NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15234335|ref|NP_192922|]
View 

phospholipase D gamma 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN03008 super family cl31965
Phospholipase D delta
37-857 0e+00

Phospholipase D delta


The actual alignment was detected with superfamily member PLN03008:

Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 913.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   37 VELLHGNLDIWVKEAKHLPNMDGFHNRLGGMLSGLG-------------RKKVE-GEKSSK-----ITSDPYVTVSISGA 97
Cdd:PLN03008   9 VMLLHGDLDLKIVKARRLPNMDMFSEHLRRLFTACNacarptdtddvdpRDKGEfGDKNIRshrkvITSDPYVTVVVPQA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   98 VIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIGSQIMGAVGIPTEQLCSGNRIEGLFPILNSSGKPCKQGA 177
Cdd:PLN03008  89 TLARTRVLKNSQEPLWDEKFNISIAHPFAYLEFQVKDDDVFGAQIIGTAKIPVRDIASGERISGWFPVLGASGKPPKAET 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  178 VLGLSIQYTPMERMRLYQMGVGSGNECVGVPGTYFPLRKGGRVTLYQDAHVDDGTLPSVHLDGGIQYRHGKCWEDMADAI 257
Cdd:PLN03008 169 AIFIDMKFTPFDQIHSYRCGIAGDPERRGVRRTYFPVRKGSQVRLYQDAHVMDGTLPAIGLDNGKVYEHGKCWEDICYAI 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  258 RQARRLIYITGWSVFHPVRLVRRTNDPTEG--TLGELLKVKSQEGVRVLVLVWDDPTSRSLLGFKTQGVMNTSDEETRRF 335
Cdd:PLN03008 249 SEAHHMIYIVGWSIFHKIKLVRETKVPRDKdmTLGELLKYKSQEGVRVLLLVWDDKTSHDKFGIKTPGVMGTHDEETRKF 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  336 FKHSSVQVLLCPRSGGKGHSFIKKSE-----------VGTIYTHHQKTVIVDAEAAQNRRKIVAFVGGLDLCNGRFDTPK 404
Cdd:PLN03008 329 FKHSSVICVLSPRYASSKLGLFKQQAspifsiyvmtvVGTLFTHHQKCVLVDTQAVGNNRKVTAFIGGLDLCDGRYDTPE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  405 HPLFRTLKTLHKDDFHNPNFvTTADDGPREPWHDLHSKIDGPAAYDVLANFEERWMKASKPRGIG-KLKSSS---DDSLL 480
Cdd:PLN03008 409 HRILHDLDTVFKDDFHNPTF-PAGTKAPRQPWHDLHCRIDGPAAYDVLINFEQRWRKATRWKEFSlRLKGKThwqDDALI 487
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  481 RIDRIPDIVG-----LSEASS-----------ANDNDPESWHVQVFRSIDSSSVKGFPKDPKEATGRNLLCGKNILIDMS 544
Cdd:PLN03008 488 RIGRISWILSpvfkfLKDGTSiipeddpcvwvSKEDDPENWHVQIFRSIDSGSVKGFPKYEDEAEAQHLECAKRLVVDKS 567
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  545 IHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPEGAPTSNPIQ 624
Cdd:PLN03008 568 IQTAYIQTIRSAQHFIYIENQYFLGSSYAWPSYRDAGADNLIPMELALKIVSKIRAKERFAVYVVIPLWPEGDPKSGPVQ 647
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  625 RILYWQHKTMQMMYQTIYKALVEVGLDSQfePQDFLNFFCLGTRE-----VPVGTVSVYNSprkppqpnananaaqvqAL 699
Cdd:PLN03008 648 EILYWQSQTMQMMYDVIAKELKAVQSDAH--PLDYLNFYCLGKREqlpddMPATNGSVVSD-----------------SY 708
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  700 KSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSWAMKGSRPHGQIFGYRMSLWAEHLGFLEQ 779
Cdd:PLN03008 709 NFQRFMIYVHAKGMIVDDEYVLMGSANINQRSMAGTKDTEIAMGAYQPNHTWAHKGRHPRGQVYGYRMSLWAEHLGKTGD 788
                        810       820       830       840       850       860       870
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234335  780 GFEEPENMECVRRVRQLSELNWRQYAAEEVTEMSGHLLKYPVQVDRTGKVSSLPGCETFPDLGGKIIGSF-LALQENLT 857
Cdd:PLN03008 789 EFVEPSDLECLKKVNTISEENWKRFIDPKFSELQGHLIKYPLQVDVDGKVSPLPDYETFPDVGGKIIGAHsMALPDTLT 867
 
Name Accession Description Interval E-value
PLN03008 PLN03008
Phospholipase D delta
37-857 0e+00

Phospholipase D delta


Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 913.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   37 VELLHGNLDIWVKEAKHLPNMDGFHNRLGGMLSGLG-------------RKKVE-GEKSSK-----ITSDPYVTVSISGA 97
Cdd:PLN03008   9 VMLLHGDLDLKIVKARRLPNMDMFSEHLRRLFTACNacarptdtddvdpRDKGEfGDKNIRshrkvITSDPYVTVVVPQA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   98 VIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIGSQIMGAVGIPTEQLCSGNRIEGLFPILNSSGKPCKQGA 177
Cdd:PLN03008  89 TLARTRVLKNSQEPLWDEKFNISIAHPFAYLEFQVKDDDVFGAQIIGTAKIPVRDIASGERISGWFPVLGASGKPPKAET 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  178 VLGLSIQYTPMERMRLYQMGVGSGNECVGVPGTYFPLRKGGRVTLYQDAHVDDGTLPSVHLDGGIQYRHGKCWEDMADAI 257
Cdd:PLN03008 169 AIFIDMKFTPFDQIHSYRCGIAGDPERRGVRRTYFPVRKGSQVRLYQDAHVMDGTLPAIGLDNGKVYEHGKCWEDICYAI 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  258 RQARRLIYITGWSVFHPVRLVRRTNDPTEG--TLGELLKVKSQEGVRVLVLVWDDPTSRSLLGFKTQGVMNTSDEETRRF 335
Cdd:PLN03008 249 SEAHHMIYIVGWSIFHKIKLVRETKVPRDKdmTLGELLKYKSQEGVRVLLLVWDDKTSHDKFGIKTPGVMGTHDEETRKF 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  336 FKHSSVQVLLCPRSGGKGHSFIKKSE-----------VGTIYTHHQKTVIVDAEAAQNRRKIVAFVGGLDLCNGRFDTPK 404
Cdd:PLN03008 329 FKHSSVICVLSPRYASSKLGLFKQQAspifsiyvmtvVGTLFTHHQKCVLVDTQAVGNNRKVTAFIGGLDLCDGRYDTPE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  405 HPLFRTLKTLHKDDFHNPNFvTTADDGPREPWHDLHSKIDGPAAYDVLANFEERWMKASKPRGIG-KLKSSS---DDSLL 480
Cdd:PLN03008 409 HRILHDLDTVFKDDFHNPTF-PAGTKAPRQPWHDLHCRIDGPAAYDVLINFEQRWRKATRWKEFSlRLKGKThwqDDALI 487
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  481 RIDRIPDIVG-----LSEASS-----------ANDNDPESWHVQVFRSIDSSSVKGFPKDPKEATGRNLLCGKNILIDMS 544
Cdd:PLN03008 488 RIGRISWILSpvfkfLKDGTSiipeddpcvwvSKEDDPENWHVQIFRSIDSGSVKGFPKYEDEAEAQHLECAKRLVVDKS 567
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  545 IHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPEGAPTSNPIQ 624
Cdd:PLN03008 568 IQTAYIQTIRSAQHFIYIENQYFLGSSYAWPSYRDAGADNLIPMELALKIVSKIRAKERFAVYVVIPLWPEGDPKSGPVQ 647
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  625 RILYWQHKTMQMMYQTIYKALVEVGLDSQfePQDFLNFFCLGTRE-----VPVGTVSVYNSprkppqpnananaaqvqAL 699
Cdd:PLN03008 648 EILYWQSQTMQMMYDVIAKELKAVQSDAH--PLDYLNFYCLGKREqlpddMPATNGSVVSD-----------------SY 708
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  700 KSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSWAMKGSRPHGQIFGYRMSLWAEHLGFLEQ 779
Cdd:PLN03008 709 NFQRFMIYVHAKGMIVDDEYVLMGSANINQRSMAGTKDTEIAMGAYQPNHTWAHKGRHPRGQVYGYRMSLWAEHLGKTGD 788
                        810       820       830       840       850       860       870
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234335  780 GFEEPENMECVRRVRQLSELNWRQYAAEEVTEMSGHLLKYPVQVDRTGKVSSLPGCETFPDLGGKIIGSF-LALQENLT 857
Cdd:PLN03008 789 EFVEPSDLECLKKVNTISEENWKRFIDPKFSELQGHLIKYPLQVDVDGKVSPLPDYETFPDVGGKIIGAHsMALPDTLT 867
PLDc_pPLDbeta_2 cd09200
Catalytic domain, repeat 2, of plant beta-type phospholipase D; Catalytic domain, repeat 2, of ...
537-754 1.47e-123

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: 370.81  E-value: 1.47e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 537 KNILIDMSIHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPEG 616
Cdd:cd09200   1 KNVLIDMSIHTAYVKAIRSAQHFIYIENQYFIGSSYNWPAYKDAGADNLIPMEIALKIAEKIRAGERFAVYIVIPMWPEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 617 APTSNPIQRILYWQHKTMQMMYQTIYKALVEVGLDSQFEPQDFLNFFCLGTREV-----PVGTvsvyNSPRKPPQPNANA 691
Cdd:cd09200  81 VPTGAAVQEILYWQHQTMQMMYETIAKALVDTGLEGAFSPQDYLNFYCLGNREMkdgiePSPT----NSPRQNSTQGRSQ 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234335 692 naaqvqalKSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSWAMK 754
Cdd:cd09200 157 --------KSRRFMIYVHSKGMIVDDEYVIIGSANINQRSMDGSRDTEIAMGAYQPHHTWARK 211
PLD_C pfam12357
Phospholipase D C terminal; This domain family is found in eukaryotes, and is approximately 70 ...
781-849 4.45e-39

Phospholipase D C terminal; This domain family is found in eukaryotes, and is approximately 70 amino acids in length. The family is found in association with pfam00168, pfam00614. There is a conserved FPD sequence motif. This family is the C terminal of phospholipase D. PLD is a major plant lipid-degrading enzyme which is involved in signal transduction.


Pssm-ID: 463548 [Multi-domain]  Cd Length: 69  Bit Score: 138.74  E-value: 4.45e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234335   781 FEEPENMECVRRVRQLSELNWRQYAAEEVTEMSGHLLKYPVQVDRTGKVSSLPGCETFPDLGGKIIGSF 849
Cdd:pfam12357   1 FLEPESLECVRRVNKIAEENWKLYASEEVVDLPGHLLKYPVEVDRDGKVTPLPGCEFFPDTGAKVLGSK 69
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
212-742 7.39e-31

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: 125.05  E-value: 7.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 212 FPLRKGGRVTLYQDAhvDDGtlpsvhldggiqyrhgkcWEDMADAIRQARRLIYITGWSVfhpvrlvrrTNDPTEGTLGE 291
Cdd:COG1502   9 LPLVGGNRVTLLVDG--DEA------------------FAALLEAIEAARRSIDLEYYIF---------DDDEVGRRLAD 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 292 LLKVKSQEGVRVLVLvWDDPTSRSLlgfktqgvmntsDEETRRFFKHSSVQVLLC-PRSGGKGHSFikksevgtiYTHHQ 370
Cdd:COG1502  60 ALIAAARRGVKVRVL-LDGIGSRAL------------NRDFLRRLRAAGVEVRLFnPVRLLFRRLN---------GRNHR 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 371 KTVIVDAEaaqnrrkiVAFVGGLDLCNGRFDTPKHPlfrtlktlhkddfhnpnfvttaddgprEPWHDLHSKIDGPAAYD 450
Cdd:COG1502 118 KIVVIDGR--------VAFVGGANITDEYLGRDPGF---------------------------GPWRDTHVRIEGPAVAD 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 451 VLANFEERWMKASKPRgigklksssddsllriDRIPDIVGLSEassandndpeswhVQVFRSidsssvkgFPKDPKEatg 530
Cdd:COG1502 163 LQAVFAEDWNFATGEA----------------LPFPEPAGDVR-------------VQVVPS--------GPDSPRE--- 202
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 531 rnllcgknilidmSIHAAYVKAIRSAQHFIYIENQYFLGSSfnwdsnkdlgannliPMEIALKIAnkirAREKFAAYIVI 610
Cdd:COG1502 203 -------------TIERALLAAIASARRRIYIETPYFVPDR---------------SLLRALIAA----ARRGVDVRILL 250
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 611 PMWPEgaptsnpiqrilywqHKTMQMMYQTIYKALVEVGldsqfepqdflnffclgtrevpvgtVSVYNSPRkppqpnan 690
Cdd:COG1502 251 PAKSD---------------HPLVHWASRSYYEELLEAG-------------------------VRIYEYEP-------- 282
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|..
gi 15234335 691 anaaqvqalksrrfmIYVHSKGMVVDDEFVLIGSANINQRSLegTRDTEIAM 742
Cdd:COG1502 283 ---------------GFLHAKVMVVDDEWALVGSANLDPRSL--RLNFEVNL 317
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
44-162 5.24e-17

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 77.14  E-value: 5.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335     44 LDIWVKEAKHLPNMDGFHnrlggmlsglgrkkvegeksskiTSDPYVTVSISGA--VIGRTFVISNSENPVWMQHFDVPV 121
Cdd:smart00239   2 LTVKIISARNLPPKDKGG-----------------------KSDPYVKVSLDGDpkEKKKTKVVKNTLNPVWNETFEFEV 58
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 15234335    122 AHS-AAEVHFVVKDSDIIGS-QIMGAVGIPTEQLCSGNRIEGL 162
Cdd:smart00239  59 PPPeLAELEIEVYDKDRFGRdDFIGQVTIPLSDLLLGGRHEKL 101
 
Name Accession Description Interval E-value
PLN03008 PLN03008
Phospholipase D delta
37-857 0e+00

Phospholipase D delta


Pssm-ID: 178585 [Multi-domain]  Cd Length: 868  Bit Score: 913.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   37 VELLHGNLDIWVKEAKHLPNMDGFHNRLGGMLSGLG-------------RKKVE-GEKSSK-----ITSDPYVTVSISGA 97
Cdd:PLN03008   9 VMLLHGDLDLKIVKARRLPNMDMFSEHLRRLFTACNacarptdtddvdpRDKGEfGDKNIRshrkvITSDPYVTVVVPQA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   98 VIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIGSQIMGAVGIPTEQLCSGNRIEGLFPILNSSGKPCKQGA 177
Cdd:PLN03008  89 TLARTRVLKNSQEPLWDEKFNISIAHPFAYLEFQVKDDDVFGAQIIGTAKIPVRDIASGERISGWFPVLGASGKPPKAET 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  178 VLGLSIQYTPMERMRLYQMGVGSGNECVGVPGTYFPLRKGGRVTLYQDAHVDDGTLPSVHLDGGIQYRHGKCWEDMADAI 257
Cdd:PLN03008 169 AIFIDMKFTPFDQIHSYRCGIAGDPERRGVRRTYFPVRKGSQVRLYQDAHVMDGTLPAIGLDNGKVYEHGKCWEDICYAI 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  258 RQARRLIYITGWSVFHPVRLVRRTNDPTEG--TLGELLKVKSQEGVRVLVLVWDDPTSRSLLGFKTQGVMNTSDEETRRF 335
Cdd:PLN03008 249 SEAHHMIYIVGWSIFHKIKLVRETKVPRDKdmTLGELLKYKSQEGVRVLLLVWDDKTSHDKFGIKTPGVMGTHDEETRKF 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  336 FKHSSVQVLLCPRSGGKGHSFIKKSE-----------VGTIYTHHQKTVIVDAEAAQNRRKIVAFVGGLDLCNGRFDTPK 404
Cdd:PLN03008 329 FKHSSVICVLSPRYASSKLGLFKQQAspifsiyvmtvVGTLFTHHQKCVLVDTQAVGNNRKVTAFIGGLDLCDGRYDTPE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  405 HPLFRTLKTLHKDDFHNPNFvTTADDGPREPWHDLHSKIDGPAAYDVLANFEERWMKASKPRGIG-KLKSSS---DDSLL 480
Cdd:PLN03008 409 HRILHDLDTVFKDDFHNPTF-PAGTKAPRQPWHDLHCRIDGPAAYDVLINFEQRWRKATRWKEFSlRLKGKThwqDDALI 487
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  481 RIDRIPDIVG-----LSEASS-----------ANDNDPESWHVQVFRSIDSSSVKGFPKDPKEATGRNLLCGKNILIDMS 544
Cdd:PLN03008 488 RIGRISWILSpvfkfLKDGTSiipeddpcvwvSKEDDPENWHVQIFRSIDSGSVKGFPKYEDEAEAQHLECAKRLVVDKS 567
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  545 IHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPEGAPTSNPIQ 624
Cdd:PLN03008 568 IQTAYIQTIRSAQHFIYIENQYFLGSSYAWPSYRDAGADNLIPMELALKIVSKIRAKERFAVYVVIPLWPEGDPKSGPVQ 647
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  625 RILYWQHKTMQMMYQTIYKALVEVGLDSQfePQDFLNFFCLGTRE-----VPVGTVSVYNSprkppqpnananaaqvqAL 699
Cdd:PLN03008 648 EILYWQSQTMQMMYDVIAKELKAVQSDAH--PLDYLNFYCLGKREqlpddMPATNGSVVSD-----------------SY 708
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  700 KSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSWAMKGSRPHGQIFGYRMSLWAEHLGFLEQ 779
Cdd:PLN03008 709 NFQRFMIYVHAKGMIVDDEYVLMGSANINQRSMAGTKDTEIAMGAYQPNHTWAHKGRHPRGQVYGYRMSLWAEHLGKTGD 788
                        810       820       830       840       850       860       870
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234335  780 GFEEPENMECVRRVRQLSELNWRQYAAEEVTEMSGHLLKYPVQVDRTGKVSSLPGCETFPDLGGKIIGSF-LALQENLT 857
Cdd:PLN03008 789 EFVEPSDLECLKKVNTISEENWKRFIDPKFSELQGHLIKYPLQVDVDGKVSPLPDYETFPDVGGKIIGAHsMALPDTLT 867
PLN02270 PLN02270
phospholipase D alpha
39-848 0e+00

