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Conserved domains on  [gi|90111742|ref|NP_418780|]
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DUF2501 domain-containing protein YjjA [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

DUF2501 domain-containing protein( domain architecture ID 10013858)

uncharacterized DUF2501 domain-containing protein similar to Escherichia coli YjjA, which is found in an operon next to DnaC, a protein required for the initiation of chromosome replication

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11667 PRK11667
hypothetical protein; Provisional
 1-163 6.57e-73

hypothetical protein; Provisional


:

Pssm-ID: 236951  Cd Length: 163  Bit Score: 216.09  E-value: 6.57e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111742    1 MMKTVKHLLCCAIAASALISTGVHAASWKDALSSAASELGNQNSTTQEGGWSLASLTNLLSSGNQALSADNMNNAAGILQ 80
Cdd:PRK11667   1 MMKTIKHLLCCAILAAALISTGAHAASLGDSLSSAASQLGGQAGSSQQGGWSLSSLTGLLSGGGQALSAGSMNNAAGILQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111742   81 YCAKQKLASVTDAENIKNQVLEKLGLNSEEQKEDTNYLDGIQGLLKTKDGQQLNLDNIGTTPLAEKVKTKACDLVLKQGL 160
Cdd:PRK11667  81 YCAKNNYLSATGAESVKDQLLGKLGLGSTEQKSDTNYLSGLQGLLKTGDGQQLNLSNIGTTPLKEKVKTKACDLVLKQGK 160


                 ...
gi 90111742  161 NFI 163
Cdd:PRK11667 161 SFL 163
 
Name Accession Description Interval E-value
PRK11667 PRK11667
hypothetical protein; Provisional
 1-163 6.57e-73

hypothetical protein; Provisional


Pssm-ID: 236951  Cd Length: 163  Bit Score: 216.09  E-value: 6.57e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111742    1 MMKTVKHLLCCAIAASALISTGVHAASWKDALSSAASELGNQNSTTQEGGWSLASLTNLLSSGNQALSADNMNNAAGILQ 80
Cdd:PRK11667   1 MMKTIKHLLCCAILAAALISTGAHAASLGDSLSSAASQLGGQAGSSQQGGWSLSSLTGLLSGGGQALSAGSMNNAAGILQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111742   81 YCAKQKLASVTDAENIKNQVLEKLGLNSEEQKEDTNYLDGIQGLLKTKDGQQLNLDNIGTTPLAEKVKTKACDLVLKQGL 160
Cdd:PRK11667  81 YCAKNNYLSATGAESVKDQLLGKLGLGSTEQKSDTNYLSGLQGLLKTGDGQQLNLSNIGTTPLKEKVKTKACDLVLKQGK 160


                 ...
gi 90111742  161 NFI 163
Cdd:PRK11667 161 SFL 163
DUF2501 pfam10696
Protein of unknown function (DUF2501); Members of this family are all Proteobacteria. Several ...
 84-161 3.20e-25

Protein of unknown function (DUF2501); Members of this family are all Proteobacteria. Several are annotated as being YjjA or YjjA-like, but this protein is uncharacterized.


Pssm-ID: 431442  Cd Length: 77  Bit Score: 92.04  E-value: 3.20e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111742    84 KQKLASVTDAENIKNQVLEKLGLNSEEQKEDTNYLDGIQGLLKTKDGQQLNLDNIGTTpLAEKVKTKACDLVLKQGLN 161
Cdd:pfam10696   1 KNNYLSADGASSVKDQLLGKLGLGTQEQQKDSDYQNGLQGLLKTGNGQQFNLSNLGTT-LKEKVKTKACDLVLKQAKS 77
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
 95-137 1.99e-03

serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called PAI3, plasminogen activator inhibitor-3/PLANH3, plasma serine protease inhibitor) has many biological functions. It acts as a pro-coagulant in blood and in the seminal vesicles, it is required for spermatogenesis. It is a member of the clade A serpin family that includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381021 [Multi-domain]  Cd Length: 364  Bit Score: 37.44  E-value: 1.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 90111742  95 NIKNQVLEKLGLNSEEQKED---TNYLDGIQGLLKTKDGQQLNLDN 137
Cdd:cd19553  43 STKAQILEGLGLNPQKGSEEqlhRGFQQLLQELNQPRDGFQLSLGN 88
 
Name Accession Description Interval E-value
PRK11667 PRK11667
hypothetical protein; Provisional
 1-163 6.57e-73

hypothetical protein; Provisional


Pssm-ID: 236951  Cd Length: 163  Bit Score: 216.09  E-value: 6.57e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111742    1 MMKTVKHLLCCAIAASALISTGVHAASWKDALSSAASELGNQNSTTQEGGWSLASLTNLLSSGNQALSADNMNNAAGILQ 80
Cdd:PRK11667   1 MMKTIKHLLCCAILAAALISTGAHAASLGDSLSSAASQLGGQAGSSQQGGWSLSSLTGLLSGGGQALSAGSMNNAAGILQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111742   81 YCAKQKLASVTDAENIKNQVLEKLGLNSEEQKEDTNYLDGIQGLLKTKDGQQLNLDNIGTTPLAEKVKTKACDLVLKQGL 160
Cdd:PRK11667  81 YCAKNNYLSATGAESVKDQLLGKLGLGSTEQKSDTNYLSGLQGLLKTGDGQQLNLSNIGTTPLKEKVKTKACDLVLKQGK 160


                 ...
gi 90111742  161 NFI 163
Cdd:PRK11667 161 SFL 163
DUF2501 pfam10696
Protein of unknown function (DUF2501); Members of this family are all Proteobacteria. Several ...
 84-161 3.20e-25

Protein of unknown function (DUF2501); Members of this family are all Proteobacteria. Several are annotated as being YjjA or YjjA-like, but this protein is uncharacterized.


Pssm-ID: 431442  Cd Length: 77  Bit Score: 92.04  E-value: 3.20e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111742    84 KQKLASVTDAENIKNQVLEKLGLNSEEQKEDTNYLDGIQGLLKTKDGQQLNLDNIGTTpLAEKVKTKACDLVLKQGLN 161
Cdd:pfam10696   1 KNNYLSADGASSVKDQLLGKLGLGTQEQQKDSDYQNGLQGLLKTGNGQQFNLSNLGTT-LKEKVKTKACDLVLKQAKS 77
serpinA5_PCI cd19553
serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called ...
 95-137 1.99e-03

serpin family A member 5, protein C inhibitor; Protein C inhibitor (PCI/PROCI, also called PAI3, plasminogen activator inhibitor-3/PLANH3, plasma serine protease inhibitor) has many biological functions. It acts as a pro-coagulant in blood and in the seminal vesicles, it is required for spermatogenesis. It is a member of the clade A serpin family that includes the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, kallistatin, and non-inhibitory serpins, like corticosteroid and thyroxin binding globulins. In general, SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans.


Pssm-ID: 381021 [Multi-domain]  Cd Length: 364  Bit Score: 37.44  E-value: 1.99e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 90111742  95 NIKNQVLEKLGLNSEEQKED---TNYLDGIQGLLKTKDGQQLNLDN 137
Cdd:cd19553  43 STKAQILEGLGLNPQKGSEEqlhRGFQQLLQELNQPRDGFQLSLGN 88
 
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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