Conserved Protein Domain Family
C2_fungal_Pkc1p

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cd08689: C2_fungal_Pkc1p 
C2 domain found in protein kinase C (Pkc1p) in Saccharomyces cerevisiae
This family is named after the protein kinase C in Saccharomyces cerevisiae, Pkc1p. Protein kinase C is a member of a family of Ser/Thr phosphotransferases that are involved in many cellular signaling pathways. PKC has two antiparallel coiled-coiled regions (ACC finger domain) (AKA PKC homology region 1 (HR1)/ Rho binding domain) upstream of the C2 domain and two C1 domains downstream. 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, like those of PKC, 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.
Statistics
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PSSM-Id: 176071
View PSSM: cd08689
Aligned: 11 rows
Threshold Bit Score: 162.157
Threshold Setting Gi: 164658497
Created: 24-Mar-2010
Updated: 2-Oct-2020
Structure
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Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
EDZ73950      211 LTIGITAARDVDHiqspm--farkPESYVTIKIddtiKARTKPSRNDRW-SEDFQIPvek--gnEIEITVYDKVNDSLIP 285  Saccharomyces...
EDK40285      190 LTVVVTCVRDIDHiaspm--fskrSESYVTIKVddveSARTRPSRSGKW-NEEFRIDvdk--gnEVEFAVYDKAGSQAVP 264  Pichia guilli...
XP_001211256  245 LTLRIHAVRDVDHaagsr--fsrgPETYVVLKVedavKARTKATRNDRWqDETFNIDidk--anELELTVYDKSGDRPTP 320  Aspergillus t...
P43057        208 LTVSITCIRDVDHiata---lakkRETVVVIKVddleKARTKPSKNDNW-NEEMVIDvdk--shEIELAVMDKQNGIYVP 281  Candida albicans
AAP20604      201 LSITINSIRDILHvssi---fskkLETLVSIRLmtveKARTKPTKNQRV-NDSFQIHvek--gnELSLIVYDKVGDTLTP 274  Pichia pastoris
XP_505220     192 VTITVHALRNVEHiasv---rgkrPETMVTVKCedklVGRTKLSRTERW-NDTFQFPvdk--anEVEIIIYDRDGDHFKP 265  Yarrowia lipo...
XP_002616649  199 ITINVVCIRDIDHiaspm--shkrAESFVSFKIddveKARTSDSRTGKF-NEDFVIEvdk--ahEMEIAVYDKSNNQRIP 273  Clavispora lu...
BAA03268      213 LKITVGSLRNVTHsagi----skqTEMIVAIRAedleRARTRPSRTDRF-NETFEIDlek-tneVEIVVYEKKNEKLLLP 286  fission yeast
AAQ84896      250 LVISLRSARDLNHralprrssktySETTVVIKVegneRAVSHPSRNDKW-HEDFHIPvek-aneVEITIYDTVAPGDSAP 327  Cryptococcus ...
XP_002468782  235 LQVTLKGARELEHapryrfssakqCETYVSFKVegteRDRSHPSKTDRW-MEDFEITiekanevEITVYDKQVGESYPIP 313  Postia placen...
XP_001730374  199 LSIAIKGAKEVDHaaiss-strsmRESYVSIKVeeseRVRTPASRSDAW-NVSYELPlen-tneVELVIFDRVGTSAPVP 275  Malassezia gl...
EDZ73950      286 VAIMWLLLSDIAEEIRKKKagqtneqQGWVNASN 319  Saccharomyces cerevisiae AWRI1631
EDK40285      265 VAFAWALLSDITEELRKRKvem--gsAGWVSGND 296  Pichia guilliermondii ATCC 6260
XP_001211256  321 IGMLWVRISDIAEEMRRKKietelnaSGWVSADK 354  Aspergillus terreus NIH2624
P43057        282 VAVNWFSLFDLAEEIRKKKvakdqgsSGWLPAAN 315  Candida albicans
AAP20604      275 VAMIWFLLSDIVEEIRKKKvdrelnaTGWMSASN 308  Pichia pastoris
XP_505220     266 VGLLWLTISDVAEEIRRRKngqklaaTGWVAASE 299  Yarrowia lipolytica CLIB122
XP_002616649  274 VALTWILLSDIAEEIRKKKvaneqvtEGWMPASS 307  Clavispora lusitaniae ATCC 42720
BAA03268      287 VGLLWIRLSDLVEKQRRKKveqevsdKGWVSADK 320  fission yeast
AAQ84896      328 IGMLWLRVSDLVEALRRQKvgiegqgAGWVTAAT 361  Cryptococcus neoformans var. neoformans
XP_002468782  314 IGLLWIKISDLVDAQRKQKvlmesgqGGWVTAGA 347  Postia placenta Mad-698-R
XP_001730374  276 VGLLWLRISDIIEQLRKIKagq-vgaDGLPSASP 308  Malassezia globosa CBS 7966
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