phospholipase D alpha


Pssm-ID: 165912 [Multi-domain]  Cd Length: 808  Bit Score: 800.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   39 LLHGNLDIWVKEAKHLpNMDGFHNRLGGMLSGLGRKKVEGEKSSKItsdpYVTVSISGAVIGRTFVISN-SENPVWMQHF 117
Cdd:PLN02270   5 LLHGTLHATIYEVDKL-HSGGGPGFLGKLVANVEETVGVGKGESQL----YATIDLEKARVGRTRKIENePKNPRWYESF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  118 DVPVAHSAAEVHFVVKDSDIIGSQIMGAVGIPTEQLCSGNRIEGLFPILNSSGKPCKQGAVLGLSIQYTPMERMRLYQMG 197
Cdd:PLN02270  80 HIYCAHMASNIIFTVKDDNPIGATLIGRAYIPVEEILDGEEVDRWVEILDNDKNPIHGGSKIHVKLQYFEVTKDRNWGRG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  198 VGSGnECVGVPGTYFPLRKGGRVTLYQDAHVDDGTLPSVHLDGGIQYRHGKCWEDMADAIRQARRLIYITGWSVFHPVRL 277
Cdd:PLN02270 160 IRSA-KFPGVPYTFFSQRQGCKVSLYQDAHIPDNFVPKIPLAGGKNYEPHRCWEDVFDAITNAKHLIYITGWSVYTEISL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  278 VRRTNDPTEG---TLGELLKVKSQEGVRVLVLVWDDPTSRSLLgfKTQGVMNTSDEETRRFFKHSSVQVLLCPRSGGKGH 354
Cdd:PLN02270 239 VRDSRRPKPGgdvTIGELLKKKASEGVRVLLLVWDDRTSVDLL--KKDGLMATHDEETENFFRGTDVHCILCPRNPDDGG 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  355 SFIKKSEVGTIYTHHQKTVIVDAE---AAQNRRKIVAFVGGLDLCNGRFDTPKHPLFRTLKTLHKDDFHNPNFVTTA--D 429
Cdd:PLN02270 317 SIVQDLQISTMFTHHQKIVVVDSEmpnGGSQRRRIVSFVGGIDLCDGRYDTPFHSLFRTLDTAHHDDFHQPNFTGASitK 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  430 DGPREPWHDLHSKIDGPAAYDVLANFEERWMKASkprgiGKlksssdDSLLRIDRIPDIVgLSEASSANDNDPESWHVQV 509
Cdd:PLN02270 397 GGPREPWHDIHSRLEGPIAWDVLFNFEQRWSKQG-----GK------DILVQLRELEDVI-IPPSPVMFPDDHEVWNVQL 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  510 FRSIDSSSVKGFPKDPKEATGRNLLCGKNILIDMSIHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSN----KDLGANNL 585
Cdd:PLN02270 465 FRSIDGGAAFGFPETPEAAAEAGLVSGKDNIIDRSIQDAYIHAIRRAKDFIYIENQYFLGSSFAWSADgikpEDINALHL 544
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  586 IPMEIALKIANKIRAREKFAAYIVIPMWPEGAPTSNPIQRILYWQHKTMQMMYQTIYKALVEVGLDSqfEPQDFLNFFCL 665
Cdd:PLN02270 545 IPKELSLKIVSKIEAGEKFTVYVVVPMWPEGIPESGSVQAILDWQRRTMEMMYKDVIQALRAKGLEE--DPRNYLTFFCL 622
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  666 GTREV-PVGTVSVYNSPRKPPQPNANAnaaqvqalKSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGG 744
Cdd:PLN02270 623 GNREVkKSGEYEPSEKPEPDTDYIRAQ--------EARRFMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAMGG 694
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  745 YQPHYSWAMKGSRphGQIFGYRMSLWAEHLGFLEQGFEEPENMECVRRVRQLSELNWRQYAAEEVT-EMSGHLLKYPVQV 823
Cdd:PLN02270 695 YQPYHLSTRQPAR--GQIHGFRMSLWYEHLGMLDETFLDPESEECIQKVNQIADKYWDLYSSETLEhDLPGHLLRYPIGV 772
                        810       820
                 ....*....|....*....|....*
gi 15234335  824 DRTGKVSSLPGCETFPDLGGKIIGS 848
Cdd:PLN02270 773 ASEGDITELPGTEFFPDTKARVLGA 797
PLN02352 PLN02352
phospholipase D epsilon
89-840 0e+00

phospholipase D epsilon


Pssm-ID: 215202 [Multi-domain]  Cd Length: 758  Bit Score: 605.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   89 YVTVSISGAVIGRTfviSNSENPVWMQHFDVPVAHSAaevhfvvkDSDIIGS-----QIMGAVGIPTEQLCS-GNRIEGL 162
Cdd:PLN02352  39 YVTIKIGNKKVAKT---SHEYDRVWNQTFQILCAHPL--------DSTITITlktkcSILGRFHIQAHQIVTeASFINGF 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  163 FPILNSSGKPCKQgAVLGLSIQYTPMERMRLYQMGVGSGnECVGVPGTYFPLRKGGRVTLYQDAHVDDGTLPSVHLDGGI 242
Cdd:PLN02352 108 FPLIMENGKPNPE-LKLRFMLWFRPAELEPTWCKILENG-SFQGLRNATFPQRSNCHVILYQDAHHCSTFQPPVDLCGSP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  243 QyrhgKCWEDMADAIRQARRLIYITGWSVFHPVRLVR--RTNDP-TEG-TLGELLKVKSQEGVRVLVLVWDDPTSRSLLg 318
Cdd:PLN02352 186 R----KLWEDVYKAIEGAKHLIYIAGWSFNPKMVLVRdpETDIPhARGvKLGELLKRKAEEGVAVRVMLWDDETSLPII- 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  319 fKTQGVMNTSDEETRRFFKHSSVQVLLCPRSGGKghsfikkseVGTIYTHHQKTVIVDAEA--AQNRRKIVAFVGGLDLC 396
Cdd:PLN02352 261 -KNKGVMGTHDEDAFAYFKHTKVVCKLCPRLHKK---------FPTLFAHHQKTITVDTRAndSISEREIMSFVGGLDLC 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  397 NGRFDTPKHPLFRTLKT-LHKDDFHNPNFV--TTADDGPREPWHDLHSKIDGPAAYDVLANFEERWMKASKPrgigklks 473
Cdd:PLN02352 331 DGRYDTEEHSLFRTLNTeSHCQDFYQTSIAgaKLQKGGPREPWHDAHACIVGEAAWDVLTNFEQRWTKQCNP-------- 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  474 ssdDSLLRIDRIPDIVGLSEASSANDNDpesWHVQVFRSIDSSSVKGFPKdpkeatgrnllcgkNILIDMSIHAAYVKAI 553
Cdd:PLN02352 403 ---SVLVPTSSIRNLVHQPGSSESNNRN---WKVQVYRSIDHVSASHMPR--------------NLPVERSIHEAYVEAI 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  554 RSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPEGAPTSNPIQRILYWQHKT 633
Cdd:PLN02352 463 RRAERFIYIENQYFIGGCHLWEKDNHCGCTNLIPIEIALKIASKIRAKERFAVYILIPMWPEGVPESEPVQDILHWTRET 542
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  634 MQMMYQTIYKALVEVGLDSQfePQDFLNFFCLGTR-EVPVGTVSVYNSPRKPPQPNANAnaaqvqalKSRRFMIYVHSKG 712
Cdd:PLN02352 543 MAMMYKLIGEAIQESGEPGH--PRDYLNFFCLANReEKRKGEFVPPYSPHQKTQYWNAQ--------KNRRFMVYVHSKL 612
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  713 MVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSwamKGSRPHGQIFGYRMSLWAEHLGFLEQGFEEPENMECVRR 792
Cdd:PLN02352 613 MIVDDTYILIGSANVNQRSMDGCRDTEIAIGCYQSKNG---TNTNNPRDIQAYRMSLWYEHTGLDEESFLEPESLECVRR 689
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|
gi 15234335  793 VRQLSELNWRQYAAEEVTEMSG-HLLKYPVQVDRTGKVSSL-PGCETFPD 840
Cdd:PLN02352 690 LRTIGEQMWEIYSGEEVVDMEGvHLVNYPISVTKDGAVEDLaDGDGNFPD 739
PLDc_pPLDbeta_2 cd09200
Catalytic domain, repeat 2, of plant beta-type phospholipase D; Catalytic domain, repeat 2, of ...
537-754 1.47e-123

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: 370.81  E-value: 1.47e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 537 KNILIDMSIHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPEG 616
Cdd:cd09200   1 KNVLIDMSIHTAYVKAIRSAQHFIYIENQYFIGSSYNWPAYKDAGADNLIPMEIALKIAEKIRAGERFAVYIVIPMWPEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 617 APTSNPIQRILYWQHKTMQMMYQTIYKALVEVGLDSQFEPQDFLNFFCLGTREV-----PVGTvsvyNSPRKPPQPNANA 691
Cdd:cd09200  81 VPTGAAVQEILYWQHQTMQMMYETIAKALVDTGLEGAFSPQDYLNFYCLGNREMkdgiePSPT----NSPRQNSTQGRSQ 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15234335 692 naaqvqalKSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSWAMK 754
Cdd:cd09200 157 --------KSRRFMIYVHSKGMIVDDEYVIIGSANINQRSMDGSRDTEIAMGAYQPHHTWARK 211
PLDc_pPLD_like_2 cd09142
Catalytic domain, repeat 2, of plant phospholipase D and similar proteins; Catalytic domain, ...
537-751 5.41e-114

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: 345.95  E-value: 5.41e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 537 KNILIDMSIHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSN-KDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPE 615
Cdd:cd09142   1 KGRTIDRSIQDAYVHAIRRAKRFIYIENQYFLGSSFMWSNRdRDIGCANLIPAELALKIAEKIRARERFAVYIVIPMWPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 616 GAPTSNPIQRILYWQHKTMQMMYQTIYKALVEVGLDsQFEPQDFLNFFCLGTREVPVGTVSV-YNSPRKppqpnanaNAA 694
Cdd:cd09142  81 GIPESESVQEILYWQRLTIEMMYKIIGKAIQATGLF-SEHPTDYLNFFCLGNREEVEGGEYEaTETPTQ--------GTD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15234335 695 QVQALKSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSW 751
Cdd:cd09142 152 YYRLQKNRRFMIYVHSKMMIVDDEYIIIGSANINQRSMDGCRDSEIAMGAYQPDHLA 208
PLDc_pPLDbeta_1 cd09198
Catalytic domain, repeat 1, of plant beta-type phospholipase D; Catalytic domain, repeat 1, of ...
240-415 2.90e-96

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: 298.73  E-value: 2.90e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 240 GGIQYRHGKCWEDMADAIRQARRLIYITGWSVFHPVRLVRRTNDPT----EGTLGELLKVKSQEGVRVLVLVWDDPTSRS 315
Cdd:cd09198   1 GGKVYEHGKCWEDMCDAIREARRLIYITGWSVYHKVKLIRDKLRPVppggELTLGELLKSKSQEGVRVLLLVWDDKTSHS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 316 LLGFKTQGVMNTSDEETRRFFKHSSVQVLLCPRSGGKGHSFIKKSEVGTIYTHHQKTVIVDAEAAQNRRKIVAFVGGLDL 395
Cdd:cd09198  81 ILGYKTDGVMATHDEETKRFFKHSSVQCVLAPRYAGKKHSWFKQQVVGTLYTHHQKNVIVDADAGGNRRKITAFIGGLDL 160
                       170       180
                ....*....|....*....|
gi 15234335 396 CNGRFDTPKHPLFRTLKTLH 415
Cdd:cd09198 161 CDGRYDTPQHPLFRTLETIH 180
PLDc_pPLD_like_1 cd09139
Catalytic domain, repeat 1, of plant phospholipase D and similar proteins; Catalytic domain, ...
240-413 2.68e-84

