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Conserved domains on  [gi|446532648|ref|WP_000609994|]
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phospholipase D family protein [Acinetobacter baumannii]

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 ...
 289-515 1.46e-83

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: 258.30  E-value: 1.46e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 289 VADSPKKILGTATQHEMLYGQVMSIMGKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNSFAANDVAIVHAFYS 368
Cdd:cd09113    1 LSDPPEKALKEAGPEPVLAYQLAELLKNAKREVLIVSPYFVPGDEGVALLAELARRGVRVRILTNSLAATDVPAVHSGYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 369 QYRVEMLKNGIELYEFKPVLERRRRTWyeivtgsviPAKGKNKSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVI 447
Cdd:cd09113   81 RYRKRLLKAGVELYELKPDAAKRKRLR---------GLFGSSRASLHAKSFVIDDRlVFVGSFNLDPRSAYLNTEMGLVI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 448 ESSQLQTQISVMLDQHLPQVAYQLKLNSQGQITWlDYQANGQVIEYDKDPGTSRFQRTMIKAVSYLPI 515
Cdd:cd09113  152 DSPELAAQLRAAMEEDLAPSAYWVLLLDDGGLVW-ETEEDGKEKEYDSEPETSFWRRLGAWLLSLLPI 218
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 63-224 1.26e-80

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: 248.60  E-value: 1.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  63 LDDAFMSIASRIYLIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIR 142
Cdd:cd09111    1 LEDGLDALAARLALIRSAERSIDLQYYIWHDDESGRLLLGELLEAADRGVRVRLLLDDLGTSGRDRLLAALDAHPNIEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 143 LFNPYKFRYLRIFDYLFRFKKVNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKFQFTDMDILFYGHAVRHAQAVFADF 222
Cdd:cd09111   81 LFNPFRNRGGRLLEFLTDFSRLNRRMHNKLFIVDGAVAIVGGRNIGDEYFGASPEVNFRDLDVLAVGPVVRQLSESFDTY 160


                 ..
gi 446532648 223 WE 224
Cdd:cd09111  161 WN 162
 
Name Accession Description Interval E-value
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 289-515 1.46e-83

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: 258.30  E-value: 1.46e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 289 VADSPKKILGTATQHEMLYGQVMSIMGKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNSFAANDVAIVHAFYS 368
Cdd:cd09113    1 LSDPPEKALKEAGPEPVLAYQLAELLKNAKREVLIVSPYFVPGDEGVALLAELARRGVRVRILTNSLAATDVPAVHSGYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 369 QYRVEMLKNGIELYEFKPVLERRRRTWyeivtgsviPAKGKNKSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVI 447
Cdd:cd09113   81 RYRKRLLKAGVELYELKPDAAKRKRLR---------GLFGSSRASLHAKSFVIDDRlVFVGSFNLDPRSAYLNTEMGLVI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 448 ESSQLQTQISVMLDQHLPQVAYQLKLNSQGQITWlDYQANGQVIEYDKDPGTSRFQRTMIKAVSYLPI 515
Cdd:cd09113  152 DSPELAAQLRAAMEEDLAPSAYWVLLLDDGGLVW-ETEEDGKEKEYDSEPETSFWRRLGAWLLSLLPI 218
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 63-224 1.26e-80

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: 248.60  E-value: 1.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  63 LDDAFMSIASRIYLIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIR 142
Cdd:cd09111    1 LEDGLDALAARLALIRSAERSIDLQYYIWHDDESGRLLLGELLEAADRGVRVRLLLDDLGTSGRDRLLAALDAHPNIEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 143 LFNPYKFRYLRIFDYLFRFKKVNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKFQFTDMDILFYGHAVRHAQAVFADF 222
Cdd:cd09111   81 LFNPFRNRGGRLLEFLTDFSRLNRRMHNKLFIVDGAVAIVGGRNIGDEYFGASPEVNFRDLDVLAVGPVVRQLSESFDTY 160


                 ..
gi 446532648 223 WE 224
Cdd:cd09111  161 WN 162
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 64-481 3.72e-77

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: 246.78  E-value: 3.72e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  64 DDAFmsiASRIYLIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRL 143
Cdd:COG1502   24 DEAF---AALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAARRGVKVRVLLDGIGSRALNRDFLRRLRAAGVEVRL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 144 FNPYKFRYLRIfdylfrfkkvNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKF-QFTDMDILFYGHAVRHAQAVFADF 222
Cdd:COG1502  101 FNPVRLLFRRL----------NGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFgPWRDTHVRIEGPAVADLQAVFAED 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 223 WESTlsvnateiigtcaehhlkalrehyeqlhhedhslTEDKLYDAQsylkellehnPIQWSKAHFVADSPkkilgtATQ 302
Cdd:COG1502  171 WNFA----------------------------------TGEALPFPE----------PAGDVRVQVVPSGP------DSP 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 303 HEMLYGQVMSIMGKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNsfAANDVAIVHAFYSQYRVEMLKNGIELY 382
Cdd:COG1502  201 RETIERALLAAIASARRRIYIETPYFVPDRSLLRALIAAARRGVDVRILLP--AKSDHPLVHWASRSYYEELLEAGVRIY 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 383 EFKPvlerrrrtwyeivtgsvipakgknkSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVIESSQLQTQISVMLD 461
Cdd:COG1502  279 EYEP-------------------------GFLHAKVMVVDDEwALVGSANLDPRSLRLNFEVNLVIYDPEFAAQLRARFE 333

                        410       420
                 ....*....|....*....|
gi 446532648 462 QHLpQVAYQLKLNSQGQITW 481
Cdd:COG1502  334 EDL-AHSREVTLEEWRKRPL 352
PRK12452 PRK12452
cardiolipin synthase;
76-451 1.54e-25

cardiolipin synthase;


Pssm-ID: 171510 [Multi-domain]  Cd Length: 509  Bit Score: 109.62  E-value: 1.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  76 LIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPykfrylrIF 155
Cdd:PRK12452 158 AIEQAKHHIHIQYYIYKSDEIGTKVRDALIKKAKDGVIVRFLYDGLGSNTLRRRFLQPMKEAGIEIVEFDP-------IF 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 156 DYLFRFKkVNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKFQF-TDMDILFYGHAVRHAQAVFADFWestlsvnatei 234
Cdd:PRK12452 231 SAWLLET-VNYRNHRKIVIVDGEIGFTGGLNVGDEYLGRSKKFPVwRDSHLKVEGKALYKLQAIFLEDW----------- 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 235 igtcaehhLKAlrehyeqlHHEDHSLTEDKLYDAQSYLKELLEHNPiqwSKAHFVADSPkkilgtATQHEMLYGQVMSIM 314
Cdd:PRK12452 299 --------LYA--------SSGLNTYSWDPFMNRQYFPGKEISNAE---GAVQIVASGP------SSDDKSIRNTLLAVM 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 315 GKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNsfAANDVAIVHAFYSQYRVEMLKNGIELYEFkpvlerrrrt 394
Cdd:PRK12452 354 GSAKKSIWIATPYFIPDQETLTLLRLSAISGIDVRILYP--GKSDSIISDQASQSYFTPLLKAGASIYSY---------- 421

