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Conserved domains on  [gi|1064291325|ref|NP_001332827|]
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DNA-directed primase/polymerase protein isoform 8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PrimPol_RBD cd22256
C-terminal RPA-binding domain (RBD) of DNA-directed primase/polymerase protein and similar ...
 247-325 4.99e-18

C-terminal RPA-binding domain (RBD) of DNA-directed primase/polymerase protein and similar proteins; DNA-directed primase/polymerase protein (PrimPol), also called coiled-coil domain-containing protein 111, is a DNA primase-polymerase required for the maintenance of genome integrity. It facilitates mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions. PrimPol is regulated by single-stranded DNA binding proteins. This model corresponds to the C-terminal RPA-binding domain (RBD) of PrimPol, which interacts directly with the RPA70N domain of RPA70.


:

Pssm-ID: 412077  Cd Length: 81  Bit Score: 77.44  E-value: 4.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064291325 247 TTDEADETRSNETQNPHKP-SPSRLSTGASADAVWDNGIDDAYFLEATEDAELAEAAENSLLSYNSEVDEIPDELIIEVL 325
Cdd:cd22256     2 DENGNIKETQNTEDSTPLEsSESSLSISGSSDAEWDNGIDDACFLEATEDAELAEAADNSLSELNDEVDEIPDELLLEAL 81
Herpes_UL52 pfam03121
Herpesviridae UL52/UL70 DNA primase; Herpes simplex virus type 1 DNA replication in host cells ...
 169-233 5.08e-15

Herpesviridae UL52/UL70 DNA primase; Herpes simplex virus type 1 DNA replication in host cells is known to be mediated by seven viral-encoded proteins, three of which form a heterotrimeric DNA helicase-primase complex. This complex consists of UL5, UL8, and UL52 subunits. Heterodimers consisting of UL5 and UL52 have been shown to retain both helicase and primase activities. Nevertheless, UL8 is still essential for replication: though it lacks any DNA binding or catalytic activities, it is involved in the transport of UL5-UL52 and it also interacts with other replication proteins. The molecular mechanisms of the UL5-UL52 catalytic activities are not known. While UL5 is associated with DNA helicase activity and UL52 with DNA primase activity, the helicase activity requires the interaction of UL5 and UL52. It is not known if the primase activity can be maintained by UL52 alone. The region encompassed by residues 610-636 of HSV1 UL52 is thought to contain a divalent metal cation binding motif. Indeed, this region contains several aspartate and glutamate residues that might be involved in divalent cation binding. The biological significance of UL52-UL8 interaction is not known. Yeast two-hybrid analysis together with immunoprecipitation experiments have shown that the HSV1 UL52 region between residues 366-914 is essential for this interaction, while the first 349 N-terminal residues are dispensable. This family also includes protein UL70 from cytomegalovirus (CMV, a subgroup of the Herpesviridae) strains, which, by analogy with UL52, is thought to have DNA primase activity. Indeed, CMV strains also possess a DNA helicase-primase complex, the other subunits being protein UL105 (with known similarity to HSV1 UL5) and protein UL102.


:

Pssm-ID: 367342 [Multi-domain]  Cd Length: 75  Bit Score: 68.98  E-value: 5.08e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1064291325 169 YFFPEELLVYDICKYR-----WCENIGRAHKSNNIMILVDLKNEV------WYQKCHDPVCKaENFKSDCFPLPAE 233
Cdd:pfam03121   1 VFSKEGLNLVQVKRSRrgrnfSCLNIGHRHKSNNVRVFLDLRVDGhglcvtLYQKCFAPKCG-SNYRSTHFSVPVD 75
 
Name Accession Description Interval E-value
PrimPol_RBD cd22256
C-terminal RPA-binding domain (RBD) of DNA-directed primase/polymerase protein and similar ...
 247-325 4.99e-18

C-terminal RPA-binding domain (RBD) of DNA-directed primase/polymerase protein and similar proteins; DNA-directed primase/polymerase protein (PrimPol), also called coiled-coil domain-containing protein 111, is a DNA primase-polymerase required for the maintenance of genome integrity. It facilitates mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions. PrimPol is regulated by single-stranded DNA binding proteins. This model corresponds to the C-terminal RPA-binding domain (RBD) of PrimPol, which interacts directly with the RPA70N domain of RPA70.


Pssm-ID: 412077  Cd Length: 81  Bit Score: 77.44  E-value: 4.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064291325 247 TTDEADETRSNETQNPHKP-SPSRLSTGASADAVWDNGIDDAYFLEATEDAELAEAAENSLLSYNSEVDEIPDELIIEVL 325
Cdd:cd22256     2 DENGNIKETQNTEDSTPLEsSESSLSISGSSDAEWDNGIDDACFLEATEDAELAEAADNSLSELNDEVDEIPDELLLEAL 81
Herpes_UL52 pfam03121
Herpesviridae UL52/UL70 DNA primase; Herpes simplex virus type 1 DNA replication in host cells ...
 169-233 5.08e-15

