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Conserved domains on  [gi|447016301|ref|WP_001093557|]
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MULTISPECIES: DM13 domain-containing protein [Staphylococcus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DM13 super family cl02735
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ...
 64-145 1.72e-10

Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme.


The actual alignment was detected with superfamily member pfam10517:

Pssm-ID: 470661  Cd Length: 105  Bit Score: 54.56  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447016301   64 VEGKAEIKNGK-LMLTNYK-SSKGPDLYVYLTKNGDIKNGKEIAMVDYD----------KEKQTFDLK---NVDLSKYDE 128
Cdd:pfam10517   9 TSGTVYIVDDRtLELEGFAtDGPGPDLYVWLGDSPVPSGKDGFKVPDEDgvtlgplkgySGEQRYTLTlpaGVDLADYKS 88

                          90
                  ....*....|....*..
gi 447016301  129 VTIYCKKAHVIFGGAKL 145
Cdd:pfam10517  89 VSIWCERFNVNFGAAPL 105
 
Name Accession Description Interval E-value
DM13 pfam10517
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ...
 64-145 1.72e-10

Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme.


Pssm-ID: 463130  Cd Length: 105  Bit Score: 54.56  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447016301   64 VEGKAEIKNGK-LMLTNYK-SSKGPDLYVYLTKNGDIKNGKEIAMVDYD----------KEKQTFDLK---NVDLSKYDE 128
Cdd:pfam10517   9 TSGTVYIVDDRtLELEGFAtDGPGPDLYVWLGDSPVPSGKDGFKVPDEDgvtlgplkgySGEQRYTLTlpaGVDLADYKS 88

                          90
                  ....*....|....*..
gi 447016301  129 VTIYCKKAHVIFGGAKL 145
Cdd:pfam10517  89 VSIWCERFNVNFGAAPL 105
 
Name Accession Description Interval E-value
DM13 pfam10517
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ...
 64-145 1.72e-10

Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme.


Pssm-ID: 463130  Cd Length: 105  Bit Score: 54.56  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447016301   64 VEGKAEIKNGK-LMLTNYK-SSKGPDLYVYLTKNGDIKNGKEIAMVDYD----------KEKQTFDLK---NVDLSKYDE 128
Cdd:pfam10517   9 TSGTVYIVDDRtLELEGFAtDGPGPDLYVWLGDSPVPSGKDGFKVPDEDgvtlgplkgySGEQRYTLTlpaGVDLADYKS 88

                          90
                  ....*....|....*..
gi 447016301  129 VTIYCKKAHVIFGGAKL 145
Cdd:pfam10517  89 VSIWCERFNVNFGAAPL 105
 
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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