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 395 wyeivtgsvipakgkNKSSLHAKFFDVDGKV-FIGSFNFDPRSTYLNTEVGLVIESSQ 451
Cdd:PRK12452 422 ---------------KDGFMHAKIVLVDDKIaTIGTANMDVRSFELNYEIISVLYESE 464
PLDc_2 pfam13091
PLD-like domain;
314-463 1.67e-16

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 76.18  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  314 MGKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNSFAANDVAIVHAFYSQYRvEMLKNGIELYEFKPVLerrrr 393
Cdd:pfam13091   5 INSAKKSIDIATYYFVPDREIIDALIAAAKRGVDVRIILDSNKDDAGGPKKASLKELR-SLLRAGVEIREYQSFL----- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446532648  394 twyeivtgsvipakgknkSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVIESSQLQTQISVMLDQH 463
Cdd:pfam13091  79 ------------------RSMHAKFYIIDGKtVIVGSANLTRRALRLNLENNVVIKDPELAQELEKEFDRL 131
PLDc_2 pfam13091
PLD-like domain;
74-223 7.06e-12

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 62.69  E-value: 7.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648   74 IYLIRNAKETIDLQ-YYIWTNDFvgnlILHELLKAADRGIKVRLLIDDQNG------IKLDDILRSLLQHtNFEIRLFNP 146
Cdd:pfam13091   2 IDLINSAKKSIDIAtYYFVPDRE----IIDALIAAAKRGVDVRIILDSNKDdaggpkKASLKELRSLLRA-GVEIREYQS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648  147 YkfrylrifdylfrfkkvNHRMHNKLIIADGSIAVTGGRNISSEYFEASskfqfTDMDILFYG-HAVRHAQAVFADFW 223
Cdd:pfam13091  77 F-----------------LRSMHAKFYIIDGKTVIVGSANLTRRALRLN-----LENNVVIKDpELAQELEKEFDRLW 132
PRK11263 PRK11263
cardiolipin synthase ClsB;
77-190 2.91e-10

cardiolipin synthase ClsB;


Pssm-ID: 236888 [Multi-domain]  Cd Length: 411  Bit Score: 62.27  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYIWTNDFVGNLiLHE-LLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPYKfRYLRIF 155
Cdd:PRK11263  27 IAAAQEEILLETFILFEDKVGKQ-LHAaLLAAAQRGVKVEVLVDGYGSPDLSDEFVNELTAAGVRFRYFDPRP-RLLGMR 104

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446532648 156 DYLFRfkkvnhRMHNKLIIADGSIAVTGGRNISSE 190
Cdd:PRK11263 105 TNLFR------RMHRKIVVIDGRIAFVGGINYSAD 133
YrhO COG1378
Sugar-specific transcriptional regulator TrmB [Transcription];
69-190 2.34e-05

Sugar-specific transcriptional regulator TrmB [Transcription];


Pssm-ID: 440988 [Multi-domain]  Cd Length: 238  Bit Score: 45.78  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  69 SIASRIY-LIRNAKETIDLqyYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQngiklDDILRSLLQHTNFEIRLFNPy 147
Cdd:COG1378  117 AILERLReLIASAEEEILI--VLSPPELLLEELEEALEEALERGVKVRVLVSPE-----VLEVPERLEEEGEEVRVLPG- 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446532648 148 kfrylrifdylfrfkkvnhrMHNKLIIADGSIAVTGGRNISSE 190
Cdd:COG1378  189 --------------------LPGRLLIVDDKEALISVSEPDGE 211
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 414-436 1.10e-03

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 36.60  E-value: 1.10e-03
                           10        20
                   ....*....|....*....|....
gi 446532648   414 LHAKFFDVDGK-VFIGSFNFDPRS 436
Cdd:smart00155   5 LHTKLMIVDDEiAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 289-515 1.46e-83

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: 258.30  E-value: 1.46e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 289 VADSPKKILGTATQHEMLYGQVMSIMGKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNSFAANDVAIVHAFYS 368
Cdd:cd09113    1 LSDPPEKALKEAGPEPVLAYQLAELLKNAKREVLIVSPYFVPGDEGVALLAELARRGVRVRILTNSLAATDVPAVHSGYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 369 QYRVEMLKNGIELYEFKPVLERRRRTWyeivtgsviPAKGKNKSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVI 447
Cdd:cd09113   81 RYRKRLLKAGVELYELKPDAAKRKRLR---------GLFGSSRASLHAKSFVIDDRlVFVGSFNLDPRSAYLNTEMGLVI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 448 ESSQLQTQISVMLDQHLPQVAYQLKLNSQGQITWlDYQANGQVIEYDKDPGTSRFQRTMIKAVSYLPI 515
Cdd:cd09113  152 DSPELAAQLRAAMEEDLAPSAYWVLLLDDGGLVW-ETEEDGKEKEYDSEPETSFWRRLGAWLLSLLPI 218
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
 63-224 1.26e-80

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: 248.60  E-value: 1.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  63 LDDAFMSIASRIYLIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIR 142
Cdd:cd09111    1 LEDGLDALAARLALIRSAERSIDLQYYIWHDDESGRLLLGELLEAADRGVRVRLLLDDLGTSGRDRLLAALDAHPNIEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 143 LFNPYKFRYLRIFDYLFRFKKVNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKFQFTDMDILFYGHAVRHAQAVFADF 222
Cdd:cd09111   81 LFNPFRNRGGRLLEFLTDFSRLNRRMHNKLFIVDGAVAIVGGRNIGDEYFGASPEVNFRDLDVLAVGPVVRQLSESFDTY 160


                 ..
gi 446532648 223 WE 224
Cdd:cd09111  161 WN 162
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 64-481 3.72e-77

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: 246.78  E-value: 3.72e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  64 DDAFmsiASRIYLIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRL 143
Cdd:COG1502   24 DEAF---AALLEAIEAARRSIDLEYYIFDDDEVGRRLADALIAAARRGVKVRVLLDGIGSRALNRDFLRRLRAAGVEVRL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 144 FNPYKFRYLRIfdylfrfkkvNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKF-QFTDMDILFYGHAVRHAQAVFADF 222
Cdd:COG1502  101 FNPVRLLFRRL----------NGRNHRKIVVIDGRVAFVGGANITDEYLGRDPGFgPWRDTHVRIEGPAVADLQAVFAED 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 223 WESTlsvnateiigtcaehhlkalrehyeqlhhedhslTEDKLYDAQsylkellehnPIQWSKAHFVADSPkkilgtATQ 302
Cdd:COG1502  171 WNFA----------------------------------TGEALPFPE----------PAGDVRVQVVPSGP------DSP 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 303 HEMLYGQVMSIMGKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNsfAANDVAIVHAFYSQYRVEMLKNGIELY 382
Cdd:COG1502  201 RETIERALLAAIASARRRIYIETPYFVPDRSLLRALIAAARRGVDVRILLP--AKSDHPLVHWASRSYYEELLEAGVRIY 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 383 EFKPvlerrrrtwyeivtgsvipakgknkSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVIESSQLQTQISVMLD 461
Cdd:COG1502  279 EYEP-------------------------GFLHAKVMVVDDEwALVGSANLDPRSLRLNFEVNLVIYDPEFAAQLRARFE 333

