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Conserved domains on  [gi|156564407|ref|NP_002654|]
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phospholipase D2 isoform PLD2A [Homo sapiens]

Protein Classification

phospholipase D( domain architecture ID 1002279)

phospholipase D (PLD) catalyzes hydrolysis of the diester bond of phospholipids to generate phosphatidic acid and the free lipid headgroup

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02866 super family cl33584
phospholipase D
66-918 0e+00

phospholipase D


The actual alignment was detected with superfamily member PLN02866:

Pssm-ID: 215467 [Multi-domain]  Cd Length: 1068  Bit Score: 607.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407   66 TAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKK-----YRHF--------QELH------RDLLRHKVLMSLLPL 126
Cdd:PLN02866   14 KATIVSVSRPDAGDISPVLLSYTIELQYKQFKWTLYKKasqvlYLHFalkkrafiEELHekqeqvKEWLQNLGIGDHPAV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  127 AR-------FAVAYSPARDAGNREMPSL-------PRAG--PEGSTRHAASKQKYLENYLNRLLTMsfyrNYHAMTEFLE 190
Cdd:PLN02866   94 VQdddepddGTVPLHHDESAKNRDVPSSaalpvirPALGrqQSISDRAKVAMQEYLNHFLGNLDIV----NSREVCKFLE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  191 VSQLSFIPDLGRKGLEGMIRKRsggH--RVPG----LTCCGRDQVCY---RWSKRWLVVKDSFLLYmcLE---TGAISFV 258
Cdd:PLN02866  170 VSKLSFSPEYGPKLKEGYVMVK---HlpKIPKsddsRGCFPCCCFSCcndNWQKVWAVLKPGFLAL--LEdpfDAKPLDI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  259 QLFD--PGFEVQVGKRSTEA---------RHGVRIDTSHRSLILKCSSYRQARWWAQEITELAQGPGRDFLQLHRHDSYA 327
Cdd:PLN02866  245 IVFDvlPASNGNGEGQISLAkeikernplRFGFKVTCGNRSIRLRTKSSAKVKDWVAAINDAGLRPPEGWCHPHRFGSFA 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  328 PPR----PGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDW-RLDIMLKRKAEEGVRVSILLF 402
Cdd:PLN02866  325 PPRglteDGSQAQWFIDGHAAFEAIASAIENAKSEIFITGWWLCPELYLRRPFHDHESsRLDSLLEAKAKQGVQIYILLY 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  403 KEVELALGINSGYSKRALMLLHPNIKVMRHPDQ----VTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDlgds 478
Cdd:PLN02866  405 KEVALALKINSVYSKRRLLGIHENVKVLRYPDHfssgVYLWSHHEKLVIVDYQICFIGGLDLCFGRYDTPEHRVGD---- 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  479 sesaasQPPTprpdspatpdlshnqfFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGLPARDLARH 558
Cdd:PLN02866  481 ------CPPV----------------IWPGKDYYNPRESEPNSWEDTMKDELDRRKYPRMPWHDVHCALWGPPCRDVARH 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  559 FIQRWNF-------------------------------------------------TKTTKAKYKTPTYPYLLPKST--- 586
Cdd:PLN02866  539 FVQRWNYakrnkapneqaipllmphhhmviphylggseeeeiesknqednqkgiarQDSFSSRSSLQDIPLLLPQEAdat 618
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  587 -------------STANQLPFTLPGGQCTTV------------------------------------------------- 604
Cdd:PLN02866  619 dgsggghklngmnSTNGSLSFSFRKSKIEPVlpdtpmkgfvddlgfldlsvkmssaergskesdsewwetqergdqvgsa 698
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  605 --------------QVLRSVDRWSAGT--LENSILNAYLHTIRESQHFLYIENQFFISCSDG-RTVLNKVGDEIVDRILK 667
Cdd:PLN02866  699 devgqvgprvscrcQVIRSVSQWSAGTsqVEESIHAAYCSLIEKAEHFIYIENQFFISGLSGdDTIQNRVLEALYRRILR 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  668 AHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGEL--G 745
Cdd:PLN02866  779 AHKEKKCFRVIIVIPLLPGFQGGVDDGGAASVRAIMHWQYRTICRGKNSILHNLYDLLGPKTHDYISFYGLRAYGRLfeG 858
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  746 GHPVSELIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILG 825
Cdd:PLN02866  859 GPLATSQIYVHSKIMIVDDRAALIGSANINDRSLLGSRDSEIGVVIEDKEFVDSSMNGKPWKAGKFAHSLRLSLWSEHLG 938
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  826 ANTRPDLDLRDPICDDFFQ-LWQDMAESNANIYEQIFRCLPSNATRSLRTLREY----------------VAVEPLAT-- 886
Cdd:PLN02866  939 LRAGEIDKIIDPVCDTTYKdLWMATAKTNTDIYQDVFSCIPNDLIHSRAALRQSmasrkeklghttidlgIAPEKLESye 1018
                        1050      1060      1070
                  ....*....|....*....|....*....|....*..
gi 156564407  887 -----VSPPLARseLTQVQGHLVHFPLKFLEDESLLP 918
Cdd:PLN02866 1019 ngdikSSDPMER--LKSVRGHLVSFPLDFMCQEDLRP 1053
 
Name Accession Description Interval E-value
PLN02866 PLN02866
phospholipase D
66-918 0e+00

phospholipase D


Pssm-ID: 215467 [Multi-domain]  Cd Length: 1068  Bit Score: 607.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407   66 TAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKK-----YRHF--------QELH------RDLLRHKVLMSLLPL 126
Cdd:PLN02866   14 KATIVSVSRPDAGDISPVLLSYTIELQYKQFKWTLYKKasqvlYLHFalkkrafiEELHekqeqvKEWLQNLGIGDHPAV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  127 AR-------FAVAYSPARDAGNREMPSL-------PRAG--PEGSTRHAASKQKYLENYLNRLLTMsfyrNYHAMTEFLE 190
Cdd:PLN02866   94 VQdddepddGTVPLHHDESAKNRDVPSSaalpvirPALGrqQSISDRAKVAMQEYLNHFLGNLDIV----NSREVCKFLE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  191 VSQLSFIPDLGRKGLEGMIRKRsggH--RVPG----LTCCGRDQVCY---RWSKRWLVVKDSFLLYmcLE---TGAISFV 258
Cdd:PLN02866  170 VSKLSFSPEYGPKLKEGYVMVK---HlpKIPKsddsRGCFPCCCFSCcndNWQKVWAVLKPGFLAL--LEdpfDAKPLDI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  259 QLFD--PGFEVQVGKRSTEA---------RHGVRIDTSHRSLILKCSSYRQARWWAQEITELAQGPGRDFLQLHRHDSYA 327
Cdd:PLN02866  245 IVFDvlPASNGNGEGQISLAkeikernplRFGFKVTCGNRSIRLRTKSSAKVKDWVAAINDAGLRPPEGWCHPHRFGSFA 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  328 PPR----PGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDW-RLDIMLKRKAEEGVRVSILLF 402
Cdd:PLN02866  325 PPRglteDGSQAQWFIDGHAAFEAIASAIENAKSEIFITGWWLCPELYLRRPFHDHESsRLDSLLEAKAKQGVQIYILLY 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  403 KEVELALGINSGYSKRALMLLHPNIKVMRHPDQ----VTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDlgds 478
Cdd:PLN02866  405 KEVALALKINSVYSKRRLLGIHENVKVLRYPDHfssgVYLWSHHEKLVIVDYQICFIGGLDLCFGRYDTPEHRVGD---- 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  479 sesaasQPPTprpdspatpdlshnqfFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGLPARDLARH 558
Cdd:PLN02866  481 ------CPPV----------------IWPGKDYYNPRESEPNSWEDTMKDELDRRKYPRMPWHDVHCALWGPPCRDVARH 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  559 FIQRWNF-------------------------------------------------TKTTKAKYKTPTYPYLLPKST--- 586
Cdd:PLN02866  539 FVQRWNYakrnkapneqaipllmphhhmviphylggseeeeiesknqednqkgiarQDSFSSRSSLQDIPLLLPQEAdat 618
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  587 -------------STANQLPFTLPGGQCTTV------------------------------------------------- 604
Cdd:PLN02866  619 dgsggghklngmnSTNGSLSFSFRKSKIEPVlpdtpmkgfvddlgfldlsvkmssaergskesdsewwetqergdqvgsa 698
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  605 --------------QVLRSVDRWSAGT--LENSILNAYLHTIRESQHFLYIENQFFISCSDG-RTVLNKVGDEIVDRILK 667
Cdd:PLN02866  699 devgqvgprvscrcQVIRSVSQWSAGTsqVEESIHAAYCSLIEKAEHFIYIENQFFISGLSGdDTIQNRVLEALYRRILR 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  668 AHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGEL--G 745
Cdd:PLN02866  779 AHKEKKCFRVIIVIPLLPGFQGGVDDGGAASVRAIMHWQYRTICRGKNSILHNLYDLLGPKTHDYISFYGLRAYGRLfeG 858
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  746 GHPVSELIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILG 825
Cdd:PLN02866  859 GPLATSQIYVHSKIMIVDDRAALIGSANINDRSLLGSRDSEIGVVIEDKEFVDSSMNGKPWKAGKFAHSLRLSLWSEHLG 938
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  826 ANTRPDLDLRDPICDDFFQ-LWQDMAESNANIYEQIFRCLPSNATRSLRTLREY----------------VAVEPLAT-- 886
Cdd:PLN02866  939 LRAGEIDKIIDPVCDTTYKdLWMATAKTNTDIYQDVFSCIPNDLIHSRAALRQSmasrkeklghttidlgIAPEKLESye 1018
                        1050      1060      1070
                  ....*....|....*....|....*....|....*..
gi 156564407  887 -----VSPPLARseLTQVQGHLVHFPLKFLEDESLLP 918
Cdd:PLN02866 1019 ngdikSSDPMER--LKSVRGHLVSFPLDFMCQEDLRP 1053
PLDc_vPLD2_2 cd09845
Catalytic domain, repeat 2, of vertebrate phospholipase D2; Catalytic domain, repeat 2, of ...
614-795 1.25e-126

Catalytic domain, repeat 2, of vertebrate phospholipase D2; Catalytic domain, repeat 2, of vertebrate phospholipase D2 (PLD2). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. They also catalyze a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Vertebrate PLD2 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These 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: 197303 [Multi-domain]  Cd Length: 182  Bit Score: 379.61  E-value: 1.25e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 614 SAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPGFEGDIST 693
Cdd:cd09845    1 SAGTLENSILNAYLHTIENSQHYLYLENQFFISCADGRTVLNKIGDAIVKRILKAHSQGWCFRVFVVIPLLPGFEGDIST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 694 GGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSAN 773
Cdd:cd09845   81 GGGNSIQAILHFTYRTICRGEYSILSRLKEAMGTAWTDYISICGLRTHGELGGSPVTELIYIHSKVLIADDRTVIIGSAN 160
                        170       180
                 ....*....|....*....|..
gi 156564407 774 INDRSLLGKRDSELAVLIEDTE 795
Cdd:cd09845  161 INDRSMLGKRDSELAVLVEDTE 182
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
319-795 1.20e-35

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: 139.31  E-value: 1.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 319 QLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIFItdwwlspEVYLkrpAHSDDWRLDIM--LKRKAEEGVR 396
Cdd:COG1502    1 KAAPLAAGLPLVGGNRVTLLVDGDEAFAALLEAIEAARRSIDL-------EYYI---FDDDEVGRRLAdaLIAAARRGVK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 397 VSILlfkeVElalGINSGYSKRALM--LLHPNIKVMR-HPDQVTLWA----HHEKLLVVDQVVAFLGGLDLAYGRWDDLH 469
Cdd:COG1502   71 VRVL----LD---GIGSRALNRDFLrrLRAAGVEVRLfNPVRLLFRRlngrNHRKIVVIDGRVAFVGGANITDEYLGRDP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 470 yrltdlgdssesaasqpptprpdspatpdlshnqffwlgkdysnlitkdwvqldrpfedfidrettPRMPWRDVGVVVHG 549
Cdd:COG1502  144 ------------------------------------------------------------------GFGPWRDTHVRIEG 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 550 LPARDLARHFIQRWNFtkttkakyktptypyllpkstSTANQLPFTLPGGQcTTVQVLRSvdrwSAGTLENSILNAYLHT 629
Cdd:COG1502  158 PAVADLQAVFAEDWNF---------------------ATGEALPFPEPAGD-VRVQVVPS----GPDSPRETIERALLAA 211
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 630 IRESQHFLYIENQFFIscsdgrtvlnkVGDEIVDRILKAHKQGwcYRVYVLLPllpgfegdistggGNSIQAILHFTYRt 709
Cdd:COG1502  212 IASARRRIYIETPYFV-----------PDRSLLRALIAAARRG--VDVRILLP-------------AKSDHPLVHWASR- 264
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 710 lcrgeySILHRLKAAmgtawrdyisicGLRTHgELGGhpvselIYIHSKVLIADDRTVIIGSANINDRSLlgKRDSELAV 789
Cdd:COG1502  265 ------SYYEELLEA------------GVRIY-EYEP------GFLHAKVMVVDDEWALVGSANLDPRSL--RLNFEVNL 317

                 ....*.
gi 156564407 790 LIEDTE 795
Cdd:COG1502  318 VIYDPE 323
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
92-192 5.40e-13

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 65.34  E-value: 5.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407   92 THGDFSWTTKKKYRHFQELHRDLLRHK--VLMSLLPLARFAVAYSPardagnrempslpragpegstRHAASKQKYLENY 169
Cdd:pfam00787   3 TFSLEEWSVRRRYSDFVELHKKLLRKFpsVIIPPLPPKRWLGRYNE---------------------EFIEKRRKGLEQY 61
                          90       100
                  ....*....|....*....|...
gi 156564407  170 LNRLLTMSFYRNYHAMTEFLEVS 192
Cdd:pfam00787  62 LQRLLQHPELRNSEVLLEFLESD 84
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
71-190 4.73e-11

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 60.44  E-value: 4.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407    71 GTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSLLPLarfavaysPARdagnREMPSLPRA 150
Cdd:smart00312   1 VVEPEKIGDGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPL--------PGK----KLFGRLNNF 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 156564407   151 GPEGSTRHAASkqkyLENYLNRLLTMS-FYRNYHAMTEFLE 190
Cdd:smart00312  69 SEEFIEKRRRG----LEKYLQSLLNHPeLINHSEVVLEFLE 105
 
Name Accession Description Interval E-value
PLN02866 PLN02866
phospholipase D
66-918 0e+00

phospholipase D


Pssm-ID: 215467 [Multi-domain]  Cd Length: 1068  Bit Score: 607.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407   66 TAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKK-----YRHF--------QELH------RDLLRHKVLMSLLPL 126
Cdd:PLN02866   14 KATIVSVSRPDAGDISPVLLSYTIELQYKQFKWTLYKKasqvlYLHFalkkrafiEELHekqeqvKEWLQNLGIGDHPAV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  127 AR-------FAVAYSPARDAGNREMPSL-------PRAG--PEGSTRHAASKQKYLENYLNRLLTMsfyrNYHAMTEFLE 190
Cdd:PLN02866   94 VQdddepddGTVPLHHDESAKNRDVPSSaalpvirPALGrqQSISDRAKVAMQEYLNHFLGNLDIV----NSREVCKFLE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  191 VSQLSFIPDLGRKGLEGMIRKRsggH--RVPG----LTCCGRDQVCY---RWSKRWLVVKDSFLLYmcLE---TGAISFV 258
Cdd:PLN02866  170 VSKLSFSPEYGPKLKEGYVMVK---HlpKIPKsddsRGCFPCCCFSCcndNWQKVWAVLKPGFLAL--LEdpfDAKPLDI 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  259 QLFD--PGFEVQVGKRSTEA---------RHGVRIDTSHRSLILKCSSYRQARWWAQEITELAQGPGRDFLQLHRHDSYA 327
Cdd:PLN02866  245 IVFDvlPASNGNGEGQISLAkeikernplRFGFKVTCGNRSIRLRTKSSAKVKDWVAAINDAGLRPPEGWCHPHRFGSFA 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  328 PPR----PGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDW-RLDIMLKRKAEEGVRVSILLF 402
Cdd:PLN02866  325 PPRglteDGSQAQWFIDGHAAFEAIASAIENAKSEIFITGWWLCPELYLRRPFHDHESsRLDSLLEAKAKQGVQIYILLY 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  403 KEVELALGINSGYSKRALMLLHPNIKVMRHPDQ----VTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDlgds 478
Cdd:PLN02866  405 KEVALALKINSVYSKRRLLGIHENVKVLRYPDHfssgVYLWSHHEKLVIVDYQICFIGGLDLCFGRYDTPEHRVGD---- 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  479 sesaasQPPTprpdspatpdlshnqfFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGLPARDLARH 558
Cdd:PLN02866  481 ------CPPV----------------IWPGKDYYNPRESEPNSWEDTMKDELDRRKYPRMPWHDVHCALWGPPCRDVARH 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  559 FIQRWNF-------------------------------------------------TKTTKAKYKTPTYPYLLPKST--- 586
Cdd:PLN02866  539 FVQRWNYakrnkapneqaipllmphhhmviphylggseeeeiesknqednqkgiarQDSFSSRSSLQDIPLLLPQEAdat 618
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  587 -------------STANQLPFTLPGGQCTTV------------------------------------------------- 604
Cdd:PLN02866  619 dgsggghklngmnSTNGSLSFSFRKSKIEPVlpdtpmkgfvddlgfldlsvkmssaergskesdsewwetqergdqvgsa 698
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  605 --------------QVLRSVDRWSAGT--LENSILNAYLHTIRESQHFLYIENQFFISCSDG-RTVLNKVGDEIVDRILK 667
Cdd:PLN02866  699 devgqvgprvscrcQVIRSVSQWSAGTsqVEESIHAAYCSLIEKAEHFIYIENQFFISGLSGdDTIQNRVLEALYRRILR 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  668 AHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGEL--G 745
Cdd:PLN02866  779 AHKEKKCFRVIIVIPLLPGFQGGVDDGGAASVRAIMHWQYRTICRGKNSILHNLYDLLGPKTHDYISFYGLRAYGRLfeG 858
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  746 GHPVSELIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILG 825
Cdd:PLN02866  859 GPLATSQIYVHSKIMIVDDRAALIGSANINDRSLLGSRDSEIGVVIEDKEFVDSSMNGKPWKAGKFAHSLRLSLWSEHLG 938
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  826 ANTRPDLDLRDPICDDFFQ-LWQDMAESNANIYEQIFRCLPSNATRSLRTLREY----------------VAVEPLAT-- 886
Cdd:PLN02866  939 LRAGEIDKIIDPVCDTTYKdLWMATAKTNTDIYQDVFSCIPNDLIHSRAALRQSmasrkeklghttidlgIAPEKLESye 1018
                        1050      1060      1070
                  ....*....|....*....|....*....|....*..
gi 156564407  887 -----VSPPLARseLTQVQGHLVHFPLKFLEDESLLP 918
Cdd:PLN02866 1019 ngdikSSDPMER--LKSVRGHLVSFPLDFMCQEDLRP 1053
PLDc_vPLD2_2 cd09845
Catalytic domain, repeat 2, of vertebrate phospholipase D2; Catalytic domain, repeat 2, of ...
614-795 1.25e-126

