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Conserved domains on  [gi|530374780|ref|XP_005247590|]
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phospholipase D1 isoform X1 [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

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List of domain hits

Name Accession Description Interval E-value
PLN02866 super family cl33584
phospholipase D
82-1059 0e+00

phospholipase D


The actual alignment was detected with superfamily member PLN02866:

Pssm-ID: 215467 [Multi-domain]  Cd Length: 1068  Bit Score: 616.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   82 KAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRK-----FKHF--------QEFH------RELLKYKAFIRIPI- 141
Cdd:PLN02866   14 KATIVSVSRPDAGDISPVLLSYTIELQYKQFKWTLYKKasqvlYLHFalkkrafiEELHekqeqvKEWLQNLGIGDHPAv 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  142 ------PTRRHTFRRQNVREEPREMPS---LPrssenMIREEqfLGR--------RKQLEDYLTKILKMPMYRNYHATTE 204
Cdd:PLN02866   94 vqdddePDDGTVPLHHDESAKNRDVPSsaaLP-----VIRPA--LGRqqsisdraKVAMQEYLNHFLGNLDIVNSREVCK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  205 FLDISQLSFIHDLGPKGIEGMIMKRsggH--RIPG------------LNCCGQgracyRWSKRWLIVKDSFL-LYMKPDS 269
Cdd:PLN02866  167 FLEVSKLSFSPEYGPKLKEGYVMVK---HlpKIPKsddsrgcfpcccFSCCND-----NWQKVWAVLKPGFLaLLEDPFD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  270 GAIAFVLLVD--------KEFKI---KVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDH 338
Cdd:PLN02866  239 AKPLDIIVFDvlpasngnGEGQIslaKEIKERNPLRFGFKVTCGNRSIRLRTKSSAKVKDWVAAINDAGLRPPEGWCHPH 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  339 RFGSYAA----IQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVR 414
Cdd:PLN02866  319 RFGSFAPprglTEDGSQAQWFIDGHAAFEAIASAIENAKSEIFITGWWLCPELYLRRPFHDHESSRLDSLLEAKAKQGVQ 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  415 IFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRL 494
Cdd:PLN02866  399 IYILLYKEVALALKINSVYSKRRLLGIHENVKVLRYPDHFSSGVYLWSHHEKLVIVDYQICFIGGLDLCFGRYDTPEHRV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  495 TDvgsvkrvtsgpslgslppaamesmeslrlkdknepvqnlpiqksiddvdsklkgigkprkfskfslykqlhrhhlhda 574
Cdd:PLN02866  479 GD------------------------------------------------------------------------------ 480
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  575 dsissidstssyfnhyrshhnlihglkphfklfHPSSEseqgltrphadtgsirslqtgvgelhgetrfWHGKDYCNFVF 654
Cdd:PLN02866  481 ---------------------------------CPPVI-------------------------------WPGKDYYNPRE 496
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  655 KD---WVQLDKpfaDFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYR------------------- 712
Cdd:PLN02866  497 SEpnsWEDTMK---DELDRRKYPRMPWHDVHCALWGPPCRDVARHFVQRWNYAKRNKAPNEqaipllmphhhmviphylg 573
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  713 -----------------------SLS-------YPFLLPK------------------SQTTAHELRY------------ 732
Cdd:PLN02866  574 gseeeeiesknqednqkgiarqdSFSsrsslqdIPLLLPQeadatdgsggghklngmnSTNGSLSFSFrkskiepvlpdt 653
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  733 -------------------------------------------------QVPGSVHANVQLLRSAADWSAGIKYHEESIH 763
Cdd:PLN02866  654 pmkgfvddlgfldlsvkmssaergskesdsewwetqergdqvgsadevgQVGPRVSCRCQVIRSVSQWSAGTSQVEESIH 733
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  764 AAYVHVIENSRHYIYIENQFFIS-CADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAI 842
Cdd:PLN02866  734 AAYCSLIEKAEHFIYIENQFFISgLSGDDTIQNRVLEALYRRILRAHKEKKCFRVIIVIPLLPGFQGGVDDGGAASVRAI 813
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  843 MHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAEL--EGNLVTELIYVHSKLLIADDNTVIIGSANINDRSML 920
Cdd:PLN02866  814 MHWQYRTICRGKNSILHNLYDLLGPKTHDYISFYGLRAYGRLfeGGPLATSQIYVHSKIMIVDDRAALIGSANINDRSLL 893
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  921 GKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDK 1000
Cdd:PLN02866  894 GSRDSEIGVVIEDKEFVDSSMNGKPWKAGKFAHSLRLSLWSEHLGLRAGEIDKIIDPVCDTTYKDLWMATAKTNTDIYQD 973
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780 1001 VFRCLPNDEVHNLIQLRDFIN------------------KPVLAKEDPIRAE---EELKKIRGFLVQFPFYFLSEESLLP 1059
Cdd:PLN02866  974 VFSCIPNDLIHSRAALRQSMAsrkeklghttidlgiapeKLESYENGDIKSSdpmERLKSVRGHLVSFPLDFMCQEDLRP 1053
 
Name Accession Description Interval E-value
PLN02866 PLN02866
phospholipase D
82-1059 0e+00

