3HSI


Conserved Protein Domain Family
PLDc_CDP-OH_P_transf_II_1
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cd09102: PLDc_CDP-OH_P_transf_II_1 
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Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members
Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily.
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Statistics
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PSSM-Id: 197201
Aligned: 3 rows
Threshold Bit Score: 260.215
Created: 2-Feb-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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putative activecatalytic sitedomain
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:putative active site [active site]
Evidence:
  • Comment:The active site is located at the interface of two catalytic domains; each domain contains one HKD motif.
  • Comment:The HKD signature motif (expanded to H-x-K-x(4)-D-x(6)-G-S-x-N, where x represents any amino acid residue) characterizes the PLD superfamily.
  • Comment:Most residues in the HKD motif are part of the active site.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                                                                                        
3HSI_A        28 QIEFLGSSAEFKTQIIELIRNAKKRIYVTALYWQkdeaGQEILDEIYRVKQen------pHLDVKVLIDWHRAQRNllga 101 Haemophilus inf...
Q32NB8        96 HVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGtgplEQELVDCLESTLEkslqakfpsNLKVSILLDFTRGSRGrkns 175 human
XP_002181856  65 HPRWLRTPSEFHQTLCDRIERARRRVHLASLYIGpa-cCHASIPESTSVSCw-------iNTERSVPCRCLRNGHPhrss 136 Phaeodactylum t...

Feature 1                                                                     # #           # #  
3HSI_A       102 e------------------ksatnADWYCEQRQtyql---pddPNXFFGVPINTREVFGVLHVKGFVFDDTVLYSGASIN 160 Haemophilus inf...
Q32NB8       176 rt-----------------mllplLRRFPEQVRvslfhtphlrGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLS 238 human
XP_002181856 137 atissaeacrralaqrpklpdeshNGTADTEHNksqihllsvlGPWLSRLPNPYNEIAGVFHVKLYVVDDAVLLSGANLS 216 Phaeodactylum t...

Feature 1                    #                       
3HSI_A       161 NVYLhqfekYRYDRYQKITH--AELADSXVNFINDY 194 Haemophilus influenzae
Q32NB8       239 DSYFt----NRQDRYVFLQDc-AEIADFFTELVDAV 269 human
XP_002181856 217 QEYFa----DRHDRYVCIYNggNGLVDTYVDLIQAL 248 Phaeodactylum tricornutum CCAP 1055/1

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