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Conserved domains on  [gi|665408893|ref|NP_001036372|]
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uncharacterized protein Dmel_CG43345, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA02820 super family cl33698
phospholipase-D-like protein; Provisional
 98-487 7.78e-88

phospholipase-D-like protein; Provisional


The actual alignment was detected with superfamily member PHA02820:

Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 275.72  E-value: 7.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  98 LVESLPLGLNYSQWQShpqlsSTFDAWQLLLGRAKASLDIVSPHWTLrgldVNDSSTGPGDQLFQQLLSNGDAGrpkLRV 177
Cdd:PHA02820  10 ITETIPIGMQFDKVYL-----STFNFWREILSNTTKTLDISSFYWSL----SDEVGTNFGTMILNEIIQLPKRG---VRV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 178 RIVVNRSHDSLwhADARILANYGA----ADVVGI--NFLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNCPHLA 251
Cdd:PHA02820  78 RIAVNKSNKPL--KDVELLQMAGVevryIDITNIlgGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 252 LDLGKIFKAYWYLGSNEVPKSWPWIYHTHINQRRPLLLNI-NKKHTMraYLSTSPPELIATGRTRELDAILEAIDKATDV 330
Cdd:PHA02820 156 ADLTQIFEVYWYLGVNNLPYNWKNFYPLYYNTDHPLSLNVsGVPHSV--FIASAPQQLCTMERTNDLTALLSCIRNASKF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 331 IYLSLMEYSPRL-RRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYSDPSEDHFLRSLQALDkiTEGVDIQMRRFVV 409
Cdd:PHA02820 234 VYVSVMNFIPIIySKAGKILFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLK--SKNINIEVKLFIV 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408893 410 PtTNELErISGGRVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLQDmeYNNNSLRTDLMAIFLRDWFSPYALPL 487
Cdd:PHA02820 312 P-DADPP-IPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITP--DDGLGLRQQLEDIFIRDWNSKYSYEL 385
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 98-487 7.78e-88

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 275.72  E-value: 7.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  98 LVESLPLGLNYSQWQShpqlsSTFDAWQLLLGRAKASLDIVSPHWTLrgldVNDSSTGPGDQLFQQLLSNGDAGrpkLRV 177
Cdd:PHA02820  10 ITETIPIGMQFDKVYL-----STFNFWREILSNTTKTLDISSFYWSL----SDEVGTNFGTMILNEIIQLPKRG---VRV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 178 RIVVNRSHDSLwhADARILANYGA----ADVVGI--NFLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNCPHLA 251
Cdd:PHA02820  78 RIAVNKSNKPL--KDVELLQMAGVevryIDITNIlgGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 252 LDLGKIFKAYWYLGSNEVPKSWPWIYHTHINQRRPLLLNI-NKKHTMraYLSTSPPELIATGRTRELDAILEAIDKATDV 330
Cdd:PHA02820 156 ADLTQIFEVYWYLGVNNLPYNWKNFYPLYYNTDHPLSLNVsGVPHSV--FIASAPQQLCTMERTNDLTALLSCIRNASKF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 331 IYLSLMEYSPRL-RRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYSDPSEDHFLRSLQALDkiTEGVDIQMRRFVV 409
Cdd:PHA02820 234 VYVSVMNFIPIIySKAGKILFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLK--SKNINIEVKLFIV 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408893 410 PtTNELErISGGRVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLQDmeYNNNSLRTDLMAIFLRDWFSPYALPL 487
Cdd:PHA02820 312 P-DADPP-IPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITP--DDGLGLRQQLEDIFIRDWNSKYSYEL 385
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 300-479 4.31e-70

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: 220.97  E-value: 4.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 300 YLSTSPPELIATGRTRELDAILEAIDKATDVIYLSLMEYSPRLRRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYS 379
Cdd:cd09107    1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 380 DPSEDHFLRSLQALDKITEGVDIQMRRFVVPTTNElERISGGRVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLqd 459
Cdd:cd09107   81 DPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQS-TKIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVSLVI-- 157

                        170       180
                 ....*....|....*....|
gi 665408893 460 meyNNNSLRTDLMAIFLRDW 479
Cdd:cd09107  158 ---NDPAIVQQLKDVFERDW 174
PLDc_3 pfam13918
PLD-like domain;
233-410 2.68e-36

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 132.44  E-value: 2.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  233 SLTQRKELGVLARNCPHLALDLGKIFKAYWYLG-SNEVPKSWPW-IYHTHINQRRpllLNINKKHTM-RAYLSTSPPELI 309
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIfENKVPFTWSKrLCCAVDNEKA---LNFHLNESGgGAFFSDSPELFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  310 ATGRTRELDAILEAIDKATDVIYLSLMEYSPRLRRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYSDPSEDHFLRS 389
Cdd:pfam13918  78 GFNRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARS 157

