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Conserved domains on  [gi|755492205|ref|XP_011236757|]
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DNA primase large subunit isoform X2 [Mus musculus]

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 ...
16-236 1.13e-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: 381.22  E-value: 1.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  16 QLTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQKNTGKISLDQIDSLSTKSFPPCMRQLHKALRENHHLRHGGRMQYG 95
Cdd:cd07322  171 ALTARSLPRLEEDDRLLPLLKSLSKSYTGKDYSKNGNGGGLTLSSIDELSKKSFPLCMRQLHEALRKNHHLKHGGRLQLG 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  96 LFLKGIGLTLEQALQFWKQEFIRgKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCMKIILTNPPGQGDYHGCPFRHSD 175
Cdd:cd07322  251 LFLKGIGLSLEEALKFWRSEFTK-KMDADKFDKEYAYNIRHNYGKEGKRANYTPYSCSKIISQNPPGPGDCHGCPFRHFD 329
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492205 176 AELLKQKMQSYKIPASGISQILDLVKGNHYQVACQKYFEMTHNVDDCGFSLNHPNQFFFES 236
Cdd:cd07322  330 SDSLKQLLQSYGLSDSDIEEIIDLVKSGHYQLACTKYFELTHPGAESDTGINHPNQYFEES 390
 
Name Accession Description Interval E-value
PriL_PriS_Eukaryotic cd07322
Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for ...
16-236 1.13e-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: 381.22  E-value: 1.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  16 QLTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQKNTGKISLDQIDSLSTKSFPPCMRQLHKALRENHHLRHGGRMQYG 95
Cdd:cd07322  171 ALTARSLPRLEEDDRLLPLLKSLSKSYTGKDYSKNGNGGGLTLSSIDELSKKSFPLCMRQLHEALRKNHHLKHGGRLQLG 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  96 LFLKGIGLTLEQALQFWKQEFIRgKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCMKIILTNPPGQGDYHGCPFRHSD 175
Cdd:cd07322  251 LFLKGIGLSLEEALKFWRSEFTK-KMDADKFDKEYAYNIRHNYGKEGKRANYTPYSCSKIISQNPPGPGDCHGCPFRHFD 329
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492205 176 AELLKQKMQSYKIPASGISQILDLVKGNHYQVACQKYFEMTHNVDDCGFSLNHPNQFFFES 236
Cdd:cd07322  330 SDSLKQLLQSYGLSDSDIEEIIDLVKSGHYQLACTKYFELTHPGAESDTGINHPNQYFEES 390
DNA_primase_lrg pfam04104
Eukaryotic and archaeal DNA primase, large subunit; DNA primase is the polymerase that ...
14-233 1.65e-70

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: 217.31  E-value: 1.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205   14 IPQLTARSLPAVQSDER--LQPLLNHLSHSYTGQDYSTQKNTGKISldqiDSLSTKSFPPCMRQLHKALRENHHLRHGGR 91
Cdd:pfam04104  52 TYESLPELLEEILEDERekLEPLLEHLSKSYVSPELFQEADDGKIS----DELSKKHFPPCMRNLLEGLRRGGHLKHEGR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205   92 MQYGLFLKGIGLTLEQALQFWKQEFIRgkmDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCMKIIlTNPPGQGDYHGCPF 171
Cdd:pfam04104 128 FQLGLFLKGIGLSLDEILEFWREAFTR---TVEDFDKEYRYNIRHNYGLEGKRTNYSPPSCAKIL-NLPPGRGDAHGCPF 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492205  172 RhsdaellkqkmqsykipasgisqildlvkgnhyqvacqkyfemTHNVDDCGFSLNHPNQFF 233
Cdd:pfam04104 204 R-------------------------------------------APDPLCRSCGIKHPLQYY 222
PRI2 COG2219
Eukaryotic-type DNA primase, large subunit [Replication, recombination and repair];
55-154 1.59e-09

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


Pssm-ID: 441821 [Multi-domain]  Cd Length: 346  Bit Score: 58.01  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  55 KISLDQIDSLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLEQALQFWkqefirgKMDPDkFD-KGYSYN 133
Cdd:COG2219  214 KSTLREIGTVEPELFPPCMKALLDRLRKGENLPHSARFALASFLLNIGMDVDEIVELF-------KVAPD-FDeEKTRYQ 285
                         90       100
                 ....*....|....*....|...
gi 755492205 134 IRHSFGkEGKRTDYTPFSC--MK 154
Cdd:COG2219  286 VEHIAG-DGSGTEYSPPSCetMK 307
PRK02249 PRK02249
DNA primase regulatory subunit PriL;
19-154 9.82e-08

DNA primase regulatory subunit PriL;


