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Conserved domains on  [gi|636385645|gb|KDL62849|]
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primosomal protein 1 [Klebsiella variicola]

Protein Classification

primosomal protein 1( domain architecture ID 10011852)

primosomal protein 1 is required for primosome-dependent normal DNA replication and is also involved in inducing stable DNA replication during SOS response

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK02854 PRK02854
primosomal protein DnaT;
1-179 5.92e-124

primosomal protein DnaT;


:

Pssm-ID: 179484  Cd Length: 179  Bit Score: 346.41  E-value: 5.92e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385645   1 MSSRILTSHFSGLEEFLQQHAALLAKSTDGTVAVFANNAPAFYALTPARLAQLLELEARLARPGSDIALDPQFFEEPAAA 80
Cdd:PRK02854   1 MSSRILTSDVIGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVALDDQLYQEPQAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385645  81 PVAVPMGKFAMYADWQPDADFQRLAALWGIALSQPVTPEELAAFVAYWQAEGKVFHHVQWQQKLARSVQISRASNGGQPK 160
Cdd:PRK02854  81 PVAVPMGKFAMYPDWQPDADFIRQAALWGVALREPVTAEELASFIAYWQAEGKVFHHIQWQQKLARSLQISRASNGGQPK 160

                        170
                 ....*....|....*....
gi 636385645 161 RDVNSVSEPDSHIPRGFRG 179
Cdd:PRK02854 161 RDINTVSEPDSQIPPGFRG 179
 
Name Accession Description Interval E-value
PRK02854 PRK02854
primosomal protein DnaT;
1-179 5.92e-124

primosomal protein DnaT;


Pssm-ID: 179484  Cd Length: 179  Bit Score: 346.41  E-value: 5.92e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385645   1 MSSRILTSHFSGLEEFLQQHAALLAKSTDGTVAVFANNAPAFYALTPARLAQLLELEARLARPGSDIALDPQFFEEPAAA 80
Cdd:PRK02854   1 MSSRILTSDVIGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVALDDQLYQEPQAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385645  81 PVAVPMGKFAMYADWQPDADFQRLAALWGIALSQPVTPEELAAFVAYWQAEGKVFHHVQWQQKLARSVQISRASNGGQPK 160
Cdd:PRK02854  81 PVAVPMGKFAMYPDWQPDADFIRQAALWGVALREPVTAEELASFIAYWQAEGKVFHHIQWQQKLARSLQISRASNGGQPK 160

                        170
                 ....*....|....*....
gi 636385645 161 RDVNSVSEPDSHIPRGFRG 179
Cdd:PRK02854 161 RDINTVSEPDSQIPPGFRG 179
DnaT pfam17948
DnaT DNA-binding domain; This domain is found in E.coli primosomal protein 1 (Pp1). PP1 domain ...
 89-160 7.15e-23

DnaT DNA-binding domain; This domain is found in E.coli primosomal protein 1 (Pp1). PP1 domain (residues 84-153) in Swiss:P0A8J2 can bind to different types of ssDNA, which is fundamental for its physiological substrate bindings. Functional analysis indicate that both N- and C- terminals are essential to having the cooperative effect in binding ssDNA. The ssDNA bound complex displays a spiral filament assembly that is adopted by many proteins that are involved in DNA replication, such as DnaA, RecA and PriB. This domain is similar to pfam08585 except that it contains an extra loop at the N-terminus (84-99). Structural analysis indicate that this extra loop might be essential for the stabilization of the three-helix bundle.