                         170       180
                  ....*....|....*....|.
gi 665408893  390 LQALDKITEGVDIQMRRFVVP 410
Cdd:pfam13918 158 LDAFCTEIANCDLKVKFFDLE 178
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 127-262 3.35e-09

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: 58.42  E-value: 3.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 127 LLGRAKASLDIVSPHWTlrgldvndsstgPGDQLFQQLLSNGDAGrpkLRVRIVVNRSHDSL--WHADARILANYGAADV 204
Cdd:COG1502  211 AIASARRRIYIETPYFV------------PDRSLLRALIAAARRG---VDVRILLPAKSDHPlvHWASRSYYEELLEAGV 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408893 205 ----VGINFLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNcPHLALDLGKIFKAYW 262
Cdd:COG1502  276 riyeYEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYD-PEFAAQLRARFEEDL 336
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 208-233 5.21e-07

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: 45.84  E-value: 5.21e-07
                           10        20
                   ....*....|....*....|....*.
gi 665408893   208 NFLHSKLWLVDGEHFYLGTASMDWRS 233
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
 
Name Accession Description Interval E-value
PHA02820 PHA02820
phospholipase-D-like protein; Provisional
 98-487 7.78e-88

phospholipase-D-like protein; Provisional


Pssm-ID: 222934 [Multi-domain]  Cd Length: 424  Bit Score: 275.72  E-value: 7.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  98 LVESLPLGLNYSQWQShpqlsSTFDAWQLLLGRAKASLDIVSPHWTLrgldVNDSSTGPGDQLFQQLLSNGDAGrpkLRV 177
Cdd:PHA02820  10 ITETIPIGMQFDKVYL-----STFNFWREILSNTTKTLDISSFYWSL----SDEVGTNFGTMILNEIIQLPKRG---VRV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 178 RIVVNRSHDSLwhADARILANYGA----ADVVGI--NFLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNCPHLA 251
Cdd:PHA02820  78 RIAVNKSNKPL--KDVELLQMAGVevryIDITNIlgGVLHTKFWISDNTHIYLGSANMDWRSLTQVKELGIAIFNNSNLA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 252 LDLGKIFKAYWYLGSNEVPKSWPWIYHTHINQRRPLLLNI-NKKHTMraYLSTSPPELIATGRTRELDAILEAIDKATDV 330
Cdd:PHA02820 156 ADLTQIFEVYWYLGVNNLPYNWKNFYPLYYNTDHPLSLNVsGVPHSV--FIASAPQQLCTMERTNDLTALLSCIRNASKF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 331 IYLSLMEYSPRL-RRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYSDPSEDHFLRSLQALDkiTEGVDIQMRRFVV 409
Cdd:PHA02820 234 VYVSVMNFIPIIySKAGKILFWPYIEDELRRAAIDRKVSVKLLISCWQRSSFIMRNFLRSIAMLK--SKNINIEVKLFIV 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665408893 410 PtTNELErISGGRVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLQDmeYNNNSLRTDLMAIFLRDWFSPYALPL 487
Cdd:PHA02820 312 P-DADPP-IPYSRVNHAKYMVTDKTAYIGTSNWTGNYFTDTCGVSINITP--DDGLGLRQQLEDIFIRDWNSKYSYEL 385
PLDc_vPLD3_4_5_like_2 cd09107
Putative catalytic domain, repeat 2, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 300-479 4.31e-70

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: 220.97  E-value: 4.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 300 YLSTSPPELIATGRTRELDAILEAIDKATDVIYLSLMEYSPRLRRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYS 379
Cdd:cd09107    1 FLSSSPPELCPPGRTDDLDALLSTIDSAKKFIDISVMDYVPLSRYADPRKYWPVIDNALRRAAVDRGVKVRLLVSNWKHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 380 DPSEDHFLRSLQALDKITEGVDIQMRRFVVPTTNElERISGGRVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLqd 459
Cdd:cd09107   81 DPSMDAFLKSLQLLKSGVGNGDIEVKIFTVPGDQS-TKIPFARVNHAKYMVTDERAYIGTSNWSGDYFYNTAGVSLVI-- 157

                        170       180
                 ....*....|....*....|
gi 665408893 460 meyNNNSLRTDLMAIFLRDW 479
Cdd:cd09107  158 ---NDPAIVQQLKDVFERDW 174
PLDc_vPLD3_2 cd09147
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD3; Putative catalytic ...
 300-484 7.98e-64