phospholipase D


Pssm-ID: 215467 [Multi-domain]  Cd Length: 1068  Bit Score: 616.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   82 KAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRK-----FKHF--------QEFH------RELLKYKAFIRIPI- 141
Cdd:PLN02866   14 KATIVSVSRPDAGDISPVLLSYTIELQYKQFKWTLYKKasqvlYLHFalkkrafiEELHekqeqvKEWLQNLGIGDHPAv 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  142 ------PTRRHTFRRQNVREEPREMPS---LPrssenMIREEqfLGR--------RKQLEDYLTKILKMPMYRNYHATTE 204
Cdd:PLN02866   94 vqdddePDDGTVPLHHDESAKNRDVPSsaaLP-----VIRPA--LGRqqsisdraKVAMQEYLNHFLGNLDIVNSREVCK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  205 FLDISQLSFIHDLGPKGIEGMIMKRsggH--RIPG------------LNCCGQgracyRWSKRWLIVKDSFL-LYMKPDS 269
Cdd:PLN02866  167 FLEVSKLSFSPEYGPKLKEGYVMVK---HlpKIPKsddsrgcfpcccFSCCND-----NWQKVWAVLKPGFLaLLEDPFD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  270 GAIAFVLLVD--------KEFKI---KVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDH 338
Cdd:PLN02866  239 AKPLDIIVFDvlpasngnGEGQIslaKEIKERNPLRFGFKVTCGNRSIRLRTKSSAKVKDWVAAINDAGLRPPEGWCHPH 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  339 RFGSYAA----IQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVR 414
Cdd:PLN02866  319 RFGSFAPprglTEDGSQAQWFIDGHAAFEAIASAIENAKSEIFITGWWLCPELYLRRPFHDHESSRLDSLLEAKAKQGVQ 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  415 IFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRL 494
Cdd:PLN02866  399 IYILLYKEVALALKINSVYSKRRLLGIHENVKVLRYPDHFSSGVYLWSHHEKLVIVDYQICFIGGLDLCFGRYDTPEHRV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  495 TDvgsvkrvtsgpslgslppaamesmeslrlkdknepvqnlpiqksiddvdsklkgigkprkfskfslykqlhrhhlhda 574
Cdd:PLN02866  479 GD------------------------------------------------------------------------------ 480
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  575 dsissidstssyfnhyrshhnlihglkphfklfHPSSEseqgltrphadtgsirslqtgvgelhgetrfWHGKDYCNFVF 654
Cdd:PLN02866  481 ---------------------------------CPPVI-------------------------------WPGKDYYNPRE 496
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  655 KD---WVQLDKpfaDFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYR------------------- 712
Cdd:PLN02866  497 SEpnsWEDTMK---DELDRRKYPRMPWHDVHCALWGPPCRDVARHFVQRWNYAKRNKAPNEqaipllmphhhmviphylg 573
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  713 -----------------------SLS-------YPFLLPK------------------SQTTAHELRY------------ 732
Cdd:PLN02866  574 gseeeeiesknqednqkgiarqdSFSsrsslqdIPLLLPQeadatdgsggghklngmnSTNGSLSFSFrkskiepvlpdt 653
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  733 -------------------------------------------------QVPGSVHANVQLLRSAADWSAGIKYHEESIH 763
Cdd:PLN02866  654 pmkgfvddlgfldlsvkmssaergskesdsewwetqergdqvgsadevgQVGPRVSCRCQVIRSVSQWSAGTSQVEESIH 733
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  764 AAYVHVIENSRHYIYIENQFFIS-CADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAI 842
Cdd:PLN02866  734 AAYCSLIEKAEHFIYIENQFFISgLSGDDTIQNRVLEALYRRILRAHKEKKCFRVIIVIPLLPGFQGGVDDGGAASVRAI 813
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  843 MHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAEL--EGNLVTELIYVHSKLLIADDNTVIIGSANINDRSML 920
Cdd:PLN02866  814 MHWQYRTICRGKNSILHNLYDLLGPKTHDYISFYGLRAYGRLfeGGPLATSQIYVHSKIMIVDDRAALIGSANINDRSLL 893
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  921 GKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDK 1000
Cdd:PLN02866  894 GSRDSEIGVVIEDKEFVDSSMNGKPWKAGKFAHSLRLSLWSEHLGLRAGEIDKIIDPVCDTTYKDLWMATAKTNTDIYQD 973
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780 1001 VFRCLPNDEVHNLIQLRDFIN------------------KPVLAKEDPIRAE---EELKKIRGFLVQFPFYFLSEESLLP 1059
Cdd:PLN02866  974 VFSCIPNDLIHSRAALRQSMAsrkeklghttidlgiapeKLESYENGDIKSSdpmERLKSVRGHLVSFPLDFMCQEDLRP 1053
PLDc_vPLD1_2 cd09844
Catalytic domain, repeat 2, of vertebrate phospholipase D1; Catalytic domain, repeat 2, of ...
754-935 2.01e-131

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: 395.85  E-value: 2.01e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  754 GIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDIST 833
Cdd:cd09844     1 GIKYHEESIHAAYVSVIENSKHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENKRYRVYVVIPLLPGFEGDIST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  834 GGGNALQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSAN 913
Cdd:cd09844    81 GGGNALQAIMHFNYRTMCRGEHSIIGQLKAEMGDQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSAN 160
                         170       180
                  ....*....|....*....|..
gi 530374780  914 INDRSMLGKRDSEMAVIVQDTE 935
Cdd:cd09844   161 INDRSMLGKRDSEMAVVVQDTE 182
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
665-937 6.07e-20

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: 93.08  E-value: 6.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  665 ADFIDRY---STPRMPWHDIASAVHGKAARDVARHFIQRWNFTkimkskyrslsypfllpksqTTAHELRYQVPGSVHan 741
Cdd:COG1502   132 ANITDEYlgrDPGFGPWRDTHVRIEGPAVADLQAVFAEDWNFA--------------------TGEALPFPEPAGDVR-- 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  742 VQLLRSAADwsagikYHEESIHAAYVHVIENSRHYIYIENQFFIscaddkvvfnkIGDAIAQRILKAHRENqkyrVYVVI 821
Cdd:COG1502   190 VQVVPSGPD------SPRETIERALLAAIASARRRIYIETPYFV-----------PDRSLLRALIAAARRG----VDVRI 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  822 pLLPGfegdistgggnalqaimHFNYRTMCRGENSILGQLKAelgnqwinyisfCGLRTHaELEGNlvteliYVHSKLLI 901
Cdd:COG1502   249 -LLPA-----------------KSDHPLVHWASRSYYEELLE------------AGVRIY-EYEPG------FLHAKVMV 291
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 530374780  902 ADDNTVIIGSANINDRSMlgKRDSEMAVIVQDTETV 937
Cdd:COG1502   292 VDDEWALVGSANLDPRSL--RLNFEVNLVIYDPEFA 325
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
87-207 3.30e-16

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: 75.07  E-value: 3.30e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780     87 EVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRqnvreeprempsLPRS 166
Cdd:smart00312    1 VVEPEKIGDGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGR------------LNNF 68
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 530374780    167 SENMIREeqflgRRKQLEDYLTKILKMPMYRN-YHATTEFLD 207
Cdd:smart00312   69 SEEFIEK-----RRRGLEKYLQSLLNHPELINhSEVVLEFLE 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
108-206 2.71e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 69.19  E-value: 2.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   108 THGEFKWQVKRKFKHFQEFHRELLKYKAFIRIP-IPTRRHTFRRqnvreeprempslprsSENMIREeqflgRRKQLEDY 186
Cdd:pfam00787    3 TFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPpLPPKRWLGRY----------------NEEFIEK-----RRKGLEQY 61
                           90       100
                   ....*....|....*....|
gi 530374780   187 LTKILKMPMYRNYHATTEFL 206
Cdd:pfam00787   62 LQRLLQHPELRNSEVLLEFL 81
 
Name Accession Description Interval E-value
PLN02866 PLN02866
phospholipase D
82-1059 0e+00