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: 266.96  E-value: 2.68e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 240 GGIQYRHGKCWEDMADAIRQARRLIYITGWSVFHPVRLVR---RTNDPTEG-TLGELLKVKSQEGVRVLVLVWDDPTSrs 315
Cdd:cd09139   1 NGQVYNPRRLWEDMYDAICNAKHLIYIAGWSVNPEISLIRdseREDPPKYSpTLGELLKRKAEEGVAVLLLLWDDKTV-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 316 lLGFKTQGVMNTSDEETRRFFKHSSVQVLLCPRSGGKGHSFIKKSEVGTIYTHHQKTVIVDAEAAQ-NRRKIVAFVGGLD 394
Cdd:cd09139  79 -NGFKNDGVMATHDEETRNFFRNTKVNCLLCPRNGDAGNTYVEQIEVSTAFTHHQKTVIVDAPAPNgERREIVAFVGGID 157
                       170
                ....*....|....*....
gi 15234335 395 LCNGRFDTPKHPLFRTLKT 413
Cdd:cd09139 158 LCDGRYDNPEHSLFRTLDT 176
PLDc_pPLDalpha_2 cd09199
Catalytic domain, repeat 2, of plant alpha-type phospholipase D; Catalytic domain, repeat 2, ...
537-749 6.26e-83

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: 264.56  E-value: 6.26e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 537 KNILIDMSIHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSN----KDLGANNLIPMEIALKIANKIRAREKFAAYIVIPM 612
Cdd:cd09199   1 KDNIIDRSIQDAYINAIRRAKDFIYIENQYFLGSSYAWSPDgikpQDIGALHLIPKELSLKIVSKIEAGERFRVYVVVPM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 613 WPEGAPTSNPIQRILYWQHKTMQMMYQTIYKALVEVGLDSQfEPQDFLNFFCLGTREVPV-GTVSVYNSPRKPPQPNANA 691
Cdd:cd09199  81 WPEGIPESGSVQAILDWQKRTMEMMYTDIAQALRAQGIDDE-DPRDYLTFFCLANREVKKeGEYEPAEKPEEDSDYARAQ 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15234335 692 naaqvqalKSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHY 749
Cdd:cd09199 160 --------EARRFMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAMGAYQPHH 209
PLDc_pPLDalpha_1 cd09197
Catalytic domain, repeat 1, of plant alpha-type phospholipase D; Catalytic domain, repeat 1, ...
240-413 9.04e-66

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: 217.48  E-value: 9.04e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 240 GGIQYRHGKCWEDMADAIRQARRLIYITGWSVFHPVRLVRRTNDPTEG---TLGELLKVKSQEGVRVLVLVWDDPTSRSL 316
Cdd:cd09197   1 GGQKYEPTRCWEDVFDAIMNAKHLIYITGWSVYCEIVLVRDSRRPKPGgdlTLGELLKKKASEGVRVLMLVWDDRTSVEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 317 LgfKTQGVMNTSDEETRRFFKHSSVQVLLCPRSGGKGHSFIKKSEVGTIYTHHQKTVIVDAE---AAQNRRKIVAFVGGL 393
Cdd:cd09197  81 L--KKDGLMATHDEETEAFFQDSDVHCFLCPRNPDDGGSKVQGLQISTMFTHHQKIVVVDSPmpgSDSGRRRIVSFVGGI 158
                       170       180
                ....*....|....*....|
gi 15234335 394 DLCNGRFDTPKHPLFRTLKT 413
Cdd:cd09197 159 DLCDGRYDNPFHSLFRTLDD 178
C2_plant_PLD cd04015
C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds ...
39-186 2.93e-60

C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds in diester glycerophospholipids resulting in the degradation of phospholipids. In vitro PLD transfers phosphatidic acid to primary alcohols. In plants PLD plays a role in germination, seedling growth, phosphatidylinositol metabolism, and changes in phospholipid composition. There is a single Ca(2+)/phospholipid-binding C2 domain in PLD. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175982 [Multi-domain]  Cd Length: 158  Bit Score: 201.38  E-value: 2.93e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  39 LLHGNLDIWVKEAKHLPNMDGFHNRLGGMLSGL-------GRKKVEGEKSSKITSDPYVTVSISGAVIGRTFVISNSENP 111
Cdd:cd04015   4 LLHGTLDVTIYEADNLPNMDMFSEKLRRFFSKLvgcseptLKRPSSHRHVGKITSDPYATVDLAGARVARTRVIENSENP 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15234335 112 VWMQHFDVPVAHSAAEVHFVVKDSDIIGSQIMGAVGIPTEQLCSGNRIEGLFPILNSSGKPCKQGAVLGLSIQYT 186
Cdd:cd04015  84 VWNESFHIYCAHYASHVEFTVKDNDVVGAQLIGRAYIPVEDLLSGEPVEGWLPILDSNGKPPKPGAKIRVSLQFT 158
PLDc_vPLD1_2_yPLD_like_2 cd09141
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and ...
544-742 5.06e-44

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: 157.34  E-value: 5.06e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 544 SIHAAYVKAIRSAQHFIYIENQYFLgSSFNWDSNkdlgANNLIPMEIALKIANKIRAREKFAAYIVIPMWP--EG---AP 618
Cdd:cd09141   8 SIQNAYLDLIENAEHFIYIENQFFI-SSTGGEDP----VKNRIGEALVDRIIRAHKEGEKFRVYIVLPLLPgfEGdldDP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 619 TSNPIQRILYWQHKTM----QMMYQTIYKALVEvgldsqfEPQDFLNFFCLGTREVpvgtvsvynsprkppqpnananaa 694
Cdd:cd09141  83 GGSSIRAIMHWQYQSIcrgeHSLLERLKKEEGV-------DPEQYISFLSLRTHGK------------------------ 131
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15234335 695 qvqaLKSRRF--MIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAM 742
Cdd:cd09141 132 ----LGGRPVteQIYVHSKLMIVDDRIVIIGSANINDRSMLGDRDSEIAV 177
PLN02866 PLN02866
phospholipase D
229-776 3.73e-43

phospholipase D


Pssm-ID: 215467 [Multi-domain]  Cd Length: 1068  Bit Score: 169.94  E-value: 3.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   229 DDGTLPSVHLDGGIQYrhgkcwEDMADAIRQARRLIYITGWSVFHPVRLVRRTNDPTEGTLGELLKVKSQEGVRVLVLVW 308
Cdd:PLN02866  331 EDGSQAQWFIDGHAAF------EAIASAIENAKSEIFITGWWLCPELYLRRPFHDHESSRLDSLLEAKAKQGVQIYILLY 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   309 DDPTsrslLGFKtqgvMNTSDEETRRFFKHSSVQVLLCPRSGGKGhsfikksevgtIY--THHQKTVIVDAEaaqnrrki 386
Cdd:PLN02866  405 KEVA----LALK----INSVYSKRRLLGIHENVKVLRYPDHFSSG-----------VYlwSHHEKLVIVDYQ-------- 457
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   387 VAFVGGLDLCNGRFDTPKH------PLFRTLKtlhkdDFHNPNFV-------TTADD-----GPREPWHDLHSKIDGPAA 448
Cdd:PLN02866  458 ICFIGGLDLCFGRYDTPEHrvgdcpPVIWPGK-----DYYNPRESepnswedTMKDEldrrkYPRMPWHDVHCALWGPPC 532
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   449 YDVLANFEERW--MKASK--------------------------------------PRGIGKLKSSSDDSLLR------- 481
Cdd:PLN02866  533 RDVARHFVQRWnyAKRNKapneqaipllmphhhmviphylggseeeeiesknqednQKGIARQDSFSSRSSLQdiplllp 612
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   482 -----------------IDRIPDIVGLSEASS------------ANDNDPESWHVQVFRSIDSSSVKGFPKD-------- 524
Cdd:PLN02866  613 qeadatdgsggghklngMNSTNGSLSFSFRKSkiepvlpdtpmkGFVDDLGFLDLSVKMSSAERGSKESDSEwwetqerg 692
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   525 ----PKEATGR---NLLCGKNIL------------IDMSIHAAYVKAIRSAQHFIYIENQYFLgSSFNWDS---NKDLGA 582
Cdd:PLN02866  693 dqvgSADEVGQvgpRVSCRCQVIrsvsqwsagtsqVEESIHAAYCSLIEKAEHFIYIENQFFI-SGLSGDDtiqNRVLEA 771
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   583 nnlipmeIALKIANKIRAREKFAAYIVIPMWP--------EGAPTsnpIQRILYWQHKTMQMMYQTIYKALVEVgLDSQf 654
Cdd:PLN02866  772 -------LYRRILRAHKEKKCFRVIIVIPLLPgfqggvddGGAAS---VRAIMHWQYRTICRGKNSILHNLYDL-LGPK- 839
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335   655 ePQDFLNFFCLGT-----REVPVGTVSvynsprkppqpnananaaqvqalksrrfmIYVHSKGMVVDDEFVLIGSANINQ 729
Cdd:PLN02866  840 -THDYISFYGLRAygrlfEGGPLATSQ-----------------------------IYVHSKIMIVDDRAALIGSANIND 889
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15234335   730 RSLEGTRDTEIA------------MGGYQphysWaMKGSRPHgqifGYRMSLWAEHLGF 776
Cdd:PLN02866  890 RSLLGSRDSEIGvviedkefvdssMNGKP----W-KAGKFAH----SLRLSLWSEHLGL 939
PLD_C pfam12357
Phospholipase D C terminal; This domain family is found in eukaryotes, and is approximately 70 ...
781-849 4.45e-39

Phospholipase D C terminal; This domain family is found in eukaryotes, and is approximately 70 amino acids in length. The family is found in association with pfam00168, pfam00614. There is a conserved FPD sequence motif. This family is the C terminal of phospholipase D. PLD is a major plant lipid-degrading enzyme which is involved in signal transduction.