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: 205.20  E-value: 7.98e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 300 YLSTSPPELIATGRTRELDAILEAIDKATDVIYLSLMEYSPRLRRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYS 379
Cdd:cd09147    1 YLSSSPPPLCASGRTPDLQSILNVIDNARSFVYIAVMNYLPTLEFSHPHRYWPAIDDGLRRATYERGVKVRLLISCWGHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 380 DPSEDHFLRSLQALDKITEGVDIQMRRFVVPTTNELERISGGRVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVL-Q 458
Cdd:cd09147   81 EPSMFAFLRSLAALRDNTTHSDIQVKIFVVPADEAQKKIPYARVNHNKYMVTDRVAYIGTSNWSGDYFTNTAGSALVVnQ 160

                        170       180
                 ....*....|....*....|....*.
gi 665408893 459 DMEYNNNSLRTDLMAIFLRDWFSPYA 484
Cdd:cd09147  161 TGRSASGTLQSQLQAVFERDWDSPYS 186
PLDc_vPLD4_2 cd09148
Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic ...
 300-484 1.05e-58

Putative catalytic domain, repeat 2, of vertebrate phospholipase PLD4; Putative catalytic domain, repeat 2, of vertebrate phospholipases D4 (PLD4, EC 3.1.4.4), homologs of the vaccinia virus protein K4 which is encoded by the HindIII K4L gene. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD4 has been assigned to PLD superfamily although no catalytic activity has been detected to date. Unlike PLD1 and PLD2, PLD4 does not contain Phox (PX) and Pleckstrin homology (PH) domains but has a putative transmembrane domain. Like other vertebrate homologs of protein K4, PLD4 might be associated with Golgi membranes and alter their lipid content by selectively hydrolyze phosphatidylcholine (PC) into corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement.


Pssm-ID: 197246  Cd Length: 187  Bit Score: 191.98  E-value: 1.05e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 300 YLSTSPPELIATGRTRELDAILEAIDKATDVIYLSLMEYSPRLRRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYS 379
Cdd:cd09148    1 YLSASPPALCPTGRTSDLQAILSVISQAQEFIYISVMEYFPTCRFCHPKRYWSVLDNALRAAAFDRRVLIRLLISCGRHS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 380 DPSEDHFLRSLQALDKITEGVDIQMRRFVVPTTNElERISGGRVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLQD 459
Cdd:cd09148   81 DPDMFPFLRSLNALSNPPLSISVHVKLFIVPVGNQ-TNIPYSRVNHNKFMVTDKAAYIGTSNWSEDYFLNTAGVGLVILQ 159

                        170       180
                 ....*....|....*....|....*...
gi 665408893 460 MEYNNN---SLRTDLMAIFLRDWFSPYA 484
Cdd:cd09148  160 SPGANEemlPVQEQLRSLFERDWSSPYA 187
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
 98-247 3.49e-54

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: 178.98  E-value: 3.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  98 LVESLPLGLNYSQWQSHPqlsSTFDAWQLLLGRAKASLDIVSPHWTLRGLDVNDSSTGP-GDQLFQQLLsngDAGRPKLR 176
Cdd:cd09106    1 LVESIPEGLTFLSSSSHL---STFEAWMELISSAKKSIDIASFYWNLRGTDTNPDSSAQeGEDIFNALL---EAAKRGVK 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665408893 177 VRIVVNRSHDSLWHADARILANYGAADVVGINF--------LHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNC 247
Cdd:cd09106   75 IRILQDKPSKDKPDEDDLELAALGGAEVRSLDFtkligggvLHTKFWIVDGKHFYLGSANLDWRSLTQVKELGVYIYNC 153
PHA03003 PHA03003
palmytilated EEV membrane glycoprotein; Provisional
 87-488 4.44e-50