phospholipase D


Pssm-ID: 215467 [Multi-domain]  Cd Length: 1068  Bit Score: 616.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   82 KAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRK-----FKHF--------QEFH------RELLKYKAFIRIPI- 141
Cdd:PLN02866   14 KATIVSVSRPDAGDISPVLLSYTIELQYKQFKWTLYKKasqvlYLHFalkkrafiEELHekqeqvKEWLQNLGIGDHPAv 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  142 ------PTRRHTFRRQNVREEPREMPS---LPrssenMIREEqfLGR--------RKQLEDYLTKILKMPMYRNYHATTE 204
Cdd:PLN02866   94 vqdddePDDGTVPLHHDESAKNRDVPSsaaLP-----VIRPA--LGRqqsisdraKVAMQEYLNHFLGNLDIVNSREVCK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  205 FLDISQLSFIHDLGPKGIEGMIMKRsggH--RIPG------------LNCCGQgracyRWSKRWLIVKDSFL-LYMKPDS 269
Cdd:PLN02866  167 FLEVSKLSFSPEYGPKLKEGYVMVK---HlpKIPKsddsrgcfpcccFSCCND-----NWQKVWAVLKPGFLaLLEDPFD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  270 GAIAFVLLVD--------KEFKI---KVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDH 338
Cdd:PLN02866  239 AKPLDIIVFDvlpasngnGEGQIslaKEIKERNPLRFGFKVTCGNRSIRLRTKSSAKVKDWVAAINDAGLRPPEGWCHPH 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  339 RFGSYAA----IQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVR 414
Cdd:PLN02866  319 RFGSFAPprglTEDGSQAQWFIDGHAAFEAIASAIENAKSEIFITGWWLCPELYLRRPFHDHESSRLDSLLEAKAKQGVQ 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  415 IFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRL 494
Cdd:PLN02866  399 IYILLYKEVALALKINSVYSKRRLLGIHENVKVLRYPDHFSSGVYLWSHHEKLVIVDYQICFIGGLDLCFGRYDTPEHRV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  495 TDvgsvkrvtsgpslgslppaamesmeslrlkdknepvqnlpiqksiddvdsklkgigkprkfskfslykqlhrhhlhda 574
Cdd:PLN02866  479 GD------------------------------------------------------------------------------ 480
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  575 dsissidstssyfnhyrshhnlihglkphfklfHPSSEseqgltrphadtgsirslqtgvgelhgetrfWHGKDYCNFVF 654
Cdd:PLN02866  481 ---------------------------------CPPVI-------------------------------WPGKDYYNPRE 496
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  655 KD---WVQLDKpfaDFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYR------------------- 712
Cdd:PLN02866  497 SEpnsWEDTMK---DELDRRKYPRMPWHDVHCALWGPPCRDVARHFVQRWNYAKRNKAPNEqaipllmphhhmviphylg 573
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  713 -----------------------SLS-------YPFLLPK------------------SQTTAHELRY------------ 732
Cdd:PLN02866  574 gseeeeiesknqednqkgiarqdSFSsrsslqdIPLLLPQeadatdgsggghklngmnSTNGSLSFSFrkskiepvlpdt 653
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  733 -------------------------------------------------QVPGSVHANVQLLRSAADWSAGIKYHEESIH 763
Cdd:PLN02866  654 pmkgfvddlgfldlsvkmssaergskesdsewwetqergdqvgsadevgQVGPRVSCRCQVIRSVSQWSAGTSQVEESIH 733
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  764 AAYVHVIENSRHYIYIENQFFIS-CADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAI 842
Cdd:PLN02866  734 AAYCSLIEKAEHFIYIENQFFISgLSGDDTIQNRVLEALYRRILRAHKEKKCFRVIIVIPLLPGFQGGVDDGGAASVRAI 813
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  843 MHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAEL--EGNLVTELIYVHSKLLIADDNTVIIGSANINDRSML 920
Cdd:PLN02866  814 MHWQYRTICRGKNSILHNLYDLLGPKTHDYISFYGLRAYGRLfeGGPLATSQIYVHSKIMIVDDRAALIGSANINDRSLL 893
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  921 GKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDK 1000
Cdd:PLN02866  894 GSRDSEIGVVIEDKEFVDSSMNGKPWKAGKFAHSLRLSLWSEHLGLRAGEIDKIIDPVCDTTYKDLWMATAKTNTDIYQD 973
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780 1001 VFRCLPNDEVHNLIQLRDFIN------------------KPVLAKEDPIRAE---EELKKIRGFLVQFPFYFLSEESLLP 1059
Cdd:PLN02866  974 VFSCIPNDLIHSRAALRQSMAsrkeklghttidlgiapeKLESYENGDIKSSdpmERLKSVRGHLVSFPLDFMCQEDLRP 1053
PLDc_vPLD1_2 cd09844
Catalytic domain, repeat 2, of vertebrate phospholipase D1; Catalytic domain, repeat 2, of ...
754-935 2.01e-131

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: 395.85  E-value: 2.01e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  754 GIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDIST 833
Cdd:cd09844     1 GIKYHEESIHAAYVSVIENSKHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENKRYRVYVVIPLLPGFEGDIST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  834 GGGNALQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSAN 913
Cdd:cd09844    81 GGGNALQAIMHFNYRTMCRGEHSIIGQLKAEMGDQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSAN 160
                         170       180
                  ....*....|....*....|..
gi 530374780  914 INDRSMLGKRDSEMAVIVQDTE 935
Cdd:cd09844   161 INDRSMLGKRDSEMAVVVQDTE 182
PLDc_vPLD1_2_yPLD_like_2 cd09141
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and ...
754-935 4.65e-108

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: 334.14  E-value: 4.65e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  754 GIKYHEESIHAAYVHVIENSRHYIYIENQFFIS-CADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDIS 832
Cdd:cd09141     1 GGIQTEDSIQNAYLDLIENAEHFIYIENQFFISsTGGEDPVKNRIGEALVDRIIRAHKEGEKFRVYIVLPLLPGFEGDLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  833 TGGGNALQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSA 912
Cdd:cd09141    81 DPGGSSIRAIMHWQYQSICRGEHSLLERLKKEEGVDPEQYISFLSLRTHGKLGGRPVTEQIYVHSKLMIVDDRIVIIGSA 160
                         170       180
                  ....*....|....*....|...
gi 530374780  913 NINDRSMLGKRDSEMAVIVQDTE 935
Cdd:cd09141   161 NINDRSMLGDRDSEIAVVIEDTE 183
PLDc_vPLD1_1 cd09842
Catalytic domain, repeat 1, of vertebrate phospholipase D1; Catalytic domain, repeat 1, of ...
352-502 4.71e-107

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: 330.45  E-value: 4.71e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  352 AKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINS 431
Cdd:cd09842     1 SKWYVNAKCYFEDVANAMEEAKEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFVMLYKEVELALGINS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530374780  432 EYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKR 502
Cdd:cd09842    81 EYSKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKIVVIDQSVAFVGGIDLAYGRWDDDEHRLTDVGSVKR 151
PLDc_vPLD2_2 cd09845
Catalytic domain, repeat 2, of vertebrate phospholipase D2; Catalytic domain, repeat 2, of ...
759-935 4.82e-98

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: 307.57  E-value: 4.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  759 EESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNA 838
Cdd:cd09845     6 ENSILNAYLHTIENSQHYLYLENQFFISCADGRTVLNKIGDAIVKRILKAHSQGWCFRVFVVIPLLPGFEGDISTGGGNS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  839 LQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRS 918
Cdd:cd09845    86 IQAILHFTYRTICRGEYSILSRLKEAMGTAWTDYISICGLRTHGELGGSPVTELIYIHSKVLIADDRTVIIGSANINDRS 165
                         170
                  ....*....|....*..
gi 530374780  919 MLGKRDSEMAVIVQDTE 935
Cdd:cd09845   166 MLGKRDSELAVLVEDTE 182
PLDc_vPLD1_2_yPLD_like_1 cd09138
Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and ...
352-497 4.09e-93

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: 292.93  E-value: 4.09e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  352 AKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINS 431
Cdd:cd09138     1 AKWYVDGKDYFWAVADAIENAKEEIFITDWWLSPELYLRRPPAGNERWRLDRLLKRKAEEGVKIYILLYKEVELALTINS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530374780  432 EYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDV 497
Cdd:cd09138    81 KYTKRTLENLHPNIKVLRHPDHLPQGPLLWSHHEKIVVIDQSIAFVGGLDLCYGRWDTHQHPLTDD 146
PLDc_vPLD2_1 cd09843
Catalytic domain, repeat 1, of vertebrate phospholipase D2; Catalytic domain, repeat 1, of ...
352-497 1.14e-82

