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Conserved domains on  [gi|2532990806|ref|WP_290379034|]
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toprim domain-containing protein [Duncaniella muris]

Protein Classification

zf-CHC2 and Toprim_2 domain-containing protein( domain architecture ID 10418264)

zf-CHC2 and Toprim_2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Toprim_2 pfam13155
Toprim-like; This is a family or Toprim-like proteins.
 195-280 1.78e-16

Toprim-like; This is a family or Toprim-like proteins.


:

Pssm-ID: 463793 [Multi-domain]  Cd Length: 88  Bit Score: 72.98  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532990806 195 VFEGFIDYLSALTLGIINgADAIILNSVVNVNKAVPYLKDYT-TINCYLDNDNAGQTALAELKAIYGSI-VIDRSTLYSE 272
Cdd:pfam13155   2 VFEGYIDALSLAQAGIKN-VLYVATLGTALTEAQIKLLKRYPkEVILAFDNDEAGRKAAKRLAELLKEAgVDVKIRLLPD 80


                  ....*...
gi 2532990806 273 FNDLNDFL 280
Cdd:pfam13155  81 GKDWNEYL 88
zf-CHC2 super family cl21601
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
 24-65 1.98e-03

CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.


The actual alignment was detected with superfamily member pfam01807:

Pssm-ID: 451328 [Multi-domain]  Cd Length: 95  Bit Score: 36.84  E-value: 1.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2532990806  24 RKGTRLWYKSPLRQEQTPSFKVETTLNCWYDFGLGRGGNIID 65
Cdd:pfam01807  26 KRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIK 67
 
Name Accession Description Interval E-value
Toprim_2 pfam13155
Toprim-like; This is a family or Toprim-like proteins.
 195-280 1.78e-16

Toprim-like; This is a family or Toprim-like proteins.


Pssm-ID: 463793 [Multi-domain]  Cd Length: 88  Bit Score: 72.98  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532990806 195 VFEGFIDYLSALTLGIINgADAIILNSVVNVNKAVPYLKDYT-TINCYLDNDNAGQTALAELKAIYGSI-VIDRSTLYSE 272
Cdd:pfam13155   2 VFEGYIDALSLAQAGIKN-VLYVATLGTALTEAQIKLLKRYPkEVILAFDNDEAGRKAAKRLAELLKEAgVDVKIRLLPD 80


                  ....*...
gi 2532990806 273 FNDLNDFL 280
Cdd:pfam13155  81 GKDWNEYL 88
TOPRIM_primases cd01029
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
 195-258 5.35e-05

TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.


Pssm-ID: 173779 [Multi-domain]  Cd Length: 79  Bit Score: 40.72  E-value: 5.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2532990806 195 VFEGFIDYLSALTLGIINgadAIILNSVVNVNKAVPYLKDYT-TINCYLDNDNAGQTALAELKAI 258
Cdd:cd01029     5 IVEGYMDVLALHQAGIKN---VVAALGTANTEEQLRLLKRFArTVILAFDNDEAGKKAAARALEL 66
zf-CHC2 pfam01807
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
 24-65 1.98e-03

CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.


Pssm-ID: 426447 [Multi-domain]  Cd Length: 95  Bit Score: 36.84  E-value: 1.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2532990806  24 RKGTRLWYKSPLRQEQTPSFKVETTLNCWYDFGLGRGGNIID 65
Cdd:pfam01807  26 KRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIK 67
DnaG COG0358
DNA primase (bacterial type) [Replication, recombination and repair];
24-65 2.19e-03

DNA primase (bacterial type) [Replication, recombination and repair];


Pssm-ID: 440127 [Multi-domain]  Cd Length: 465  Bit Score: 39.35  E-value: 2.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2532990806  24 RKGTRLWYKSPLRQEQTPSFKVETTLNCWYDFGLGRGGNIID 65
Cdd:COG0358    28 KAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVIS 69
ZnF_CHCC smart00400
zinc finger;
34-65 6.33e-03

zinc finger;


Pssm-ID: 128681 [Multi-domain]  Cd Length: 55  Bit Score: 34.19  E-value: 6.33e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2532990806   34 PLRQEQTPSFKVETTLNCWYDFGLGRGGNIID 65
Cdd:smart00400   6 PFHGEKTPSFSVSPDKQFFHCFGCGAGGNVIS 37
 
Name Accession Description Interval E-value
Toprim_2 pfam13155
Toprim-like; This is a family or Toprim-like proteins.
 195-280 1.78e-16

Toprim-like; This is a family or Toprim-like proteins.


Pssm-ID: 463793 [Multi-domain]  Cd Length: 88  Bit Score: 72.98  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532990806 195 VFEGFIDYLSALTLGIINgADAIILNSVVNVNKAVPYLKDYT-TINCYLDNDNAGQTALAELKAIYGSI-VIDRSTLYSE 272
Cdd:pfam13155   2 VFEGYIDALSLAQAGIKN-VLYVATLGTALTEAQIKLLKRYPkEVILAFDNDEAGRKAAKRLAELLKEAgVDVKIRLLPD 80


                  ....*...
gi 2532990806 273 FNDLNDFL 280
Cdd:pfam13155  81 GKDWNEYL 88
TOPRIM_primases cd01029
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
 195-258 5.35e-05

TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.


Pssm-ID: 173779 [Multi-domain]  Cd Length: 79  Bit Score: 40.72  E-value: 5.35e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2532990806 195 VFEGFIDYLSALTLGIINgadAIILNSVVNVNKAVPYLKDYT-TINCYLDNDNAGQTALAELKAI 258
Cdd:cd01029     5 IVEGYMDVLALHQAGIKN---VVAALGTANTEEQLRLLKRFArTVILAFDNDEAGKKAAARALEL 66
zf-CHC2 pfam01807
CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.
 24-65 1.98e-03

CHC2 zinc finger; This domain is principally involved in DNA binding in DNA primases.


Pssm-ID: 426447 [Multi-domain]  Cd Length: 95  Bit Score: 36.84  E-value: 1.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2532990806  24 RKGTRLWYKSPLRQEQTPSFKVETTLNCWYDFGLGRGGNIID 65
Cdd:pfam01807  26 KRGKDYVGLCPFHHEKTPSFTVSPDKQFYHCFGCGAGGDVIK 67
DnaG COG0358
DNA primase (bacterial type) [Replication, recombination and repair];
24-65 2.19e-03

DNA primase (bacterial type) [Replication, recombination and repair];


Pssm-ID: 440127 [Multi-domain]  Cd Length: 465  Bit Score: 39.35  E-value: 2.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2532990806  24 RKGTRLWYKSPLRQEQTPSFKVETTLNCWYDFGLGRGGNIID 65
Cdd:COG0358    28 KAGRNYKGLCPFHDEKTPSFTVSPEKQFYHCFGCGAGGDVIS 69
ZnF_CHCC smart00400
zinc finger;
34-65 6.33e-03

zinc finger;


Pssm-ID: 128681 [Multi-domain]  Cd Length: 55  Bit Score: 34.19  E-value: 6.33e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2532990806   34 PLRQEQTPSFKVETTLNCWYDFGLGRGGNIID 65
Cdd:smart00400   6 PFHGEKTPSFSVSPDKQFFHCFGCGAGGNVIS 37
 
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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