Pssm-ID: 465580  Cd Length: 69  Bit Score: 86.53  E-value: 7.15e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636385645   89 FAMYADWQPDADFQRLAALWGIaLSQPVTPEELAAFVAYWQAEGkvFHHVQWQQKLARSVQISRASNGGQPK 160
Cdd:pfam17948   1 FPMHLDWQPSADFLEILALAGG-IDRDFAEDELPEFVLYWRERG--FAQHQWNQKFVQHVKRQWARYQSSLG 69
ECs1768 COG5529
Phage-encoded DNA-binding protein ECs1768, contains HTH and DnaT DNA-binding domains [Mobilome: ...
 101-171 1.33e-19

Phage-encoded DNA-binding protein ECs1768, contains HTH and DnaT DNA-binding domains [Mobilome: prophages, transposons];


Pssm-ID: 444280  Cd Length: 104  Bit Score: 79.15  E-value: 1.33e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636385645 101 FQRLAALWGIALsqpvtpEELAAFVAYWQAEGKVFHHvqwQQKLARSVQISRASNGGQPKRDVNSVSEPDS 171
Cdd:COG5529    1 FSRQAALWGIAL------PELAAFRAHWQKHGKEFGS---QQKLARYVQQARAFVNRPPRRDRGTLTKTRP 62
 
Name Accession Description Interval E-value
PRK02854 PRK02854
primosomal protein DnaT;
1-179 5.92e-124

primosomal protein DnaT;


Pssm-ID: 179484  Cd Length: 179  Bit Score: 346.41  E-value: 5.92e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385645   1 MSSRILTSHFSGLEEFLQQHAALLAKSTDGTVAVFANNAPAFYALTPARLAQLLELEARLARPGSDIALDPQFFEEPAAA 80
Cdd:PRK02854   1 MSSRILTSDVIGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVALDDQLYQEPQAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636385645  81 PVAVPMGKFAMYADWQPDADFQRLAALWGIALSQPVTPEELAAFVAYWQAEGKVFHHVQWQQKLARSVQISRASNGGQPK 160
Cdd:PRK02854  81 PVAVPMGKFAMYPDWQPDADFIRQAALWGVALREPVTAEELASFIAYWQAEGKVFHHIQWQQKLARSLQISRASNGGQPK 160

                        170
                 ....*....|....*....
gi 636385645 161 RDVNSVSEPDSHIPRGFRG 179
Cdd:PRK02854 161 RDINTVSEPDSQIPPGFRG 179
DnaT pfam17948
DnaT DNA-binding domain; This domain is found in E.coli primosomal protein 1 (Pp1). PP1 domain ...
 89-160 7.15e-23

DnaT DNA-binding domain; This domain is found in E.coli primosomal protein 1 (Pp1). PP1 domain (residues 84-153) in Swiss:P0A8J2 can bind to different types of ssDNA, which is fundamental for its physiological substrate bindings. Functional analysis indicate that both N- and C- terminals are essential to having the cooperative effect in binding ssDNA. The ssDNA bound complex displays a spiral filament assembly that is adopted by many proteins that are involved in DNA replication, such as DnaA, RecA and PriB. This domain is similar to pfam08585 except that it contains an extra loop at the N-terminus (84-99). Structural analysis indicate that this extra loop might be essential for the stabilization of the three-helix bundle.


Pssm-ID: 465580  Cd Length: 69  Bit Score: 86.53  E-value: 7.15e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 636385645   89 FAMYADWQPDADFQRLAALWGIaLSQPVTPEELAAFVAYWQAEGkvFHHVQWQQKLARSVQISRASNGGQPK 160
Cdd:pfam17948   1 FPMHLDWQPSADFLEILALAGG-IDRDFAEDELPEFVLYWRERG--FAQHQWNQKFVQHVKRQWARYQSSLG 69
ECs1768 COG5529
Phage-encoded DNA-binding protein ECs1768, contains HTH and DnaT DNA-binding domains [Mobilome: ...
 101-171 1.33e-19

Phage-encoded DNA-binding protein ECs1768, contains HTH and DnaT DNA-binding domains [Mobilome: prophages, transposons];


Pssm-ID: 444280  Cd Length: 104  Bit Score: 79.15  E-value: 1.33e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636385645 101 FQRLAALWGIALsqpvtpEELAAFVAYWQAEGKVFHHvqwQQKLARSVQISRASNGGQPKRDVNSVSEPDS 171
Cdd:COG5529    1 FSRQAALWGIAL------PELAAFRAHWQKHGKEFGS---QQKLARYVQQARAFVNRPPRRDRGTLTKTRP 62
 
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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