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: 264.55  E-value: 1.14e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  352 AKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVvEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINS 431
Cdd:cd09843     1 TKWFVNGHGYFAAVADALEQAQEEIFITDWWLSPEVFLKRPA-HGDDWRLDIILKRKAEQGVRVCVLLFKEVELALGINS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530374780  432 EYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDV 497
Cdd:cd09843    80 GYSKRKLMLLHPNIKVMRHPDHVASVVVLWAHHEKMVAIDQSVAFLGGLDLAYGRWDDSDYRLTDL 145
PX_PLD1 cd07296
The phosphoinositide binding Phox Homology domain of Phospholipase D1; The PX domain is a ...
78-209 1.82e-79

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: 255.62  E-value: 1.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   78 GCPIKAQVLEVERFTST--TRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNV-R 154
Cdd:cd07296     1 GCPIKARVLEVERFTSTsdVKKPSLNVYTIELTHGEFTWQVKRKFKHFQELHRELLRYKAFIRIPIPTRSHTVRRQTIkR 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530374780  155 EEPREMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDIS 209
Cdd:cd07296    81 GEPRHMPSLPRGAEEEAREEQFSSRRKQLEDYLSKLLKMPMYRNYHATMEFIDVS 135
PH_PLD cd01254
Phospholipase D pleckstrin homology (PH) domain; PLD hydrolyzes phosphatidylcholine to ...
197-326 4.64e-57

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: 192.86  E-value: 4.64e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  197 RNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC---CGQGRACYRWSKRWLIVKDSFLLYMKP-DSGAI 272
Cdd:cd01254     1 RNHLETFEFLEVSSLSFAPELGPKGKEGYLKKRSGGHRQGWRVChfyCCCKAMCGRWSKRWFIVKDSFLAYVKDpDSGAI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530374780  273 AFVLLVDKEFKIKVGKKET--ETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEF 326
Cdd:cd01254    81 LDVFLFDQEFKVSRGGKETkyGSRHGLKITNLSRKLKLKCKSERKAKQWVESIEEA 136
PX_PLD cd06895
The phosphoinositide binding Phox Homology domain of Phospholipase D; The PX domain is a ...
78-209 5.23e-56

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: 190.29  E-value: 5.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   78 GCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRR------- 150
Cdd:cd06895     1 GEPIKARITDVERSGTTRHLLNPNLYTIELQHGQFTWTIKRRYKHFQELHQALKLYRALLRIPLPTRRHKEERlslkrsr 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  151 -QNVREEPREMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDIS 209
Cdd:cd06895    81 kPEREKKNRRLPSLPALPDILVSEEQLDSRKKQLENYLQNLLKIPDYRNHPETLEFLEVS 140
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
754-933 4.05e-43

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: 153.61  E-value: 4.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  754 GIKYHEESIHAAYVHVIENSRHYIYIENQFFIScaddkvvfNKIGDAIAQRIlkahRENQKYRVYVVIPLLPGFEGDIST 833
Cdd:cd09105     1 FAPSGEFEIADAYLKAIRNARRYIYIEDQYLWS--------PELLDALAEAL----KANPGLRVVLVLPALPDAVAFGAD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  834 GGGNALQaimhfnyrtmcrgensiLGQLKAELGNQWINYISFCGLRTHAELEGnlvTELIYVHSKLLIADDNTVIIGSAN 913
Cdd:cd09105    69 DGLDALA-----------------LLALLLLADAAPDRVAVFSLATHRRGLLG---GPPIYVHSKVVIVDDEWATVGSAN 128
                         170       180
                  ....*....|....*....|
gi 530374780  914 INDRSMLgkRDSEMAVIVQD 933
Cdd:cd09105   129 LNRRSMT--WDTELNLAVVD 146
PLDc_vPLD1_2_like_1 cd09104
Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
352-497 4.69e-43

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: 153.71  E-value: 4.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  352 AKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLkrPVVEGNRWRLDCILKRKAQ-QGVRIFIMLYKEVELALG-- 428
Cdd:cd09104     1 VEPLIDGEEYFDDLAEALDGARHSVYITGWQVSADIIL--APLLAGPDRLGDTLRTLAArRGVDVRVLLWDSPLLVLLgp 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530374780  429 --INSEYTKRTLMRLHPNIKVMRHPDHVSstvYLWAHHEKLVIIDQ-SVAFVGGIDLAYGRWDDNEHRLTDV 497
Cdd:cd09104    79 ddKDLNLGFPTFLRLTTALLVLDLRLRRH---TLFSHHQKLVVIDSaEVAFVGGIDLAYGRYDDPDHALAAP 147
PX_PLD2 cd07297
The phosphoinositide binding Phox Homology domain of Phospholipase D2; The PX domain is a ...
78-209 9.86e-37

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: 134.66  E-value: 9.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   78 GCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP 157
Cdd:cd07297     1 GVPVTAKVENTERYTTGSKVHVCTLYTVRLTHGEFTWTVKKKFKHFQELHRDLYRHKVMLSFLPLGRFAIQHRQQLEGLT 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530374780  158 REMPSLPRSSENMIREEQflGRRKQLEDYLTKILKMPMYRNYHATTEFLDIS 209
Cdd:cd07297    81 EEMPSLPGTDREASRRTA--SKPKYLENYLNNLLENSFYRNYHAMMEFLAVS 130
PLDc_pPLD_like_2 cd09142
Catalytic domain, repeat 2, of plant phospholipase D and similar proteins; Catalytic domain, ...
759-928 1.37e-33

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: 128.70  E-value: 1.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  759 EESIHAAYVHVIENSRHYIYIENQFFI-SCA------DDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPgfEGdI 831
Cdd:cd09142     6 DRSIQDAYVHAIRRAKRFIYIENQYFLgSSFmwsnrdRDIGCANLIPAELALKIAEKIRARERFAVYIVIPMWP--EG-I 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  832 STGGgnALQAIMHFNYRTMCRGENSILGQLKAELGNQW--INYISFCGLRTHAELEG--NLVTE---------------- 891
Cdd:cd09142    83 PESE--SVQEILYWQRLTIEMMYKIIGKAIQATGLFSEhpTDYLNFFCLGNREEVEGgeYEATEtptqgtdyyrlqknrr 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 530374780  892 -LIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMA 928
Cdd:cd09142   161 fMIYVHSKMMIVDDEYIIIGSANINQRSMDGCRDSEIA 198
PLN02270 PLN02270
phospholipase D alpha
362-986 3.18e-32