Pssm-ID: 463548 [Multi-domain]  Cd Length: 69  Bit Score: 138.74  E-value: 4.45e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15234335   781 FEEPENMECVRRVRQLSELNWRQYAAEEVTEMSGHLLKYPVQVDRTGKVSSLPGCETFPDLGGKIIGSF 849
Cdd:pfam12357   1 FLEPESLECVRRVNKIAEENWKLYASEEVVDLPGHLLKYPVEVDRDGKVTPLPGCEFFPDTGAKVLGSK 69
PLDc_vPLD1_2_like_2 cd09105
Catalytic domain, repeat 2, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
541-743 5.16e-37

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: 135.89  E-value: 5.16e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 541 IDMSIHAAYVKAIRSAQHFIYIENQYFlgssfnwdsnkdlgannlIPMEIALKIANKIRAREKFAAYIVIPMWPEGAPTs 620
Cdd:cd09105   5 GEFEIADAYLKAIRNARRYIYIEDQYL------------------WSPELLDALAEALKANPGLRVVLVLPALPDAVAF- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 621 npiqriLYWQHKtmqmmyqtIYKALVEVGLDSQFEPQDFLNFFCLGTREVPvgtvsvynsprkppqpnananaaqvqalk 700
Cdd:cd09105  66 ------GADDGL--------DALALLALLLLADAAPDRVAVFSLATHRRGL----------------------------- 102
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15234335 701 SRRFMIYVHSKGMVVDDEFVLIGSANINQRSLegTRDTEIAMG 743
Cdd:cd09105 103 LGGPPIYVHSKVVIVDDEWATVGSANLNRRSM--TWDTELNLA 143
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
212-742 7.39e-31

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: 125.05  E-value: 7.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 212 FPLRKGGRVTLYQDAhvDDGtlpsvhldggiqyrhgkcWEDMADAIRQARRLIYITGWSVfhpvrlvrrTNDPTEGTLGE 291
Cdd:COG1502   9 LPLVGGNRVTLLVDG--DEA------------------FAALLEAIEAARRSIDLEYYIF---------DDDEVGRRLAD 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 292 LLKVKSQEGVRVLVLvWDDPTSRSLlgfktqgvmntsDEETRRFFKHSSVQVLLC-PRSGGKGHSFikksevgtiYTHHQ 370
Cdd:COG1502  60 ALIAAARRGVKVRVL-LDGIGSRAL------------NRDFLRRLRAAGVEVRLFnPVRLLFRRLN---------GRNHR 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 371 KTVIVDAEaaqnrrkiVAFVGGLDLCNGRFDTPKHPlfrtlktlhkddfhnpnfvttaddgprEPWHDLHSKIDGPAAYD 450
Cdd:COG1502 118 KIVVIDGR--------VAFVGGANITDEYLGRDPGF---------------------------GPWRDTHVRIEGPAVAD 162
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 451 VLANFEERWMKASKPRgigklksssddsllriDRIPDIVGLSEassandndpeswhVQVFRSidsssvkgFPKDPKEatg 530
Cdd:COG1502 163 LQAVFAEDWNFATGEA----------------LPFPEPAGDVR-------------VQVVPS--------GPDSPRE--- 202
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 531 rnllcgknilidmSIHAAYVKAIRSAQHFIYIENQYFLGSSfnwdsnkdlgannliPMEIALKIAnkirAREKFAAYIVI 610
Cdd:COG1502 203 -------------TIERALLAAIASARRRIYIETPYFVPDR---------------SLLRALIAA----ARRGVDVRILL 250
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 611 PMWPEgaptsnpiqrilywqHKTMQMMYQTIYKALVEVGldsqfepqdflnffclgtrevpvgtVSVYNSPRkppqpnan 690
Cdd:COG1502 251 PAKSD---------------HPLVHWASRSYYEELLEAG-------------------------VRIYEYEP-------- 282
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|..
gi 15234335 691 anaaqvqalksrrfmIYVHSKGMVVDDEFVLIGSANINQRSLegTRDTEIAM 742
Cdd:COG1502 283 ---------------GFLHAKVMVVDDEWALVGSANLDPRSL--RLNFEVNL 317
PLDc_vPLD1_2_like_1 cd09104
Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, and similar proteins; ...
249-409 9.90e-27

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: 106.33  E-value: 9.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 249 CWEDMADAIRQARRLIYITGWSV-FHPVRLVRRTNDPTegtLGELLKVK-SQEGVRVLVLVWDDPTSRsllgfKTQGVMN 326
Cdd:cd09104  10 YFDDLAEALDGARHSVYITGWQVsADIILAPLLAGPDR---LGDTLRTLaARRGVDVRVLLWDSPLLV-----LLGPDDK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 327 TSDEETRRFFKHSSVQVLLCPRSGgkghsfikkseVGTIYTHHQKTVIVDaeaaqnrRKIVAFVGGLDLCNGRFDTPKHP 406
Cdd:cd09104  82 DLNLGFPTFLRLTTALLVLDLRLR-----------RHTLFSHHQKLVVID-------SAEVAFVGGIDLAYGRYDDPDHA 143

                ...
gi 15234335 407 LFR 409
Cdd:cd09104 144 LAA 146
PLDc_vPLD1_2_yPLD_like_1 cd09138
Catalytic domain, repeat 1, of vertebrate phospholipases, PLD1 and PLD2, yeast PLDs, and ...
251-408 2.62e-24

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: 99.56  E-value: 2.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 251 EDMADAIRQARRLIYITGWSVFHPVRLVRRTNDPTEGTLGELLKVKSQEGVRVLVLVWDDPTSrsllgfktqgVMNTSDE 330
Cdd:cd09138  12 WAVADAIENAKEEIFITDWWLSPELYLRRPPAGNERWRLDRLLKRKAEEGVKIYILLYKEVEL----------ALTINSK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 331 ETRRFFK--HSSVQVLLCPrsggkghSFIKKsevGTIY-THHQKTVIVDAEaaqnrrkiVAFVGGLDLCNGRFDTPKHPL 407
Cdd:cd09138  82 YTKRTLEnlHPNIKVLRHP-------DHLPQ---GPLLwSHHEKIVVIDQS--------IAFVGGLDLCYGRWDTHQHPL 143

                .
gi 15234335 408 F 408
Cdd:cd09138 144 T 144
PLDc_vPLD1_2 cd09844
Catalytic domain, repeat 2, of vertebrate phospholipase D1; Catalytic domain, repeat 2, of ...
544-742 2.17e-23

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: 98.09  E-value: 2.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 544 SIHAAYVKAIRSAQHFIYIENQYFLGSSfnwdsnKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWP--EGAPTS- 620
Cdd:cd09844   8 SIHAAYVSVIENSKHYIYIENQFFISCA------DDKVVFNKIGDAIAQRILKAHRENKRYRVYVVIPLLPgfEGDISTg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 621 --NPIQRILYWQHKTMQMMYQTIYKALVEVGLDSQFepqDFLNFFCLGTREVPVGTVSVYnsprkppqpnananaaqvqa 698
Cdd:cd09844  82 ggNALQAIMHFNYRTMCRGEHSIIGQLKAEMGDQWI---NYISFCGLRTHAELEGNLVTE-------------------- 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15234335 699 lksrrfMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAM 742
Cdd:cd09844 139 ------LIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAV 176
PLDc_vPLD2_2 cd09845
Catalytic domain, repeat 2, of vertebrate phospholipase D2; Catalytic domain, repeat 2, of ...
544-742 1.97e-20

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: 89.55  E-value: 1.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 544 SIHAAYVKAIRSAQHFIYIENQYFLGSSfnwdsnKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWP--EGAPTS- 620
Cdd:cd09845   8 SILNAYLHTIENSQHYLYLENQFFISCA------DGRTVLNKIGDAIVKRILKAHSQGWCFRVFVVIPLLPgfEGDISTg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 621 --NPIQRILYWQHKTMQMMYQTIYKALVEVGLDSQfepQDFLNFFCLGTR-EVPVGTVSVynsprkppqpnananaaqvq 697
Cdd:cd09845  82 ggNSIQAILHFTYRTICRGEYSILSRLKEAMGTAW---TDYISICGLRTHgELGGSPVTE-------------------- 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15234335 698 alksrrfMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAM 742
Cdd:cd09845 139 -------LIYIHSKVLIADDRTVIIGSANINDRSMLGKRDSELAV 176
C2 pfam00168
C2 domain;
42-165 2.49e-18

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 80.83  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335    42 GNLDIWVKEAKHLPNMDGFhnrlggmlsglgrkkvegeksskITSDPYVTVSI-SGAVIGRTFVISNSENPVWMQHFDVP 120
Cdd:pfam00168   1 GRLTVTVIEAKNLPPKDGN-----------------------GTSDPYVKVYLlDGKQKKKTKVVKNTLNPVWNETFTFS 57
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15234335   121 VAHSA-AEVHFVVKDSDIIGS-QIMGAVGIPTEQLCSGNRIEGLFPI 165
Cdd:pfam00168  58 VPDPEnAVLEIEVYDYDRFGRdDFIGEVRIPLSELDSGEGLDGWYPL 104
PLDc_vPLD1_2_like_bac_1 cd09140
Catalytic domain, repeat 1, of uncharacterized bacterial proteins with similarity to ...
253-405 1.35e-17

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


Pssm-ID: 197238 [Multi-domain]  Cd Length: 146  Bit Score: 80.28  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 253 MADAIRQARRLIYITGWSvFHP-VRLVRRTNDPTEG-TLGELLK--VKSQEGVRVLVLVWDdptsRSLLGFKTQGVMNTS 328
Cdd:cd09140  14 LREALLRARRSILIVGWD-FDSrIRLRRGGDDDGGPeRLGDFLNwlAERRPDLDIRILKWD----FAMLYALERELLPLF 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 329 DeetRRFFKHSSVQVLL---CPRSGgkghsfikksevgtiyTHHQKTVIVDAEaaqnrrkiVAFVGGLDLCNGRFDTPKH 405
Cdd:cd09140  89 L---LRWKTHPRIHFRLdghHPLGA----------------SHHQKIVVIDDA--------LAFCGGIDLTVDRWDTREH 141
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
44-162 5.24e-17

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 77.14  E-value: 5.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335     44 LDIWVKEAKHLPNMDGFHnrlggmlsglgrkkvegeksskiTSDPYVTVSISGA--VIGRTFVISNSENPVWMQHFDVPV 121
Cdd:smart00239   2 LTVKIISARNLPPKDKGG-----------------------KSDPYVKVSLDGDpkEKKKTKVVKNTLNPVWNETFEFEV 58
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 15234335    122 AHS-AAEVHFVVKDSDIIGS-QIMGAVGIPTEQLCSGNRIEGL 162
Cdd:smart00239  59 PPPeLAELEIEVYDKDRFGRdDFIGQVTIPLSDLLLGGRHEKL 101
PLDc_vPLD1_2_like_bac_2 cd09143
Catalytic domain, repeat 2, of uncharacterized bacterial proteins with similarity to ...
545-739 4.95e-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: 72.94  E-value: 4.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 545 IHAAYVKAIRSAQHFIYIENQYFlgSSFnwdsnkdlgannlipmEIALKIANKIRAREKFAAYIVIPMWPEGaptsnpiq 624
Cdd:cd09143   9 IEALYLDAIAAARRFIYIENQYF--TSR----------------RIAEALAERLREPDGPEIVIVLPRTSDG-------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 625 rilyW-QHKTMQMMYQTIYKALVEVGLdsqfepQDFLNFFClgtrevPVGTvsvynsprkppqpnananaaqvqalKSRR 703
Cdd:cd09143  63 ----WlEQLTMGVARARLLRRLREADR------HGRLRVYY------PVTA-------------------------GGGG 101
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15234335 704 FMIYVHSKGMVVDDEFVLIGSANINQRSLeGTrDTE 739
Cdd:cd09143 102 RPIYVHSKLMIVDDRLLRVGSANLNNRSM-GL-DTE 135
PLDc_vPLD1_1 cd09842
Catalytic domain, repeat 1, of vertebrate phospholipase D1; Catalytic domain, repeat 1, of ...
244-407 3.59e-13

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: 67.75  E-value: 3.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 244 YRHGKCW-EDMADAIRQARRLIYITGWSVFHPVRLVRRTNDPTEGTLGELLKVKSQEGVRVLVLVWDDptsrsllgfkTQ 322
Cdd:cd09842   4 YVNAKCYfEDVANAMEEAKEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFVMLYKE----------VE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 323 GVMNTSDEETRRFFK--HSSVQVLLCPRsggkghsfiKKSEVGTIYTHHQKTVIVDAEaaqnrrkiVAFVGGLDLCNGRF 400
Cdd:cd09842  74 LALGINSEYSKRTLMrlHPNIKVMRHPD---------HVSSSVYLWAHHEKIVVIDQS--------VAFVGGIDLAYGRW 136

                ....*..
gi 15234335 401 DTPKHPL 407
Cdd:cd09842 137 DDDEHRL 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
44-165 7.00e-13

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 65.55  E-value: 7.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  44 LDIWVKEAKHLPNMDgfhnrlggmlsglgrkkvegeksSKITSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAH 123
Cdd:cd00030   1 LRVTVIEARNLPAKD-----------------------LNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLD 57
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15234335 124 SA-AEVHFVVKDSDIIGSQ-IMGAVGIPTEQLC-SGNRIEGLFPI 165
Cdd:cd00030  58 PEsDTLTVEVWDKDRFSKDdFLGEVEIPLSELLdSGKEGELWLPL 102
PLDc_vPLD2_1 cd09843
Catalytic domain, repeat 1, of vertebrate phospholipase D2; Catalytic domain, repeat 1, of ...
252-401 1.56e-12

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: 65.79  E-value: 1.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 252 DMADAIRQARRLIYITGWSVFHPVRLvRRTNDPTEGTLGELLKVKSQEGVRVLVLVWDDptSRSLLGfktqgvMNTSDEE 331
Cdd:cd09843  13 AVADALEQAQEEIFITDWWLSPEVFL-KRPAHGDDWRLDIILKRKAEQGVRVCVLLFKE--VELALG------INSGYSK 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 332 TRRFFKHSSVQVLLCPRsggkghsfiKKSEVGTIYTHHQKTVIVDaeaaqnrrKIVAFVGGLDLCNGRFD 401
Cdd:cd09843  84 RKLMLLHPNIKVMRHPD---------HVASVVVLWAHHEKMVAID--------QSVAFLGGLDLAYGRWD 136
C2C_Tricalbin-like cd04045
C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
42-153 3.74e-09

C2 domain third repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 176010 [Multi-domain]  Cd Length: 120  Bit Score: 55.29  E-value: 3.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  42 GNLDIWVKEAKHLPNmdgfhnrlggmLSGLGRkkvegeksskitSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPV 121
Cdd:cd04045   1 GVLRLHIRKANDLKN-----------LEGVGK------------IDPYVRVLVNGIVKGRTVTISNTLNPVWDEVLYVPV 57
                        90       100       110
                ....*....|....*....|....*....|....
gi 15234335 122 aHSAAEVHFV-VKDSDIIGS-QIMGAVGIPTEQL 153
Cdd:cd04045  58 -TSPNQKITLeVMDYEKVGKdRSLGSVEINVSDL 90
C2_PLC_like cd00275
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ...
68-172 1.03e-08

C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175974 [Multi-domain]  Cd Length: 128  Bit Score: 54.08  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  68 LSGLGRKKVEGEKSSKItsDPYVTVSISGA-----VIGRTFVIS-NSENPVWMQHFDVPVAH-SAAEVHFVVKDSDIIGS 140
Cdd:cd00275   9 ISGQQLPKPKGDKGSIV--DPYVEVEIHGLpaddsAKFKTKVVKnNGFNPVWNETFEFDVTVpELAFLRFVVYDEDSGDD 86
                        90       100       110
                ....*....|....*....|....*....|..
gi 15234335 141 QIMGAVGIPTEQLCSGNRIEglfPILNSSGKP 172
Cdd:cd00275  87 DFLGQACLPLDSLRQGYRHV---PLLDSKGEP 115
C2A_Ferlin cd08373
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ...
86-189 3.73e-08

C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176019 [Multi-domain]  Cd Length: 127  Bit Score: 52.64  E-value: 3.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  86 SDPYVTVSISGaVIGRTFVISNSENPVWMQHFDVPVAHSA---AEVHFVVKDSDIIGS-QIMGAVGIPTEQLCSGNRIEG 161
Cdd:cd08373  15 GDRIAKVTFRG-VKKKTRVLENELNPVWNETFEWPLAGSPdpdESLEIVVKDYEKVGRnRLIGSATVSLQDLVSEGLLEV 93
                        90       100
                ....*....|....*....|....*...
gi 15234335 162 LFPILNSSGKPckQGAVLGLSIQYTPME 189
Cdd:cd08373  94 TEPLLDSNGRP--TGATISLEVSYQPPD 119
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
42-137 1.79e-07

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 50.37  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  42 GNLDIWVKEAKHLPNMDGFhnrLGGMLSGlgrkkvegeksskiTSDPYVTVSIsGAVIGRTFVISNSENPVWMQHFDVPV 121
Cdd:cd08391   1 GVLRIHVIEAQDLVAKDKF---VGGLVKG--------------KSDPYVIVRV-GAQTFKSKVIKENLNPKWNEVYEAVV 62
                        90
                ....*....|....*..
gi 15234335 122 -AHSAAEVHFVVKDSDI 137
Cdd:cd08391  63 dEVPGQELEIELFDEDP 79
PLDc_CLS_2 cd09112
catalytic domain repeat 2 of bacterial cardiolipin synthase and similar proteins; This CD ...
544-733 2.54e-07

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: 51.32  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 544 SIHAAYVKAIRSAQHFIYIENQYFlgssfnwdsnkdlgannlIP---MEIALKIAN----KIRarekfaayIVIPmwpeg 616
Cdd:cd09112  11 SIEQAYLKAINSAKKSIYIQTPYF------------------IPdesLLEALKTAAlsgvDVR--------IMIP----- 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 617 aptSNPIQRILYWQHKTmqmmYqtiYKALVEVGldsqfepqdflnffclgtrevpvgtVSVYnsprkppqpnananaaqv 696
Cdd:cd09112  60 ---GKPDHKLVYWASRS----Y---FEELLKAG-------------------------VKIY------------------ 86
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15234335 697 qaLKSRRFMiyvHSKGMVVDDEFVLIGSANINQRSLE 733
Cdd:cd09112  87 --EYNKGFL---HSKTLIVDDEIASVGTANLDIRSFE 118
PLDc smart00155
Phospholipase D. Active site motifs; Phosphatidylcholine-hydrolyzing phospholipase D (PLD) ...
704-731 5.08e-07

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


Pssm-ID: 197546 [Multi-domain]  Cd Length: 28  Bit Score: 46.61  E-value: 5.08e-07
                           10        20
                   ....*....|....*....|....*...
gi 15234335    704 FMIYVHSKGMVVDDEFVLIGSANINQRS 731
Cdd:smart00155   1 YDGVLHTKLMIVDDEIAYIGSANLDGRS 28
PLDc_CLS_1 cd09110
Catalytic domain, repeat 1, of bacterial cardiolipin synthase and similar proteins; Catalytic ...
250-459 1.14e-06

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: 49.01  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 250 WEDMADAIRQARRLI----YItgwsvFhpvrlvrrTNDPTEGTLGELLKVKSQEGVRVLVLVwDD----PTSRSLL-GFK 320
Cdd:cd09110   7 FPALLEAIRAARHSIhleyYI-----F--------RDDEIGRRFRDALIEKARRGVEVRLLY-DGfgslGLSRRFLrELR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 321 TQGVmntsdeETRRFFKhssvqvLLCPRSGGKGHsfikksevgtiYTHHQKTVIVDAEaaqnrrkiVAFVGGLDLCngrf 400
Cdd:cd09110  73 EAGV------EVRAFNP------LSFPLFLLRLN-----------YRNHRKILVIDGK--------IAFVGGFNIG---- 117
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15234335 401 dtpkhplfrtlktlhkDDFhnpnfvtTADDGPREPWHDLHSKIDGPAAYDVLANFEERW 459
Cdd:cd09110 118 ----------------DEY-------LGKDPGFGPWRDTHVRIEGPAVADLQAAFLEDW 153
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
42-160 1.65e-06

C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 47.80  E-value: 1.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  42 GNLDIWVKEAKHLPNMDgfhnrlggmLSGLGrkkvegeksskiTSDPYVTVSIsGAVIGRTFVISNSENPVWMQHFDVPV 121
Cdd:cd04024   1 GVLRVHVVEAKDLAAKD---------RSGKG------------KSDPYAILSV-GAQRFKTQTIPNTLNPKWNYWCEFPI 58
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15234335 122 -AHSAAEVHFVVKDSD-IIGSQIMGAVGIPTEQLCSGNRIE 160
Cdd:cd04024  59 fSAQNQLLKLILWDKDrFAGKDYLGEFDIALEEVFADGKTG 99
COG5038 COG5038
Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];
74-121 2.11e-06

Ca2+-dependent lipid-binding protein, contains C2 domain [General function prediction only];


Pssm-ID: 227371 [Multi-domain]  Cd Length: 1227  Bit Score: 51.68  E-value: 2.11e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15234335   74 KKVEGEKSS----KITSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPV 121
Cdd:COG5038  443 KSAEGLKKSdstiNGTVDPYITVTFSDRVIGKTRVKKNTLNPVWNETFYILL 494
C2_cPLA2 cd04036
C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is ...
85-171 5.08e-06

C2 domain present in cytosolic PhosphoLipase A2 (cPLA2); A single copy of the C2 domain is present in cPLA2 which releases arachidonic acid from membranes initiating the biosynthesis of potent inflammatory mediators such as prostaglandins, leukotrienes, and platelet-activating factor. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members of this cd have a type-II topology.