Pssm-ID: 179392 [Multi-domain]  Cd Length: 343  Bit Score: 52.28  E-value: 9.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  19 ARSLPAVQSD---ERLQPLLNHLSHSYTGQDYSTQkntgkisLDQIDslsTKSFPPCMRQLHKALRENHHLRHGGRMQYG 95
Cdd:PRK02249 179 LDGLPLAVPEeiaEALLPLLEEIREELEELDLETE-------FGTVD---PELFPPCMKALLSALQAGENLPHTARFAIT 248
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492205  96 LFLKGIGLTLEQALQFWkqefirgKMDPDkFD-KGYSYNIRHSFGKEGKrTDYTPFSC--MK 154
Cdd:PRK02249 249 SFLLNIGMSVDEIVELF-------RNAPD-FDeEKTRYQVEHIAGETGG-TEYTPPSCetMR 301
 
Name Accession Description Interval E-value
PriL_PriS_Eukaryotic cd07322
Eukaryotic core primase: Large subunit, PriL; Primases synthesize the RNA primers required for ...
16-236 1.13e-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: 381.22  E-value: 1.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  16 QLTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQKNTGKISLDQIDSLSTKSFPPCMRQLHKALRENHHLRHGGRMQYG 95
Cdd:cd07322  171 ALTARSLPRLEEDDRLLPLLKSLSKSYTGKDYSKNGNGGGLTLSSIDELSKKSFPLCMRQLHEALRKNHHLKHGGRLQLG 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  96 LFLKGIGLTLEQALQFWKQEFIRgKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCMKIILTNPPGQGDYHGCPFRHSD 175
Cdd:cd07322  251 LFLKGIGLSLEEALKFWRSEFTK-KMDADKFDKEYAYNIRHNYGKEGKRANYTPYSCSKIISQNPPGPGDCHGCPFRHFD 329
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755492205 176 AELLKQKMQSYKIPASGISQILDLVKGNHYQVACQKYFEMTHNVDDCGFSLNHPNQFFFES 236
Cdd:cd07322  330 SDSLKQLLQSYGLSDSDIEEIIDLVKSGHYQLACTKYFELTHPGAESDTGINHPNQYFEES 390
DNA_primase_lrg pfam04104
Eukaryotic and archaeal DNA primase, large subunit; DNA primase is the polymerase that ...
14-233 1.65e-70

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: 217.31  E-value: 1.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205   14 IPQLTARSLPAVQSDER--LQPLLNHLSHSYTGQDYSTQKNTGKISldqiDSLSTKSFPPCMRQLHKALRENHHLRHGGR 91
Cdd:pfam04104  52 TYESLPELLEEILEDERekLEPLLEHLSKSYVSPELFQEADDGKIS----DELSKKHFPPCMRNLLEGLRRGGHLKHEGR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205   92 MQYGLFLKGIGLTLEQALQFWKQEFIRgkmDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCMKIIlTNPPGQGDYHGCPF 171
Cdd:pfam04104 128 FQLGLFLKGIGLSLDEILEFWREAFTR---TVEDFDKEYRYNIRHNYGLEGKRTNYSPPSCAKIL-NLPPGRGDAHGCPF 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492205  172 RhsdaellkqkmqsykipasgisqildlvkgnhyqvacqkyfemTHNVDDCGFSLNHPNQFF 233
Cdd:pfam04104 204 R-------------------------------------------APDPLCRSCGIKHPLQYY 222
PRI2 COG2219
Eukaryotic-type DNA primase, large subunit [Replication, recombination and repair];
55-154 1.59e-09

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


Pssm-ID: 441821 [Multi-domain]  Cd Length: 346  Bit Score: 58.01  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  55 KISLDQIDSLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLEQALQFWkqefirgKMDPDkFD-KGYSYN 133
Cdd:COG2219  214 KSTLREIGTVEPELFPPCMKALLDRLRKGENLPHSARFALASFLLNIGMDVDEIVELF-------KVAPD-FDeEKTRYQ 285
                         90       100
                 ....*....|....*....|...
gi 755492205 134 IRHSFGkEGKRTDYTPFSC--MK 154
Cdd:COG2219  286 VEHIAG-DGSGTEYSPPSCetMK 307
PRK02249 PRK02249
DNA primase regulatory subunit PriL;
19-154 9.82e-08

DNA primase regulatory subunit PriL;


Pssm-ID: 179392 [Multi-domain]  Cd Length: 343  Bit Score: 52.28  E-value: 9.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755492205  19 ARSLPAVQSD---ERLQPLLNHLSHSYTGQDYSTQkntgkisLDQIDslsTKSFPPCMRQLHKALRENHHLRHGGRMQYG 95
Cdd:PRK02249 179 LDGLPLAVPEeiaEALLPLLEEIREELEELDLETE-------FGTVD---PELFPPCMKALLSALQAGENLPHTARFAIT 248
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755492205  96 LFLKGIGLTLEQALQFWkqefirgKMDPDkFD-KGYSYNIRHSFGKEGKrTDYTPFSC--MK 154
Cdd:PRK02249 249 SFLLNIGMSVDEIVELF-------RNAPD-FDeEKTRYQVEHIAGETGG-TEYTPPSCetMR 301
 
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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