                        410       420
                 ....*....|....*....|
gi 446532648 462 QHLpQVAYQLKLNSQGQITW 481
Cdd:COG1502  334 EDL-AHSREVTLEEWRKRPL 352
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
 77-223 2.38e-37

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: 134.91  E-value: 2.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPYKFRylrifd 156
Cdd:cd09110   14 IRAARHSIHLEYYIFRDDEIGRRFRDALIEKARRGVEVRLLYDGFGSLGLSRRFLRELREAGVEVRAFNPLSFP------ 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 157 ylFRFKKVNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKFQ-FTDMDILFYGHAVRHAQAVFADFW 223
Cdd:cd09110   88 --LFLLRLNYRNHRKILVIDGKIAFVGGFNIGDEYLGKDPGFGpWRDTHVRIEGPAVADLQAAFLEDW 153
PLDc_CLS_unchar1_1 cd09156
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 74-224 2.01e-26

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: 104.65  E-value: 2.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  74 IYLIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPykfrylr 153
Cdd:cd09156   11 IQLIESAKHSIDVCTFILGDDATGRRVIDALARKAREGVEVRLLLDALGSFFLSRRALKKLRAAGGKVAFFMP------- 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446532648 154 ifdyLFRFK---KVNHRMHNKLIIADGSIAVTGGRNISSEYFEAS-SKFQFTDMDILFYGHAVRHAQAVFADFWE 224
Cdd:cd09156   84 ----VFRLPfrgRTNLRNHRKIAIADGSTAISGGMNLANEYMGPEpDDGRWVDLSFLIEGPAVAQYQEVFRSDWA 154
PRK12452 PRK12452
cardiolipin synthase;
76-451 1.54e-25

cardiolipin synthase;


Pssm-ID: 171510 [Multi-domain]  Cd Length: 509  Bit Score: 109.62  E-value: 1.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  76 LIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPykfrylrIF 155
Cdd:PRK12452 158 AIEQAKHHIHIQYYIYKSDEIGTKVRDALIKKAKDGVIVRFLYDGLGSNTLRRRFLQPMKEAGIEIVEFDP-------IF 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 156 DYLFRFKkVNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKFQF-TDMDILFYGHAVRHAQAVFADFWestlsvnatei 234
Cdd:PRK12452 231 SAWLLET-VNYRNHRKIVIVDGEIGFTGGLNVGDEYLGRSKKFPVwRDSHLKVEGKALYKLQAIFLEDW----------- 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 235 igtcaehhLKAlrehyeqlHHEDHSLTEDKLYDAQSYLKELLEHNPiqwSKAHFVADSPkkilgtATQHEMLYGQVMSIM 314
Cdd:PRK12452 299 --------LYA--------SSGLNTYSWDPFMNRQYFPGKEISNAE---GAVQIVASGP------SSDDKSIRNTLLAVM 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 315 GKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNsfAANDVAIVHAFYSQYRVEMLKNGIELYEFkpvlerrrrt 394
Cdd:PRK12452 354 GSAKKSIWIATPYFIPDQETLTLLRLSAISGIDVRILYP--GKSDSIISDQASQSYFTPLLKAGASIYSY---------- 421

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 395 wyeivtgsvipakgkNKSSLHAKFFDVDGKV-FIGSFNFDPRSTYLNTEVGLVIESSQ 451
Cdd:PRK12452 422 ---------------KDGFMHAKIVLVDDKIaTIGTANMDVRSFELNYEIISVLYESE 464
PLDc_CLS_unchar2_1 cd09157
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 77-224 2.35e-23

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: 96.10  E-value: 2.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPykfryLRIFD 156
Cdd:cd09157   14 IDAARHSIALSSYIFDNDGVGREFVDALAEAVARGVDVRVLIDGVGARYSRPSIRRRLRRAGVPVARFLP-----PRLPP 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446532648 157 YLFRFkkvNHRMHNKLIIADGSIAVTGGRNISSEYF-EASSKFQFTDMDILFYGHAVRHAQAVFADFWE 224
Cdd:cd09157   89 RLPFI---NLRNHRKILVVDGRTGFTGGMNIRDGHLvADDPKNPVQDLHFRVEGPVVAQLQEVFAEDWY 154
cls PRK01642
cardiolipin synthetase; Reviewed
 77-464 1.02e-22

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 101.01  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLddiLRS----LLQHTNFEIRLFNPykFRYL 152
Cdd:PRK01642 135 IELARHYILMEFYIWRPDGLGDQVAEALIAAAKRGVRVRLLYDSIGSFAF---FRSpypeELRNAGVEVVEFLK--VNLG 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 153 RIFdylfrFKKVNHRMHNKLIIADGSIAVTGGRNIS-SEYFEASSKF-QFTDMDILFYGHAVRHAQAVFADFWEStlsvn 230
Cdd:PRK01642 210 RVF-----RRRLDLRNHRKIVVIDGYIAYTGSMNVVdPEYFKQDPGVgQWRDTHVRIEGPVVTALQLIFAEDWEW----- 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 231 ATEiigtcaEHHLkalrehyeqlhhedhslteDKLYDAQSYLKELLEHNPIQwskahFVADSPkkilgtATQHEMLYGQV 310
Cdd:PRK01642 280 ETG------ERIL-------------------PPPPDVLIMPFEEASGHTVQ-----VIASGP------GDPEETIHQFL 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 311 MSIMGKPKQHLELASAYFVPTQQGTYYLK--QLRveGIKVRALTNSFaaNDVAIV-HAFYSQYRvEMLKNGIELYEFKPV 387
Cdd:PRK01642 324 LTAIYSARERLWITTPYFVPDEDLLAALKtaALR--GVDVRIIIPSK--NDSLLVfWASRAFFT-ELLEAGVKIYRYEGG 398

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 388 LerrrrtwyeivtgsvipakgknkssLHAKFFDVDGKV-FIGSFNFDPRSTYLNTEVGLVIESSQLQTQISVMLDQHL 464
Cdd:PRK01642 399 L-------------------------LHTKSVLVDDELaLVGTVNLDMRSFWLNFEITLVIDDTGFAADLAAMQEDYF 451
PLDc_EcCLS_like_1 cd09152
Catalytic domain, repeat 1, of Escherichia coli cardiolipin synthase and similar proteins; ...
 63-224 2.81e-21