palmytilated EEV membrane glycoprotein; Provisional


Pssm-ID: 177506 [Multi-domain]  Cd Length: 369  Bit Score: 175.24  E-value: 4.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  87 PVEKPLP---CQLelVESLP--LGLNysqwQSHpqlSSTFDAWQLLLGRAKASLDIVSphwtlrgLDVNDSSTGPGDQLF 161
Cdd:PHA03003   3 PFSKPPPgagCRI--VETLPksLGIA----TQH---MSTYECFDEIISQAKKYIYIAS-------FCCNLRSTPEGRLIL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 162 QQLLsngDAGRPKLRVRIVVNRSHDslwHADARILA----NYGAADVVGIN---FLHSKLWLVDGEHFYLGTASMDWRSL 234
Cdd:PHA03003  67 DKLK---EAAESGVKVTILVDEQSG---DKDEEELQssniNYIKVDIGKLNnvgVLLGSFWVSDDRRCYIGNASLTGGSI 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 235 TQRKELGVLArNCPHLALDLGKIFKAYWYLGSNevpKSWPWIYHTHINQRRPLLLNINKKHtMRAYLSTSPPELIATGRT 314
Cdd:PHA03003 141 STIKTLGVYS-TYPPLATDLRRRFDTFKAFNKN---KSVFNRLCCACCLPVSTKYHINNPI-GGVFFSDSPEHLLGYSRT 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 315 RELDAILEAIDKATDVIYLSLMEYSPRLRRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYSDPSEDHFLRSLQALd 394
Cdd:PHA03003 216 LDADVVLHKIKSAKKSIDLELLSLVPVIREDDKTTYWPDIYNALIRAAINRGVKVRLLVGSWKKNDVYSMASVKSLQAL- 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 395 kiTEGVDIQMRRFVVPTTNELerisggrvncnsYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLQDMEynnnsLRTDLMAI 474
Cdd:PHA03003 295 --CVGNDLSVKVFRIPNNTKL------------LIVDDEFAHITSANFDGTHYLHHAFVSFNTIDKE-----LVKELSAI 355

                        410
                 ....*....|....
gi 665408893 475 FLRDWFSPYALPLK 488
Cdd:PHA03003 356 FERDWTSSYSKPLK 369
PLDc_vPLD3_1 cd09144
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic ...
 98-265 2.29e-44

Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD3; Putative catalytic domain, repeat 1, of phospholipase D3 (PLD3, EC 3.1.4.4). The human protein is also known as Hu-K4 or HUK4 and it was identified as a human homolog of the vaccinia virus protein K4, which is encoded by the HindIII K4L gene. PLD3 is found in many human organs with highest expression levels found in the central nervous system. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD3 has been assigned to the PLD superfamily although no catalytic activity has been detected experimentally. PLD3 is a membrane-bound protein that colocalizes with protein disulfide isomerase, an endoplasmic reticulum (ER) protein. Like other homologs of protein K4, PLD3 might alter the lipid content of associated membranes by selectively hydrolyzing phosphatidylcholine (PC) into the corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement.


Pssm-ID: 197242 [Multi-domain]  Cd Length: 172  Bit Score: 153.95  E-value: 2.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  98 LVESLPLGLNY-SQWQSHPqlsSTFDAWQLLLGRAKASLDIVSPHWTLRGLDVN--DSSTGPGDQLFQQLLSNGDAGrpk 174
Cdd:cd09144    2 LVESIPEGLVFnSSSTINP---SIYQAWLNLISAAQSSLDIASFYWTLTNSDTHtqEPSANQGEQILKKLGQLSQSG--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 175 LRVRIVVNRSHDSLWHADARILANYGAaDVVGINF-------LHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNC 247
Cdd:cd09144   76 VYVRIAVDKPADPKPMEDINALSSYGA-DVRMVDMrklttgvLHTKFWVVDKKHFYIGSANMDWRSLTQVKELGAVVYNC 154

                        170
                 ....*....|....*...
gi 665408893 248 PHLALDLGKIFKAYWYLG 265
Cdd:cd09144  155 SCLAEDLGKIFEAYWYLG 172
PLDc_vPLD5_2 cd09149
Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative ...
 300-487 2.26e-40

Putative catalytic domain, repeat 2, of inactive veterbrate phospholipase PLD5; Putative catalytic domain, repeat 2, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD.


Pssm-ID: 197247  Cd Length: 188  Bit Score: 143.84  E-value: 2.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 300 YLSTSPPELIATGRTRELDAILEAIDKATDVIYLSLMEYSPRLRRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYS 379
Cdd:cd09149    1 YVSTSPKLFCPKHRSNDLEAIYRVIQDAKQFIYISVMDYLPLLSRSYARRYWSRIDSKIREALVLRSVRVRLLISFWRKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 380 DPSEDHFLRSLQALDKITEGVDIQMRRFvvpttnELERISGG---RVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLV 456
Cdd:cd09149   81 DPLTFNFVSSLKSLCTEQANCSLEVKFF------DLEEESDCtspRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGVGLV 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 665408893 457 LQD---MEYNNNSLRTDLMAIFLRDWFSPYALPL 487
Cdd:cd09149  155 INQadgVEENNATIIEQLRAAFERDWYSNYAKSL 188
PLDc_3 pfam13918
PLD-like domain;
233-410 2.68e-36

PLD-like domain;


Pssm-ID: 464040  Cd Length: 180  Bit Score: 132.44  E-value: 2.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  233 SLTQRKELGVLARNCPHLALDLGKIFKAYWYLG-SNEVPKSWPW-IYHTHINQRRpllLNINKKHTM-RAYLSTSPPELI 309
Cdd:pfam13918   1 SLGQIKELGLVFTNCKCLALDLMNIFALFSSLIfENKVPFTWSKrLCCAVDNEKA---LNFHLNESGgGAFFSDSPELFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  310 ATGRTRELDAILEAIDKATDVIYLSLMEYSPRLRRSNKLEYWPVIDNALRRAALERGVAIKVLISWWKYSDPSEDHFLRS 389
Cdd:pfam13918  78 GFNRSFDEDAILHRIDDAKLSIDIALLDMLPIIKHAGAREYWPDIDDAILEAAILRGVKVRLIISEWKEADPLSFNAARS 157

                         170       180
                  ....*....|....*....|.
gi 665408893  390 LQALDKITEGVDIQMRRFVVP 410
Cdd:pfam13918 158 LDAFCTEIANCDLKVKFFDLE 178
PLDc_vPLD4_1 cd09145
Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic ...
 98-264 1.18e-33

Putative catalytic domain, repeat 1, of vertebrate phospholipase PLD4; Putative catalytic domain, repeat 1, of vertebrate phospholipases D4 (PLD4, EC 3.1.4.4), homologs of the vaccinia virus protein K4 which is encoded by the HindIII K4L gene. Due to the presence of two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), PLD4 has been assigned to PLD superfamily although no catalytic activity has been detected to date. Unlike PLD1 and PLD2, PLD4 does not contain Phox (PX) and Pleckstrin homology (PH) domains but has a putative transmembrane domain. Like other vertebrate homologs of protein K4, PLD4 might be associated with Golgi membranes and alter their lipid content by selectively hydrolyze phosphatidylcholine (PC) into corresponding phosphatidic acid, which is thought to be involved in the regulation of lipid movement.


Pssm-ID: 197243 [Multi-domain]  Cd Length: 170  Bit Score: 125.02  E-value: 1.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  98 LVESLPLGLNYSQwqSHPQLSSTFDAWQLLLGRAKASLDIVSPHWTLRGLD--VNDSSTGPGDQL---FQQLLSNgdagr 172
Cdd:cd09145    1 LVESIPEDLTYEG--NSTFALPLQKAWTKLLDMAQEQVHVASYYWSLTGEDigVNDSSSLPGEDIlkeLAELLSR----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 173 pKLRVRIVVNRSHDSLWHADARILANYGAaDVVGINF-------LHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLAR 245
Cdd:cd09145   74 -NVSVRAAASIPTLAANSTDLKILRQKGA-HVRKVNFgrltggvLHSKFWIIDKKHIYVGSANMDWRSLTQVKELGAVIY 151

                        170
                 ....*....|....*....
gi 665408893 246 NCPHLALDLGKIFKAYWYL 264
Cdd:cd09145  152 NCSSLAKDLHKTFQTYWVL 170
PLDc_vPLD5_1 cd09146
Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative ...
 97-264 9.82e-32

Putative catalytic domain, repeat 1, of inactive veterbrate phospholipase PLD5; Putative catalytic domain, repeat 1, of inactive veterbrate phospholipases D5 (PLD5, EC 3.1.4.4), homologs of the vaccinia virus protein K4 encoded by the HindIII K4L gene. Vertebrate PLD5 has been assigned to the PLD superfamily, since it shows high sequence similarity to other human homologs of protein K4, which contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). However, due to the lack of functionally important histidine and lysine residues in the HKD motif, vetebrate PLD5 has been characterized as an inactive PLD.


Pssm-ID: 197244 [Multi-domain]  Cd Length: 163  Bit Score: 119.58  E-value: 9.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  97 ELVESLPLGLNYSQwQSHPQLSsTFDAWQLLLGRAKASLDIVSPHWTLRGLDVndsSTGPGDQLFQQLLSNGDAGrpkLR 176
Cdd:cd09146    1 ALVENIPDGINFSE-HAPPHLP-LSQGWMNLLDMAVKSVEIVSPLWDLNASHP---SACQGQRLFERLLGLASRG---VE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 177 VRIVVNRSHDSlwhADARILANYGAaDVVGINF-------LHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNCPH 249
Cdd:cd09146   73 LKIVSGITDST---EVLVLLKKKGA-EVHYVNMtaltkgrLQSSFWIVDKRHVYIGSASMDWRSLGQRKELGVIVYNCSC 148

                        170
                 ....*....|....*
gi 665408893 250 LALDLGKIFKAYWYL 264
Cdd:cd09146  149 LALDLHRVFALYWSL 163
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 122-243 3.10e-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: 60.61  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 122 DAWQLLLGRAKASLDIVSPHWtlrgldvndsSTGPGDQLFQQLLsngDAGRPKLRVRIVVNRSHDSLWHADARILANYGA 201
Cdd:cd00138    1 EALLELLKNAKESIFIATPNF----------SFNSADRLLKALL---AAAERGVDVRLIIDKPPNAAGSLSAALLEALLR 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665408893 202 ADV---------VGINFLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVL 243
Cdd:cd00138   68 AGVnvrsyvtppHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREAGVL 118
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 127-262 3.35e-09

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: 58.42  E-value: 3.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 127 LLGRAKASLDIVSPHWTlrgldvndsstgPGDQLFQQLLSNGDAGrpkLRVRIVVNRSHDSL--WHADARILANYGAADV 204
Cdd:COG1502  211 AIASARRRIYIETPYFV------------PDRSLLRALIAAARRG---VDVRILLPAKSDHPlvHWASRSYYEELLEAGV 275

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408893 205 ----VGINFLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNcPHLALDLGKIFKAYW 262
Cdd:COG1502  276 riyeYEPGFLHAKVMVVDDEWALVGSANLDPRSLRLNFEVNLVIYD-PEFAAQLRARFEEDL 336
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 317-481 3.15e-08

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: 55.33  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 317 LDAILEAIDKATDVIYLSLMEYSPRlrrsnklEYWPVIDNALRRAAlERGVAIKVLISWWkYSDPSEDHFLRSLQAldki 396
Cdd:COG1502   27 FAALLEAIEAARRSIDLEYYIFDDD-------EVGRRLADALIAAA-RRGVKVRVLLDGI-GSRALNRDFLRRLRA---- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 397 tEGVDIqmrRFVVPTTNELERIsgGRVNCNSYLVTD-RVAFIGTSSFSGEHFTYSAGIGlvlqdmEYNNNSLR------T 469
Cdd:COG1502   94 -AGVEV---RLFNPVRLLFRRL--NGRNHRKIVVIDgRVAFVGGANITDEYLGRDPGFG------PWRDTHVRiegpavA 161

                        170
                 ....*....|..
gi 665408893 470 DLMAIFLRDWFS 481
Cdd:COG1502  162 DLQAVFAEDWNF 173
PLDc_2 pfam13091
PLD-like domain;
127-262 1.99e-07

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 49.98  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  127 LLGRAKASLDIVSPHWTlrgldvndsstgPGDQLFQQLLSngDAGRPKlRVRIVVNRSHDSLW---HADARILANYGAAD 203
Cdd:pfam13091   4 LINSAKKSIDIATYYFV------------PDREIIDALIA--AAKRGV-DVRIILDSNKDDAGgpkKASLKELRSLLRAG 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665408893  204 V------VGINFLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNcPHLALDLGKIFKAYW 262
Cdd:pfam13091  69 VeireyqSFLRSMHAKFYIIDGKTVIVGSANLTRRALRLNLENNVVIKD-PELAQELEKEFDRLW 132
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 120-374 4.09e-07

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: 51.87  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 120 TFDAWQLLLGRAKASLDIVSphWTLRgldvndsSTGPGDQLFQQLLsngDAGRPKLRVRIVVnrshDSL--WHADARILA 197
Cdd:COG1502   26 AFAALLEAIEAARRSIDLEY--YIFD-------DDEVGRRLADALI---AAARRGVKVRVLL----DGIgsRALNRDFLR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 198 NYGAADV------------VGINF-LHSKLWLVDGEHFYLGTASMDWRSLTQRKELG------VLARNcPHLAlDLGKIF 258
Cdd:COG1502   90 RLRAAGVevrlfnpvrllfRRLNGrNHRKIVVIDGRVAFVGGANITDEYLGRDPGFGpwrdthVRIEG-PAVA-DLQAVF 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 259 KAYWYLGSNEVPKSWPWIYHTHInqrrplllninkkhtmrAYLSTSPpeliatGRTRE--LDAILEAIDKATDVIYLSLM 336
Cdd:COG1502  168 AEDWNFATGEALPFPEPAGDVRV-----------------QVVPSGP------DSPREtiERALLAAIASARRRIYIETP 224

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 665408893 337 EYSPRlrrsnkleywPVIDNALRRAAlERGVAIKVLIS 374
Cdd:COG1502  225 YFVPD----------RSLLRALIAAA-RRGVDVRILLP 251
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
 208-233 5.21e-07

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: 45.84  E-value: 5.21e-07
                           10        20
                   ....*....|....*....|....*.
gi 665408893   208 NFLHSKLWLVDGEHFYLGTASMDWRS 233
Cdd:smart00155   3 GVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
 208-233 6.65e-06

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


Pssm-ID: 395489 [Multi-domain]  Cd Length: 28  Bit Score: 42.79  E-value: 6.65e-06
                          10        20
                  ....*....|....*....|....*.
gi 665408893  208 NFLHSKLWLVDGEHFYLGTASMDWRS 233
Cdd:pfam00614   3 GRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 127-262 8.35e-06

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 45.34  E-value: 8.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 127 LLGRAKASLDIVSPhwtlrgldvndsSTGPGDQLFQQLLSNGDAGRpklRVRIVVNRSH-DSLWH-ADARILANYGAAD- 203
Cdd:cd09128   18 LIDSAEESLLIQNE------------EMGDDAPILDALVDAAKRGV---DVRVLLPSAWsAEDERqARLRALEGAGVPVr 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665408893 204 --VVGINFLHSKLWLVDGEHFYLGtaSMDWR--SLTQRKELGVLARNcPHLALDLGKIFKAYW 262
Cdd:cd09128   83 llKDKFLKIHAKGIVVDGKTALVG--SENWSanSLDRNREVGLIFDD-PEVAAYLQAVFESDW 142
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
 172-242 7.57e-05

Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; Catalytic domain, repeat 2, of phospholipase D (PLD, EC 3.1.4.4) found in yeast, plants, and vertebrates, and their bacterial homologs. PLDs are involved in signal transduction, vesicle formation, protein transport, and mitosis by participating in phospholipid metabolism. They hydrolyze the terminal phosphodiester bond of phospholipids resulting in the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. PLDs also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Both prokaryotic and eukaryotic PLDs have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. PLDs are active as bi-lobed monomers. Each monomer contains two domains, each of which carries one copy of the HKD motif. Two HKD motifs from two domains form a single active site. PLDs utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197204 [Multi-domain]  Cd Length: 146  Bit Score: 42.67  E-value: 7.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 172 RPKLRVRIVVNRSHD-----SLWHADARILAN-YGAADVVGINFL-------------------HSKLWLVDGEHFYLGT 226
Cdd:cd09105   47 NPGLRVVLVLPALPDavafgADDGLDALALLAlLLLADAAPDRVAvfslathrrgllggppiyvHSKVVIVDDEWATVGS 126

                         90
                 ....*....|....*.
gi 665408893 227 ASMDWRSLTQRKELGV 242
Cdd:cd09105  127 ANLNRRSMTWDTELNL 142
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
 127-276 1.02e-04

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: 43.75  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 127 LLGRAKASLDIVSPHWTLrgldvndssTGPGDQLFQQLLSNGdagrpkLRVRIVVN--RSHDSLW-HAD-----ARILAN 198
Cdd:cd09113   25 LLKNAKREVLIVSPYFVP---------GDEGVALLAELARRG------VRVRILTNslAATDVPAvHSGyaryrKRLLKA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 199 ----Y---GAADVVGINF---------LHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNcPHLALDLGKIFK--- 259
Cdd:cd09113   90 gvelYelkPDAAKRKRLRglfgssrasLHAKSFVIDDRLVFVGSFNLDPRSAYLNTEMGLVIDS-PELAAQLRAAMEedl 168

                        170       180
                 ....*....|....*....|
gi 665408893 260 ---AYWYLGSNEVPKSWPWI 276
Cdd:cd09113  169 apsAYWVLLLDDGGLVWETE 188
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
 318-479 1.05e-04

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 42.26  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 318 DAILEAIDKATDVIYLslmeYSPRLRRSNKLEywpvidNALRRAAlERGVAIKVLISwwkYSDPSEDHFLRSLQALdkit 397
Cdd:cd09128   13 EALLALIDSAEESLLI----QNEEMGDDAPIL------DALVDAA-KRGVDVRVLLP---SAWSAEDERQARLRAL---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 398 EGVDIQMRRFVVPTtnelerisgGRVNCNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLQDMEYNNnslrtDLMAIFLR 477
Cdd:cd09128   75 EGAGVPVRLLKDKF---------LKIHAKGIVVDGKTALVGSENWSANSLDRNREVGLIFDDPEVAA-----YLQAVFES 140


                 ..
gi 665408893 478 DW 479
Cdd:cd09128  141 DW 142
PLDc_2 pfam13091
PLD-like domain;
320-479 4.44e-04

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 40.35  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  320 ILEAIDKATDVIYLSLMEYSPRLRrsnkleywpvIDNALRRAALeRGVAIKVLISWWKYSDPSEDHFLRSlQALDKITEG 399
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPDRE----------IIDALIAAAK-RGVDVRIILDSNKDDAGGPKKASLK-ELRSLLRAG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893  400 VDIqmrRFVVPTTNELERisggrvncNSYLVTDRVAFIGTSSFSGEHFTYSAGIGLVLQDMEynnnsLRTDLMAIFLRDW 479
Cdd:pfam13091  69 VEI---REYQSFLRSMHA--------KFYIIDGKTVIVGSANLTRRALRLNLENNVVIKDPE-----LAQELEKEFDRLW 132
PLDc_SMU_988_like_2 cd09160
Putative catalytic domain, repeat 2, of Streptococcus mutans uncharacterized protein SMU_988 ...
 209-248 8.33e-04

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: 40.17  E-value: 8.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 665408893 209 FLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARNCP 248
Cdd:cd09160   92 FIHAKTFVSDDKAAVVGTINLDYRSLYLHFECGVYMYDTP 131
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
 127-234 8.97e-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: 40.15  E-value: 8.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 127 LLGRAKASLDIVSPHWTlrgldvndsstgPGDQLFQQLLSngdAGRPKLRVRIVVNRSHDS---LWHADARI--LANYGa 201
Cdd:cd09112   19 AINSAKKSIYIQTPYFI------------PDESLLEALKT---AALSGVDVRIMIPGKPDHklvYWASRSYFeeLLKAG- 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 665408893 202 advVGI-----NFLHSKLWLVDGEHFYLGTASMDWRSL 234
Cdd:cd09112   83 ---VKIyeynkGFLHSKTLIVDDEIASVGTANLDIRSF 117
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
 125-258 3.99e-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: 38.29  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 125 QLLLGRAKASLDIVSPHWTlrgldvndsstgPGDQLFQQLLsngDAGRPKLRVRIVV-NRSHDSLWHADARILanYGAAD 203
Cdd:cd09159   17 LVAIAAARRRIWIANAYFV------------PDRRLRRALI---EAARRGVDVRLLLpGKSDDPLTVAASRAL--YGKLL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408893 204 VVGIN-------FLHSKLWLVDGEHFYLGTASMDWRSLTQRKELGVLARnCPHLALDLGKIF 258
Cdd:cd09159   80 RAGVRifeyqpsMLHAKTAVIDGDWATVGSSNLDPRSLRLNLEANLVVE-DPAFAAQLEELF 140
cls PRK01642
cardiolipin synthetase; Reviewed
 177-234 6.66e-03

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 38.99  E-value: 6.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665408893 177 VRIVVNRSHDSL--WHAdARilANYGAADVVGIN-------FLHSKLWLVDGEHFYLGTASMDWRSL 234
Cdd:PRK01642 361 VRIIIPSKNDSLlvFWA-SR--AFFTELLEAGVKiyryeggLLHTKSVLVDDELALVGTVNLDMRSF 424
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 318-457 7.59e-03

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: 36.34  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408893 318 DAILEAIDKATDVIYLSLMEYSPrlrrsnklEYWPVIDNALRRAAlERGVAIKVLISWWKYSDPSedhfLRSLQALDKIT 397
Cdd:cd00138    1 EALLELLKNAKESIFIATPNFSF--------NSADRLLKALLAAA-ERGVDVRLIIDKPPNAAGS----LSAALLEALLR 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665408893 398 EGVDIqmrRFVVPTTNELERisggrvNCNSYLVTD-RVAFIGTSSFSGEHFTYSAGIGLVL 457
Cdd:cd00138   68 AGVNV---RSYVTPPHFFER------LHAKVVVIDgEVAYVGSANLSTASAAQNREAGVLV 119
PLDc_CLS_unchar2_1 cd09157
Putative catalytic domain, repeat 1, of uncharacterized proteins similar to bacterial ...
 319-388 9.74e-03

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


Pssm-ID: 197254 [Multi-domain]  Cd Length: 155  Bit Score: 36.77  E-value: 9.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665408893 319 AILEAIDKATDVIYLS--LMEYSPRLRRsnkleywpvIDNALRRAAlERGVAIKVLI----SWwkYSDPSEDHFLR 388
Cdd:cd09157    9 AMLEAIDAARHSIALSsyIFDNDGVGRE---------FVDALAEAV-ARGVDVRVLIdgvgAR--YSRPSIRRRLR 72
 
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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