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Conserved domains on  [gi|542133063|ref|NP_001269416|]
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DNA primase large subunit isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PriL super family cl11970
Archaeal/eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers ...
 28-155 5.17e-37

Archaeal/eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for DNA replication. Primases are grouped into two classes, bacteria/bacteriophage and archaeal/eukaryotic. The proteins in the two classes differ in structure and the replication apparatus components. The DNA replication machinery of archaeal organisms contains only the core primase, a simpler arrangement compared to eukaryotes. Archaeal/eukaryotic core primase is a heterodimeric enzyme consisting of a small catalytic subunit (PriS) and a large subunit (PriL). Although the catalytic activity resides within PriS, the PriL subunit is essential for primase function as disruption of the PriL gene in yeast is lethal. PriL is composed of two structural domains. Several functions have been proposed for PriL, such as the stabilization of PriS, involvement in the initiation of synthesis, the improvement of primase processivity, and the determination of product size.


The actual alignment was detected with superfamily member cd07322:

Pssm-ID: 416393 [Multi-domain]  Cd Length: 390  Bit Score: 130.46  E-value: 5.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133063  28 FYLQPPSENISLIEFENLAIDRVKLLKSVENLgvsyvkgteqyqskleselrklkfsyrenledeYEPRRRDHISHFILR 107
Cdd:cd07322    1 FYDTPPTGNISLEEFEEIAIDRLKLLREIEQL---------------------------------EEERRKDHISHFILR 47

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 542133063 108 LAYCQSEELRRWFIQQEMDLLRFRFSILPKDKIQDFLKDSQLQFEAVS 155
Cdd:cd07322   48 LAYCRSEELRRWFVRQETELFRYRLELLSLEGLKQFLKSNGLDYQPVS 95
 
Name Accession Description Interval E-value
PriL_PriS_Eukaryotic cd07322
Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for ...
 28-155 5.17e-37

Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for DNA replication. Primases are grouped into two classes, bacteria/bacteriophage and archaeal/eukaryotic. The proteins in the two classes differ in structure and the replication apparatus components. Archaeal/eukaryotic core primase is a heterodimeric enzyme consisting of a small catalytic subunit (PriS) and a large subunit (PriL). In eukaryotic organisms, a heterotetrameric enzyme formed by DNA polymerase alpha, the B subunit and two primase subunits has primase activity. Although the catalytic activity resides within PriS, the PriL subunit is essential for primase function as disruption of the PriL gene in yeast is lethal. PriL is composed of two structural domains. Several functions have been proposed for PriL such as stabilization of the PriS, involvement in synthesis initiation, improvement of primase processivity, determination of product size and transfer of the products to DNA polymerase alpha.


Pssm-ID: 143474 [Multi-domain]  Cd Length: 390  Bit Score: 130.46  E-value: 5.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133063  28 FYLQPPSENISLIEFENLAIDRVKLLKSVENLgvsyvkgteqyqskleselrklkfsyrenledeYEPRRRDHISHFILR 107
Cdd:cd07322    1 FYDTPPTGNISLEEFEEIAIDRLKLLREIEQL---------------------------------EEERRKDHISHFILR 47

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 542133063 108 LAYCQSEELRRWFIQQEMDLLRFRFSILPKDKIQDFLKDSQLQFEAVS 155
Cdd:cd07322   48 LAYCRSEELRRWFVRQETELFRYRLELLSLEGLKQFLKSNGLDYQPVS 95
 
Name Accession Description Interval E-value
PriL_PriS_Eukaryotic cd07322
Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for ...
 28-155 5.17e-37

Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for DNA replication. Primases are grouped into two classes, bacteria/bacteriophage and archaeal/eukaryotic. The proteins in the two classes differ in structure and the replication apparatus components. Archaeal/eukaryotic core primase is a heterodimeric enzyme consisting of a small catalytic subunit (PriS) and a large subunit (PriL). In eukaryotic organisms, a heterotetrameric enzyme formed by DNA polymerase alpha, the B subunit and two primase subunits has primase activity. Although the catalytic activity resides within PriS, the PriL subunit is essential for primase function as disruption of the PriL gene in yeast is lethal. PriL is composed of two structural domains. Several functions have been proposed for PriL such as stabilization of the PriS, involvement in synthesis initiation, improvement of primase processivity, determination of product size and transfer of the products to DNA polymerase alpha.


Pssm-ID: 143474 [Multi-domain]  Cd Length: 390  Bit Score: 130.46  E-value: 5.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542133063  28 FYLQPPSENISLIEFENLAIDRVKLLKSVENLgvsyvkgteqyqskleselrklkfsyrenledeYEPRRRDHISHFILR 107
Cdd:cd07322    1 FYDTPPTGNISLEEFEEIAIDRLKLLREIEQL---------------------------------EEERRKDHISHFILR 47

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 542133063 108 LAYCQSEELRRWFIQQEMDLLRFRFSILPKDKIQDFLKDSQLQFEAVS 155
Cdd:cd07322   48 LAYCRSEELRRWFVRQETELFRYRLELLSLEGLKQFLKSNGLDYQPVS 95
 
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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