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: 90.73  E-value: 2.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  63 LDDAFMSIASRIYLIRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQnGIKldDILRS----LLQHTN 138
Cdd:cd09152    7 LTDYDAVIDRLIADIDAAKHHVHLLFYIWADDGTGDRVAEALERAAKRGVTCRLLLDAV-GSR--AFFRSslwkRLREAG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 139 FEIRLFNPykFRYLRIFdyLFRFKKVNHRmhnKLIIADGSIAVTGGRNISS-EYFEASSKFQFTDMDILFYGHAVRHAQA 217
Cdd:cd09152   84 VEVVEALP--LRLFRRR--LARFDLRNHR---KIAVIDGRIAYTGSQNIIDpEFFKKAGGGPWVDLMVRVEGPVVSQLQA 156


                 ....*..
gi 446532648 218 VFADFWE 224
Cdd:cd09152  157 VFASDWY 163
PLDc_2 pfam13091
PLD-like domain;
314-463 1.67e-16

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 76.18  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  314 MGKPKQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNSFAANDVAIVHAFYSQYRvEMLKNGIELYEFKPVLerrrr 393
Cdd:pfam13091   5 INSAKKSIDIATYYFVPDREIIDALIAAAKRGVDVRIILDSNKDDAGGPKKASLKELR-SLLRAGVEIREYQSFL----- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446532648  394 twyeivtgsvipakgknkSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVIESSQLQTQISVMLDQH 463
Cdd:pfam13091  79 ------------------RSMHAKFYIIDGKtVIVGSANLTRRALRLNLENNVVIKDPELAQELEKEFDRL 131
PLDc_PaCLS_like_1 cd09155
Putative catalytic domain, repeat 1, of Pseudomonas aeruginosa cardiolipin synthase and ...
 77-223 2.25e-16

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: 76.51  E-value: 2.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPYKFRylrifd 156
Cdd:cd09155   14 IASAEEYILVQFYIIRDDDLGRELKDALIARAQAGVRVYLLYDEIGSHSLSRSYIERLRKAGVEVSAFNTTRGW------ 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 157 yLFRFkKVNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKF-QFTDMDILFYGHAVRHAQAVFADFW 223
Cdd:cd09155   88 -GNRF-QLNFRNHRKIVVVDGQTAFVGGHNVGDEYLGRDPRLgPWRDTHVKLEGPAVQQLQLSFAEDW 153
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 318-466 9.89e-16

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: 74.88  E-value: 9.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 318 KQHLELASAYFVPtqqGTYYLKQLRV---EGIKVRALTNsfAANDV-AIVHAFYSQYRvEMLKNGIELYEFKPvlerrrr 393
Cdd:cd09159   24 RRRIWIANAYFVP---DRRLRRALIEaarRGVDVRLLLP--GKSDDpLTVAASRALYG-KLLRAGVRIFEYQP------- 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446532648 394 twyeivtgsvipakgknkSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVIESSQLQTQISVMLDQHLPQ 466
Cdd:cd09159   91 ------------------SMLHAKTAVIDGDwATVGSSNLDPRSLRLNLEANLVVEDPAFAAQLEELFEEDLAR 146
PLDc_SMU_988_like_1 cd09154
Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 ...
 77-224 2.88e-14

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: 70.25  E-value: 2.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQNGI-KLDDILRSLLQHTNFEIRLFNPYKfRYLRIF 155
Cdd:cd09154   15 LKKAEKFIFMEYFIIEEGYMWDSILEILKEKAKEGVEVRIMYDDFGSItTLPKDYPKELEKIGIKCRVFNPFK-PILSLY 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 156 dylfrfkkVNHRMHNKLIIADGSIAVTGGRNISSEYFEASSKF-QFTDMDILFYGHAVRHAQAVFADFWE 224
Cdd:cd09154   94 --------MNNRDHRKITVIDGKVAFTGGINLADEYINKIERFgYWKDTGIRLEGEAVWSLTVMFLEMWN 155
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
 304-462 3.70e-14

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: 70.58  E-value: 3.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 304 EMLYgqvMSIMGKPKQHLELASAYFVPTQQGtyyLKQLRV---EGIKVRALTNSFAANDVAiVHAFYSQYRvEMLKNGIE 380
Cdd:cd09112   13 EQAY---LKAINSAKKSIYIQTPYFIPDESL---LEALKTaalSGVDVRIMIPGKPDHKLV-YWASRSYFE-ELLKAGVK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 381 LYEFkpvlerrrrtwyeivtgsvipakgkNKSSLHAKFFDVDGKV-FIGSFNFDPRSTYLNTEVGLVIESSQLQTQISVM 459
Cdd:cd09112   85 IYEY-------------------------NKGFLHSKTLIVDDEIaSVGTANLDIRSFELNFEVNAVIYDKEVAKKLEEI 139


                 ...
gi 446532648 460 LDQ 462
Cdd:cd09112  140 FEE 142
PLDc_2 pfam13091
PLD-like domain;
74-223 7.06e-12

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 62.69  E-value: 7.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648   74 IYLIRNAKETIDLQ-YYIWTNDFvgnlILHELLKAADRGIKVRLLIDDQNG------IKLDDILRSLLQHtNFEIRLFNP 146
Cdd:pfam13091   2 IDLINSAKKSIDIAtYYFVPDRE----IIDALIAAAKRGVDVRIILDSNKDdaggpkKASLKELRSLLRA-GVEIREYQS 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648  147 YkfrylrifdylfrfkkvNHRMHNKLIIADGSIAVTGGRNISSEYFEASskfqfTDMDILFYG-HAVRHAQAVFADFW 223
Cdd:pfam13091  77 F-----------------LRSMHAKFYIIDGKTVIVGSANLTRRALRLN-----LENNVVIKDpELAQELEKEFDRLW 132
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 76-188 1.82e-11

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: 61.38  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  76 LIRNAKETIDLQYYIWTNDFVGNlILHELLKAADRGIKVRLLIDDQNGIK--LDDILRSLLQHTNFEIRLFNPYKFRylr 153
Cdd:cd00138    6 LLKNAKESIFIATPNFSFNSADR-LLKALLAAAERGVDVRLIIDKPPNAAgsLSAALLEALLRAGVNVRSYVTPPHF--- 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446532648 154 ifdylfrfkkvNHRMHNKLIIADGSIAVTGGRNIS 188
Cdd:cd00138   82 -----------FERLHAKVVVIDGEVAYVGSANLS 105
PLDc_EcCLS_like_2 cd09158
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins; ...
 323-456 2.17e-10

