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Conserved domains on  [gi|577646931|gb|EUI58363|]
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hypothetical protein Q186_02003 [Staphylococcus aureus M1184]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
auto_Ata super family cl41274
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 36-128 2.92e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


The actual alignment was detected with superfamily member NF033481:

Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 37.15  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577646931   36 DIMELNENDDSGGGNMGNYVTrdEFNNSMREFKDEMRAMRTDMNNNMNSLRSELNTNINNLRIETQNSISKLPSNFDVKn 115
Cdd:NF033481  787 NITNLNQKLDDTKTNLGNQIT--DTNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQINDTKTELNNTIGNTKTELNTK- 863

                          90
                  ....*....|....
gi 577646931  116 mlLENNK-ELEREA 128
Cdd:NF033481  864 --IDNTKtELENKG 875
 
Name Accession Description Interval E-value
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 36-128 2.92e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 37.15  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577646931   36 DIMELNENDDSGGGNMGNYVTrdEFNNSMREFKDEMRAMRTDMNNNMNSLRSELNTNINNLRIETQNSISKLPSNFDVKn 115
Cdd:NF033481  787 NITNLNQKLDDTKTNLGNQIT--DTNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQINDTKTELNNTIGNTKTELNTK- 863

                          90
                  ....*....|....
gi 577646931  116 mlLENNK-ELEREA 128
Cdd:NF033481  864 --IDNTKtELENKG 875
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 35-102 3.98e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 36.77  E-value: 3.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577646931   35 DDIMELNENDDSGGGNMGNYVT--RDEFNNSMREFKDEMRAMRTDMNNNMNSLRSELNTNINNLRIETQN 102
Cdd:NF033481  804 NQITDTNKNLNDAKKDLGNQITdtNTKLNTTKDQLTTQINDTKTELNNTIGNTKTELNTKIDNTKTELEN 873
 
Name Accession Description Interval E-value
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 36-128 2.92e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 37.15  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577646931   36 DIMELNENDDSGGGNMGNYVTrdEFNNSMREFKDEMRAMRTDMNNNMNSLRSELNTNINNLRIETQNSISKLPSNFDVKn 115
Cdd:NF033481  787 NITNLNQKLDDTKTNLGNQIT--DTNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQINDTKTELNNTIGNTKTELNTK- 863

                          90
                  ....*....|....
gi 577646931  116 mlLENNK-ELEREA 128
Cdd:NF033481  864 --IDNTKtELENKG 875
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 35-102 3.98e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 36.77  E-value: 3.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577646931   35 DDIMELNENDDSGGGNMGNYVT--RDEFNNSMREFKDEMRAMRTDMNNNMNSLRSELNTNINNLRIETQN 102
Cdd:NF033481  804 NQITDTNKNLNDAKKDLGNQITdtNTKLNTTKDQLTTQINDTKTELNNTIGNTKTELNTKIDNTKTELEN 873
 
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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