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Conserved domains on  [gi|45504116|dbj|BAD12566|]
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CRUMPLED LEAF [Arabidopsis thaliana]

Protein Classification

chromophore lyase CpcT/CpeT( domain architecture ID 10533215)

chromophore lyase CpcT/CpeT covalently attaches a chromophore to Cys residue(s) of phycobiliproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CpeT pfam06206
CpeT/CpcT family (DUF1001); This family consists of proteins of proteins belonging to the CpeT ...
 52-235 1.12e-53

CpeT/CpcT family (DUF1001); This family consists of proteins of proteins belonging to the CpeT/CpcT family. These proteins are around 200 amino acids in length. The proteins contain a conserved motif PYR in the amino terminal half of the protein that may be functionally important. The species distribution of the family is interesting. So far it is restricted to cyanobacteria, cryptomonads and plants. It has been shown that CpcT encodes a bilin lyase responsible for attachment of phycocyanobilin to the beta subunit of phycocyanin.


:

Pssm-ID: 428824  Cd Length: 179  Bit Score: 172.00  E-value: 1.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116    52 VSRSLTGEKFTREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPKElkcDVEVSSYA 131
Cdd:pfam06206   2 LARWLAGDFSNQEQAIANPPWFAHIRVWTRPLPVELFDGIGLYSEQAYDYDLDQPYRQRVLRLLPSPDG---SIEIENYK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116   132 IRDAEEYKNFCDRP-KDQRPLPEEVIGDIGehlttihlncCDRGKRC---LYEGSTSPG-GFPNSWNG-ASYCTSDLAVL 205
Cdd:pfam06206  79 LKDPERFAGAGRDPeLLRTLTPDDLELLPG----------CTMIVKRtgnGFRGSTEPGkGCPVNRNGkATYLTSEFELT 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 45504116   206 KnNEIHLWDRGFD-ENRNQVWGPKEGPYEFK 235
Cdd:pfam06206 149 E-DELISWDRGFDpETGEQVWGSKAGPYRFR 178
 
Name Accession Description Interval E-value
CpeT pfam06206
CpeT/CpcT family (DUF1001); This family consists of proteins of proteins belonging to the CpeT ...
 52-235 1.12e-53

CpeT/CpcT family (DUF1001); This family consists of proteins of proteins belonging to the CpeT/CpcT family. These proteins are around 200 amino acids in length. The proteins contain a conserved motif PYR in the amino terminal half of the protein that may be functionally important. The species distribution of the family is interesting. So far it is restricted to cyanobacteria, cryptomonads and plants. It has been shown that CpcT encodes a bilin lyase responsible for attachment of phycocyanobilin to the beta subunit of phycocyanin.


Pssm-ID: 428824  Cd Length: 179  Bit Score: 172.00  E-value: 1.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116    52 VSRSLTGEKFTREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPKElkcDVEVSSYA 131
Cdd:pfam06206   2 LARWLAGDFSNQEQAIANPPWFAHIRVWTRPLPVELFDGIGLYSEQAYDYDLDQPYRQRVLRLLPSPDG---SIEIENYK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116   132 IRDAEEYKNFCDRP-KDQRPLPEEVIGDIGehlttihlncCDRGKRC---LYEGSTSPG-GFPNSWNG-ASYCTSDLAVL 205
Cdd:pfam06206  79 LKDPERFAGAGRDPeLLRTLTPDDLELLPG----------CTMIVKRtgnGFRGSTEPGkGCPVNRNGkATYLTSEFELT 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 45504116   206 KnNEIHLWDRGFD-ENRNQVWGPKEGPYEFK 235
Cdd:pfam06206 149 E-DELISWDRGFDpETGEQVWGSKAGPYRFR 178
CpcT cd16338
T-type phycobiliprotein (PBP) lyase; This family contains the T-type phycobiliprotein (PBP) ...
 52-237 4.70e-49

T-type phycobiliprotein (PBP) lyase; This family contains the T-type phycobiliprotein (PBP) lyase (includes CpcT/CpeT, also known as CpcT bilin lyase). 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 T-type lyase is distantly related to CpcS and is responsible for covalent attachment of phycocyanobilin (PCB) or phycoerythrobilin to a specific cysteine residue in the beta-subunit of phycocyanin (CpcB) and the beta-subunit of phycoerythrocyanin (PecB), and with a different stereochemistry than CpcS. In CpcT (All5339) from Nostoc (Anabaena) sp. PCC7120, sequential binding studies indicate that beta-subunit chromophorylation with PCB at a specific C- terminal cysteine residue in cyanobacterial phycocyanin and phycoerythrocyanin is hindered by a preceding chromophorylation at a specific N-terminal cysteine residue by CpcS. T-type PBP lyases adopt a beta-barrel structure with a modified lipocalin fold, similar to S-type PBP lyases.


Pssm-ID: 319976  Cd Length: 180  Bit Score: 160.17  E-value: 4.70e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116  52 VSRSLTGEkF-TREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPkelKCDVEVSSY 130
Cdd:cd16338   3 LAQWLAGE-FsNQEQAAADPPWFAHIRLWTRPLPVEALGGYWLYVEQAYAGDPDKPYRQRVLRLTPDP---DGAIRLENY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116 131 AIRDAEEYKNFCDRPKDQRPLPEEVIgdigehlttIHLNCCD----RGKRCLYEGSTSPGGFP-NSWNGASYCTSDLAVL 205
Cdd:cd16338  79 TLKDPERFAGAWRDPERLATLTPDDL---------ELLPGCDlilrRQGKGRFRGSTPPGGCRfNVKGGATYLTSTFELS 149

                       170       180       190
                ....*....|....*....|....*....|..
gi 45504116 206 KnNEIHLWDRGFDENRNQVWGPKEGPYEFKPA 237
Cdd:cd16338 150 K-DEFWSWDRGFDATGEQVWGAEAGPYEFRRV 180
CpeT COG5691
Phycocyanobilin lyase CpeT/CpcT [Energy production and conversion];
54-234 1.29e-12

Phycocyanobilin lyase CpeT/CpcT [Energy production and conversion];


Pssm-ID: 444405  Cd Length: 195  Bit Score: 64.86  E-value: 1.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116  54 RSLTGEKFTREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPKELkcdvEVSSYAIR 133
Cdd:COG5691  12 RWMAGDFSNQEQAFANPPWYAHIRVCMRPLPLEFFDGIGLYSEQAYDYDLDQPYRQRVLRLVDVGDHI----EIENYMLK 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116 134 DAEEYKN-FCDRpkdqrplpeevigDIGEHLTTIHLNC---CD---------------RGKRCL--YEGSTSpggfpnsw 192
Cdd:COG5691  88 DEELFYGaGRNP-------------EILKTLTPDQLEKlpgCTmivewtgnsfkgsvePGKGCLvtRNGKTT-------- 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 45504116 193 ngasYCTSDLaVLKNNEIHLWDRGFD-ENRNQVWGPKEGPYEF 234
Cdd:COG5691 147 ----YLDSEF-EITENTFISLDRGRDpETDEQVWGSLAGPFHF 184
 
Name Accession Description Interval E-value
CpeT pfam06206
CpeT/CpcT family (DUF1001); This family consists of proteins of proteins belonging to the CpeT ...
 52-235 1.12e-53

CpeT/CpcT family (DUF1001); This family consists of proteins of proteins belonging to the CpeT/CpcT family. These proteins are around 200 amino acids in length. The proteins contain a conserved motif PYR in the amino terminal half of the protein that may be functionally important. The species distribution of the family is interesting. So far it is restricted to cyanobacteria, cryptomonads and plants. It has been shown that CpcT encodes a bilin lyase responsible for attachment of phycocyanobilin to the beta subunit of phycocyanin.


Pssm-ID: 428824  Cd Length: 179  Bit Score: 172.00  E-value: 1.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116    52 VSRSLTGEKFTREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPKElkcDVEVSSYA 131
Cdd:pfam06206   2 LARWLAGDFSNQEQAIANPPWFAHIRVWTRPLPVELFDGIGLYSEQAYDYDLDQPYRQRVLRLLPSPDG---SIEIENYK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116   132 IRDAEEYKNFCDRP-KDQRPLPEEVIGDIGehlttihlncCDRGKRC---LYEGSTSPG-GFPNSWNG-ASYCTSDLAVL 205
Cdd:pfam06206  79 LKDPERFAGAGRDPeLLRTLTPDDLELLPG----------CTMIVKRtgnGFRGSTEPGkGCPVNRNGkATYLTSEFELT 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 45504116   206 KnNEIHLWDRGFD-ENRNQVWGPKEGPYEFK 235
Cdd:pfam06206 149 E-DELISWDRGFDpETGEQVWGSKAGPYRFR 178
CpcT cd16338
T-type phycobiliprotein (PBP) lyase; This family contains the T-type phycobiliprotein (PBP) ...
 52-237 4.70e-49

T-type phycobiliprotein (PBP) lyase; This family contains the T-type phycobiliprotein (PBP) lyase (includes CpcT/CpeT, also known as CpcT bilin lyase). 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 T-type lyase is distantly related to CpcS and is responsible for covalent attachment of phycocyanobilin (PCB) or phycoerythrobilin to a specific cysteine residue in the beta-subunit of phycocyanin (CpcB) and the beta-subunit of phycoerythrocyanin (PecB), and with a different stereochemistry than CpcS. In CpcT (All5339) from Nostoc (Anabaena) sp. PCC7120, sequential binding studies indicate that beta-subunit chromophorylation with PCB at a specific C- terminal cysteine residue in cyanobacterial phycocyanin and phycoerythrocyanin is hindered by a preceding chromophorylation at a specific N-terminal cysteine residue by CpcS. T-type PBP lyases adopt a beta-barrel structure with a modified lipocalin fold, similar to S-type PBP lyases.


Pssm-ID: 319976  Cd Length: 180  Bit Score: 160.17  E-value: 4.70e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116  52 VSRSLTGEkF-TREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPkelKCDVEVSSY 130
Cdd:cd16338   3 LAQWLAGE-FsNQEQAAADPPWFAHIRLWTRPLPVEALGGYWLYVEQAYAGDPDKPYRQRVLRLTPDP---DGAIRLENY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116 131 AIRDAEEYKNFCDRPKDQRPLPEEVIgdigehlttIHLNCCD----RGKRCLYEGSTSPGGFP-NSWNGASYCTSDLAVL 205
Cdd:cd16338  79 TLKDPERFAGAWRDPERLATLTPDDL---------ELLPGCDlilrRQGKGRFRGSTPPGGCRfNVKGGATYLTSTFELS 149

                       170       180       190
                ....*....|....*....|....*....|..
gi 45504116 206 KnNEIHLWDRGFDENRNQVWGPKEGPYEFKPA 237
Cdd:cd16338 150 K-DEFWSWDRGFDATGEQVWGAEAGPYEFRRV 180
CpeT COG5691
Phycocyanobilin lyase CpeT/CpcT [Energy production and conversion];
54-234 1.29e-12

Phycocyanobilin lyase CpeT/CpcT [Energy production and conversion];


Pssm-ID: 444405  Cd Length: 195  Bit Score: 64.86  E-value: 1.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116  54 RSLTGEKFTREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPKELkcdvEVSSYAIR 133
Cdd:COG5691  12 RWMAGDFSNQEQAFANPPWYAHIRVCMRPLPLEFFDGIGLYSEQAYDYDLDQPYRQRVLRLVDVGDHI----EIENYMLK 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45504116 134 DAEEYKN-FCDRpkdqrplpeevigDIGEHLTTIHLNC---CD---------------RGKRCL--YEGSTSpggfpnsw 192
Cdd:COG5691  88 DEELFYGaGRNP-------------EILKTLTPDQLEKlpgCTmivewtgnsfkgsvePGKGCLvtRNGKTT-------- 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 45504116 193 ngasYCTSDLaVLKNNEIHLWDRGFD-ENRNQVWGPKEGPYEF 234
Cdd:COG5691 147 ----YLDSEF-EITENTFISLDRGRDpETDEQVWGSLAGPFHF 184
 
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.
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