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: 59.51  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 323 LASAYFVPTQQGTYYLKQLRVEGIKVRALTNsfAANDVAIVHAFYSQYRVEMLKNGIELYEFKPVLerrrrtwyeivtgs 402
Cdd:cd09158   29 ITTPYFVPDESLLQALCTAALRGVEVTLILP--AKNDSFLVGAASRSYYEELLEAGVKIYLYRGGL-------------- 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446532648 403 vipakgknkssLHAKFFDVDGKV-FIGSFNFDPRSTYLNTEVGLVIESSQLQTQI 456
Cdd:cd09158   93 -----------LHAKTVTVDDEVaLVGSSNFDIRSFALNFEISLILYDKEFTAQL 136
PRK11263 PRK11263
cardiolipin synthase ClsB;
77-190 2.91e-10

cardiolipin synthase ClsB;


Pssm-ID: 236888 [Multi-domain]  Cd Length: 411  Bit Score: 62.27  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYIWTNDFVGNLiLHE-LLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPYKfRYLRIF 155
Cdd:PRK11263  27 IAAAQEEILLETFILFEDKVGKQ-LHAaLLAAAQRGVKVEVLVDGYGSPDLSDEFVNELTAAGVRFRYFDPRP-RLLGMR 104

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446532648 156 DYLFRfkkvnhRMHNKLIIADGSIAVTGGRNISSE 190
Cdd:PRK11263 105 TNLFR------RMHRKIVVIDGRIAFVGGINYSAD 133
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 76-223 3.78e-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: 58.06  E-value: 3.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  76 LIRNAKETIDLQY-YIwtNDFvgNLILHELLKAADRGIKVRLLIDDQNGIKlDDILRSL--LQHTNFEIRLfnpykfryl 152
Cdd:cd09128   18 LIDSAEESLLIQNeEM--GDD--APILDALVDAAKRGVDVRVLLPSAWSAE-DERQARLraLEGAGVPVRL--------- 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446532648 153 RIFDYLfrfkkvnhRMHNKLIIADGSIAVTGGRNISSEYFEASSkfqftDMDILFYGHAV-RHAQAVFADFW 223
Cdd:cd09128   84 LKDKFL--------KIHAKGIVVDGKTALVGSENWSANSLDRNR-----EVGLIFDDPEVaAYLQAVFESDW 142
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
 58-221 5.82e-09

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: 54.58  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  58 TAFVALDDAFMSIasrIYLIRNAKETIDLQYYIWTnDFVgnlILHELLKAADRGIKVRLLIDDQN--GIKLDDILRSLLQ 135
Cdd:cd09127    1 TLFVQPDDGVAPV---VDAIASAKRSILLKMYEFT-DPA---LEKALAAAAKRGVRVRVLLEGGPvgGISRAEKLLDYLN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 136 HTNFEIRLFNP-YKFRYLrifdylfrfkkvnhrmHNKLIIADGSIAVTGGRNISSEYFEASSKFQFtdmdILFYGHAVRH 214
Cdd:cd09127   74 EAGVEVRWTNGtARYRYT----------------HAKYIVVDDERALVLTENFKPSGFTGTRGFGV----VTDDPAVVAE 133


                 ....*..
gi 446532648 215 AQAVFAD 221
Cdd:cd09127  134 IADVFDA 140
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 76-188 9.43e-09

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


Pssm-ID: 197215 [Multi-domain]  Cd Length: 138  Bit Score: 53.84  E-value: 9.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  76 LIRNAKETIDLQYYIWTNdfvgNLILHELLKAADRGIKVRLLID-DQNGIKLDDILRSLLQHTNFEIRLfnpykfrylri 154
Cdd:cd09116   17 LIANAKSSIDVAMYALTD----PEIAEALKRAAKRGVRVRIILDkDSLADNLSITLLALLSNLGIPVRT----------- 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446532648 155 fdylfrfKKVNHRMHNKLIIADGSIAVTGGRNIS 188
Cdd:cd09116   82 -------DSGSKLMHHKFIIIDGKIVITGSANWT 108
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 65-178 6.77e-08

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: 51.86  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  65 DAFMSiasriyLIRNAKETIDLQYYIWTND----------FVGNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLL 134
Cdd:cd09106   22 EAWME------LISSAKKSIDIASFYWNLRgtdtnpdssaQEGEDIFNALLEAAKRGVKIRILQDKPSKDKPDEDDLELA 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446532648 135 QHTNFEIRLFNpykfrylriFDylfrfKKVNH-RMHNKLIIADGS 178
Cdd:cd09106   96 ALGGAEVRSLD---------FT-----KLIGGgVLHTKFWIVDGK 126
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
 74-188 2.52e-07

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: 50.03  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  74 IYLIRNAKETIDLQYYI---WTNDFVG-NLILHELLKAADRGIKVRLLIDDQNGIKlddilrsllqhtnfEIRLFNPYKF 149
Cdd:cd09131    9 LDLINNAKRSIYIAMYMfkyYENPGNGvNTLLEALIDAHKRGVDVKVVLEDSIDDD--------------EVTEENDNTY 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446532648 150 RYLRIFDYLFRFKKVNHRMHNKLIIADGSIAVTGGRNIS 188
Cdd:cd09131   75 RYLKDNGVEVRFDSPSVTTHTKLVVIDGRTVYVGSHNWT 113
PRK13912 PRK13912
nuclease NucT; Provisional
 64-193 3.54e-07

nuclease NucT; Provisional


Pssm-ID: 184389 [Multi-domain]  Cd Length: 177  Bit Score: 50.16  E-value: 3.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  64 DDAFMSIASriyLIRNAKETIDLQYYIWTNdfvgNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQhtnfeirl 143
Cdd:PRK13912  32 KDALNKLVS---LISNARSSIKIAIYSFTH----KDIAKALKSAAKRGVKISIIYDYESNHNNDQSTIGYLD-------- 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446532648 144 fnpyKFRYLRIfDYLFRFKKVNHR----MHNKLIIADGSIAVTGGRNISSEYFE 193
Cdd:PRK13912  97 ----KYPNIKV-CLLKGLKAKNGKyygiMHQKVAIIDDKIVVLGSANWSKNAFE 145
PLDc_CLS_unchar2_2 cd09163
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 318-463 2.61e-06

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


Pssm-ID: 197260 [Multi-domain]  Cd Length: 176  Bit Score: 47.93  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 318 KQHLELASAYFVPTQQGTYYLKQLRVEGIKVRALTNsfAANDVAIVH-AFYSQYRvEMLKNGIELYEFKPVLErrrrtwy 396
Cdd:cd09163   24 RHSIRIMTPYFLPDRTLITALQAAALRGVEVDIVLP--ERNNLPLVDwAMRANLW-ELLEHGVRIYLQPPPFD------- 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446532648 397 eivtgsvipakgknksslHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVIESSQLQTQISVMLDQH 463
Cdd:cd09163   94 ------------------HSKLMVVDGAwALIGSANWDPRSLRLNFELNLEVYDTALAGQLDALFDSK 143
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 74-195 4.58e-06

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: 46.86  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  74 IYLIRNAKETIDLQyyiwTNDFVGnLILHE------------LLKAA-DRGIKVRLLIDDQNG--------IKLDDILRS 132
Cdd:cd09107   22 LSTIDSAKKFIDIS----VMDYVP-LSRYAdprkywpvidnaLRRAAvDRGVKVRLLVSNWKHtdpsmdafLKSLQLLKS 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446532648 133 LLQHTNFEIRLFnpykfrylRIFDYLFRFKKVNHRMHNKLIIADgSIAVTGGRNISSEYFEAS 195
Cdd:cd09107   97 GVGNGDIEVKIF--------TVPGDQSTKIPFARVNHAKYMVTD-ERAYIGTSNWSGDYFYNT 150
PLDc_Nuc cd09170
Catalytic domain of EDTA-resistant nuclease Nuc from Salmonella typhimurium and similar ...
 74-189 4.72e-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: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  74 IYLIRNAKETIDLQYYIWTNDfvgnLILHELLKAADRGIKVRLLID----DQNGIKLDdilrsLLQHTNFEIRLFNPYKF 149
Cdd:cd09170   17 LDVIDSARRSIDVAAYSFTSP----PIARALIAAKKRGVDVRVVLDksqaGGKYSALN-----YLANAGIPVRIDDNYAI 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446532648 150 rylrifdylfrfkkvnhrMHNKLIIADGSIAVTGGRNISS 189
Cdd:cd09170   88 ------------------MHNKVMVIDGKTVITGSFNFTA 109
PLDc_Nuc_like_unchar2 cd09174
Putative catalytic domain of uncharacterized hypothetical proteins closely related to Nuc, , ...
 67-188 1.76e-05

Putative catalytic domain of uncharacterized hypothetical proteins closely related to Nuc, , an endonuclease from Salmonella typhimurium; Putative catalytic domain of uncharacterized hypothetical proteins, which show high sequence homology to the endonuclease from Salmonella typhimurium and vertebrate phospholipase D6. Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which characterizes the PLD superfamily and is essential for catalysis. Nuc and PLD6 utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. However, proteins in this subfamily have two HKD motifs in a single polypeptide chain.


Pssm-ID: 197271 [Multi-domain]  Cd Length: 136  Bit Score: 44.62  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  67 FMSIASRIY-LIRNAKETIdlqyYI---WTNDFVgnlILHELLKAADRGIKVRLLIDDqngiklDDILRSLLQHTNFEIr 142
Cdd:cd09174    5 FDDIENRIIeEIKKAKFSI----WIavaWFTNKD---IFNALKNKKKEGVNIQIIIND------DDINKKDVLILDEDS- 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446532648 143 lFNPYKFRYLRifdylfrfKKVNHRMHNKLIIADGSIAVTGGRNIS 188
Cdd:cd09174   71 -FEIYKLPGNG--------SRYGNLMHNKFCVIDFKTVITGSYNWT 107
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 306-465 1.87e-05

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


Pssm-ID: 197259 [Multi-domain]  Cd Length: 172  Bit Score: 45.33  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 306 LYGQVMSIMGKPKQHLELASAYFVPTQQgtyYLKQLRV---EGIKVRALTNsfAANDVAIVHAFYSQYRVEMLKNGIELY 382
Cdd:cd09162   12 LYEALLSAIFEAEHRIWIVTPYFVPDEV---LLRALRLaarRGVDVRLIVP--KRSNHRIADLARGSYLRDLQEAGAEIY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 383 EFKPvlerrrrtwyeivtgsvipakgknkSSLHAKFFDVDGKV-FIGSFNFDPRSTYLNTEVGLVIESSQ--------LQ 453
Cdd:cd09162   87 LYQP-------------------------GMLHAKAVVVDDKLaLVGSANLDMRSLFLNYEVAVFFYSPAdikelsdwIE 141

                        170
                 ....*....|..
gi 446532648 454 TQISVMLDQHLP 465
Cdd:cd09162  142 SLISQCTEGAPP 153
YrhO COG1378
Sugar-specific transcriptional regulator TrmB [Transcription];
69-190 2.34e-05

Sugar-specific transcriptional regulator TrmB [Transcription];


Pssm-ID: 440988 [Multi-domain]  Cd Length: 238  Bit Score: 45.78  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  69 SIASRIY-LIRNAKETIDLqyYIWTNDFVGNLILHELLKAADRGIKVRLLIDDQngiklDDILRSLLQHTNFEIRLFNPy 147
Cdd:COG1378  117 AILERLReLIASAEEEILI--VLSPPELLLEELEEALEEALERGVKVRVLVSPE-----VLEVPERLEEEGEEVRVLPG- 188

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446532648 148 kfrylrifdylfrfkkvnhrMHNKLIIADGSIAVTGGRNISSE 190
Cdd:COG1378  189 --------------------LPGRLLIVDDKEALISVSEPDGE 211
PLDc_vPLD6_like cd09171
Catalytic domain of vertebrate phospholipase D6 and similar proteins; Catalytic domain of ...
 77-186 3.01e-05

Catalytic domain of vertebrate phospholipase D6 and similar proteins; Catalytic domain of vertebrate phospholipase D6 (PLD6, EC 3.1.4.4), a homolog of the EDTA-resistant nuclease Nuc from Salmonella typhimurium, and similar proteins. PLD6 can selectively hydrolyze the terminal phosphodiester bond of phosphatidylcholine (PC) with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. It also catalyzes the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. PLD6 belongs to the phospholipase D (PLD) superfamily. Its monomer contains a short conserved sequence motif, H-x-K-x(4)-D (where x represents any amino acid residue), termed the HKD motif, which is essential in catalysis. PLD6 is more closely related to the nuclease Nuc than to other vertebrate phospholipases, which have two copies of the HKD motif in a single polypeptide chain. Like Nuc, PLD6 may utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from the HKD motif of one subunit to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit.


Pssm-ID: 197268 [Multi-domain]  Cd Length: 136  Bit Score: 43.75  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYIWTNDFVGNlilhELLKAADRGIKVRLLID-DQNGIKLDDILrsllqhtnfeirlfnpyKFRYLRIF 155
Cdd:cd09171   17 LLSARKSLDVCVFTITCDDLAD----AILDLHRRGVRVRIITDdDQMEDKGSDIG-----------------KLRKAGIP 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446532648 156 dylFRFKKVNHRMHNKLIIADGSIAVTGGRN 186
Cdd:cd09171   76 ---VRTDLSSGHMHHKFAVIDGKILITGSFN 103
PLDc_PMFPLD_like_1 cd09108
Catalytic domain, repeat 1, of phospholipase D from Streptomyces Sp. Strain PMF and similar ...
 169-223 5.77e-05

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: 44.35  E-value: 5.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446532648 169 HNKLIIADGSIAVTGGRNISSEYFEASSKFQfTDMDILFYGHAVRHAQAVFADFW 223
Cdd:cd09108  157 HAKLLVVDGEELLTGGYNLWDDHYLDGGNPV-HDLSLVVRGPAARSGVRFFDDLW 210
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 100-228 1.19e-04

Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic domain, repeat 2, of phospholipase D3 (PLD3, EC 3.1.4.4). The human protein is also known as Hu-K4 or HUK4 and it was identified as a human homolog of the vaccinia virus protein K4, which is encoded by the HindIII K4L gene. PLD3 is found in many human organs with highest expression levels found in the central nervous system. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD3 has been assigned to the PLD superfamily although no catalytic activity has been detected experimentally. PLD3 is a membrane-bound protein that colocalizes with protein disulfide isomerase, an endoplasmic reticulum (ER) protein. Like other homologs of protein K4, PLD3 might alter the lipid content of associated membranes by selectively hydrolyzing phosphatidylcholine (PC) into the corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement.


Pssm-ID: 197245  Cd Length: 186  Bit Score: 43.03  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 100 ILHELLKAA-DRGIKVRLLIDDQNGIK--LDDILRSL--LQ----HTNFEIRLFN-PYKFRYLRIfdylfRFKKVNhrmH 169
Cdd:cd09147   55 IDDGLRRATyERGVKVRLLISCWGHSEpsMFAFLRSLaaLRdnttHSDIQVKIFVvPADEAQKKI-----PYARVN---H 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446532648 170 NKLIIADgSIAVTGGRNISSEYF--EASSKFQFTDMDILFYGHAVRHAQAVFADFWESTLS 228
Cdd:cd09147  127 NKYMVTD-RVAYIGTSNWSGDYFtnTAGSALVVNQTGRSASGTLQSQLQAVFERDWDSPYS 186
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
 74-183 2.19e-04

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: 42.08  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  74 IYLIRNAKETIDLQ--YYIWTNDfvgnlILHELLKAADRGIKVRLLIDDQNGIKLddilrsllqhtnfeIRLFNPYKFRY 151
Cdd:cd09112   17 LKAINSAKKSIYIQtpYFIPDES-----LLEALKTAALSGVDVRIMIPGKPDHKL--------------VYWASRSYFEE 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446532648 152 L-----RIFDYLFRFkkvnhrMHNKLIIADGSIAVTG 183
Cdd:cd09112   78 LlkagvKIYEYNKGF------LHSKTLIVDDEIASVG 108
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 406-447 2.99e-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: 40.58  E-value: 2.99e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446532648 406 AKGKNKSSLHAKFFDVDGKVF-IGSFNFDPRSTYLNTEVGLVI 447
Cdd:cd00138   77 TPPHFFERLHAKVVVIDGEVAyVGSANLSTASAAQNREAGVLV 119
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
 74-187 4.03e-04

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


Pssm-ID: 197259 [Multi-domain]  Cd Length: 172  Bit Score: 41.09  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  74 IYLIRNAKETIdlqyYIWTNDFV-GNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSL----LQHTNFEIRLFNPyk 148
Cdd:cd09162   17 LSAIFEAEHRI----WIVTPYFVpDEVLLRALRLAARRGVDVRLIVPKRSNHRIADLARGSylrdLQEAGAEIYLYQP-- 90

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446532648 149 frylrifdylfrfkkvnHRMHNKLIIADGSIAVTGGRNI 187
Cdd:cd09162   91 -----------------GMLHAKAVVVDDKLALVGSANL 112
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 414-449 6.83e-04

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 39.95  E-value: 6.83e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446532648 414 LHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVIES 449
Cdd:cd09128   91 IHAKGIVVDGKtALVGSENWSANSLDRNREVGLIFDD 127
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 414-436 1.10e-03

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 36.60  E-value: 1.10e-03
                           10        20
                   ....*....|....*....|....
gi 446532648   414 LHAKFFDVDGK-VFIGSFNFDPRS 436
Cdd:smart00155   5 LHTKLMIVDDEiAYIGSANLDGRS 28
PLDc_N_DEXD_b cd09180
N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family ...
 98-189 1.33e-03

N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain; N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. Other characterized members of the superfamily that have a related domain architecture ( containing a DEAD/DEAH box helicase domain), include the DNA/RNA helicase superfamily II (SF2) and Res-subunit of type III restriction endonucleases. In addition to the helicase-like region, members of this subfamily also contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in the N-terminal putative catalytic domain. The HKD motif characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. A few family members contain additional domains, like a C-terminal peptidase S24-like domain.


Pssm-ID: 197277 [Multi-domain]  Cd Length: 142  Bit Score: 39.24  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  98 NLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNPYKFRYLRIFDYLFrfkkvnHRMHNKliiadg 177
Cdd:cd09180   30 QLLIPELEELINKGVPIRIITSTYLGITEPKALRELADYDNVEVKIYNNIKSESFHAKAYLF------ERETGY------ 97

                         90
                 ....*....|..
gi 446532648 178 SIAVTGGRNISS 189
Cdd:cd09180   98 SSAIIGSSNLSQ 109
PLDc_SMU_988_like_2 cd09160
Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 ...
 345-445 1.35e-03

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: 39.79  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 345 GIKVRALTNSFAanDVAIVHAFYSQYRVEMLKNGIELYEFKPvlerrrrtwyeivtGSVipakgknksslHAKFFDVDGK 424
Cdd:cd09160   51 GVDVRIITPHIP--DKKYVFLVTRSNYPELLEAGVKIYEYTP--------------GFI-----------HAKTFVSDDK 103

                         90       100
                 ....*....|....*....|..
gi 446532648 425 V-FIGSFNFDPRSTYLNTEVGL 445
Cdd:cd09160  104 AaVVGTINLDYRSLYLHFECGV 125
PLDc_like_TrmB_middle cd09124
Middle phospholipase D-like domain of the transcriptional regulator TrmB and similar proteins; ...
 76-144 1.39e-03

Middle phospholipase D-like domain of the transcriptional regulator TrmB and similar proteins; Middle phospholipase D (PLD)-like domain of the transcriptional regulator TrmB and similar proteins. TrmB acts as a bifunctional sugar-sensing transcriptional regulator which controls two operons encoding maltose/trehalose and maltodextrin ABC transporters of Pyrococcus fruiosus. It functions as a dimer. Full length TrmB includes an N-terminal DNA-binding domain, a C-terminal sugar-binding domain and middle region that has been named as a PLD-like domain. The middle domain displays homology to PLD enzymes, which contain one or two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) per chain. The HKD motif characterizes the PLD superfamily. Due to the lack of key residues related to PLD activity in the PLD-like domain, members of this subfamily are unlikely to carry PLD activity.


Pssm-ID: 197223 [Multi-domain]  Cd Length: 126  Bit Score: 38.85  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446532648  76 LIRNAKETIDLQyyIWTNDFvgNLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLF 144
Cdd:cd09124   18 MINSAKEEIYIS--LPSEEL--EELLEELEKAAERGVKVVIIIFGDDDLDDLDSPAIEVRVREGGGRPF 82
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
 317-455 1.85e-03

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


Pssm-ID: 197235  Cd Length: 186  Bit Score: 39.48  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 317 PKQHLELASAYFVPTQqgtYYLKQLRVEGIKVRALTNSFAAND---------------VAIVHAFYSQYRVEMLKNGIEL 381
Cdd:cd09137   30 RGSSLTLASGYFNLTP---EYLNLLLNSSANLDVLTASPEANGfygskgvsgyippayTYIARQFLKRVRKNGKQPRIKL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 382 YEFKpvlerrRRTWyeivtgsvipakgknksSLHAK---FFDVDGK----VFIGSFNFDPRSTYLNTEVGLVI--ESSQL 452
Cdd:cd09137  107 FEYK------RPGW-----------------TFHAKglwIYLPGTDlpslTLIGSSNYGYRSVHRDLEAQFLIvtNNPKL 163


                 ...
gi 446532648 453 QTQ 455
Cdd:cd09137  164 QQQ 166
PLDc_Nuc_like_unchar1_1 cd09172
Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, ...
 77-224 3.49e-03

Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins similar to Nuc, an endonuclease from Salmonella typhimurium; Putative catalytic domain, repeat 1, of uncharacterized hypothetical proteins, which show high sequence homology to the endonuclease from Salmonella typhimurium and vertebrate phospholipase D6. Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which characterizes the PLD superfamily and is essential for catalysis. Nuc and PLD6 utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. However, proteins in this subfamily have two HKD motifs in a single polypeptide chain.


Pssm-ID: 197269 [Multi-domain]  Cd Length: 144  Bit Score: 38.11  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  77 IRNAKETIDLQYYiwtnDFVGNLILHELLKAADRGIKVRLLIDDQNGiklddilrsllQHTNFEirlfNPYKFRYLRIFD 156
Cdd:cd09172   18 ARSAGSSIRLAIY----ELDDPEIIDALKAAKDRGVRVRIILDDSSV-----------TGDPTE----ESAAATLSKGPG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446532648 157 YLFRFKKVNHRMHNKLIIADGSIA----VTGGRNisseyFEASSKF-QFTDmdilfyGHAVRHAQ--AVFADFWE 224
Cdd:cd09172   79 ALVKRRHSSGLMHNKFLVVDRKDGpnrvLTGSTN-----FTTSGLYgQSNN------VLIFRNPAfaAAYLAYWN 142
COG3886 COG3886
HKD family nuclease [Replication, recombination and repair];
98-278 4.18e-03

HKD family nuclease [Replication, recombination and repair];


Pssm-ID: 443094 [Multi-domain]  Cd Length: 941  Bit Score: 39.97  E-value: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  98 NLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSLLQHTNFEIRLFNpykfrylrifdylfrfkKVNHRMHNKLII--- 174
Cdd:COG3886   58 RLLLDALKELLERGVKGRILTSTYLGFTEPKALRELLDLPNIEVRVSY-----------------DRKTRFHAKAYIfer 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648 175 ADGSIAVTGGRNIS----SEYFEASSKFQFTDMdilfyGHAVRHAQAVFADFWESTLSVNATEIIGtcAEHHLKALREHY 250
Cdd:COG3886  121 TGYGTAIIGSSNLTrsalTDNLEWNVKLSSAED-----PDLIEKFRAEFESLWEDSEFVTLDPWID--KEEERYRRALKK 193

                        170       180
                 ....*....|....*....|....*...
gi 446532648 251 EQLHHEDHSLTEDKLYDAQSYLKELLEH 278
Cdd:COG3886  194 EQRSDQPSPEEEEEPPPPPPQQQQALLL 221
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 407-448 4.98e-03

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: 37.61  E-value: 4.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446532648 407 KGKNKSSLHAKFFDVDGK-VFIGSFNFDPRStyLNT--EVGLVIE 448
Cdd:cd09106  109 KLIGGGVLHTKFWIVDGKhFYLGSANLDWRS--LTQvkELGVYIY 151
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 76-183 5.08e-03

Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; Catalytic domain, repeat 2, of Escherichia coli cardiolipin (CL) synthase ybhO and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli CL synthase. The prototype of this subfamily is Escherichia coli CL synthase ybhO specified by the f413 (ybhO) gene. ybhO is a membrane-bound protein that catalyzes the formation of cardiolipin (CL) by transferring phosphatidyl group between two phosphatidylglycerol molecules. It can also catalyze phosphatidyl group transfer to water to form phosphatidate. In contrast to the Escherichia coli CL synthase encoded by the cls gene (EcCLS), ybhO does not hydrolyze CL. Moreover, ybhO lacks an N-terminal segment encoded by Escherichia coli cls, which makes ybhO easy to denature. The monomer of ybhO consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. ybhO can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily.


Pssm-ID: 197256 [Multi-domain]  Cd Length: 170  Bit Score: 37.90  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446532648  76 LIRNAKETIDLQ--YyiwtndFV-GNLILHELLKAADRGIKVRLLIddqNGIKLDDILRSLLQHTnfeirlfnpykFRYL 152
Cdd:cd09159   19 AIAAARRRIWIAnaY------FVpDRRLRRALIEAARRGVDVRLLL---PGKSDDPLTVAASRAL-----------YGKL 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446532648 153 -----RIFDYLFRFkkvnhrMHNKLIIADGSIAVTG 183
Cdd:cd09159   79 lragvRIFEYQPSM------LHAKTAVIDGDWATVG 108
PLDc_Nuc_like cd09116
Catalytic domain of EDTA-resistant nuclease Nuc, vertebrate phospholipase D6, and similar ...
 407-452 5.84e-03

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


Pssm-ID: 197215 [Multi-domain]  Cd Length: 138  Bit Score: 37.28  E-value: 5.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446532648 407 KGKNKSSLHAKFFDVDGK-VFIGSFNFDPRSTYLNTEVGLVIESSQL 452
Cdd:cd09116   81 TDSGSKLMHHKFIIIDGKiVITGSANWTKSGFHRNDENLLIIDDPKL 127
PLDc_N_DEXD_b3 cd09205
N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family ...
 98-145 8.00e-03

N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain; N-terminal putative catalytic domain of uncharacterized prokaryotic and archeal HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. Other characterized members of the superfamily that have a related domain architecture ( containing a DEAD/DEAH box helicase domain), include the DNA/RNA helicase superfamily II (SF2) and Res-subunit of type III restriction endonucleases. In addition to the helicase-like region, members of this subfamily also contain one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) in the N-terminal putative catalytic domain. The HKD motif characterizes the phospholipase D (PLD, EC 3.1.4.4) superfamily. A few family members contain additional domains, like a C-terminal peptidase S24-like domain.


Pssm-ID: 197299 [Multi-domain]  Cd Length: 143  Bit Score: 36.83  E-value: 8.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446532648  98 NLILHELLKAADRGIKVRLLIDDQNGIKLDDILRSL--LQHTNFEIRLFN 145
Cdd:cd09205   30 DLLLPALKEALSRGARIRILTGDYLDITQPEALRRLldLLGDGIEIRVFE 79
 
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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