3HSI,3HSI


Conserved Protein Domain Family
PLDc

?
pfam00614: PLDc 
Click on image for an interactive view with Cn3D
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.
Statistics
?
PSSM-Id: 279008
View PSSM: pfam00614
Aligned: 30 rows
Threshold Bit Score: 30.4648
Threshold Setting Gi: 32363495
Created: 12-Jul-2016
Updated: 4-Aug-2016
Structure
?
Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                          10        20        30
                  ....*....|....*....|....*....|....*....
3HSI_C        137 VFGVLHVKGFVFDDT------------VLYSGASINNVY 163
gi 62288028   219 MDLRQHRKMIMIDNy-----------iAYTGSMNMVDPR 246
gi 115502456  791 YFWAHHEKFVVIDETf-----------AFIGGTDLCYGR 818
gi 1175378    641 LFWAHHEKLVVVDDAi-----------TFIGGIDLCFGR 668
gi 1176955    141 MQKRNHRKITVIDGKi-----------GYIGGFNIAEEY 168
gi 1176950    237 LNFRNHRKIVIIDGKt-----------GFVGGLNVGKEY 264
gi 26007041   197 YNYRDHRKILVIDNKv-----------AFNGGINLADEY 224
gi 732076     276 LVNRVHSKIVIEDEEl-----------LCVGSFNWFSAT 303
gi 32363495   419 NGWSYHAKGIWLSARdkndannwkpfiTVIGSSNYTRRA 457
3HSI_C        359 GDNTYHLKGVWVDDRy-----------ILLTGNNLNPRA 386
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap