NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2184920545|ref|WP_236473614|]
View 

MULTISPECIES: hypothetical protein [Mesorhizobium]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SufI super family cl43615
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1-85 3.88e-09

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


The actual alignment was detected with superfamily member COG2132:

Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 51.86  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184920545   1 MLGPAMRTDLILDMTGKPGSRLSIFDQFYEGLEYELVDLVYSDTPLRARVPDWPLTLPTIPLPEPDldtaSRNEVVFTGG 80
Cdd:COG2132   237 LLAPGERADVLVDFSADPGEEVTLANPFEGRSGRALLTLRVTGAAASAPLPANLAPLPDLEDREAV----RTRELVLTGG 312


                  ....*
gi 2184920545  81 MMGEM 85
Cdd:COG2132   313 MAGYV 317
 
Name Accession Description Interval E-value
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1-85 3.88e-09

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 51.86  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184920545   1 MLGPAMRTDLILDMTGKPGSRLSIFDQFYEGLEYELVDLVYSDTPLRARVPDWPLTLPTIPLPEPDldtaSRNEVVFTGG 80
Cdd:COG2132   237 LLAPGERADVLVDFSADPGEEVTLANPFEGRSGRALLTLRVTGAAASAPLPANLAPLPDLEDREAV----RTRELVLTGG 312


                  ....*
gi 2184920545  81 MMGEM 85
Cdd:COG2132   313 MAGYV 317
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 2-29 1.65e-06

The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida. CumA is involved in the oxidation of Mn(II) in Pseudomonas putida; however, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCOs catalyze the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. The MCOs in this subfamily are composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259952 [Multi-domain]  Cd Length: 132  Bit Score: 43.09  E-value: 1.65e-06
                          10        20
                  ....*....|....*....|....*...
gi 2184920545   2 LGPAMRTDLILDMTGKPGSRLSIFDQFY 29
Cdd:cd13885   100 LAPGMRIDLVIDAPQAAGTRFAVLDHDG 127
 
Name Accession Description Interval E-value
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1-85 3.88e-09

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 51.86  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184920545   1 MLGPAMRTDLILDMTGKPGSRLSIFDQFYEGLEYELVDLVYSDTPLRARVPDWPLTLPTIPLPEPDldtaSRNEVVFTGG 80
Cdd:COG2132   237 LLAPGERADVLVDFSADPGEEVTLANPFEGRSGRALLTLRVTGAAASAPLPANLAPLPDLEDREAV----RTRELVLTGG 312


                  ....*
gi 2184920545  81 MMGEM 85
Cdd:COG2132   313 MAGYV 317
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 2-29 1.65e-06

The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida. CumA is involved in the oxidation of Mn(II) in Pseudomonas putida; however, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCOs catalyze the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. The MCOs in this subfamily are composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259952 [Multi-domain]  Cd Length: 132  Bit Score: 43.09  E-value: 1.65e-06
                          10        20
                  ....*....|....*....|....*...
gi 2184920545   2 LGPAMRTDLILDMTGKPGSRLSIFDQFY 29
Cdd:cd13885   100 LAPGMRIDLVIDAPQAAGTRFAVLDHDG 127
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH