaaGSLSAALLEALLRAGVNVRSYV------- 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 90111207 114 rplgyitDFSRLNRRMHNKSFTVDGVVTLVGGRN 147
Cdd:cd00138  77 -------TPPHFFERLHAKVVVIDGEVAYVGSAN 103
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 29-153 5.41e-04

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


Pssm-ID: 197225 [Multi-domain]  Cd Length: 141  Bit Score: 40.32  E-value: 5.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  29 DAFAARYRLAEMAEHTLDVQYYIWQDdmsgRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLD--SHPRIEVRLFN 106
Cdd:cd09127   8 DGVAPVVDAIASAKRSILLKMYEFTD----PALEKALAAAAKRGVRVRVLLEGGPVGGISRAEKLLDylNEAGVEVRWTN 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 90111207 107 PfSFRLlrplgyitdfsrlnRRMHNKSFTVDGVVTLVGGRNIGDAYF 153
Cdd:cd09127  84 G-TARY--------------RYTHAKYIVVDDERALVLTENFKPSGF 115
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 298-421 8.88e-04

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: 40.28  E-value: 8.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207 298 QLLRMVRKGVKIAILTNSLAANDVAVVHAGYARWR------KKLLRYGVELYELK--PTREQSST----LHDRGITGN-- 363
Cdd:cd09145  27 KLLDMAQEQVHVASYYWSLTGEDIGVNDSSSLPGEdilkelAELLSRNVSVRAAAsiPTLAANSTdlkiLRQKGAHVRkv 106

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111207 364 -----SGASLHAKTFSIDGKTVFIGSFNFDPRSTLLNTEMGFVI-ESETLAQLIDKRFiQSQYD 421
Cdd:cd09145 107 nfgrlTGGVLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIyNCSSLAKDLHKTF-QTYWV 169
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 367-391 1.93e-03

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: 35.47  E-value: 1.93e-03
                          10        20
                  ....*....|....*....|....*
gi 90111207   367 SLHAKTFSIDGKTVFIGSFNFDPRS 391
Cdd:pfam00614   4 RLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_PMFPLD_like_1 cd09108
Catalytic domain, repeat 1, of phospholipase D from Streptomyces Sp. Strain PMF and similar ...
 130-179 7.72e-03

Catalytic domain, repeat 1, of phospholipase D from Streptomyces Sp. Strain PMF and similar proteins; Catalytic domain, repeat 1, of phospholipases D (PLD, EC 3.1.4.4) from Streptomyces Sp. Strain PMF (PMFPLD) and similar proteins, which are generally extracellular and bear N-terminal signal sequences. PMFPLD hydrolyzes the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. It also catalyzes a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. In contrast to eukaryotic PLDs, PMFPLD has a compact structure, which consists of two catalytic domains, but lacks the regulatory domains. Each catalytic domain contains one copy of the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the PLD superfamily. Two HKD motifs from two domains form a single active site. Like other PLD enzymes, PMFPLD may 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. A calcium-dependent PLD from Streptomyce chromofuscus is excluded from this family, since it displays very little sequence homology with other Streptomyces PLDs. Moreover, it does not contain the conserved HKD motif and hydrolyzes the phospholipids via a different mechanism.


Pssm-ID: 197207 [Multi-domain]  Cd Length: 210  Bit Score: 37.80  E-value: 7.72e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 90111207 130 HNKSFTVDGVVTLVGGRNIGDAYFGAGEEPLfSDLDVMAIGPVVED---VADD 179
Cdd:cd09108 157 HAKLLVVDGEELLTGGYNLWDDHYLDGGNPV-HDLSLVVRGPAARSgvrFFDD 208
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 70-147 7.82e-03

Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar proteins; Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), and similar proteins. Nuc is an endonuclease from Salmonella typhimurium and the smallest known member of the PLD superfamily. It cleaves both single- and double-stranded DNA. PLD6 selectively hydrolyzes the terminal phosphodiester bond of phosphatidylcholine (PC), with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLD6 also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which is essential for catalysis. PLDs utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. This subfamily also includes some uncharacterized hypothetical proteins, which have two HKD motifs in a single polypeptide chain.


Pssm-ID: 197215 [Multi-domain]  Cd Length: 138  Bit Score: 36.89  E-value: 7.82e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111207  70 KRGVRVRLLLD-DNNTPGLDDILRLLDSHPRIEVRlfnpfsfrllrplgyiTDFSRlnRRMHNKSFTVDGVVTLVGGRN 147
Cdd:cd09116  46 KRGVRVRIILDkDSLADNLSITLLALLSNLGIPVR----------------TDSGS--KLMHHKFIIIDGKIVITGSAN 106
PLN02866 PLN02866
phospholipase D
 355-431 8.52e-03

phospholipase D


Pssm-ID: 215467 [Multi-domain]  Cd Length: 1068  Bit Score: 38.98  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207   355 LHDRGITGNSGASLHAKTFSIDGKTVFIGSFNFDPRSTL--LNTEMGFVIESEtlaQLIDKRFIQSQYDA---AWQLRLD 429
Cdd:PLN02866  855 LFEGGPLATSQIYVHSKIMIVDDRAALIGSANINDRSLLgsRDSEIGVVIEDK---EFVDSSMNGKPWKAgkfAHSLRLS 931


                  ..
gi 90111207   430 RW 431
Cdd:PLN02866  932 LW 933
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 33-148 8.65e-03

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 36.87  E-value: 8.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111207  33 ARYRLAEM---AEHTLDVQY-YIWQDDmsgrLLFSALLAAAKRGVRVRLLLDD--NNTPGLDDILRLLDSHPrIEVRLfn 106
Cdd:cd09128  11 AREALLALidsAEESLLIQNeEMGDDA----PILDALVDAAKRGVDVRVLLPSawSAEDERQARLRALEGAG-VPVRL-- 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 90111207 107 pfsfrLLRPLGYitdfsrlnrrMHNKSFTVDGVVTLVGGRNI 148
Cdd:cd09128  84 -----LKDKFLK----------IHAKGIVVDGKTALVGSENW 110
 
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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