Pssm-ID: 176001 [Multi-domain]  Cd Length: 119  Bit Score: 46.49  E-value: 5.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  85 TSDPYVTVSISGAVIG--RTFVISNSENPVWMQHFDVPVaHSA----AEVHfvVKDSDIIGSQIMGAVGIPTEQLCSGNR 158
Cdd:cd04036  20 TPDCYVELWLPTASDEkkRTKTIKNSINPVWNETFEFRI-QSQvknvLELT--VMDEDYVMDDHLGTVLFDVSKLKLGEK 96
                        90
                ....*....|...
gi 15234335 159 IEGLFPiLNSSGK 171
Cdd:cd04036  97 VRVTFS-LNPQGK 108
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
80-172 8.71e-06

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 45.62  E-value: 8.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  80 KSSKI---TSDPYVTVSISGA-VIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKD-SDIIGSQIMGAVGIPTEQLC 154
Cdd:cd04044  15 KGSDIiggTVDPYVTFSISNRrELARTKVKKDTSNPVWNETKYILVNSLTEPLNLTVYDfNDKRKDKLIGTAEFDLSSLL 94
                        90
                ....*....|....*...
gi 15234335 155 SGNRIEGLFPILNSSGKP 172
Cdd:cd04044  95 QNPEQENLTKNLLRNGKP 112
C2D_Tricalbin-like cd04040
C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
86-140 1.96e-05

C2 domain fourth repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the fifth C2 repeat, C2E, and has a type-II topology.


Pssm-ID: 176005 [Multi-domain]  Cd Length: 115  Bit Score: 44.48  E-value: 1.96e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15234335  86 SDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAH-SAAEVHFVVKDSDIIGS 140
Cdd:cd04040  20 SDPFVKFYLNGEKVFKTKTIKKTLNPVWNESFEVPVPSrVRAVLKVEVYDWDRGGK 75
C2B_Munc13-like cd04009
C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are ...
86-141 2.04e-05

C2 domain second repeat in Munc13 (mammalian uncoordinated)-like proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology.


Pssm-ID: 175976 [Multi-domain]  Cd Length: 133  Bit Score: 44.92  E-value: 2.04e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15234335  86 SDPYVTVSI------SGAVIGRTFVISNSENPVWMQHFDVPVAHS-----AAEVHFVVKDSDIIGSQ 141
Cdd:cd04009  37 SDPFVKVELlprhlfPDVPTPKTQVKKKTLFPLFDESFEFNVPPEqcsveGALLLFTVKDYDLLGSN 103
PLDc_unchar1_2 cd09128
Putative catalytic domain, repeat 2, of uncharacterized phospholipase D-like proteins; ...
706-742 2.81e-05

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


Pssm-ID: 197226 [Multi-domain]  Cd Length: 142  Bit Score: 44.96  E-value: 2.81e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15234335 706 IYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAM 742
Cdd:cd09128  89 LKIHAKGIVVDGKTALVGSENWSANSLDRNREVGLIF 125
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
705-731 2.82e-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: 41.64  E-value: 2.82e-05
                          10        20
                  ....*....|....*....|....*..
gi 15234335   705 MIYVHSKGMVVDDEFVLIGSANINQRS 731
Cdd:pfam00614   2 DGRLHRKIVVVDDELAYIGGANLDGRS 28
PLDc_CLS_unchar2_2 cd09163
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
709-732 2.98e-05

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


Pssm-ID: 197260 [Multi-domain]  Cd Length: 176  Bit Score: 45.24  E-value: 2.98e-05
                        10        20
                ....*....|....*....|....
gi 15234335 709 HSKGMVVDDEFVLIGSANINQRSL 732
Cdd:cd09163  94 HSKLMVVDGAWALIGSANWDPRSL 117
PLDc_2 pfam13091
PLD-like domain;
703-738 3.09e-05

PLD-like domain;


Pssm-ID: 463784 [Multi-domain]  Cd Length: 132  Bit Score: 44.59  E-value: 3.09e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 15234335   703 RFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDT 738
Cdd:pfam13091  76 SFLRSMHAKFYIIDGKTVIVGSANLTRRALRLNLEN 111
C2A_Rasal1_RasA4 cd04054
C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 ...
85-155 7.00e-05

C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 (GTPase activating protein 1). Rasal1 responds to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. RasA4 suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. Both of these proteins contains two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176018 [Multi-domain]  Cd Length: 121  Bit Score: 43.27  E-value: 7.00e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15234335  85 TSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIG-SQIMGAVGIPTEQLCS 155
Cdd:cd04054  20 SSDPYCIVKVDNEVIIRTATVWKTLNPFWGEEYTVHLPPGFHTVSFYVLDEDTLSrDDVIGKVSLTREVISA 91
cls PRK01642
cardiolipin synthetase; Reviewed
253-732 1.16e-04

cardiolipin synthetase; Reviewed


Pssm-ID: 234967 [Multi-domain]  Cd Length: 483  Bit Score: 45.54  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  253 MADAIRQARRLIYItgwsVF---HPVRLVRRtndptegtLGELLKVKSQEGVRVLVLVwDDPTSRsllgfktqgvmntsd 329
Cdd:PRK01642 131 IIRDIELARHYILM----EFyiwRPDGLGDQ--------VAEALIAAAKRGVRVRLLY-DSIGSF--------------- 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  330 eetrRFFKHSSVQVLlcpRSGG-KGHSFIKKSeVGTIYTH------HQKTVIVDAEaaqnrrkiVAFVGGLDLCNGRFdt 402
Cdd:PRK01642 183 ----AFFRSPYPEEL---RNAGvEVVEFLKVN-LGRVFRRrldlrnHRKIVVIDGY--------IAYTGSMNVVDPEY-- 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  403 pkhplfrtLKTlhkddfhNPNFvttaddgprEPWHDLHSKIDGPAAYDVLANFEERWMKASKPRgigklksssddsllRI 482
Cdd:PRK01642 245 --------FKQ-------DPGV---------GQWRDTHVRIEGPVVTALQLIFAEDWEWETGER--------------IL 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  483 DRIPDIVGLSEAssandnDPESWHVQVFRSidsssvkGfPKDPKEAtgrnllcgknilidmsIHAAYVKAIRSAQHFIYI 562
Cdd:PRK01642 287 PPPPDVLIMPFE------EASGHTVQVIAS-------G-PGDPEET----------------IHQFLLTAIYSARERLWI 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  563 ENQYFlgssfnwdsnkdlgannlIPME---IALKIANK--IRARekfaayIVIPmwpegaptSNPIQRILYWQHKTmqmm 637
Cdd:PRK01642 337 TTPYF------------------VPDEdllAALKTAALrgVDVR------IIIP--------SKNDSLLVFWASRA---- 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  638 YqtiYKALVEVGldsqfepqdflnffclgtrevpvgtVSVYnsprkppqpnananaaqvqalksrR----FMiyvHSKGM 713
Cdd:PRK01642 381 F---FTELLEAG-------------------------VKIY------------------------RyeggLL---HTKSV 405
                        490
                 ....*....|....*....
gi 15234335  714 VVDDEFVLIGSANINQRSL 732
Cdd:PRK01642 406 LVDDELALVGTVNLDMRSF 424
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
702-738 2.16e-04

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


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 41.73  E-value: 2.16e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15234335 702 RRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDT 738
Cdd:cd00138  79 PHFFERLHAKVVVIDGEVAYVGSANLSTASAAQNREA 115
PLDc_EcCLS_like_2 cd09158
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins; ...
709-733 2.55e-04

Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase and similar proteins; Catalytic domain, repeat 2, of Escherichia coli cardiolipin (CL) synthase and similar proteins. Escherichia coli CL synthase (EcCLS), specified by the cls gene, is the prototype of this family. EcCLS is a multi-pass membrane protein that catalyzes reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form cardiolipin (CL) and glycerol. The monomer of EcCLS consists of two catalytic domains. Each catalytic domain contains one copy of the conserved HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. Two HKD motifs from two domains form a single active site involved in phosphatidyl group transfer. EcCLS can be stimulated by phosphate and inhibited by CL, the product of the reaction, and by phosphatidate. Phosphate stimulation may be unique to enzymes with CL synthase activity belonging to the PLD superfamily. Like other PLD enzymes, EcCLS utilizes a common two-step ping-pong catalytic mechanism involving an enzyme-substrate intermediate to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine residue from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197255 [Multi-domain]  Cd Length: 174  Bit Score: 42.56  E-value: 2.55e-04
                        10        20
                ....*....|....*....|....*
gi 15234335 709 HSKGMVVDDEFVLIGSANINQRSLE 733
Cdd:cd09158  94 HAKTVTVDDEVALVGSSNFDIRSFA 118
PLDc_CLS_unchar1_2 cd09162
Putative catalytic domain, repeat 2, of uncharacterized proteins similar to bacterial ...
708-732 3.11e-04

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


Pssm-ID: 197259 [Multi-domain]  Cd Length: 172  Bit Score: 42.25  E-value: 3.11e-04
                        10        20
                ....*....|....*....|....*
gi 15234335 708 VHSKGMVVDDEFVLIGSANINQRSL 732
Cdd:cd09162  93 LHAKAVVVDDKLALVGSANLDMRSL 117
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
78-126 3.66e-04

C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176008 [Multi-domain]  Cd Length: 126  Bit Score: 41.09  E-value: 3.66e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15234335  78 GEKSSKItSDPYVTVSISGA--VIGRTFVISNSENPVWMQHFDVPVAHSAA 126
Cdd:cd04043  15 ADSSNGL-SDPYVTLVDTNGkrRIAKTRTIYDTLNPRWDEEFELEVPAGEP 64
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
76-165 3.89e-04

C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain either a single C2 domain or two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176029 [Multi-domain]  Cd Length: 117  Bit Score: 40.71  E-value: 3.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  76 VEGEK-SSKITSDPYVTVSISGAVIGRTFVISnSENPVWMQHF---DVPVAHSAAEVHFVVKDSDIIGSQI-MGAVGIPT 150
Cdd:cd08383   7 LEAKNlPSKGTRDPYCTVSLDQVEVARTKTVE-KLNPFWGEEFvfdDPPPDVTFFTLSFYNKDKRSKDRDIvIGKVALSK 85
                        90
                ....*....|....*
gi 15234335 151 EQLCSGnrIEGLFPI 165
Cdd:cd08383  86 LDLGQG--KDEWFPL 98
C2A_MCTP_PRT cd04042
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
85-153 3.95e-04

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); MCTPs are involved in Ca2+ signaling at the membrane. MCTP is composed of a variable N-terminal sequence, three C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176007 [Multi-domain]  Cd Length: 121  Bit Score: 41.11  E-value: 3.95e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  85 TSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIGSQ-IMGAVGIPTEQL 153
Cdd:cd04042  20 TSDPYVKFKYGGKTVYKSKTIYKNLNPVWDEKFTLPIEDVTQPLYIKVFDYDRGLTDdFMGSAFVDLSTL 89
PLDc_ybhO_like_2 cd09159
Catalytic domain, repeat 2, of Escherichia coli cardiolipin synthase ybhO and similar proteins; ...
709-732 4.08e-04

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


Pssm-ID: 197256 [Multi-domain]  Cd Length: 170  Bit Score: 41.76  E-value: 4.08e-04
                        10        20
                ....*....|....*....|....
gi 15234335 709 HSKGMVVDDEFVLIGSANINQRSL 732
Cdd:cd09159  94 HAKTAVIDGDWATVGSSNLDPRSL 117
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
80-140 4.19e-04

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 41.10  E-value: 4.19e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234335  80 KSSKITSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVaHSAAEVHFVVKDSDIIGS 140
Cdd:cd04014  29 KKGSQLLDPYVSIDVDDTHIGKTSTKPKTNSPVWNEEFTTEV-HNGRNLELTVFHDAAIGP 88
C2_ArfGAP cd04038
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ...
85-137 5.33e-04

C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (PKC). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176003 [Multi-domain]  Cd Length: 145  Bit Score: 41.16  E-value: 5.33e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15234335  85 TSDPYVTVSIsGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDI 137
Cdd:cd04038  21 SSDPYVVLTL-GNQKVKTRVIKKNLNPVWNEELTLSVPNPMAPLKLEVFDKDT 72
C2B_SLP_1-2-3-4 cd04020
C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically ...
24-113 5.65e-04

C2 domain second repeat present in Synaptotagmin-like proteins 1-4; All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175987 [Multi-domain]  Cd Length: 162  Bit Score: 41.54  E-value: 5.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  24 QYVPFATSSGSLRVELLHGNLDIWVKEAKHLPNMdgfhnRLGGmlsglgrkkvegeksskiTSDPYVTVSI----SGAVI 99
Cdd:cd04020   9 KYVPPESEGALKSKKPSTGELHVWVKEAKNLPAL-----KSGG------------------TSDSFVKCYLlpdkSKKSK 65
                        90
                ....*....|....
gi 15234335 100 GRTFVISNSENPVW 113
Cdd:cd04020  66 QKTPVVKKSVNPVW 79
PLDc_ymdC_like_2 cd09113
Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and ...
709-742 8.72e-04

Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and similar proteins; Putative catalytic domain, repeat 2, of Escherichia coli uncharacterized protein ymdC and similar proteins. In Escherichia coli, there are two genes, f413 (ybhO) and o493 (ymdC), which are homologous to gene cls that encodes the Escherichia coli cardiolipin (CL) synthase. The prototype of this subfamily is an uncharacterized protein ymdC specified by the o493 (ymdC) gene. Although the functional characterization of ymdC and similar proteins remains unknown, members of this subfamily show high sequence homology to bacterial CL synthases, which catalyze the reversible phosphatidyl group transfer between two phosphatidylglycerol molecules to form CL and glycerol. Moreover, ymdC and its similar proteins contain two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characteriszes the phospholipase D (PLD) superfamily. The two motifs may be part of the active site and may be involved in phosphatidyl group transfer.


Pssm-ID: 197212 [Multi-domain]  Cd Length: 218  Bit Score: 41.82  E-value: 8.72e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15234335 709 HSKGMVVDDEFVLIGSANINQRS--LegtrDTEIAM 742
Cdd:cd09113 118 HAKSFVIDDRLVFVGSFNLDPRSayL----NTEMGL 149
C2_KIAA0528-like cd08688
C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the ...
44-165 9.30e-04

C2 domain found in the Human KIAA0528 cDNA clone; The members of this CD are named after the Human KIAA0528 cDNA clone. All members here contain a single C2 repeat. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176070 [Multi-domain]  Cd Length: 110  Bit Score: 39.60  E-value: 9.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  44 LDIWVKEAKHLPNMDgfhnrlggmlsglgrkkvegeKSSKITsDPYVTVSIsGAVIGRTFVISNSENPVWMQH---FDVP 120
Cdd:cd08688   1 LKVRVVAARDLPVMD---------------------RSSDLT-DAFVEVKF-GSTTYKTDVVKKSLNPVWNSEwfrFEVD 57
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15234335 121 VAHSAAEV-HFVVKDSDIIgSQ--IMGAVGIPTEQLC---SGNRIEGLFPI 165
Cdd:cd08688  58 DEELQDEPlQIRVMDHDTY-SAndAIGKVYIDLNPLLlkdSVSQISGWFPI 107
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
102-189 1.00e-03

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 40.04  E-value: 1.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335 102 TFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIG-SQIMGAVGIPTEQLCSGNRIEGLFPIlnsSGKPCKQGAVLG 180
Cdd:cd08678  35 SSTQKNTSNPFWDEHFLFELSPNSKELLFEVYDNGKKSdSKFLGLAIVPFDELRKNPSGRQIFPL---QGRPYEGDSVSG 111
                        90
                ....*....|
gi 15234335 181 -LSIQYTPME 189
Cdd:cd08678 112 sITVEFLFME 121
PLDc pfam00614
Phospholipase D Active site motif; Phosphatidylcholine-hydrolysing phospholipase D (PLD) ...
366-399 1.77e-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: 36.63  E-value: 1.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 15234335   366 YTHHQKTVIVDAEaaqnrrkiVAFVGGLDLCNGR 399
Cdd:pfam00614   3 GRLHRKIVVVDDE--------LAYIGGANLDGRS 28
C2_E3_ubiquitin_ligase cd04021
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ...
79-132 2.19e-03

C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175988 [Multi-domain]  Cd Length: 125  Bit Score: 38.80  E-value: 2.19e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15234335  79 EKSSKITSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVaHSAAEVHFVV 132
Cdd:cd04021  15 SNSKSFKPDPYVEVTVDGQPPKKTEVSKKTSNPKWNEHFTVLV-TPQSTLEFKV 67
PLDc_unchar1_1 cd09127
Putative catalytic domain, repeat 1, of uncharacterized phospholipase D-like proteins; ...
707-737 2.87e-03

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


Pssm-ID: 197225 [Multi-domain]  Cd Length: 141  Bit Score: 38.78  E-value: 2.87e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 15234335 707 YVHSKGMVVDDEFVLIGSANINQRSLEGTRD 737
Cdd:cd09127  90 YTHAKYIVVDDERALVLTENFKPSGFTGTRG 120
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
87-142 6.20e-03

C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have type-II topology.


Pssm-ID: 176028 [Multi-domain]  Cd Length: 123  Bit Score: 37.67  E-value: 6.20e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15234335  87 DPYVTVSISGAVIGRTFVISNSENPVWMQHFDVpvahsaaevhfVVKDSDIIGSQI 142
Cdd:cd08382  22 DPFAVITVDGGQTHSTDVAKKTLDPKWNEHFDL-----------TVGPSSIITIQV 66
C2B_Munc13 cd04027
C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are ...
85-136 8.00e-03

C2 domain second repeat in Munc13 (mammalian uncoordinated) proteins; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 175993 [Multi-domain]  Cd Length: 127  Bit Score: 37.55  E-value: 8.00e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15234335  85 TSDPYVTVSIsGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSD 136
Cdd:cd04027  21 TSDPYVTVQV-GKTKKRTKTIPQNLNPVWNEKFHFECHNSSDRIKVRVWDED 71
C2B_Synaptotagmin cd00276
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ...
48-151 8.74e-03

C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 175975 [Multi-domain]  Cd Length: 134  Bit Score: 37.18  E-value: 8.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234335  48 VKEAKHLPNMDGfhnrlggmlsglgrkkvegekssKITSDPYVTVSI--SGAVIG--RTFVISNSENPVWMQH--FDVPV 121
Cdd:cd00276  20 VLKARNLPPSDG-----------------------KGLSDPYVKVSLlqGGKKLKkkKTSVKKGTLNPVFNEAfsFDVPA 76
                        90       100       110
                ....*....|....*....|....*....|..
gi 15234335 122 AH-SAAEVHFVVKDSDIIGS-QIMGAVGIPTE 151
Cdd:cd00276  77 EQlEEVSLVITVVDKDSVGRnEVIGQVVLGPD 108
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH