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Conserved domains on  [gi|686422277|ref|WP_031917486|]
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Dyp-type peroxidase, partial [Staphylococcus aureus]

Protein Classification

Dyp-type peroxidase( domain architecture ID 3967)

Dyp-type peroxidase similar to Escherichia coli dye-decolorizing peroxidase YfeX that catalyzes the oxidation of both protoporphyrinogen IX and coproporphyrinogen III to their corresponding porphyrins; has both general peroxidase and dye-decolorizing activities

EC:  1.11.1.-
Gene Ontology:  GO:0020037|GO:0004601
SCOP:  4003595

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dyp_perox_fam super family cl01067
Dyp-type peroxidase family; A defined member of this superfamily is Dyp, a dye-decolorizing ...
1-151 1.09e-83

Dyp-type peroxidase family; A defined member of this superfamily is Dyp, a dye-decolorizing peroxidase that lacks a typical heme-binding region. A distinct, uncharacterized branch (TIGR01412) of this superfamily has a typical twin-arginine dependent signal sequence characteristic of exported proteins with bound redox cofactors.


The actual alignment was detected with superfamily member TIGR01412:

Pssm-ID: 470055 [Multi-domain]  Cd Length: 414  Bit Score: 251.63  E-value: 1.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277    1 YCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGKEFDEIDLkAKDSHGEyIIDKDAHTRLAKEA---NTSILRR 77
Cdd:TIGR01412 264 YQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDL-AKDPEGE-VIPKDAHVRLAKPDqngGAAMLRR 341
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686422277   78 AFNYVDGTDDrTGNFETGLLFIAFQK-ATQQFIDIQNNLgSNDKLNEYITHRGSASFLVLPGVSKGGYLGETLFD 151
Cdd:TIGR01412 342 AFSYTDGTDA-TGQLDAGLLFVCYQAdPLKGFIPVQRNL-AGDALNEYIQHIGSGLFAVPPGVKKGEYLGQRLLE 414
 
Name Accession Description Interval E-value
tat_substr_1 TIGR01412
Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat ...
1-151 1.09e-83

Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat (twin-arginine translocation) signal sequence, suggesting that the family is exported in a folded state, perhaps with a bound redox cofactor. Members of this family show homology to Dyp, a dye-decolorizing peroxidase from Geotrichum candidum that lacks any typical heme-binding site.


Pssm-ID: 273606 [Multi-domain]  Cd Length: 414  Bit Score: 251.63  E-value: 1.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277    1 YCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGKEFDEIDLkAKDSHGEyIIDKDAHTRLAKEA---NTSILRR 77
Cdd:TIGR01412 264 YQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDL-AKDPEGE-VIPKDAHVRLAKPDqngGAAMLRR 341
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686422277   78 AFNYVDGTDDrTGNFETGLLFIAFQK-ATQQFIDIQNNLgSNDKLNEYITHRGSASFLVLPGVSKGGYLGETLFD 151
Cdd:TIGR01412 342 AFSYTDGTDA-TGQLDAGLLFVCYQAdPLKGFIPVQRNL-AGDALNEYIQHIGSGLFAVPPGVKKGEYLGQRLLE 414
EfeB COG2837
Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];
1-147 6.51e-48

Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];


Pssm-ID: 442085  Cd Length: 334  Bit Score: 157.36  E-value: 6.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277   1 YCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGKEFDEIDLKAkdshGEYIIDKDAHTRLA--KEANTS--ILR 76
Cdd:COG2837  187 YVVVRRIRHDLEAWDRLSLEEQEKVIGRTKDDGAPLDGGPEFDDPDFAA----DAGVIPADSHVRRAnpRDDGNElrILR 262
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686422277  77 RAFNYVDGTDDrTGNFETGLLFIAFQK-ATQQFIDIQNNLGSN-----DKLNEYITHRGSASFLVLPgvskGGYLGE 147
Cdd:COG2837  263 RGMPYGDGLDP-AGELDAGLLFIAYQAdPARQFEMLQRMLGGDpdgnyDRLLDFTTPVGGAYFFVPS----GDFLGQ 334
Dyp_perox pfam04261
Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical ...
1-141 2.40e-43

Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical heme-binding region.


Pssm-ID: 461241  Cd Length: 315  Bit Score: 145.22  E-value: 2.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277    1 YCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGkefdeidlkakdshgeYIIDKDAHTRLAKEA----NTSILR 76
Cdd:pfam04261 187 YVVVQRIRHNLEAWDRLSLKEQEDVIGRRKESGAELGGD----------------KVKPADSHVRLANPKengkGLKILR 250
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277   77 RAFNYVDgtddrTGNFETGLLFIAFQKAT-QQFIDIQNNL----GSNDKLNEYITHRGSASFLVLPGVSK 141
Cdd:pfam04261 251 RSLPYGD-----VGQGDHGLLFIAYQRTLhNGEQMLQNMLggtdGKTDALLEFITAVTGGYFFAPSGVKL 315
 
Name Accession Description Interval E-value
tat_substr_1 TIGR01412
Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat ...
1-151 1.09e-83

Tat-translocated enzyme; This model represents a small family of proteins with a typical Tat (twin-arginine translocation) signal sequence, suggesting that the family is exported in a folded state, perhaps with a bound redox cofactor. Members of this family show homology to Dyp, a dye-decolorizing peroxidase from Geotrichum candidum that lacks any typical heme-binding site.


Pssm-ID: 273606 [Multi-domain]  Cd Length: 414  Bit Score: 251.63  E-value: 1.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277    1 YCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGKEFDEIDLkAKDSHGEyIIDKDAHTRLAKEA---NTSILRR 77
Cdd:TIGR01412 264 YQVVRRIRMHLETWDRTSLKEQEDVFGRRKSSGAPLGGAKESDEPDL-AKDPEGE-VIPKDAHVRLAKPDqngGAAMLRR 341
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 686422277   78 AFNYVDGTDDrTGNFETGLLFIAFQK-ATQQFIDIQNNLgSNDKLNEYITHRGSASFLVLPGVSKGGYLGETLFD 151
Cdd:TIGR01412 342 AFSYTDGTDA-TGQLDAGLLFVCYQAdPLKGFIPVQRNL-AGDALNEYIQHIGSGLFAVPPGVKKGEYLGQRLLE 414
EfeB COG2837
Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];
1-147 6.51e-48

Periplasmic deferrochelatase/peroxidase EfeB [Inorganic ion transport and metabolism];


Pssm-ID: 442085  Cd Length: 334  Bit Score: 157.36  E-value: 6.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277   1 YCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGKEFDEIDLKAkdshGEYIIDKDAHTRLA--KEANTS--ILR 76
Cdd:COG2837  187 YVVVRRIRHDLEAWDRLSLEEQEKVIGRTKDDGAPLDGGPEFDDPDFAA----DAGVIPADSHVRRAnpRDDGNElrILR 262
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 686422277  77 RAFNYVDGTDDrTGNFETGLLFIAFQK-ATQQFIDIQNNLGSN-----DKLNEYITHRGSASFLVLPgvskGGYLGE 147
Cdd:COG2837  263 RGMPYGDGLDP-AGELDAGLLFIAYQAdPARQFEMLQRMLGGDpdgnyDRLLDFTTPVGGAYFFVPS----GDFLGQ 334
Dyp_perox pfam04261
Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical ...
1-141 2.40e-43

Dyp-type peroxidase family; This family of dye-decolourising peroxidases lack a typical heme-binding region.


Pssm-ID: 461241  Cd Length: 315  Bit Score: 145.22  E-value: 2.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277    1 YCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLTGGkefdeidlkakdshgeYIIDKDAHTRLAKEA----NTSILR 76
Cdd:pfam04261 187 YVVVQRIRHNLEAWDRLSLKEQEDVIGRRKESGAELGGD----------------KVKPADSHVRLANPKengkGLKILR 250
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277   77 RAFNYVDgtddrTGNFETGLLFIAFQKAT-QQFIDIQNNL----GSNDKLNEYITHRGSASFLVLPGVSK 141
Cdd:pfam04261 251 RSLPYGD-----VGQGDHGLLFIAYQRTLhNGEQMLQNMLggtdGKTDALLEFITAVTGGYFFAPSGVKL 315
Dyp_perox_fam TIGR01413
Dyp-type peroxidase family; A defined member of this superfamily is Dyp, a dye-decolorizing ...
1-141 4.29e-39

Dyp-type peroxidase family; A defined member of this superfamily is Dyp, a dye-decolorizing peroxidase that lacks a typical heme-binding region. A distinct, uncharacterized branch (TIGR01412) of this superfamily has a typical twin-arginine dependent signal sequence characteristic of exported proteins with bound redox cofactors.


Pssm-ID: 273607  Cd Length: 308  Bit Score: 134.02  E-value: 4.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277    1 YCVVRRIQIHIETWDRTALEEQEATFGRKRHSGAPLtGGKEfdeidlkakdshgeyIIDKDAHTRLAK----EANTSILR 76
Cdd:TIGR01413 177 YVVVQRIQHDLEEWDRLPLAEQEDVIGRRKSSGAEL-DGKE---------------RAPADSHVRLTNpredGKGLKILR 240
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686422277   77 RAFNYVDGTDDRTGnfETGLLFIAFQKATQ-QFIDIQNNLGSN----DKLNEYITHRGSASFLVLPGVSK 141
Cdd:TIGR01413 241 RGLPYGDGSDDTGQ--DAGLLFIAYQRSLEnGEVQLQRMLGGTdgatDRLLEFIRPVGGGYFFAPSGVAL 308
 
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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