Herpesviridae UL52/UL70 DNA primase; Herpes simplex virus type 1 DNA replication in host cells is known to be mediated by seven viral-encoded proteins, three of which form a heterotrimeric DNA helicase-primase complex. This complex consists of UL5, UL8, and UL52 subunits. Heterodimers consisting of UL5 and UL52 have been shown to retain both helicase and primase activities. Nevertheless, UL8 is still essential for replication: though it lacks any DNA binding or catalytic activities, it is involved in the transport of UL5-UL52 and it also interacts with other replication proteins. The molecular mechanisms of the UL5-UL52 catalytic activities are not known. While UL5 is associated with DNA helicase activity and UL52 with DNA primase activity, the helicase activity requires the interaction of UL5 and UL52. It is not known if the primase activity can be maintained by UL52 alone. The region encompassed by residues 610-636 of HSV1 UL52 is thought to contain a divalent metal cation binding motif. Indeed, this region contains several aspartate and glutamate residues that might be involved in divalent cation binding. The biological significance of UL52-UL8 interaction is not known. Yeast two-hybrid analysis together with immunoprecipitation experiments have shown that the HSV1 UL52 region between residues 366-914 is essential for this interaction, while the first 349 N-terminal residues are dispensable. This family also includes protein UL70 from cytomegalovirus (CMV, a subgroup of the Herpesviridae) strains, which, by analogy with UL52, is thought to have DNA primase activity. Indeed, CMV strains also possess a DNA helicase-primase complex, the other subunits being protein UL105 (with known similarity to HSV1 UL5) and protein UL102.


Pssm-ID: 367342 [Multi-domain]  Cd Length: 75  Bit Score: 68.98  E-value: 5.08e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1064291325 169 YFFPEELLVYDICKYR-----WCENIGRAHKSNNIMILVDLKNEV------WYQKCHDPVCKaENFKSDCFPLPAE 233
Cdd:pfam03121   1 VFSKEGLNLVQVKRSRrgrnfSCLNIGHRHKSNNVRVFLDLRVDGhglcvtLYQKCFAPKCG-SNYRSTHFSVPVD 75
 
Name Accession Description Interval E-value
PrimPol_RBD cd22256
C-terminal RPA-binding domain (RBD) of DNA-directed primase/polymerase protein and similar ...
 247-325 4.99e-18

C-terminal RPA-binding domain (RBD) of DNA-directed primase/polymerase protein and similar proteins; DNA-directed primase/polymerase protein (PrimPol), also called coiled-coil domain-containing protein 111, is a DNA primase-polymerase required for the maintenance of genome integrity. It facilitates mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions. PrimPol is regulated by single-stranded DNA binding proteins. This model corresponds to the C-terminal RPA-binding domain (RBD) of PrimPol, which interacts directly with the RPA70N domain of RPA70.


Pssm-ID: 412077  Cd Length: 81  Bit Score: 77.44  E-value: 4.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1064291325 247 TTDEADETRSNETQNPHKP-SPSRLSTGASADAVWDNGIDDAYFLEATEDAELAEAAENSLLSYNSEVDEIPDELIIEVL 325
Cdd:cd22256     2 DENGNIKETQNTEDSTPLEsSESSLSISGSSDAEWDNGIDDACFLEATEDAELAEAADNSLSELNDEVDEIPDELLLEAL 81
Herpes_UL52 pfam03121
Herpesviridae UL52/UL70 DNA primase; Herpes simplex virus type 1 DNA replication in host cells ...
 169-233 5.08e-15

Herpesviridae UL52/UL70 DNA primase; Herpes simplex virus type 1 DNA replication in host cells is known to be mediated by seven viral-encoded proteins, three of which form a heterotrimeric DNA helicase-primase complex. This complex consists of UL5, UL8, and UL52 subunits. Heterodimers consisting of UL5 and UL52 have been shown to retain both helicase and primase activities. Nevertheless, UL8 is still essential for replication: though it lacks any DNA binding or catalytic activities, it is involved in the transport of UL5-UL52 and it also interacts with other replication proteins. The molecular mechanisms of the UL5-UL52 catalytic activities are not known. While UL5 is associated with DNA helicase activity and UL52 with DNA primase activity, the helicase activity requires the interaction of UL5 and UL52. It is not known if the primase activity can be maintained by UL52 alone. The region encompassed by residues 610-636 of HSV1 UL52 is thought to contain a divalent metal cation binding motif. Indeed, this region contains several aspartate and glutamate residues that might be involved in divalent cation binding. The biological significance of UL52-UL8 interaction is not known. Yeast two-hybrid analysis together with immunoprecipitation experiments have shown that the HSV1 UL52 region between residues 366-914 is essential for this interaction, while the first 349 N-terminal residues are dispensable. This family also includes protein UL70 from cytomegalovirus (CMV, a subgroup of the Herpesviridae) strains, which, by analogy with UL52, is thought to have DNA primase activity. Indeed, CMV strains also possess a DNA helicase-primase complex, the other subunits being protein UL105 (with known similarity to HSV1 UL5) and protein UL102.


Pssm-ID: 367342 [Multi-domain]  Cd Length: 75  Bit Score: 68.98  E-value: 5.08e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1064291325 169 YFFPEELLVYDICKYR-----WCENIGRAHKSNNIMILVDLKNEV------WYQKCHDPVCKaENFKSDCFPLPAE 233
Cdd:pfam03121   1 VFSKEGLNLVQVKRSRrgrnfSCLNIGHRHKSNNVRVFLDLRVDGhglcvtLYQKCFAPKCG-SNYRSTHFSVPVD 75
 
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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