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Conserved domains on  [gi|2462609271|ref|XP_054211787|]
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DNA primase large subunit isoform X5 [Homo sapiens]

Protein Classification

DNA primase large subunit( domain architecture ID 10164070)

DNA primase large subunit is the regulatory subunit of the DNA primase complex and a component of the DNA polymerase alpha complex (called the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PriL_PriS_Eukaryotic cd07322
Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for ...
 41-260 9.93e-132

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: 380.07  E-value: 9.93e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  41 LTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQGNVGKISLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGL 120
Cdd:cd07322   172 LTARSLPRLEEDDRLLPLLKSLSKSYTGKDYSKNGNGGGLTLSSIDELSKKSFPLCMRQLHEALRKNHHLKHGGRLQLGL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271 121 FLKGIGLTLEQALQFWKQEFIKgKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKIILSNPPSQGDYHGCPFRHSDP 200
Cdd:cd07322   252 FLKGIGLSLEEALKFWRSEFTK-KMDADKFDKEYAYNIRHNYGKEGKRANYTPYSCSKIISQNPPGPGDCHGCPFRHFDS 330

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271 201 ELLKQKLQSYKISPGGISQILDLVKGTHYQVACQKYFEMIHNVDDCGFSLNHPNQFFCES 260
Cdd:cd07322   331 DSLKQLLQSYGLSDSDIEEIIDLVKSGHYQLACTKYFELTHPGAESDTGINHPNQYFEES 390
 
Name Accession Description Interval E-value
PriL_PriS_Eukaryotic cd07322
Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for ...
 41-260 9.93e-132

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: 380.07  E-value: 9.93e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  41 LTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQGNVGKISLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGL 120
Cdd:cd07322   172 LTARSLPRLEEDDRLLPLLKSLSKSYTGKDYSKNGNGGGLTLSSIDELSKKSFPLCMRQLHEALRKNHHLKHGGRLQLGL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271 121 FLKGIGLTLEQALQFWKQEFIKgKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKIILSNPPSQGDYHGCPFRHSDP 200
Cdd:cd07322   252 FLKGIGLSLEEALKFWRSEFTK-KMDADKFDKEYAYNIRHNYGKEGKRANYTPYSCSKIISQNPPGPGDCHGCPFRHFDS 330

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271 201 ELLKQKLQSYKISPGGISQILDLVKGTHYQVACQKYFEMIHNVDDCGFSLNHPNQFFCES 260
Cdd:cd07322   331 DSLKQLLQSYGLSDSDIEEIIDLVKSGHYQLACTKYFELTHPGAESDTGINHPNQYFEES 390
DNA_primase_lrg pfam04104
Eukaryotic and archaeal DNA primase, large subunit; DNA primase is the polymerase that ...
 31-200 9.62e-67

Eukaryotic and archaeal DNA primase, large subunit; DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. DNA primase is a heterodimer of two subunits, the small subunit Pri1 (48 kDa in yeast), and the large subunit Pri2 (58 kDa in the yeast S. cerevisiae). The large subunit of DNA primase forms interactions with the small subunit and the structure implicates that it is not directly involved in catalysis, but plays roles in correctly positioning the primase/DNA complex, and in the transfer of RNA to DNA polymerase.


Pssm-ID: 397980  Cd Length: 222  Bit Score: 208.45  E-value: 9.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  31 REEVAKsASVLTARSLPAVQS----DER--LQPLLNHLSHSYTGQDYSTQGNVGKISldqiDLLSTKSFPPCMRQLHKAL 104
Cdd:pfam04104  42 RSRLEK-ALELTYESLPELLEeileDERekLEPLLEHLSKSYVSPELFQEADDGKIS----DELSKKHFPPCMRNLLEGL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271 105 RENHHLRHGGRMQYGLFLKGIGLTLEQALQFWKQEFIKgkmDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKIIlSNP 184
Cdd:pfam04104 117 RRGGHLKHEGRFQLGLFLKGIGLSLDEILEFWREAFTR---TVEDFDKEYRYNIRHNYGLEGKRTNYSPPSCAKIL-NLP 192

                         170
                  ....*....|....*.
gi 2462609271 185 PSQGDYHGCPFRHSDP 200
Cdd:pfam04104 193 PGRGDAHGCPFRAPDP 208
PRI2 COG2219
Eukaryotic-type DNA primase, large subunit [Replication, recombination and repair];
79-176 2.99e-09

Eukaryotic-type DNA primase, large subunit [Replication, recombination and repair];


Pssm-ID: 441821 [Multi-domain]  Cd Length: 346  Bit Score: 57.24  E-value: 2.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  79 KISLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLEQALQFWkqefikgKMDPDkFD-KGYSYN 157
Cdd:COG2219   214 KSTLREIGTVEPELFPPCMKALLDRLRKGENLPHSARFALASFLLNIGMDVDEIVELF-------KVAPD-FDeEKTRYQ 285

                          90
                  ....*....|....*....
gi 2462609271 158 IRHSFGkEGKRTDYTPFSC 176
Cdd:COG2219   286 VEHIAG-DGSGTEYSPPSC 303
PRK02249 PRK02249
DNA primase regulatory subunit PriL;
43-176 1.75e-07

DNA primase regulatory subunit PriL;


Pssm-ID: 179392 [Multi-domain]  Cd Length: 343  Bit Score: 51.89  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  43 ARSLPAVQSD---ERLQPLLNHLSHSYTGQDYSTQgnvgkisldqIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYG 119
Cdd:PRK02249  179 LDGLPLAVPEeiaEALLPLLEEIREELEELDLETE----------FGTVDPELFPPCMKALLSALQAGENLPHTARFAIT 248

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462609271 120 LFLKGIGLTLEQALQFWkqefikgKMDPDkFD-KGYSYNIRHSFGKEGKrTDYTPFSC 176
Cdd:PRK02249  249 SFLLNIGMSVDEIVELF-------RNAPD-FDeEKTRYQVEHIAGETGG-TEYTPPSC 297
 
Name Accession Description Interval E-value
PriL_PriS_Eukaryotic cd07322
Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for ...
 41-260 9.93e-132

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: 380.07  E-value: 9.93e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  41 LTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQGNVGKISLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGL 120
Cdd:cd07322   172 LTARSLPRLEEDDRLLPLLKSLSKSYTGKDYSKNGNGGGLTLSSIDELSKKSFPLCMRQLHEALRKNHHLKHGGRLQLGL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271 121 FLKGIGLTLEQALQFWKQEFIKgKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKIILSNPPSQGDYHGCPFRHSDP 200
Cdd:cd07322   252 FLKGIGLSLEEALKFWRSEFTK-KMDADKFDKEYAYNIRHNYGKEGKRANYTPYSCSKIISQNPPGPGDCHGCPFRHFDS 330

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271 201 ELLKQKLQSYKISPGGISQILDLVKGTHYQVACQKYFEMIHNVDDCGFSLNHPNQFFCES 260
Cdd:cd07322   331 DSLKQLLQSYGLSDSDIEEIIDLVKSGHYQLACTKYFELTHPGAESDTGINHPNQYFEES 390
DNA_primase_lrg pfam04104
Eukaryotic and archaeal DNA primase, large subunit; DNA primase is the polymerase that ...
 31-200 9.62e-67

Eukaryotic and archaeal DNA primase, large subunit; DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. DNA primase is a heterodimer of two subunits, the small subunit Pri1 (48 kDa in yeast), and the large subunit Pri2 (58 kDa in the yeast S. cerevisiae). The large subunit of DNA primase forms interactions with the small subunit and the structure implicates that it is not directly involved in catalysis, but plays roles in correctly positioning the primase/DNA complex, and in the transfer of RNA to DNA polymerase.


Pssm-ID: 397980  Cd Length: 222  Bit Score: 208.45  E-value: 9.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  31 REEVAKsASVLTARSLPAVQS----DER--LQPLLNHLSHSYTGQDYSTQGNVGKISldqiDLLSTKSFPPCMRQLHKAL 104
Cdd:pfam04104  42 RSRLEK-ALELTYESLPELLEeileDERekLEPLLEHLSKSYVSPELFQEADDGKIS----DELSKKHFPPCMRNLLEGL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271 105 RENHHLRHGGRMQYGLFLKGIGLTLEQALQFWKQEFIKgkmDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKIIlSNP 184
Cdd:pfam04104 117 RRGGHLKHEGRFQLGLFLKGIGLSLDEILEFWREAFTR---TVEDFDKEYRYNIRHNYGLEGKRTNYSPPSCAKIL-NLP 192

                         170
                  ....*....|....*.
gi 2462609271 185 PSQGDYHGCPFRHSDP 200
Cdd:pfam04104 193 PGRGDAHGCPFRAPDP 208
PRI2 COG2219
Eukaryotic-type DNA primase, large subunit [Replication, recombination and repair];
79-176 2.99e-09

Eukaryotic-type DNA primase, large subunit [Replication, recombination and repair];


Pssm-ID: 441821 [Multi-domain]  Cd Length: 346  Bit Score: 57.24  E-value: 2.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  79 KISLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLEQALQFWkqefikgKMDPDkFD-KGYSYN 157
Cdd:COG2219   214 KSTLREIGTVEPELFPPCMKALLDRLRKGENLPHSARFALASFLLNIGMDVDEIVELF-------KVAPD-FDeEKTRYQ 285

                          90
                  ....*....|....*....
gi 2462609271 158 IRHSFGkEGKRTDYTPFSC 176
Cdd:COG2219   286 VEHIAG-DGSGTEYSPPSC 303
PRK02249 PRK02249
DNA primase regulatory subunit PriL;
43-176 1.75e-07

DNA primase regulatory subunit PriL;


Pssm-ID: 179392 [Multi-domain]  Cd Length: 343  Bit Score: 51.89  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462609271  43 ARSLPAVQSD---ERLQPLLNHLSHSYTGQDYSTQgnvgkisldqIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYG 119
Cdd:PRK02249  179 LDGLPLAVPEeiaEALLPLLEEIREELEELDLETE----------FGTVDPELFPPCMKALLSALQAGENLPHTARFAIT 248

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462609271 120 LFLKGIGLTLEQALQFWkqefikgKMDPDkFD-KGYSYNIRHSFGKEGKrTDYTPFSC 176
Cdd:PRK02249  249 SFLLNIGMSVDEIVELF-------RNAPD-FDeEKTRYQVEHIAGETGG-TEYTPPSC 297
 
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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