3BDR,4TQ2


Conserved Protein Domain Family
CpcS

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cd16339: CpcS 
Click on image for an interactive view with Cn3D
S-type phycobiliprotein (PBP) lyase
This family contains the S-type phycobiliprotein (PBP) lyase (denoted CpcS/CpcU or CpeS/CpeU). PBP lyases are employed by cyanobacteria, red algae, cryptophytes and glaucophytes for light-harvesting. Pigmentation of light-harvesting phycobiliproteins of cyanobacteria and cryptophytes requires covalent attachment of open-chain tetrapyrrole chromophores, the phycobilins, to the apoproteins. PBP lyases mediate this covalent attachment of phycobilin chromophores to apo-PBPs and also ensure the correct binding of the chromophore with regard to the specific attachment site and stereospecificity. The S-type lyase is distantly related to CpcT and similarly adopts a beta-barrel structure with a modified lipocalin fold. Many members of the CpcS/CpcU family ligate phycocyanobilin (PCB) to a specific cysteine residue in the beta-subunits of phycocyanin (CpcB) or phycoerythrocyanin (PecB) and to a related cysteine residue in the alpha and beta subunits of allophycocyanin (AP); they are typically given the designation of "CpcS" or "CpcU". Other members which attach phycoerythrobilin (PEB) to the beta-subunit of phycoerythrin (PE) are given the designation "CpeS" or "CpeU". In Guillardia theta, a Cryptophyte, which has adopted phycoerythrobilin (PEB) biosynthesis from cyanobacteria, phycobiliprotein lyase has been shown to provide structural requirements for the transfer of this chromophore to the specific cysteine residue of the apophycobiliprotein.
Statistics
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PSSM-Id: 319977
View PSSM: cd16339
Aligned: 107 rows
Threshold Bit Score: 87.7686
Threshold Setting Gi: 500469308
Created: 29-Mar-2013
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
chemical
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:chemical substrate binding site [chemical binding site]
Evidence:
  • Comment:site-directed mutagenesis identified these phycobiliprotein residues as involved in open-chain tetrapyrrole chromophores (phycobilin) binding

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
3BDR_A         9 DFFAQSAGRWFSQRTSHHLa---------fKQTESgkSQLTIELLsvddpavialc--------qqydxdpawavCGARV 71
gi 56686117   24 DYFQRSHGQWHSQRRYYTLk---------sGDVQEviSTIGVTALtqgdgdllela---------alhqldvpllCGACV 85
gi 815937009  19 QFFRDCVGRWHSKRRYHTLk---------sGLTQDviCTMEIEFLeaqssdllhlah-------rhnlrpdqafvAGVRI 82
gi 427992392  29 AFFSESAGKWRSQRRYYTLtsgasgasgtsGQTQEveSFLTVKYLepdsvelaglaq-------khqlaadfqfsCGALV 101
gi 746957834  18 SFFQACEGDWRSKRRYYTLk---------sGDVQEvvSYINIRFLsadaaeletlhq-------lhdlpertpliCGAQV 81
gi 544215259  79 LFFRCQPGRWRSERCYFYRetadv-adrggESVERseTLFQVEPLtaetttkvlrdngtdesklisegfhsleyaAGFKV 157
gi 81769332   18 EFFQESVGEWCSQRRYYTLp---------dGETKEmmSMITIRFLeqgcdelqklaq-------ihklaesvfliCGAEV 81
gi 123506031   9 HFFNCCIGAWHTERTYHYLd---------rGEVERsrTDFTIRTLtpelkekvlad--------nnypnhgvdgfLGFHL 71
gi 553883932   6 AFFDACLGKWSIERTYHYLsd-------peGRVERshTNYDIQELtadrrqkvlad--------nnrpsevtgplYGFFL 70
gi 554673156   6 AFFDACLGKWSIERTYHYLsd-------peGRVERshTNYDIQELtadrrqkvlad--------nnrpsevtgplYGFFL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
3BDR_A        72 SWDGtxew------------------------------dneKHEGSTVLVPixdqg--------srxeGKLLREXGYaek 113
gi 56686117   86 TWHSeyqg-----------------------------pegkTQTGRTVFGVl---------------gDRLYRDSGFatr 121
gi 815937009  83 SWESqyvddvsgspqatpspqsdpsppsvdasaslqkghgkTSGGSSIFGVr---------------gNFLYRDRGFatp 147
gi 427992392 102 TWEShylnv---------------------------aakkkPNLGSTIFGIk---------------gNLMYRDRGFsts 139
gi 746957834  82 TWESnyih-----------------------------tqrkPVNGSTLFGVr---------------gTTLYRDRGFata 117
gi 544215259 158 SFNTrmeh------------------------------sgdVSASTNLLFVpqvldvql-arqlglvrGLYFRDKGYeed 206
gi 81769332   82 TWCStdvl-----------------------------knrsESEGSTLFGAl---------------gNILYRDRGFats 117
gi 123506031  72 AFETvse--------------------------------kgEEAGQELNMLfvprre-----gprgleGDYLRDRAYeed 114
gi 553883932  71 AFDTl------------------------------------SDRGEAVAMDlnilfvpthtsedgiieGDYLRDRAYees 114
gi 554673156  71 AFDTl------------------------------------SDRGEAVAMDlnilfvpthtsedgiieGDYLRDRAYees 114
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
Feature 1                                      #         #                               
3BDR_A       114 apvaGRFSXGs-DGALTLITEYet--iYSEERLWFAspNLRLRTSILKrfg--------gfSXASFCSEIRL 174
gi 56686117  122 npvvAQFQLSn-PDTLTLRSEYgg--sSFEEECRLIgqHYRTRQTIISrag--------eeIMIGQYLEQRL 182
gi 815937009 148 dpvvSGYSLS--DRTLLIATAYdg--sSFSEECKLIgsHYRTRQTIISrnn--------teQVIGQYVETRL 207
gi 427992392 140 rpvtAEFSMRd-ANSLCLKTAYng--cSFEEEIRLVgdLYRTRQTIICrag--------eeQMIGQYLEKRI 200
gi 746957834 118 kpvtADFTFRe-PRTMVLKTAYdg--sSFEEEIKLIgdSTRTRQTIISrag--------eeIMIGQYLEQRC 178
gi 544215259 207 rpivGQFEFHvtTRELVMVTAYar--tVSVDRILLCseRQRLRQIANYrrpeawqrdapldRNRSLLTEVRL 276
gi 81769332  118 kpvtAQYNFPn-PKTLCLRTEYng--sVFEEELKLIgsKYRTRQTIISrag--------eqLMIGQYIEKRI 178
gi 123506031 115 rpivASFRFD--PGSLQLVMTTtytrvVAVDTITLLnpRLRLRQILTYqrpphg-qpleelLLVGFGVEQKL 183
gi 553883932 115 rpmiSHFRYDpeRAELRMITRYtr--vVSVDSITLVnpELRIRQIQNFrrnvlenlplqdlELVGFGVEKKV 184
gi 554673156 115 rpmiSHFRYDpeRAELRMITRYtr--vVSVDSITLVnpELRIRQIQNFrrnvlenlplqdlELVGFGVEKKV 184

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