phospholipase D alpha


Pssm-ID: 165912 [Multi-domain]  Cd Length: 808  Bit Score: 135.46  E-value: 3.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  362 FEDVANAMEEANEEIFITDWWLSPEIFL----KRPVvEGNRWRLDCILKRKAQQGVRIFIMLYKE---VELA-----LGI 429
Cdd:PLN02270  211 WEDVFDAITNAKHLIYITGWSVYTEISLvrdsRRPK-PGGDVTIGELLKKKASEGVRVLLLVWDDrtsVDLLkkdglMAT 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  430 NSEYTKRTLMRLHPN-IKVMRHPDHVSSTVY------LWAHHEKLVIIDQS-----------VAFVGGIDLAYGRWDDNE 491
Cdd:PLN02270  290 HDEETENFFRGTDVHcILCPRNPDDGGSIVQdlqistMFTHHQKIVVVDSEmpnggsqrrriVSFVGGIDLCDGRYDTPF 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  492 HrltdvgsvkrvtsgpslgslppaamesmeslrlkdknepvqnlpiqksiddvdsklkgigkprkfskfSLYKQLHRhhl 571
Cdd:PLN02270  370 H--------------------------------------------------------------------SLFRTLDT--- 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  572 hdadsissidstssyfnhyrSHHNLIHglKPHFklfhpsseseqgltrphadTGSirSLQTGvgelhgetrfwhgkdycn 651
Cdd:PLN02270  379 --------------------AHHDDFH--QPNF-------------------TGA--SITKG------------------ 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  652 fvfkdwvqldkpfadfidrysTPRMPWHDIASAVHGKAARDVARHFIQRWNFT--KIMKSKYRSLS------YPFLLPKS 723
Cdd:PLN02270  398 ---------------------GPREPWHDIHSRLEGPIAWDVLFNFEQRWSKQggKDILVQLRELEdviippSPVMFPDD 456
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  724 QTTAhelryqvpgsvhaNVQLLRSAaDWSAGIKYHE-------------------ESIHAAYVHVIENSRHYIYIENQFF 784
Cdd:PLN02270  457 HEVW-------------NVQLFRSI-DGGAAFGFPEtpeaaaeaglvsgkdniidRSIQDAYIHAIRRAKDFIYIENQYF 522
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  785 ISCA----------DDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPgfEGDISTGggnALQAIMHFNYRTMCRGE 854
Cdd:PLN02270  523 LGSSfawsadgikpEDINALHLIPKELSLKIVSKIEAGEKFTVYVVVPMWP--EGIPESG---SVQAILDWQRRTMEMMY 597
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  855 NSILGQLKAE-LGNQWINYISFCGL-----RTHAELEGNLVTE--------------LIYVHSKLLIADDNTVIIGSANI 914
Cdd:PLN02270  598 KDVIQALRAKgLEEDPRNYLTFFCLgnrevKKSGEYEPSEKPEpdtdyiraqearrfMIYVHTKMMIVDDEYIIIGSANI 677
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530374780  915 NDRSMLGKRDSEMAVivqdTETVPSVMDGKEYQAGRFaRGLRLQCFRVVLGYLDdpsEDIQDPVSDKFFKEV 986
Cdd:PLN02270  678 NQRSMDGARDSEIAM----GGYQPYHLSTRQPARGQI-HGFRMSLWYEHLGMLD---ETFLDPESEECIQKV 741
PLN02352 PLN02352
phospholipase D epsilon
674-952 3.52e-32

phospholipase D epsilon


Pssm-ID: 215202 [Multi-domain]  Cd Length: 758  Bit Score: 135.04  E-value: 3.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  674 PRMPWHDIASAVHGKAARDVARHFIQRWNftkimkskyRSLSYPFLLPKSQTTahELRYQVPGSVHAN----VQLLRSAA 749
Cdd:PLN02352  369 PREPWHDAHACIVGEAAWDVLTNFEQRWT---------KQCNPSVLVPTSSIR--NLVHQPGSSESNNrnwkVQVYRSID 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  750 DWSA-----GIKYhEESIHAAYVHVIENSRHYIYIENQFFISCAD------DKVVFNKIGDAIAQRILKAHRENQKYRVY 818
Cdd:PLN02352  438 HVSAshmprNLPV-ERSIHEAYVEAIRRAERFIYIENQYFIGGCHlwekdnHCGCTNLIPIEIALKIASKIRAKERFAVY 516
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  819 VVIPLLPGFEGDISTGggnalQAIMHFNYRTMCRgENSILGQLKAELGNQ-----WINYisFCGLRTHAELEGNLVTE-- 891
Cdd:PLN02352  517 ILIPMWPEGVPESEPV-----QDILHWTRETMAM-MYKLIGEAIQESGEPghprdYLNF--FCLANREEKRKGEFVPPys 588
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530374780  892 ----------------LIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFA 952
Cdd:PLN02352  589 phqktqywnaqknrrfMVYVHSKLMIVDDTYILIGSANVNQRSMDGCRDTEIAIGCYQSKNGTNTNNPRDIQAYRMS 665
PLN03008 PLN03008
Phospholipase D delta
640-929 1.25e-26

Phospholipase D delta


Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 117.50  E-value: 1.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  640 ETRFWHGKDYcnfVFKDwvqlDKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRW-------NFTKIMKSKYR 712
Cdd:PLN03008  408 EHRILHDLDT---VFKD----DFHNPTFPAGTKAPRQPWHDLHCRIDGPAAYDVLINFEQRWrkatrwkEFSLRLKGKTH 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  713 ----------------SLSYPFL------LPKSQTTAHELRYQVPGSVHanVQLLRSAADWSAG--IKYHEE-------- 760
Cdd:PLN03008  481 wqddalirigriswilSPVFKFLkdgtsiIPEDDPCVWVSKEDDPENWH--VQIFRSIDSGSVKgfPKYEDEaeaqhlec 558
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  761 --------SIHAAYVHVIENSRHYIYIENQFFISCA------DDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPg 826
Cdd:PLN03008  559 akrlvvdkSIQTAYIQTIRSAQHFIYIENQYFLGSSyawpsyRDAGADNLIPMELALKIVSKIRAKERFAVYVVIPLWP- 637
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  827 fEGDISTGggnALQAIMHFNYRTMCRGENSILGQLKA-ELGNQWINYISFCGLRTHAEL-------EGNLVTE------- 891
Cdd:PLN03008  638 -EGDPKSG---PVQEILYWQSQTMQMMYDVIAKELKAvQSDAHPLDYLNFYCLGKREQLpddmpatNGSVVSDsynfqrf 713
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 530374780  892 LIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAV 929
Cdd:PLN03008  714 MIYVHAKGMIVDDEYVLMGSANINQRSMAGTKDTEIAM 751
PLDc_pPLDalpha_2 cd09199
Catalytic domain, repeat 2, of plant alpha-type phospholipase D; Catalytic domain, repeat 2, ...
759-929 2.52e-26

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: 107.78  E-value: 2.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  759 EESIHAAYVHVIENSRHYIYIENQFFI-SC---------ADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPgfE 828
Cdd:cd09199     6 DRSIQDAYINAIRRAKDFIYIENQYFLgSSyawspdgikPQDIGALHLIPKELSLKIVSKIEAGERFRVYVVVPMWP--E 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  829 GDISTGggnALQAIMHFNYRTMCRGENSILGQLKAE--LGNQWINYISFCGL-----RTHAELEGNLVTE---------- 891
Cdd:cd09199    84 GIPESG---SVQAILDWQKRTMEMMYTDIAQALRAQgiDDEDPRDYLTFFCLanrevKKEGEYEPAEKPEedsdyaraqe 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530374780  892 ----LIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAV 929
Cdd:cd09199   161 arrfMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAM 202
PLDc_pPLDbeta_2 cd09200
Catalytic domain, repeat 2, of plant beta-type phospholipase D; Catalytic domain, repeat 2, of ...
761-929 3.77e-26