Catalytic domain, repeat 2, of vertebrate phospholipase D2; Catalytic domain, repeat 2, of vertebrate phospholipase D2 (PLD2). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. They also catalyze a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Vertebrate PLD2 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These 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: 197303 [Multi-domain]  Cd Length: 182  Bit Score: 379.61  E-value: 1.25e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 614 SAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPGFEGDIST 693
Cdd:cd09845    1 SAGTLENSILNAYLHTIENSQHYLYLENQFFISCADGRTVLNKIGDAIVKRILKAHSQGWCFRVFVVIPLLPGFEGDIST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 694 GGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSAN 773
Cdd:cd09845   81 GGGNSIQAILHFTYRTICRGEYSILSRLKEAMGTAWTDYISICGLRTHGELGGSPVTELIYIHSKVLIADDRTVIIGSAN 160
                        170       180
                 ....*....|....*....|..
gi 156564407 774 INDRSLLGKRDSELAVLIEDTE 795
Cdd:cd09845  161 INDRSMLGKRDSELAVLVEDTE 182
PLDc_vPLD1_2_yPLD_like_2 cd09141
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and ...
614-795 2.29e-110

Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and similar proteins; Catalytic domain, repeat 2, of vertebrate phospholipases D (PLD1 and PLD2), yeast phospholipase D (PLD SPO14/PLD1), and other similar eukaryotic proteins. These PLD enzymes play a pivotal role in transmembrane signaling and cellular regulation. 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. The vertebrate PLD1 and PLD2 are membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzymes that selectively hydrolyze phosphatidylcholine (PC). Protein cofactors and calcium may be required for their activation. Yeast SPO14/PLD1 is a calcium-independent PLD, which needs PIP2 for its activity. Instead of the regulatory calcium-dependent phospholipid-binding C2 domain in plants, most mammalian and yeast PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at the N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. The PX and PH domains are also present in zeta-type PLD from Arabidopsis, which is more closely related to vertebrate PLDs than to other plant PLD types. In addition, this subfamily also includes some related proteins which have either PX-like or PH domains in their N-termini. Like other members of the PLD superfamily, the monomer of mammalian and yeast PLDs consists of two catalytic domains, each containing one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from the two domains form a single active site. These 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: 197239 [Multi-domain]  Cd Length: 183  Bit Score: 337.22  E-value: 2.29e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 614 SAGTLENSILNAYLHTIRESQHFLYIENQFFIS-CSDGRTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPGFEGDIS 692
Cdd:cd09141    1 GGIQTEDSIQNAYLDLIENAEHFIYIENQFFISsTGGEDPVKNRIGEALVDRIIRAHKEGEKFRVYIVLPLLPGFEGDLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 693 TGGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSA 772
Cdd:cd09141   81 DPGGSSIRAIMHWQYQSICRGEHSLLERLKKEEGVDPEQYISFLSLRTHGKLGGRPVTEQIYVHSKLMIVDDRIVIIGSA 160
                        170       180
                 ....*....|....*....|...
gi 156564407 773 NINDRSLLGKRDSELAVLIEDTE 795
Cdd:cd09141  161 NINDRSMLGDRDSEIAVVIEDTE 183
PLDc_vPLD2_1 cd09843
Catalytic domain, repeat 1, of vertebrate phospholipase D2; Catalytic domain, repeat 1, of ...
335-475 1.64e-96

Catalytic domain, repeat 1, of vertebrate phospholipase D2; Catalytic domain, repeat 1, of vertebrate phospholipase D2 (PLD2). PLDs play a pivotal role in transmembrane signaling and cellular regulation. They hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. Phosphatidic acid is an essential compound involved in signal transduction. They also catalyze a transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Vertebrate PLD2 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These 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: 197301 [Multi-domain]  Cd Length: 145  Bit Score: 299.60  E-value: 1.64e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 335 ARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSG 414
Cdd:cd09843    1 TKWFVNGHGYFAAVADALEQAQEEIFITDWWLSPEVFLKRPAHGDDWRLDIILKRKAEQGVRVCVLLFKEVELALGINSG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156564407 415 YSKRALMLLHPNIKVMRHPDQVT----LWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDL 475
Cdd:cd09843   81 YSKRKLMLLHPNIKVMRHPDHVAsvvvLWAHHEKMVAIDQSVAFLGGLDLAYGRWDDSDYRLTDL 145
PLDc_vPLD1_2 cd09844
Catalytic domain, repeat 2, of vertebrate phospholipase D1; Catalytic domain, repeat 2, of ...
619-795 2.39e-93

Catalytic domain, repeat 2, of vertebrate phospholipase D1; Catalytic domain, repeat 2, of vertebrate phospholipase D1 (PLD1). PLDs play a pivotal role in transmembrane signaling and cellular regulation. 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. Vertebrate PLD1 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These 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: 197302 [Multi-domain]  Cd Length: 182  Bit Score: 292.61  E-value: 2.39e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 619 ENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNS 698
Cdd:cd09844    6 EESIHAAYVSVIENSKHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENKRYRVYVVIPLLPGFEGDISTGGGNA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 699 IQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRS 778
Cdd:cd09844   86 LQAIMHFNYRTMCRGEHSIIGQLKAEMGDQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRS 165
                        170
                 ....*....|....*..
gi 156564407 779 LLGKRDSELAVLIEDTE 795
Cdd:cd09844  166 MLGKRDSEMAVVVQDTE 182
PLDc_vPLD1_2_yPLD_like_1 cd09138
Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and ...
335-475 1.05e-85

Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and similar proteins; Catalytic domain, repeat 1, of vertebrate phospholipases D (PLD1 and PLD2), yeast phospholipase D (PLD SPO14/PLD1), and other similar eukaryotic proteins. These PLD enzymes play a pivotal role in transmembrane signaling and cellular regulation. 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. The vertebrate PLD1 and PLD2 are membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzymes that selectively hydrolyze phosphatidylcholine (PC). Protein cofactors and calcium may be required for their activation. Yeast SPO14/PLD1 is a calcium-independent PLD, which needs PIP2 for its activity. Instead of the regulatory calcium-dependent phospholipid-binding C2 domain in plants, most mammalian and yeast PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at the N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. The PX and PH domains are also present in zeta-type PLD from Arabidopsis, which is more closely related to vertebrate PLDs than to other plant PLD types. In addition, this subfamily also includes some related proteins which have either PX-like or PH domains in their N-termini. Like other members of the PLD superfamily, the monomer of mammalian and yeast PLDs consists of two catalytic domains, each containing one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from the two domains form a single active site. These 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: 197236 [Multi-domain]  Cd Length: 146  Bit Score: 270.59  E-value: 1.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 335 ARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRP-AHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINS 413
Cdd:cd09138    1 AKWYVDGKDYFWAVADAIENAKEEIFITDWWLSPELYLRRPpAGNERWRLDRLLKRKAEEGVKIYILLYKEVELALTINS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156564407 414 GYSKRALMLLHPNIKVMRHPDQ----VTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDL 475
Cdd:cd09138   81 KYTKRTLENLHPNIKVLRHPDHlpqgPLLWSHHEKIVVIDQSIAFVGGLDLCYGRWDTHQHPLTDD 146
PX_PLD2 cd07297
The phosphoinositide binding Phox Homology domain of Phospholipase D2; The PX domain is a ...
62-192 1.41e-74

The phosphoinositide binding Phox Homology domain of Phospholipase D2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. PLD activity has been detected in viruses, bacteria, yeast, plants, and mammals, but the PX domain is not present in PLDs from viruses and bacteria. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. PLD2 contains PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. It mediates EGF-dependent insulin secretion and EGF-induced Ras activation by the guanine nucleotide-exchange factor Son of sevenless (Sos). It regulates mast cell activation by associating and promoting the activation of the protein tyrosine kinase Syk. PLD2 also participates in the sphingosine 1-phosphate-mediated pathway that stimulates the migration of endothelial cells, an important factor in angiogenesis. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132830  Cd Length: 130  Bit Score: 240.20  E-value: 1.41e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  62 GVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSLLPLARFAVAYSPARDAGN 141
Cdd:cd07297    1 GVPVTAKVENTERYTTGSKVHVCTLYTVRLTHGEFTWTVKKKFKHFQELHRDLYRHKVMLSFLPLGRFAIQHRQQLEGLT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 156564407 142 REMPSLPRAGPEGStRHAASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVS 192
Cdd:cd07297   81 EEMPSLPGTDREAS-RRTASKPKYLENYLNNLLENSFYRNYHAMMEFLAVS 130
PLDc_vPLD1_1 cd09842
Catalytic domain, repeat 1, of vertebrate phospholipase D1; Catalytic domain, repeat 1, of ...
335-476 1.11e-70

Catalytic domain, repeat 1, of vertebrate phospholipase D1; Catalytic domain, repeat 1, of vertebrate phospholipase D1 (PLD1). PLDs play a pivotal role in transmembrane signaling and cellular regulation. 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. Vertebrate PLD1 is a membrane associated phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent enzyme that selectively hydrolyzes phosphatidylcholine (PC). Protein cofactors and calcium might be required for its activation. Most vertebrate PLDs have adjacent Phox (PX) and the Pleckstrin homology (PH) domains at their N-terminus, which have been shown to mediate membrane targeting of the protein and are closely linked to polyphosphoinositide signaling. Like other members of the PLD superfamily, the monomer of vertebrate PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. These 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: 197300 [Multi-domain]  Cd Length: 151  Bit Score: 230.68  E-value: 1.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 335 ARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPA-HSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINS 413
Cdd:cd09842    1 SKWYVNAKCYFEDVANAMEEAKEEIFITDWWLSPEIFLKRPVvEGNRWRLDCILKRKAQQGVRIFVMLYKEVELALGINS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156564407 414 GYSKRALMLLHPNIKVMRHPDQVT----LWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLG 476
Cdd:cd09842   81 EYSKRTLMRLHPNIKVMRHPDHVSssvyLWAHHEKIVVIDQSVAFVGGIDLAYGRWDDDEHRLTDVG 147
PH_PLD cd01254
Phospholipase D pleckstrin homology (PH) domain; PLD hydrolyzes phosphatidylcholine to ...
180-309 2.30e-47

Phospholipase D pleckstrin homology (PH) domain; PLD hydrolyzes phosphatidylcholine to phosphatidic acid (PtdOH), which can bind target proteins. PLD contains a PH domain, a PX domain and four conserved PLD signature domains. The PLD PH domain is specific for bisphosphorylated inositides. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269956  Cd Length: 136  Bit Score: 165.13  E-value: 2.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 180 RNYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVP---GLTCCGRDQVCYRWSKRWLVVKDSFLLYMC-LETGAI 255
Cdd:cd01254    1 RNHLETFEFLEVSSLSFAPELGPKGKEGYLKKRSGGHRQGwrvCHFYCCCKAMCGRWSKRWFIVKDSFLAYVKdPDSGAI 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156564407 256 SFVQLFDPGFEVQVGKRSTEA--RHGVRIDTSHRSLILKCSSYRQARWWAQEITEL 309
Cdd:cd01254   81 LDVFLFDQEFKVSRGGKETKYgsRHGLKITNLSRKLKLKCKSERKAKQWVESIEEA 136
PX_PLD cd06895
The phosphoinositide binding Phox Homology domain of Phospholipase D; The PX domain is a ...
62-192 7.56e-44

The phosphoinositide binding Phox Homology domain of Phospholipase D; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. Members of this subfamily contain PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. PLD activity has been detected in viruses, bacteria, yeast, plants, and mammals, but the PX domain is not present in PLDs from viruses and bacteria. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. Vertebrates contain two PLD isozymes, PLD1 and PLD2. PLD1 is located mainly in intracellular membranes while PLD2 is associated with plasma membranes. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132805  Cd Length: 140  Bit Score: 155.23  E-value: 7.56e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  62 GVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSLLPLARFAVAY-------- 133
Cdd:cd06895    1 GEPIKARITDVERSGTTRHLLNPNLYTIELQHGQFTWTIKRRYKHFQELHQALKLYRALLRIPLPTRRHKEErlslkrsr 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156564407 134 SPARDAGNREMPSLPRaGPE--GSTRHAASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVS 192
Cdd:cd06895   81 KPEREKKNRRLPSLPA-LPDilVSEEQLDSRKKQLENYLQNLLKIPDYRNHPETLEFLEVS 140
PLN02352 PLN02352
phospholipase D epsilon
348-813 3.96e-42

phospholipase D epsilon


Pssm-ID: 215202 [Multi-domain]  Cd Length: 758  Bit Score: 165.47  E-value: 3.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 348 VADAILRAQEEIFITDWWLSPEVYLKRPAHSD-----DWRLDIMLKRKAEEGVRVSILLFK-EVELAL----GINSGYSK 417
Cdd:PLN02352 192 VYKAIEGAKHLIYIAGWSFNPKMVLVRDPETDipharGVKLGELLKRKAEEGVAVRVMLWDdETSLPIiknkGVMGTHDE 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 418 RALMLLHpNIKVM------RHPDQVTLWAHHEKLLVVD----------QVVAFLGGLDLAYGRWD-DLHYRLTDLGDSSe 480
Cdd:PLN02352 272 DAFAYFK-HTKVVcklcprLHKKFPTLFAHHQKTITVDtrandsiserEIMSFVGGLDLCDGRYDtEEHSLFRTLNTES- 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 481 saasqpptprpdspatpdlsHNQFFWlgkdYSNLITKDWvqldrpfedfidRETTPRMPWRDVGVVVHGLPARDLARHFI 560
Cdd:PLN02352 350 --------------------HCQDFY----QTSIAGAKL------------QKGGPREPWHDAHACIVGEAAWDVLTNFE 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 561 QRWNftkttkakykTPTYPYLLPKSTSTAN--QLPF-TLPGGQCTTVQVLRSVDRWSAG------TLENSILNAYLHTIR 631
Cdd:PLN02352 394 QRWT----------KQCNPSVLVPTSSIRNlvHQPGsSESNNRNWKVQVYRSIDHVSAShmprnlPVERSIHEAYVEAIR 463
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 632 ESQHFLYIENQFFI-SC----SDGRT-VLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPgfEGDISTgggNSIQAILHF 705
Cdd:PLN02352 464 RAERFIYIENQYFIgGChlweKDNHCgCTNLIPIEIALKIASKIRAKERFAVYILIPMWP--EGVPES---EPVQDILHW 538
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 706 TYRTLcrgeySILHRLkaaMGTAW---------RDYISICGL-----RTHGELGG----HPVSE----------LIYIHS 757
Cdd:PLN02352 539 TRETM-----AMMYKL---IGEAIqesgepghpRDYLNFFCLanreeKRKGEFVPpyspHQKTQywnaqknrrfMVYVHS 610
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156564407 758 KVLIADDRTVIIGSANINDRSLLGKRDSELAVLIEDTETEPSLMNGAEYQAGRFAL 813
Cdd:PLN02352 611 KLMIVDDTYILIGSANVNQRSMDGCRDTEIAIGCYQSKNGTNTNNPRDIQAYRMSL 666
PLN02270 PLN02270
phospholipase D alpha
348-789 1.10e-39

phospholipase D alpha


Pssm-ID: 165912 [Multi-domain]  Cd Length: 808  Bit Score: 158.57  E-value: 1.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 348 VADAILRAQEEIFITDWWLSPEVYL----KRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEvELALGInsgYSKRALMLL 423
Cdd:PLN02270 214 VFDAITNAKHLIYITGWSVYTEISLvrdsRRPKPGGDVTIGELLKKKASEGVRVLLLVWDD-RTSVDL---LKKDGLMAT 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 424 HPN-------------IKVMRHPD---------QV-TLWAHHEKLLVVD-----------QVVAFLGGLDLAYGRWDdlh 469
Cdd:PLN02270 290 HDEetenffrgtdvhcILCPRNPDdggsivqdlQIsTMFTHHQKIVVVDsempnggsqrrRIVSFVGGIDLCDGRYD--- 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 470 yrltdlgdssesaasqppTPRPDSPATPDLSHNQFFWLGKDYSNLITKDwvqldrpfedfidretTPRMPWRDVGVVVHG 549
Cdd:PLN02270 367 ------------------TPFHSLFRTLDTAHHDDFHQPNFTGASITKG----------------GPREPWHDIHSRLEG 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 550 LPARDLARHFIQRWNFTKTTKAKYKTPTYP-YLLPKStstanqlPFTLPGGQCT-TVQVLRSVDRWSA------------ 615
Cdd:PLN02270 413 PIAWDVLFNFEQRWSKQGGKDILVQLRELEdVIIPPS-------PVMFPDDHEVwNVQLFRSIDGGAAfgfpetpeaaae 485
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 616 --------GTLENSILNAYLHTIRESQHFLYIENQFFISCS-----DGRT-----VLNKVGDEIVDRILKAHKQGWCYRV 677
Cdd:PLN02270 486 aglvsgkdNIIDRSIQDAYIHAIRRAKDFIYIENQYFLGSSfawsaDGIKpedinALHLIPKELSLKIVSKIEAGEKFTV 565
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 678 YVLLPLLPgfEGDISTGggnSIQAILHFTYRTLCRGEYSILHRLKA-AMGTAWRDYISI-C-GLRTHGELGGHPVSE--- 751
Cdd:PLN02270 566 YVVVPMWP--EGIPESG---SVQAILDWQRRTMEMMYKDVIQALRAkGLEEDPRNYLTFfClGNREVKKSGEYEPSEkpe 640
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 156564407 752 --------------LIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAV 789
Cdd:PLN02270 641 pdtdyiraqearrfMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAM 692
PX_PLD1 cd07296
The phosphoinositide binding Phox Homology domain of Phospholipase D1; The PX domain is a ...
62-192 9.68e-36

The phosphoinositide binding Phox Homology domain of Phospholipase D1; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. PLDs are implicated in many cellular functions like signaling, cytoskeletal reorganization, vesicular transport, stress responses, and the control of differentiation, proliferation, and survival. PLD1 contains PX and Pleckstrin Homology (PH) domains in addition to the catalytic domain. It acts as an effector of Rheb in the signaling of the mammalian target of rapamycin (mTOR), a serine/threonine protein kinase that transduces nutrients and other stimuli to regulate many cellular processes. PLD1 also regulates the secretion of the procoagulant von Willebrand factor (VWF) in endothelial cells. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of PLD1 specifically binds to phosphatidylinositol-3,4,5-trisphosphate [PI(3,4,5)P3], which enables PLD1 to mediate signals via the ERK1/2 pathway.


Pssm-ID: 132829  Cd Length: 135  Bit Score: 131.97  E-value: 9.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  62 GVPVTAQVVGTERYTSGS--KVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSL-LPLARFAVAYSPARD 138
Cdd:cd07296    1 GCPIKARVLEVERFTSTSdvKKPSLNVYTIELTHGEFTWQVKRKFKHFQELHRELLRYKAFIRIpIPTRSHTVRRQTIKR 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156564407 139 AGNREMPSLPR-AGPEGSTRHAASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVS 192
Cdd:cd07296   81 GEPRHMPSLPRgAEEEAREEQFSSRRKQLEDYLSKLLKMPMYRNYHATMEFIDVS 135
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
319-795 1.20e-35

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: 139.31  E-value: 1.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 319 QLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIFItdwwlspEVYLkrpAHSDDWRLDIM--LKRKAEEGVR 396
Cdd:COG1502    1 KAAPLAAGLPLVGGNRVTLLVDGDEAFAALLEAIEAARRSIDL-------EYYI---FDDDEVGRRLAdaLIAAARRGVK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 397 VSILlfkeVElalGINSGYSKRALM--LLHPNIKVMR-HPDQVTLWA----HHEKLLVVDQVVAFLGGLDLAYGRWDDLH 469
Cdd:COG1502   71 VRVL----LD---GIGSRALNRDFLrrLRAAGVEVRLfNPVRLLFRRlngrNHRKIVVIDGRVAFVGGANITDEYLGRDP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 470 yrltdlgdssesaasqpptprpdspatpdlshnqffwlgkdysnlitkdwvqldrpfedfidrettPRMPWRDVGVVVHG 549
Cdd:COG1502  144 ------------------------------------------------------------------GFGPWRDTHVRIEG 157
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 550 LPARDLARHFIQRWNFtkttkakyktptypyllpkstSTANQLPFTLPGGQcTTVQVLRSvdrwSAGTLENSILNAYLHT 629
Cdd:COG1502  158 PAVADLQAVFAEDWNF---------------------ATGEALPFPEPAGD-VRVQVVPS----GPDSPRETIERALLAA 211
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 630 IRESQHFLYIENQFFIscsdgrtvlnkVGDEIVDRILKAHKQGwcYRVYVLLPllpgfegdistggGNSIQAILHFTYRt 709
Cdd:COG1502  212 IASARRRIYIETPYFV-----------PDRSLLRALIAAARRG--VDVRILLP-------------AKSDHPLVHWASR- 264
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 710 lcrgeySILHRLKAAmgtawrdyisicGLRTHgELGGhpvselIYIHSKVLIADDRTVIIGSANINDRSLlgKRDSELAV 789
Cdd:COG1502  265 ------SYYEELLEA------------GVRIY-EYEP------GFLHAKVMVVDDEWALVGSANLDPRSL--RLNFEVNL 317

                 ....*.
gi 156564407 790 LIEDTE 795
Cdd:COG1502  318 VIYDPE 323
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
619-793 3.41e-33

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: 125.11  E-value: 3.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 619 ENSILNAYLHTIRESQHFLYIENQFFIScsdgrtvlNKVGDEIVDRILKAHKqgwcYRVYVLLPLLPGFEGDISTGGGns 698
Cdd:cd09105    6 EFEIADAYLKAIRNARRYIYIEDQYLWS--------PELLDALAEALKANPG----LRVVLVLPALPDAVAFGADDGL-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 699 iqailhftyrtlcrgEYSILHRLKAAMGTAWRDYIsICGLRTHGElgGHPVSELIYIHSKVLIADDRTVIIGSANINDRS 778
Cdd:cd09105   72 ---------------DALALLALLLLADAAPDRVA-VFSLATHRR--GLLGGPPIYVHSKVVIVDDEWATVGSANLNRRS 133
                        170
                 ....*....|....*
gi 156564407 779 LLgkRDSELAVLIED 793
Cdd:cd09105  134 MT--WDTELNLAVVD 146
PLDc_vPLD1_2_like_1 cd09104
Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
335-474 3.05e-32

Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; Catalytic domain, repeat 1, 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: 197203 [Multi-domain]  Cd Length: 147  Bit Score: 122.51  E-value: 3.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 335 ARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLkRPAHSDDWRLDIMLKRKAE-EGVRVSILLFKEVELALG--- 410
Cdd:cd09104    1 VEPLIDGEEYFDDLAEALDGARHSVYITGWQVSADIIL-APLLAGPDRLGDTLRTLAArRGVDVRVLLWDSPLLVLLgpd 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156564407 411 -INSGYSKRALMLLHPNIKVMRHP-DQVTLWAHHEKLLVVDQ-VVAFLGGLDLAYGRWDDLHYRLTD 474
Cdd:cd09104   80 dKDLNLGFPTFLRLTTALLVLDLRlRRHTLFSHHQKLVVIDSaEVAFVGGIDLAYGRYDDPDHALAA 146
PLDc_pPLD_like_2 cd09142
Catalytic domain, repeat 2, of plant phospholipase D and similar proteins; Catalytic domain, ...
617-788 6.52e-31

Catalytic domain, repeat 2, of plant phospholipase D and similar proteins; Catalytic domain, repeat 2, of plant phospholipase D (PLD, EC 3.1.4.4) and similar proteins. Plant PLDs have broad substrate specificity and can hydrolyze the terminal phosphodiester bond of several common membrane phospholipids such as phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and phosphatidylserine (PS), with 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. Most plant PLDs possess a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require calcium for activity, which is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes, the monomer of plant PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDs 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. This subfamily includes two types of plant PLDs, alpha-type and beta-type PLDs, which are derived from different gene products and distinctly regulated. The zeta-type PLD from Arabidopsis is not included in this subfamily.


Pssm-ID: 197240 [Multi-domain]  Cd Length: 208  Bit Score: 120.61  E-value: 6.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 617 TLENSILNAYLHTIRESQHFLYIENQFFISCSDG-------RTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPgfEG 689
Cdd:cd09142    4 TIDRSIQDAYVHAIRRAKRFIYIENQYFLGSSFMwsnrdrdIGCANLIPAELALKIAEKIRARERFAVYIVIPMWP--EG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 690 dISTGGgnSIQAILHFTYRTLCRGEYSILHRLKAAMGTAW--RDYISICGLRTHGELGG---------HPVSE------- 751
Cdd:cd09142   82 -IPESE--SVQEILYWQRLTIEMMYKIIGKAIQATGLFSEhpTDYLNFFCLGNREEVEGgeyeatetpTQGTDyyrlqkn 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 156564407 752 ---LIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELA 788
Cdd:cd09142  159 rrfMIYVHSKMMIVDDEYIIIGSANINQRSMDGCRDSEIA 198
PLN03008 PLN03008
Phospholipase D delta
351-789 1.02e-25

Phospholipase D delta


Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 114.42  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 351 AILRAQEEIFITDWWLSPEVYLKRPA---HSDDWRLDIMLKRKAEEGVRVSILL-------------------------- 401
Cdd:PLN03008 247 AISEAHHMIYIVGWSIFHKIKLVRETkvpRDKDMTLGELLKYKSQEGVRVLLLVwddktshdkfgiktpgvmgthdeetr 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 402 --FKEVELALGINSGYSKRALMLLH----PNIKVMRHPDQVTLWAHHEKLLVVD--------QVVAFLGGLDLAYGRWDD 467
Cdd:PLN03008 327 kfFKHSSVICVLSPRYASSKLGLFKqqasPIFSIYVMTVVGTLFTHHQKCVLVDtqavgnnrKVTAFIGGLDLCDGRYDT 406
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 468 LHYR-LTDLgdssesaasqpptprpDSPATPDLsHNQFFWLGkdysnliTKdwvqldrpfedfidretTPRMPWRDVGVV 546
Cdd:PLN03008 407 PEHRiLHDL----------------DTVFKDDF-HNPTFPAG-------TK-----------------APRQPWHDLHCR 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 547 VHGLPARDLARHFIQRWN-----------------------FTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQCTT 603
Cdd:PLN03008 446 IDGPAAYDVLINFEQRWRkatrwkefslrlkgkthwqddalIRIGRISWILSPVFKFLKDGTSIIPEDDPCVWVSKEDDP 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 604 ----VQVLRSVDRWSAG--------------------TLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGD 659
Cdd:PLN03008 526 enwhVQIFRSIDSGSVKgfpkyedeaeaqhlecakrlVVDKSIQTAYIQTIRSAQHFIYIENQYFLGSSYAWPSYRDAGA 605
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 660 ------EIVDRILKAHKQGWCYRVYVLLPLLPgfEGDISTGggnSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWR-DY 732
Cdd:PLN03008 606 dnlipmELALKIVSKIRAKERFAVYVVIPLWP--EGDPKSG---PVQEILYWQSQTMQMMYDVIAKELKAVQSDAHPlDY 680
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156564407 733 ISICGLRTHGEL-------GGHPVSE-------LIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAV 789
Cdd:PLN03008 681 LNFYCLGKREQLpddmpatNGSVVSDsynfqrfMIYVHAKGMIVDDEYVLMGSANINQRSMAGTKDTEIAM 751
PLDc_pPLDalpha_2 cd09199
Catalytic domain, repeat 2, of plant alpha-type phospholipase D; Catalytic domain, repeat 2, ...
617-789 1.16e-25

Catalytic domain, repeat 2, of plant alpha-type phospholipase D; Catalytic domain, repeat 2, of plant alpha-type phospholipase D (PLDalpha, EC 3.1.4.4). Plant PLDalpha is a phosphatidylinositol 4,5-bisphosphate (PIP2)-independent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require millimolar calcium for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes, the monomer of plant PLDalpha consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDalpha 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.


Pssm-ID: 197295 [Multi-domain]  Cd Length: 211  Bit Score: 105.86  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 617 TLENSILNAYLHTIRESQHFLYIENQFFISCS-----DGRT-----VLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPg 686
Cdd:cd09199    4 IIDRSIQDAYINAIRRAKDFIYIENQYFLGSSyawspDGIKpqdigALHLIPKELSLKIVSKIEAGERFRVYVVVPMWP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 687 fEGDISTGggnSIQAILHFTYRTLCRGEYSILHRLKA--AMGTAWRDYISICGL-----RTHGELggHPVSE-------- 751
Cdd:cd09199   83 -EGIPESG---SVQAILDWQKRTMEMMYTDIAQALRAqgIDDEDPRDYLTFFCLanrevKKEGEY--EPAEKpeedsdya 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 156564407 752 --------LIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAV 789
Cdd:cd09199  157 raqearrfMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAM 202
PLDc_pPLDbeta_2 cd09200
Catalytic domain, repeat 2, of plant beta-type phospholipase D; Catalytic domain, repeat 2, of ...
618-789 1.53e-22

Catalytic domain, repeat 2, of plant beta-type phospholipase D; Catalytic domain, repeat 2, of plant beta-type phospholipase D (PLDbeta, EC 3.1.4.4). Plant PLDbeta is a phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and requires nanomolar calcium and cytosolic factors for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Sequence analysis shows that plant PLDbeta is evolutionarily divergent from alpha-type plant PLD, and plant PLDbeta is more closely related to mammalian and yeast PLDs than to plant PLDalpha. Like other PLD enzymes, the monomer of plant PLDbeta consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDbeta 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.


Pssm-ID: 197296 [Multi-domain]  Cd Length: 211  Bit Score: 96.93  E-value: 1.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 618 LENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGD------EIVDRILKAHKQGWCYRVYVLLPLLPgfEGDI 691
Cdd:cd09200    5 IDMSIHTAYVKAIRSAQHFIYIENQYFIGSSYNWPAYKDAGAdnlipmEIALKIAEKIRAGERFAVYIVIPMWP--EGVP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 692 StggGNSIQAILHFTYRTLcRGEYSILHRLKAAMGTAW----RDYISICGL-----RTHGELGG-HPVSE---------- 751
Cdd:cd09200   83 T---GAAVQEILYWQHQTM-QMMYETIAKALVDTGLEGafspQDYLNFYCLgnremKDGIEPSPtNSPRQnstqgrsqks 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 156564407 752 ---LIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAV 789
Cdd:cd09200  159 rrfMIYVHSKGMIVDDEYVIIGSANINQRSMDGSRDTEIAM 199
PLDc_vPLD1_2_like_bac_1 cd09140
Catalytic domain, repeat 1, of uncharacterized bacterial proteins with similarity to ...
339-467 4.96e-17

Catalytic domain, repeat 1, of uncharacterized bacterial proteins with similarity to vertebrate phospholipases, PLD1 and PLD2; Catalytic domain, repeat 1, of uncharacterized bacterial counterparts of vertebrate, yeast and plant phospholipase D (PLD, EC 3.1.4.4). PLDs hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. They also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Instead of the regulatory C2 (calcium-activated lipid binding) domain in plants and the adjacent Phox (PX) and the Pleckstrin homology (PH) N-terminal domains in most mammalian and yeast PLDs, many members in this subfamily contain a SNARE associated C-terminal domain, whose functional role is unclear. Like other PLD enzymes, members in this subfamily contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), that may play an important role in the catalysis.


Pssm-ID: 197238 [Multi-domain]  Cd Length: 146  Bit Score: 78.74  E-value: 4.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 339 VNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDW--RLDIMLKRKAEE--GVRVSILLFKEVEL-ALGins 413
Cdd:cd09140    5 IDAADYFRALREALLRARRSILIVGWDFDSRIRLRRGGDDDGGpeRLGDFLNWLAERrpDLDIRILKWDFAMLyALE--- 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156564407 414 gyskRALMLL-------HPNIKVM---RHPdqvTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDD 467
Cdd:cd09140   82 ----RELLPLfllrwktHPRIHFRldgHHP---LGASHHQKIVVIDDALAFCGGIDLTVDRWDT 138
PLDc_pPLD_like_1 cd09139
Catalytic domain, repeat 1, of plant phospholipase D and similar proteins; Catalytic domain, ...
338-472 2.68e-15

Catalytic domain, repeat 1, of plant phospholipase D and similar proteins; Catalytic domain, repeat 1, of plant phospholipase D (PLD, EC 3.1.4.4) and similar proteins. Plant PLDs have broad substrate specificity and can hydrolyze the terminal phosphodiester bond of several common membrane phospholipids such as phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and phosphatidylserine (PS), with 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. Most plant PLDs possess a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require calcium for activity, which is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes, the monomer of plant PLDs consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDs 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. This subfamily includes two types of plant PLDs, alpha-type and beta-type PLDs, which are derived from different gene products and distinctly regulated. The zeta-type PLD from Arabidopsis is not included in this subfamily.


Pssm-ID: 197237 [Multi-domain]  Cd Length: 176  Bit Score: 74.74  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 338 FVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPA-----HSDDWRLDIMLKRKAEEGVRVSILLFKEVElalgiN 412
Cdd:cd09139    4 VYNPRRLWEDMYDAICNAKHLIYIAGWSVNPEISLIRDSeredpPKYSPTLGELLKRKAEEGVAVLLLLWDDKT-----V 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 413 SGYSKRALMLLHP--------NIKVM-----RHPDQ----------VTLWAHHEKLLVVD---------QVVAFLGGLDL 460
Cdd:cd09139   79 NGFKNDGVMATHDeetrnffrNTKVNcllcpRNGDAgntyveqievSTAFTHHQKTVIVDapapngerrEIVAFVGGIDL 158
                        170
                 ....*....|..
gi 156564407 461 AYGRWDDLHYRL 472
Cdd:cd09139  159 CDGRYDNPEHSL 170
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
92-192 5.40e-13

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 65.34  E-value: 5.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407   92 THGDFSWTTKKKYRHFQELHRDLLRHK--VLMSLLPLARFAVAYSPardagnrempslpragpegstRHAASKQKYLENY 169
Cdd:pfam00787   3 TFSLEEWSVRRRYSDFVELHKKLLRKFpsVIIPPLPPKRWLGRYNE---------------------EFIEKRRKGLEQY 61
                          90       100
                  ....*....|....*....|...
gi 156564407  170 LNRLLTMSFYRNYHAMTEFLEVS 192
Cdd:pfam00787  62 LQRLLQHPELRNSEVLLEFLESD 84
PLDc_vPLD1_2_like_bac_2 cd09143
Catalytic domain, repeat 2, of uncharacterized bacterial proteins with similarity to ...
626-792 1.54e-12

Catalytic domain, repeat 2, of uncharacterized bacterial proteins with similarity to vertebrate phospholipases, PLD1 and PLD2; Catalytic domain, repeat 2, of uncharacterized bacterial counterparts of vertebrate, yeast and plant phospholipase D (PLD, EC 3.1.4.4). PLDs hydrolyze the terminal phosphodiester bond of phospholipids with the formation of phosphatidic acid and alcohols. They also catalyze the transphosphatidylation of phospholipids to acceptor alcohols, by which various phospholipids can be synthesized. Instead of the regulatory C2 (calcium-activated lipid binding) domain in plants and the adjacent Phox (PX) and the Pleckstrin homology (PH) N-terminal domains in most mammalian and yeast PLDs, many members in this subfamily contain a SNARE associated C-terminal domain, whose functional role is unclear. Like other PLD enzymes, members in this subfamily contain two copies of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), that may play an important role in the catalysis.


Pssm-ID: 197241 [Multi-domain]  Cd Length: 142  Bit Score: 65.63  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 626 YLHTIRESQHFLYIENQFFIScsdgrtvlNKVGDEIVDRILKAHkqgwCYRVYVLLPL-LPGFEGDISTGGGnsiQAILH 704
Cdd:cd09143   13 YLDAIAAARRFIYIENQYFTS--------RRIAEALAERLREPD----GPEIVIVLPRtSDGWLEQLTMGVA---RARLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 705 FTYRTLCRGeysilHRLKAamgtawrdYISICGlrthgELGGHPvselIYIHSKVLIADDRTVIIGSANINDRSL-Lgkr 783
Cdd:cd09143   78 RRLREADRH-----GRLRV--------YYPVTA-----GGGGRP----IYVHSKLMIVDDRLLRVGSANLNNRSMgL--- 132

                 ....*....
gi 156564407 784 DSELAVLIE 792
Cdd:cd09143  133 DTECDLAIE 141
PLDc_pPLDalpha_1 cd09197
Catalytic domain, repeat 1, of plant alpha-type phospholipase D; Catalytic domain, repeat 1, ...
348-472 5.06e-12

Catalytic domain, repeat 1, of plant alpha-type phospholipase D; Catalytic domain, repeat 1, of plant alpha-type phospholipase D (PLDalpha, EC 3.1.4.4). Plant PLDalpha is a phosphatidylinositol 4,5-bisphosphate (PIP2)-independent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and require millimolar calcium for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Like other PLD enzymes, the monomer of plant PLDalpha consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDalpha 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.


Pssm-ID: 197293 [Multi-domain]  Cd Length: 178  Bit Score: 65.33  E-value: 5.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 348 VADAILRAQEEIFITDWWLSPEVYL----KRPAHSDDWRLDIMLKRKAEEGVRVSILLFKE---VELalginsgYSKRAL 420
Cdd:cd09197   14 VFDAIMNAKHLIYITGWSVYCEIVLvrdsRRPKPGGDLTLGELLKKKASEGVRVLMLVWDDrtsVEF-------LKKDGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 421 MLLHPN-------------IKVMRHPDQ----------VTLWAHHEKLLVVD-----------QVVAFLGGLDLAYGRWD 466
Cdd:cd09197   87 MATHDEeteaffqdsdvhcFLCPRNPDDggskvqglqiSTMFTHHQKIVVVDspmpgsdsgrrRIVSFVGGIDLCDGRYD 166

                 ....*.
gi 156564407 467 DLHYRL 472
Cdd:cd09197  167 NPFHSL 172
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
71-190 4.73e-11

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 60.44  E-value: 4.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407    71 GTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSLLPLarfavaysPARdagnREMPSLPRA 150
Cdd:smart00312   1 VVEPEKIGDGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPL--------PGK----KLFGRLNNF 68
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 156564407   151 GPEGSTRHAASkqkyLENYLNRLLTMS-FYRNYHAMTEFLE 190
Cdd:smart00312  69 SEEFIEKRRRG----LEKYLQSLLNHPeLINHSEVVLEFLE 105
PLDc_2 pfam13091
PLD-like domain;
626-795 1.47e-09

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 56.92  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  626 YLHTIRESQHFLYIENQFFISCsdgrtvlnkvgDEIVDRILKAHKQGwcYRVYVLLPllpgfeGDISTGGGNSIQAilhf 705
Cdd:pfam13091   1 LIDLINSAKKSIDIATYYFVPD-----------REIIDALIAAAKRG--VDVRIILD------SNKDDAGGPKKAS---- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  706 tyrtlcrgeYSILHRLKAAmGTAWRDYISICGLrthgelgghpvseliyIHSKVLIADDRTVIIGSANINDRSLlgKRDS 785
Cdd:pfam13091  58 ---------LKELRSLLRA-GVEIREYQSFLRS----------------MHAKFYIIDGKTVIVGSANLTRRAL--RLNL 109
                         170
                  ....*....|
gi 156564407  786 ELAVLIEDTE 795
Cdd:pfam13091 110 ENNVVIKDPE 119
PLDc_pPLDbeta_1 cd09198
Catalytic domain, repeat 1, of plant beta-type phospholipase D; Catalytic domain, repeat 1, of ...
350-472 2.30e-09

Catalytic domain, repeat 1, of plant beta-type phospholipase D; Catalytic domain, repeat 1, of plant beta-type phospholipase D (PLDbeta, EC 3.1.4.4). Plant PLDbeta is a phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent PLD that possesses a regulatory calcium-dependent phospholipid-binding C2 domain in the N-terminus and requires nanomolar calcium and cytosolic factors for optimal activity. The C2 domain is unique to plant PLDs and is not present in animal or fungal PLDs. Sequence analysis shows that plant PLDbeta is evolutionarily divergent from alpha-type plant PLD, and plant PLDbeta is more closely related to mammalian and yeast PLDs than to plant PLDalpha. Like other PLD enzymes, the monomer of plant PLDbeta consists of two catalytic domains, each of which contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue). Two HKD motifs from two domains form a single active site. Plant PLDbeta 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.


Pssm-ID: 197294 [Multi-domain]  Cd Length: 180  Bit Score: 57.59  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 350 DAILRAQEEIFITDWWLSPEVYLKR------PAHSDdWRLDIMLKRKAEEGVRVSIL----------LFKEVELALGINS 413
Cdd:cd09198   16 DAIREARRLIYITGWSVYHKVKLIRdklrpvPPGGE-LTLGELLKSKSQEGVRVLLLvwddktshsiLGYKTDGVMATHD 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156564407 414 GYSKRAL------MLLHPNIKVMRHP---DQV--TLWAHHEKLLVVD--------QVVAFLGGLDLAYGRWDDLHYRL 472
Cdd:cd09198   95 EETKRFFkhssvqCVLAPRYAGKKHSwfkQQVvgTLYTHHQKNVIVDadaggnrrKITAFIGGLDLCDGRYDTPQHPL 172
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
339-473 5.68e-09

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: 55.94  E-value: 5.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 339 VNGAGYFAAVADAILRAQEEIFItdwwlspEVYLKRPahsDDW--RLDIMLKRKAEEGVRVSILLFkevelalGINSGYS 416
Cdd:cd09110    1 TDGEEFFPALLEAIRAARHSIHL-------EYYIFRD---DEIgrRFRDALIEKARRGVEVRLLYD-------GFGSLGL 63
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156564407 417 KRALM--LLHPNIKV-----MRHPDQVTLWAH--HEKLLVVDQVVAFLGGL---------DLAYGRWDDLHYRLT 473
Cdd:cd09110   64 SRRFLreLREAGVEVrafnpLSFPLFLLRLNYrnHRKILVIDGKIAFVGGFnigdeylgkDPGFGPWRDTHVRIE 138
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
64-190 4.98e-08

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132785  Cd Length: 116  Bit Score: 52.28  E-value: 4.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  64 PVTAQVVGTErytsgsKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDL-LRHKVLMSLLPlarfavaysPARDAGNR 142
Cdd:cd06875    3 ETKIRIPSAE------TVEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLvAEHKVDKDLLP---------PKKLIGNK 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 156564407 143 EmPSLpragpegstrhAASKQKYLENYLNRLLTMSFYRNYHAMTEFLE 190
Cdd:cd06875   68 S-PSF-----------VEKRRKELEIYLQTLLSFFQKTMPRELAHFLD 103
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
66-190 9.40e-08

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 51.20  E-value: 9.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  66 TAQVVGTERYTSGSKvgTCTLYSVRLTHGDF-SWTTKKKYRHFQELHRDLLRHKvlmsllplarfavayspardaGNREM 144
Cdd:cd06093    1 SVSIPDYEKVKDGGK--KYVVYIIEVTTQGGeEWTVYRRYSDFEELHEKLKKKF---------------------PGVIL 57
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 156564407 145 PSLP--RAGPEGSTRHAASKQKYLENYLNRLLTMSFYRNYHAMTEFLE 190
Cdd:cd06093   58 PPLPpkKLFGNLDPEFIEERRKQLEQYLQSLLNHPELRNSEELKEFLE 105
PLDc_PaCLS_like_1 cd09155
Putative catalytic domain, repeat 1, of Pseudomonas aeruginosa cardiolipin synthase and ...
339-473 5.92e-07

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: 49.93  E-value: 5.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 339 VNGAGYFAAVADAILRAQEEIFItdwwlspEVYLKRpahsDDwRLDIMLKR----KAEEGVRVSiLLFKEVElALGINSG 414
Cdd:cd09155    1 IDGEATFAAIFEAIASAEEYILV-------QFYIIR----DD-DLGRELKDaliaRAQAGVRVY-LLYDEIG-SHSLSRS 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156564407 415 YSKRalmLLHPNIKVmRHPDQVTLWAH--------HEKLLVVDQVVAFLGGL---------DLAYGRWDDLHYRLT 473
Cdd:cd09155   67 YIER---LRKAGVEV-SAFNTTRGWGNrfqlnfrnHRKIVVVDGQTAFVGGHnvgdeylgrDPRLGPWRDTHVKLE 138
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
346-466 7.47e-07

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: 48.67  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 346 AAVADAILRAQEEIFITDWWLSPEvylkrpahSDDWRLDImLKRKAEEGVRVSILLFKEVELALGINSGYSKRALMLLHP 425
Cdd:cd00138    1 EALLELLKNAKESIFIATPNFSFN--------SADRLLKA-LLAAAERGVDVRLIIDKPPNAAGSLSAALLEALLRAGVN 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 156564407 426 NIKVMRHPDqvTLWAHHEKLLVVDQVVAFLGGLDLAYGRWD 466
Cdd:cd00138   72 VRSYVTPPH--FFERLHAKVVVIDGEVAYVGSANLSTASAA 110
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
752-778 3.09e-06

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 44.30  E-value: 3.09e-06
                           10        20
                   ....*....|....*....|....*..
gi 156564407   752 LIYIHSKVLIADDRTVIIGSANINDRS 778
Cdd:smart00155   2 DGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
625-791 7.56e-06

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


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 45.97  E-value: 7.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 625 AYLHTIRESQHFLYIENQFFIscsdgrtvlNKVGDEIVDRILKAHKQGwcYRVYVLLPLLPGFEGDISTgggnsiqailH 704
Cdd:cd00138    2 ALLELLKNAKESIFIATPNFS---------FNSADRLLKALLAAAERG--VDVRLIIDKPPNAAGSLSA----------A 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 705 FTYRTLCRGeysilHRLKAAMGTAWRDYisicglrthgelgghpvseliYIHSKVLIADDRTVIIGSANINDRSLlgKRD 784
Cdd:cd00138   61 LLEALLRAG-----VNVRSYVTPPHFFE---------------------RLHAKVVVIDGEVAYVGSANLSTASA--AQN 112

                 ....*..
gi 156564407 785 SELAVLI 791
Cdd:cd00138  113 REAGVLV 119
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
754-796 1.50e-05

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: 46.32  E-value: 1.50e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 156564407 754 YIHSKVLIADDRTVIIGSANINDRSLlgKRDSELAVLIEDTET 796
Cdd:cd09112   92 FLHSKTLIVDDEIASVGTANLDIRSF--ELNFEVNAVIYDKEV 132
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
205-311 1.83e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 44.46  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407   205 LEGMIRKRSGGHRvpgltccgrdqvcYRWSKRWLVVKDSFLLYM-----CLETGAISFVQLFDPGFEVQVGKRSTEARHG 279
Cdd:smart00233   3 KEGWLYKKSGGGK-------------KSWKKRYFVLFNSTLLYYkskkdKKSYKPKGSIDLSGCTVREAPDPDSSKKPHC 69
                           90       100       110
                   ....*....|....*....|....*....|...
gi 156564407   280 VRIDTSHR-SLILKCSSYRQARWWAQEITELAQ 311
Cdd:smart00233  70 FEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
PLDc_SMU_988_like_1 cd09154
Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 ...
338-481 2.70e-05

Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins; Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 and similar proteins. Although SMU_988 and similar proteins have not been functionally characterized, members in this subfamily show high sequence homology to bacterial cardiolipin (CL) synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Members of this subfamily contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197251 [Multi-domain]  Cd Length: 155  Bit Score: 45.21  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 338 FVNGAGYFAAVADAILRAQEEIFItdwwlspEVYLKRPAHSDDWRLDImLKRKAEEGVRVSIL-------------LFKE 404
Cdd:cd09154    1 FPLGEDMFEDMLEDLKKAEKFIFM-------EYFIIEEGYMWDSILEI-LKEKAKEGVEVRIMyddfgsittlpkdYPKE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 405 VElALGInsgyskRALML--LHPNIK-VMRHPDqvtlwahHEKLLVVDQVVAFLGGLDLA---------YGRWDDLHYRL 472
Cdd:cd09154   73 LE-KIGI------KCRVFnpFKPILSlYMNNRD-------HRKITVIDGKVAFTGGINLAdeyinkierFGYWKDTGIRL 138

                 ....*....
gi 156564407 473 TdlGDSSES 481
Cdd:cd09154  139 E--GEAVWS 145
PLDc_unchar3 cd09131
Putative catalytic domain of uncharacterized phospholipase D-like proteins; Putative catalytic ...
755-802 4.75e-05

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


Pssm-ID: 197229 [Multi-domain]  Cd Length: 143  Bit Score: 44.25  E-value: 4.75e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 156564407 755 IHSKVLIADDRTVIIGSANINDRSLlgKRDSELAVLIEDTETEPSLMN 802
Cdd:cd09131   93 THTKLVVIDGRTVYVGSHNWTYSAL--DYNHEASVLIESPEVADFAIN 138
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
749-795 7.30e-05

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 43.80  E-value: 7.30e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 156564407 749 VSELIYIHSKVLIADDRTVIIGSANINDRSLLGKRdsELAVLIEDTE 795
Cdd:cd09128   85 KDKFLKIHAKGIVVDGKTALVGSENWSANSLDRNR--EVGLIFDDPE 129
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
756-778 9.19e-05

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


Pssm-ID: 395489 [Multi-domain]  Cd Length: 28  Bit Score: 40.09  E-value: 9.19e-05
                          10        20
                  ....*....|....*....|...
gi 156564407  756 HSKVLIADDRTVIIGSANINDRS 778
Cdd:pfam00614   6 HRKIVVVDDELAYIGGANLDGRS 28
PLDc_C_DEXD_like cd09126
C-terminal putative phospholipase D-like domain of uncharacterized prokaryotic HKD family ...
336-467 1.68e-04

C-terminal putative phospholipase D-like domain of uncharacterized prokaryotic HKD family nucleases fused to DEAD/DEAH box helicases; C-terminal putative phospholipase D (PLD)-like domain of uncharacterized prokaryotic HKD family nucleases fused to a DEAD/DEAH box helicase domain. All members of this subfamily are uncharacterized. In addition to the helicase-like region, members of this family also contain a PLD-like domain in the C-terminal region, which is characterized by a variant HKD (H-x-K-x(4)-D motif, where x represents any amino acid residue) motif. Due to the lack of key residues related to PLD activity in the variant HKD motif, members of this subfamily are most unlikely to carry PLD activity.


Pssm-ID: 197224 [Multi-domain]  Cd Length: 126  Bit Score: 42.24  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 336 RWFvNGAGYFAAVADAILRAQEEIFITdwwlSPEVYLKRPAhsddwRLDIMLKRKAEEGVRVSILLFKEVELALGINSgy 415
Cdd:cd09126    2 SIY-DGNNYEEVFRKDLAQAKKSIIIS----SPYVSQKRIT-----KLINLLKEAQERGVEVTVVTREPKEYKELIEE-- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156564407 416 skralmLLHPNIKVMRHPDQvtlwahHEKLLVVDQVVAFLGGLD-LAYGRWDD 467
Cdd:cd09126   70 ------LRSAGVKVKLKEEI------HEKFAIIDKKIVWYGSINlLGYSNAED 110
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
755-793 3.82e-04

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: 42.14  E-value: 3.82e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 156564407 755 IHSKVLIADDRTVIIGSANINDRSLLgkRDSELAVLIED 793
Cdd:cd09159   93 LHAKTAVIDGDWATVGSSNLDPRSLR--LNLEANLVVED 129
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
437-464 5.70e-04

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: 37.78  E-value: 5.70e-04
                          10        20
                  ....*....|....*....|....*...
gi 156564407  437 TLWAHHEKLLVVDQVVAFLGGLDLAYGR 464
Cdd:pfam00614   1 YDGRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
755-795 7.43e-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: 41.82  E-value: 7.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 156564407 755 IHSKVLIADDRTVIIGSANINDRS-LLgkrDSELAVLIEDTE 795
Cdd:cd09113  117 LHAKSFVIDDRLVFVGSFNLDPRSaYL---NTEMGLVIDSPE 155
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
338-456 1.27e-03

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


Pssm-ID: 197225 [Multi-domain]  Cd Length: 141  Bit Score: 39.94  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 338 FVNGAGYFAAVADAILRAQEEIFITdwwlspeVYlkrpaHSDDWRLDIMLKRKAEEGVRVSILLfkevelaLGINSGYSK 417
Cdd:cd09127    3 FVQPDDGVAPVVDAIASAKRSILLK-------MY-----EFTDPALEKALAAAAKRGVRVRVLL-------EGGPVGGIS 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 156564407 418 RALMLLH----PNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLG 456
Cdd:cd09127   64 RAEKLLDylneAGVEVRWTNGTARYRYTHAKYIVVDDERALVL 106
PLDc_ymdC_like_1 cd09111
Putative catalytic domain, repeat 1, of Escherichia coli uncharacterized protein ymdC and ...
387-457 1.43e-03

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


Pssm-ID: 197210 [Multi-domain]  Cd Length: 162  Bit Score: 40.21  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 387 LKRKAEEGVRVSILLFkevelalGINSGYSKRALMLL--HPNIKV----------------MRHPDQVTlwaH--HEKLL 446
Cdd:cd09111   42 LLEAADRGVRVRLLLD-------DLGTSGRDRLLAALdaHPNIEVrlfnpfrnrggrllefLTDFSRLN---RrmHNKLF 111
                         90
                 ....*....|.
gi 156564407 447 VVDQVVAFLGG 457
Cdd:cd09111  112 IVDGAVAIVGG 122
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
755-780 1.74e-03

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: 40.32  E-value: 1.74e-03
                         10        20
                 ....*....|....*....|....*.
gi 156564407 755 IHSKVLIADDRTVIIGSANINDRSLL 780
Cdd:cd09162   93 LHAKAVVVDDKLALVGSANLDMRSLF 118
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
437-464 2.42e-03

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 36.21  E-value: 2.42e-03
                           10        20
                   ....*....|....*....|....*...
gi 156564407   437 TLWAHHEKLLVVDQVVAFLGGLDLAYGR 464
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_vPLD3_4_5_like_1 cd09106
Putative catalytic domain, repeat 1, of vertebrate phospholipases, PLD3, PLD4 and PLD5, viral ...
755-793 3.76e-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: 38.77  E-value: 3.76e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 156564407 755 IHSKVLIADDRTVIIGSANINDRSLLGKRdsELAVLIED 793
Cdd:cd09106  116 LHTKFWIVDGKHFYLGSANLDWRSLTQVK--ELGVYIYN 152
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
87-175 4.41e-03

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 38.13  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407  87 YSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSLLPlarfavaYSPARDAGNRempslpragpegSTRHAASKQKYL 166
Cdd:cd06874   21 FEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALE-------FPPKKLFGNK------------SERVAKERRRQL 81

                 ....*....
gi 156564407 167 ENYLNRLLT 175
Cdd:cd06874   82 ETYLRNFFS 90
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
205-306 5.97e-03

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 37.14  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156564407 205 LEGMIRKRSGGHRvpgltccgrdqvcYRWSKRWLVVKDSFLLYMCLETGAIS-FVQLFDPGFEVQV-GKRSTEARHGVRI 282
Cdd:cd00821    1 KEGYLLKRGGGGL-------------KSWKKRWFVLFEGVLLYYKSKKDSSYkPKGSIPLSGILEVeEVSPKERPHCFEL 67
                         90       100
                 ....*....|....*....|....*
gi 156564407 283 DTS-HRSLILKCSSYRQARWWAQEI 306
Cdd:cd00821   68 VTPdGRTYYLQADSEEERQEWLKAL 92
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
67-114 9.86e-03

The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132782  Cd Length: 107  Bit Score: 36.73  E-value: 9.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 156564407  67 AQVVGTERYTSGSKvgTCTLYSVRLT-HGDFSWTTKKKYRHFQELHRDL 114
Cdd:cd06872    3 CRVLGAEIVKSGSK--SFAVYSVAVTdNENETWVVKRRFRNFETLHRRL 49
 
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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