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Conserved domains on  [gi|996870413|emb|CXP93886|]
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membrane protein [Staphylococcus aureus]

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 ...
110-209 8.90e-04

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: 39.85  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996870413  110 KQVENQDGQINQQVDNAKENIKN----NQKTDDIIKNLQNQIDNlKQQEQNKADSKLTQFYQDQINKLTEANNALKNNAS 185
Cdd:NF033481  765 RQLKNVDSRVNQNTSNIGKNTQNitnlNQKLDDTKTNLGNQITD-TNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQIN 843
                          90       100       110
                  ....*....|....*....|....*....|
gi 996870413  186 QGKIE------SMLNDINTKFDSIKSKLES 209
Cdd:NF033481  844 DTKTElnntigNTKTELNTKIDNTKTELEN 873
 
Name Accession Description Interval E-value
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
110-209 8.90e-04

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: 39.85  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996870413  110 KQVENQDGQINQQVDNAKENIKN----NQKTDDIIKNLQNQIDNlKQQEQNKADSKLTQFYQDQINKLTEANNALKNNAS 185
Cdd:NF033481  765 RQLKNVDSRVNQNTSNIGKNTQNitnlNQKLDDTKTNLGNQITD-TNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQIN 843
                          90       100       110
                  ....*....|....*....|....*....|
gi 996870413  186 QGKIE------SMLNDINTKFDSIKSKLES 209
Cdd:NF033481  844 DTKTElnntigNTKTELNTKIDNTKTELEN 873
PRK11281 PRK11281
mechanosensitive channel MscK;
141-198 1.99e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 1.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 996870413  141 KNLQNQIDNLKQQEQNKADSKL-------TQFYQDQINKLTEANNALKNNASQ--GKIESMLNDINT 198
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAEDKLvqqdleqTLALLDKIDRQKEETEQLKQQLAQapAKLRQAQAELEA 105
 
Name Accession Description Interval E-value
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
110-209 8.90e-04

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: 39.85  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996870413  110 KQVENQDGQINQQVDNAKENIKN----NQKTDDIIKNLQNQIDNlKQQEQNKADSKLTQFYQDQINKLTEANNALKNNAS 185
Cdd:NF033481  765 RQLKNVDSRVNQNTSNIGKNTQNitnlNQKLDDTKTNLGNQITD-TNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQIN 843
                          90       100       110
                  ....*....|....*....|....*....|
gi 996870413  186 QGKIE------SMLNDINTKFDSIKSKLES 209
Cdd:NF033481  844 DTKTElnntigNTKTELNTKIDNTKTELEN 873
PRK11281 PRK11281
mechanosensitive channel MscK;
141-198 1.99e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 1.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 996870413  141 KNLQNQIDNLKQQEQNKADSKL-------TQFYQDQINKLTEANNALKNNASQ--GKIESMLNDINT 198
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAEDKLvqqdleqTLALLDKIDRQKEETEQLKQQLAQapAKLRQAQAELEA 105
46 PHA02562
endonuclease subunit; Provisional
110-213 4.49e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 37.69  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 996870413 110 KQVENQDGQINQQVDNAKENIKN-NQKTDDIIKNLQNQIDNLKQQEQNkadskltqfYQDQINKLTEAnnALKNNASQGK 188
Cdd:PHA02562 184 QTLDMKIDHIQQQIKTYNKNIEEqRKKNGENIARKQNKYDELVEEAKT---------IKAEIEELTDE--LLNLVMDIED 252
                         90       100
                 ....*....|....*....|....*
gi 996870413 189 IESMLNDINTKFDSIKSKLESLFKD 213
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKV 277
 
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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