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: 107.33  E-value: 3.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  761 SIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGD------AIAQRILKAHRENQKYRVYVVIPLLPgfEGDIStg 834
Cdd:cd09200     8 SIHTAYVKAIRSAQHFIYIENQYFIGSSYNWPAYKDAGAdnlipmEIALKIAEKIRAGERFAVYIVIPMWP--EGVPT-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  835 gGNALQAIMHFNYRTMCRGENSILGQLK------AELGNQWINYisFC-GLRT---HAELEGNLVTE------------- 891
Cdd:cd09200    84 -GAAVQEILYWQHQTMQMMYETIAKALVdtglegAFSPQDYLNF--YClGNREmkdGIEPSPTNSPRqnstqgrsqksrr 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 530374780  892 -LIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAV 929
Cdd:cd09200   161 fMIYVHSKGMIVDDEYVIIGSANINQRSMDGSRDTEIAM 199
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
665-937 6.07e-20

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: 93.08  E-value: 6.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  665 ADFIDRY---STPRMPWHDIASAVHGKAARDVARHFIQRWNFTkimkskyrslsypfllpksqTTAHELRYQVPGSVHan 741
Cdd:COG1502   132 ANITDEYlgrDPGFGPWRDTHVRIEGPAVADLQAVFAEDWNFA--------------------TGEALPFPEPAGDVR-- 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  742 VQLLRSAADwsagikYHEESIHAAYVHVIENSRHYIYIENQFFIscaddkvvfnkIGDAIAQRILKAHRENqkyrVYVVI 821
Cdd:COG1502   190 VQVVPSGPD------SPRETIERALLAAIASARRRIYIETPYFV-----------PDRSLLRALIAAARRG----VDVRI 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  822 pLLPGfegdistgggnalqaimHFNYRTMCRGENSILGQLKAelgnqwinyisfCGLRTHaELEGNlvteliYVHSKLLI 901
Cdd:COG1502   249 -LLPA-----------------KSDHPLVHWASRSYYEELLE------------AGVRIY-EYEPG------FLHAKVMV 291
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 530374780  902 ADDNTVIIGSANINDRSMlgKRDSEMAVIVQDTETV 937
Cdd:COG1502   292 VDDEWALVGSANLDPRSL--RLNFEVNLVIYDPEFA 325
PLDc_pPLD_like_1 cd09139
Catalytic domain, repeat 1, of plant phospholipase D and similar proteins; Catalytic domain, ...
362-494 7.17e-19

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: 85.14  E-value: 7.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  362 FEDVANAMEEANEEIFITDWWLSPEIFLKR----PVVEGNRWRLDCILKRKAQQGVRIFIMLYKEvELALGINSEYTKRT 437
Cdd:cd09139    11 WEDMYDAICNAKHLIYIAGWSVNPEISLIRdserEDPPKYSPTLGELLKRKAEEGVAVLLLLWDD-KTVNGFKNDGVMAT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  438 ----LMRLHPNIKVM-----RHPDHVSSTV------YLWAHHEKLVIIDQS---------VAFVGGIDLAYGRWDDNEHR 493
Cdd:cd09139    90 hdeeTRNFFRNTKVNcllcpRNGDAGNTYVeqievsTAFTHHQKTVIVDAPapngerreiVAFVGGIDLCDGRYDNPEHS 169

                  .
gi 530374780  494 L 494
Cdd:cd09139   170 L 170
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
87-207 3.30e-16

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: 75.07  E-value: 3.30e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780     87 EVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRqnvreeprempsLPRS 166
Cdd:smart00312    1 VVEPEKIGDGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGR------------LNNF 68
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 530374780    167 SENMIREeqflgRRKQLEDYLTKILKMPMYRN-YHATTEFLD 207
Cdd:smart00312   69 SEEFIEK-----RRRGLEKYLQSLLNHPELINhSEVVLEFLE 105
PLDc_vPLD1_2_like_bac_1 cd09140
Catalytic domain, repeat 1, of uncharacterized bacterial proteins with similarity to ...
356-493 3.46e-16

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: 76.43  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  356 VNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNR-WRLDCILKRKAQQ--GVRIFI------MLY---KEV 423
Cdd:cd09140     5 IDAADYFRALREALLRARRSILIVGWDFDSRIRLRRGGDDDGGpERLGDFLNWLAERrpDLDIRIlkwdfaMLYaleREL 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530374780  424 ELALGINseytkrtlMRLHPNIKVM---RHPDHVSstvylwaHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHR 493
Cdd:cd09140    85 LPLFLLR--------WKTHPRIHFRldgHHPLGAS-------HHQKIVVIDDALAFCGGIDLTVDRWDTREHL 142
PLDc_vPLD1_2_like_bac_2 cd09143
Catalytic domain, repeat 2, of uncharacterized bacterial proteins with similarity to ...
762-919 1.89e-15

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: 74.48  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  762 IHAAYVHVIENSRHYIYIENQFFIScaddkvvfNKIGDAIAQRIlkahRENQKYRVYVVIPL-LPGFegdistgggnalq 840
Cdd:cd09143     9 IEALYLDAIAAARRFIYIENQYFTS--------RRIAEALAERL----REPDGPEIVIVLPRtSDGW------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  841 aimhFNYRTMCRGENSILGQLK-AELGNQwinyisfcgLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSM 919
Cdd:cd09143    64 ----LEQLTMGVARARLLRRLReADRHGR---------LRVYYPVTAGGGGRPIYVHSKLMIVDDRLLRVGSANLNNRSM 130
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
108-206 2.71e-14

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 69.19  E-value: 2.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   108 THGEFKWQVKRKFKHFQEFHRELLKYKAFIRIP-IPTRRHTFRRqnvreeprempslprsSENMIREeqflgRRKQLEDY 186
Cdd:pfam00787    3 TFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPpLPPKRWLGRY----------------NEEFIEK-----RRKGLEQY 61
                           90       100
                   ....*....|....*....|
gi 530374780   187 LTKILKMPMYRNYHATTEFL 206
Cdd:pfam00787   62 LQRLLQHPELRNSEVLLEFL 81
PLDc_pPLDbeta_1 cd09198
Catalytic domain, repeat 1, of plant beta-type phospholipase D; Catalytic domain, repeat 1, of ...
362-494 1.35e-13

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: 70.30  E-value: 1.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  362 FEDVANAMEEANEEIFITDWWLSPEIFL----KRPVVEGNRWRLDCILKRKAQQGVRIF-----------IMLYKeVELA 426
Cdd:cd09198    11 WEDMCDAIREARRLIYITGWSVYHKVKLirdkLRPVPPGGELTLGELLKSKSQEGVRVLllvwddktshsILGYK-TDGV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  427 LGINSEYTKRTLMrlHPNIKVMRHPDHVSSTV---------YLWAHHEKLVIIDQS--------VAFVGGIDLAYGRWDD 489
Cdd:cd09198    90 MATHDEETKRFFK--HSSVQCVLAPRYAGKKHswfkqqvvgTLYTHHQKNVIVDADaggnrrkiTAFIGGLDLCDGRYDT 167

                  ....*
gi 530374780  490 NEHRL 494
Cdd:cd09198   168 PQHPL 172
PLDc_pPLDalpha_1 cd09197
Catalytic domain, repeat 1, of plant alpha-type phospholipase D; Catalytic domain, repeat 1, ...
362-494 8.45e-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: 64.94  E-value: 8.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  362 FEDVANAMEEANEEIFITDWWLSPEIFL----KRPVvEGNRWRLDCILKRKAQQGVRIFIMLYKEvelalGINSEYTKRT 437
Cdd:cd09197    11 WEDVFDAIMNAKHLIYITGWSVYCEIVLvrdsRRPK-PGGDLTLGELLKKKASEGVRVLMLVWDD-----RTSVEFLKKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  438 -LMRLHPN-------------IKVMRHPDHVSSTVY------LWAHHEKLVIIDQS-----------VAFVGGIDLAYGR 486
Cdd:cd09197    85 gLMATHDEeteaffqdsdvhcFLCPRNPDDGGSKVQglqistMFTHHQKIVVVDSPmpgsdsgrrriVSFVGGIDLCDGR 164

                  ....*...
gi 530374780  487 WDDNEHRL 494
Cdd:cd09197   165 YDNPFHSL 172
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
363-493 1.00e-10

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


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 60.22  E-value: 1.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  363 EDVANAMEEANEEIFITDWWLSpeiflkrpvvEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLH 442
Cdd:cd00138     1 EALLELLKNAKESIFIATPNFS----------FNSADRLLKALLAAAERGVDVRLIIDKPPNAAGSLSAALLEALLRAGV 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530374780  443 PNIKVMRHPDhvsstvYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHR 493
Cdd:cd00138    71 NVRSYVTPPH------FFERLHAKVVVIDGEVAYVGSANLSTASAAQNREA 115
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
102-208 3.94e-10

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: 58.14  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  102 LYTIELTHGEFK-WQVKRKFKHFQEFHRELLKYKAFIRIPiptrrhtfrrqnvreeprempSLPRSSENMIREEQFL-GR 179
Cdd:cd06093    19 VYIIEVTTQGGEeWTVYRRYSDFEELHEKLKKKFPGVILP---------------------PLPPKKLFGNLDPEFIeER 77
                          90       100
                  ....*....|....*....|....*....
gi 530374780  180 RKQLEDYLTKILKMPMYRNYHATTEFLDI 208
Cdd:cd06093    78 RKQLEQYLQSLLNHPELRNSEELKEFLEL 106
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
764-931 3.14e-09

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


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 55.99  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  764 AAYVHVIENSRHYIYIENQFFiscaddkvvFNKIGDAIAQRILKAHreNQKYRVYVVIPLLPGFEGdistgggnalqaim 843
Cdd:cd00138     1 EALLELLKNAKESIFIATPNF---------SFNSADRLLKALLAAA--ERGVDVRLIIDKPPNAAG-------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  844 hfnyrtmcrgenSILGQLKAELGNQWINYISFCGLRTHAElegnlvteliYVHSKLLIADDNTVIIGSANINDRSMlgKR 923
Cdd:cd00138    56 ------------SLSAALLEALLRAGVNVRSYVTPPHFFE----------RLHAKVVVIDGEVAYVGSANLSTASA--AQ 111

                  ....*...
gi 530374780  924 DSEMAVIV 931
Cdd:cd00138   112 NREAGVLV 119
PLDc_SMU_988_like_1 cd09154
Putative catalytic domain, repeat 1, of Streptococcus mutans uncharacterized protein SMU_988 ...
355-495 8.28e-08

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: 52.53  E-value: 8.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  355 YVNAKGYFEDVANAMEEANEEIFItdwwlspEIFLkrpVVEGNRWR--LDcILKRKAQQGVRIFIMlYKEVELALGINSE 432
Cdd:cd09154     1 FPLGEDMFEDMLEDLKKAEKFIFM-------EYFI---IEEGYMWDsiLE-ILKEKAKEGVEVRIM-YDDFGSITTLPKD 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530374780  433 YTKRtLMRLHpnIKVMR----HPdhVSSTVYLWAHHEKLVIIDQSVAFVGGIDLA---------YGRWDDNEHRLT 495
Cdd:cd09154    69 YPKE-LEKIG--IKCRVfnpfKP--ILSLYMNNRDHRKITVIDGKVAFTGGINLAdeyinkierFGYWKDTGIRLE 139
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
222-328 3.48e-07

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: 49.47  E-value: 3.48e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780    222 IEGMIMKRSGGHRipglnccgqgracYRWSKRWLIVKDSFLLYMKPDSGA-----IAFVLLVDKEFKIKVGKKETETKYG 296
Cdd:smart00233    3 KEGWLYKKSGGGK-------------KSWKKRYFVLFNSTLLYYKSKKDKksykpKGSIDLSGCTVREAPDPDSSKKPHC 69
                            90       100       110
                    ....*....|....*....|....*....|...
gi 530374780    297 IRIDNLSR-TLILKCNSYRHARWWGGAIEEFIQ 328
Cdd:smart00233   70 FEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
222-327 6.15e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 48.71  E-value: 6.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   222 IEGMIMKRSGGHRIpglnccgqgracyRWSKRWLIVKDSFLLYMKPDSGAIAF-----VLLVDKEFKIKVGKKETETKYG 296
Cdd:pfam00169    3 KEGWLLKKGGGKKK-------------SWKKRYFVLFDGSLLYYKDDKSGKSKepkgsISLSGCEVVEVVASDSPKRKFC 69
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 530374780   297 IRI----DNLSRTLILKCNSYRHARWWGGAIEEFI 327
Cdd:pfam00169   70 FELrtgeRTGKRTYLLQAESEEERKDWIKAIQSAI 104
PLDc_2 pfam13091
PLD-like domain;
766-937 6.50e-07

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 49.60  E-value: 6.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   766 YVHVIENSRHYIYIENQFFISCaddkvvfnkigDAIAQRILKAHRENQKYRVyvvipLLPGFEGDISTgggnalqaimhF 845
Cdd:pfam13091    1 LIDLINSAKKSIDIATYYFVPD-----------REIIDALIAAAKRGVDVRI-----ILDSNKDDAGG-----------P 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   846 NYRTmcrgensiLGQLKaELGNQWINYISFCGLRTHaelegnlvteliyVHSKLLIADDNTVIIGSANINDRSMlgKRDS 925
Cdd:pfam13091   54 KKAS--------LKELR-SLLRAGVEIREYQSFLRS-------------MHAKFYIIDGKTVIVGSANLTRRAL--RLNL 109
                          170
                   ....*....|..
gi 530374780   926 EMAVIVQDTETV 937
Cdd:pfam13091  110 ENNVVIKDPELA 121
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
892-918 1.56e-05

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: 42.38  E-value: 1.56e-05
                            10        20
                    ....*....|....*....|....*..
gi 530374780    892 LIYVHSKLLIADDNTVIIGSANINDRS 918
Cdd:smart00155    2 DGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
459-486 2.68e-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: 42.02  E-value: 2.68e-05
                           10        20
                   ....*....|....*....|....*...
gi 530374780   459 YLWAHHEKLVIIDQSVAFVGGIDLAYGR 486
Cdd:pfam00614    1 YDGRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
459-486 9.30e-05

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: 40.45  E-value: 9.30e-05
                            10        20
                    ....*....|....*....|....*...
gi 530374780    459 YLWAHHEKLVIIDQSVAFVGGIDLAYGR 486
Cdd:smart00155    1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
92-208 1.63e-04

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; 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. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 41.87  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   92 TSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELlkykafiripiptrrhtfRRQNVREEPREMPS----LPRSS 167
Cdd:cd06897     7 TTSVSPKPYTVYNIQVRLPLRSYTVSRRYSEFVALHKQL------------------ESEVGIEPPYPLPPkswfLSTSS 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 530374780  168 ENMIREEqflgRRKQLEDYLTKILKMPM--YRNYHATTEFLDI 208
Cdd:cd06897    69 NPKLVEE----RRVGLEAFLRALLNDEDsrWRNSPAVKEFLNL 107
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
888-935 1.68e-04

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 42.65  E-value: 1.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 530374780  888 LVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRdsEMAVIVQDTE 935
Cdd:cd09128    84 LKDKFLKIHAKGIVVDGKTALVGSENWSANSLDRNR--EVGLIFDDPE 129
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
98-194 4.25e-04

The phosphoinositide binding Phox Homology domain of yeast MDM1p; 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. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as 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.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 41.53  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780   98 PSINLYTIELTH--GEFK---WQVKRKFKHFQEFHRELL-KYKAFIRIPIPTRRhtfrrqnvreepreMPSLPRSSENMI 171
Cdd:cd06876    36 KEFVVYLIEVQRlnNDDQssgWVVARRYSEFLELHKYLKkRYPGVLKLDFPQKR--------------KISLKYSKTLLV 101
                          90       100
                  ....*....|....*....|...
gi 530374780  172 REeqflgRRKQLEDYLTKILKMP 194
Cdd:cd06876   102 EE-----RRKALEKYLQELLKIP 119
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
356-480 5.10e-04

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


Pssm-ID: 197209 [Multi-domain]  Cd Length: 154  Bit Score: 41.69  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  356 VNAKGYFEDVANAMEEANEEIFItdwwlspEIFLKRPVVEGNRWRlDcILKRKAQQGVRIFIMLYkevelalGINSEYTK 435
Cdd:cd09110     1 TDGEEFFPALLEAIRAARHSIHL-------EYYIFRDDEIGRRFR-D-ALIEKARRGVEVRLLYD-------GFGSLGLS 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 530374780  436 RTLMRLHPN--IKVMR-HPDHVSSTVYLWAH--HEKLVIIDQSVAFVGGI 480
Cdd:cd09110    65 RRFLRELREagVEVRAfNPLSFPLFLLRLNYrnHRKILVIDGKIAFVGGF 114
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
222-323 5.30e-04

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: 40.22  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  222 IEGMIMKRSGGHRIpglnccgqgracyRWSKRWLIVKDSFLLYMKPDSGAIAF---VLLVDKEFKIKVGKKETEtKYGIR 298
Cdd:cd00821     1 KEGYLLKRGGGGLK-------------SWKKRWFVLFEGVLLYYKSKKDSSYKpkgSIPLSGILEVEEVSPKER-PHCFE 66
                          90       100
                  ....*....|....*....|....*.
gi 530374780  299 IDNL-SRTLILKCNSYRHARWWGGAI 323
Cdd:cd00821    67 LVTPdGRTYYLQADSEEERQEWLKAL 92
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
894-937 6.70e-04

catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD corresponds to the catalytic domain repeat 2 of bacterial cardiolipin synthase (CL synthase, EC 2.7.8.-) and a few homologs found in eukaryotes and archea. Bacterial CL synthases catalyze reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form cardiolipin (CL) and glycerol. The monomer of bacterial CL synthase consists of two catalytic domains. Each catalytic domain contains one copy of conserved HKD motifs (H-X-K-X(4)-D, X represents any amino acid residue) that are the characteristic of the phospholipase D (PLD) superfamily. Two HKD motifs from two domains together form a single active site involving in phosphatidyl group transfer. Bacterial CL synthases can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity in PLD superfamily. Like other PLD enzymes, bacterial CL synthase utilize a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid stabilizing the leaving group.


Pssm-ID: 197211 [Multi-domain]  Cd Length: 174  Bit Score: 41.69  E-value: 6.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 530374780  894 YVHSKLLIADDNTVIIGSANINDRSMlgKRDSEMAVIVQDTETV 937
Cdd:cd09112    92 FLHSKTLIVDDEIASVGTANLDIRSF--ELNFEVNAVIYDKEVA 133
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
892-918 1.60e-03

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


Pssm-ID: 395489 [Multi-domain]  Cd Length: 28  Bit Score: 37.01  E-value: 1.60e-03
                           10        20
                   ....*....|....*....|....*..
gi 530374780   892 LIYVHSKLLIADDNTVIIGSANINDRS 918
Cdd:pfam00614    2 DGRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
895-920 1.64e-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: 40.71  E-value: 1.64e-03
                          10        20
                  ....*....|....*....|....*.
gi 530374780  895 VHSKLLIADDNTVIIGSANINDRSML 920
Cdd:cd09162    93 LHAKAVVVDDKLALVGSANLDMRSLF 118
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
896-933 2.58e-03

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


Pssm-ID: 197256 [Multi-domain]  Cd Length: 170  Bit Score: 39.83  E-value: 2.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 530374780  896 HSKLLIADDNTVIIGSANINDRSMLgkRDSEMAVIVQD 933
Cdd:cd09159    94 HAKTAVIDGDWATVGSSNLDPRSLR--LNLEANLVVED 129
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
896-935 3.42e-03

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: 40.28  E-value: 3.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530374780  896 HSKLLIADDNTVIIGSANINDRSMlgKRDSEMAVIVQDTE 935
Cdd:cd09113   118 HAKSFVIDDRLVFVGSFNLDPRSA--YLNTEMGLVIDSPE 155
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
97-132 7.45e-03

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: 37.64  E-value: 7.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 530374780   97 VPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLK 132
Cdd:cd06875    14 VEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVA 49
PLDc_C_DEXD_like cd09126
C-terminal putative phospholipase D-like domain of uncharacterized prokaryotic HKD family ...
355-496 8.13e-03

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: 37.62  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530374780  355 YVNAKGYFEDVANAMEEANEEIFITdwwlSPEIFLKRpvvegnRWRLDCILKRKAQQGVRIFIMLYKEVELalginseyt 434
Cdd:cd09126     3 IYDGNNYEEVFRKDLAQAKKSIIIS----SPYVSQKR------ITKLINLLKEAQERGVEVTVVTREPKEY--------- 63
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530374780  435 KRTLMRL-HPNIKVMRHPDHvsstvylwahHEKLVIIDQSVAFVGGID-LAYGRWDDNEHRLTD 496
Cdd:cd09126    64 KELIEELrSAGVKVKLKEEI----------HEKFAIIDKKIVWYGSINlLGYSNAEDSIIRLKS 117
 
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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