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Conserved domains on  [gi|1864381942|ref|YP_009886756|]
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DNA helicase loader [Acinetobacter phage vB_AbaM_Kimel]

Protein Classification

59 family protein( domain architecture ID 11476030)

59 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
59 PHA02559
59 protein; Provisional
 1-216 2.08e-84

59 protein; Provisional


:

Pssm-ID: 222876 [Multi-domain]  Cd Length: 216  Bit Score: 249.17  E-value: 2.08e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942   1 MVKLLLPPNNNIRIDAKSVYNLYLQLKNHFNGRRCVIKSSWRMKVSDASYAKRKDKFFFEKLSEKFTLKELCLIFISNLV 80
Cdd:PHA02559    1 MIKLRMPPDPDRRINGKSVYKLYLMMKQHFAGKYDVIKYNWKMRASDAAFNKRRDKYFFEKLAEKYTLKELYDIFLSNFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942  81 ANQDAWIGEISDSDAVNFYKTYLARLRTVMTRYEDDVKNIYYFSQKVNVKtLNDIFVYNESIQSSYIFKLLQSGIISFET 160
Cdd:PHA02559   81 ANPDAWIGDISDADALTFYREYIGRLERFSYKFKEDVKNLYYFSKKVEVP-LKKIFEYNKKSHTSYIFKLLQSGEISFET 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1864381942 161 FIMLDSFLNIIEEHDKH-DNIIWSSYSVRLKAYRKIFIVSSDECKAKFISAIKAAKF 216
Cdd:PHA02559  160 FLILDSFLGIIDKHDKVlDDLIWQNYSTKLKAYRKLLVIDCEKAKKLFIQTVKECKE 216
 
Name Accession Description Interval E-value
59 PHA02559
59 protein; Provisional
 1-216 2.08e-84

59 protein; Provisional


Pssm-ID: 222876 [Multi-domain]  Cd Length: 216  Bit Score: 249.17  E-value: 2.08e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942   1 MVKLLLPPNNNIRIDAKSVYNLYLQLKNHFNGRRCVIKSSWRMKVSDASYAKRKDKFFFEKLSEKFTLKELCLIFISNLV 80
Cdd:PHA02559    1 MIKLRMPPDPDRRINGKSVYKLYLMMKQHFAGKYDVIKYNWKMRASDAAFNKRRDKYFFEKLAEKYTLKELYDIFLSNFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942  81 ANQDAWIGEISDSDAVNFYKTYLARLRTVMTRYEDDVKNIYYFSQKVNVKtLNDIFVYNESIQSSYIFKLLQSGIISFET 160
Cdd:PHA02559   81 ANPDAWIGDISDADALTFYREYIGRLERFSYKFKEDVKNLYYFSKKVEVP-LKKIFEYNKKSHTSYIFKLLQSGEISFET 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1864381942 161 FIMLDSFLNIIEEHDKH-DNIIWSSYSVRLKAYRKIFIVSSDECKAKFISAIKAAKF 216
Cdd:PHA02559  160 FLILDSFLGIIDKHDKVlDDLIWQNYSTKLKAYRKLLVIDCEKAKKLFIQTVKECKE 216
T4_Gp59_N pfam08993
T4 gene Gp59 loader of gp41 DNA helicase; Bacteriophage T4 gene-59 helicase assembly protein ...
 14-106 8.59e-35

T4 gene Gp59 loader of gp41 DNA helicase; Bacteriophage T4 gene-59 helicase assembly protein is required for recombination-dependent DNA replication, which is the predominant mode of DNA replication in the late stage of T4 infection. T4 gene-59 helicase assembly protein accelerates the loading of the T4 gene-41 helicase during DNA synthesis by the T4 replication system in vitro. T4 gene-59 helicase assembly protein binds to both T4 gene-41 helicase and T4 gene-32 single-stranded DNA binding protein, and to single and double-stranded DNA. The structure of T4 gene-59 helicase assembly protein reveals a novel alpha-helical bundle fold with two domains of similar size, this being the N-terminal domain that consists of six alpha-helices linked by loop segments and short turns. The surface of the domain contains large regions of exposed hydrophobic residues and clusters of acidic and basic residues. This domain has structural similarity to members of the high-mobility-group (HMG) family of DNA minor groove binding proteins including rat HMG1A and lymphoid enhancer-binding factor, and is required for binding of the helicase to the DNA minor groove.


Pssm-ID: 401080  Cd Length: 93  Bit Score: 118.91  E-value: 8.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942  14 IDAKSVYNLYLQLKNHFNGRRCVIKSSWRMKVSDASYAKRKDKFFFEKLSEKFTLKELCLIFISNLVANQDAWIGEISDS 93
Cdd:pfam08993   1 IDGKSVFKLYCAIKAHMNGKYDIIKYKLCMKTPDAAFEKRRDKVFFEKLAEKLKLKDCALIFISNLAANPDAIIGDIADA 80

                          90
                  ....*....|...
gi 1864381942  94 DAVNFYKTYLARL 106
Cdd:pfam08993  81 DAHEFWLEHIGFL 93
 
Name Accession Description Interval E-value
59 PHA02559
59 protein; Provisional
 1-216 2.08e-84

59 protein; Provisional


Pssm-ID: 222876 [Multi-domain]  Cd Length: 216  Bit Score: 249.17  E-value: 2.08e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942   1 MVKLLLPPNNNIRIDAKSVYNLYLQLKNHFNGRRCVIKSSWRMKVSDASYAKRKDKFFFEKLSEKFTLKELCLIFISNLV 80
Cdd:PHA02559    1 MIKLRMPPDPDRRINGKSVYKLYLMMKQHFAGKYDVIKYNWKMRASDAAFNKRRDKYFFEKLAEKYTLKELYDIFLSNFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942  81 ANQDAWIGEISDSDAVNFYKTYLARLRTVMTRYEDDVKNIYYFSQKVNVKtLNDIFVYNESIQSSYIFKLLQSGIISFET 160
Cdd:PHA02559   81 ANPDAWIGDISDADALTFYREYIGRLERFSYKFKEDVKNLYYFSKKVEVP-LKKIFEYNKKSHTSYIFKLLQSGEISFET 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1864381942 161 FIMLDSFLNIIEEHDKH-DNIIWSSYSVRLKAYRKIFIVSSDECKAKFISAIKAAKF 216
Cdd:PHA02559  160 FLILDSFLGIIDKHDKVlDDLIWQNYSTKLKAYRKLLVIDCEKAKKLFIQTVKECKE 216
T4_Gp59_N pfam08993
T4 gene Gp59 loader of gp41 DNA helicase; Bacteriophage T4 gene-59 helicase assembly protein ...
 14-106 8.59e-35

T4 gene Gp59 loader of gp41 DNA helicase; Bacteriophage T4 gene-59 helicase assembly protein is required for recombination-dependent DNA replication, which is the predominant mode of DNA replication in the late stage of T4 infection. T4 gene-59 helicase assembly protein accelerates the loading of the T4 gene-41 helicase during DNA synthesis by the T4 replication system in vitro. T4 gene-59 helicase assembly protein binds to both T4 gene-41 helicase and T4 gene-32 single-stranded DNA binding protein, and to single and double-stranded DNA. The structure of T4 gene-59 helicase assembly protein reveals a novel alpha-helical bundle fold with two domains of similar size, this being the N-terminal domain that consists of six alpha-helices linked by loop segments and short turns. The surface of the domain contains large regions of exposed hydrophobic residues and clusters of acidic and basic residues. This domain has structural similarity to members of the high-mobility-group (HMG) family of DNA minor groove binding proteins including rat HMG1A and lymphoid enhancer-binding factor, and is required for binding of the helicase to the DNA minor groove.


Pssm-ID: 401080  Cd Length: 93  Bit Score: 118.91  E-value: 8.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942  14 IDAKSVYNLYLQLKNHFNGRRCVIKSSWRMKVSDASYAKRKDKFFFEKLSEKFTLKELCLIFISNLVANQDAWIGEISDS 93
Cdd:pfam08993   1 IDGKSVFKLYCAIKAHMNGKYDIIKYKLCMKTPDAAFEKRRDKVFFEKLAEKLKLKDCALIFISNLAANPDAIIGDIADA 80

                          90
                  ....*....|...
gi 1864381942  94 DAVNFYKTYLARL 106
Cdd:pfam08993  81 DAHEFWLEHIGFL 93
T4_Gp59_C pfam08994
T4 gene Gp59 loader of gp41 DNA helicase C-term; Bacteriophage T4 gene-59 helicase assembly ...
 113-215 3.07e-25

T4 gene Gp59 loader of gp41 DNA helicase C-term; Bacteriophage T4 gene-59 helicase assembly protein is required for recombination-dependent DNA replication, which is the predominant mode of DNA replication in the late stage of T4 infection. T4 gene-59 helicase assembly protein accelerates the loading of the T4 gene-41 helicase during DNA synthesis by the T4 replication system in vitro. T4 gene-59 helicase assembly protein binds to both T4 gene-41 helicase and T4 gene-32 single-stranded DNA binding protein, and to single and double-stranded DNA. The structure of T4 gene-59 helicase assembly protein reveals a novel alpha-helical bundle fold with two domains of similar size, this being the C-terminal domain that consists of seven alpha-helices with short intervening loops and turns. The surface of the domain contains large regions of exposed hydrophobic residues and clusters of acidic and basic residues. The hydrophobic region on the 'bottom' surface of the domain near the C-terminal helix binds the leading strand DNA, whilst the hydrophobic region on the 'top' surface of the domain lies between the two arms of the fork DNA, allowing for T4 gene 41 helicase binding and assembly into a hexameric complex around the lagging strand.


Pssm-ID: 401081  Cd Length: 109  Bit Score: 95.10  E-value: 3.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864381942 113 YEDDVKNIYYFSQKVNVKTLNDIFV--YNESIQSSYIFKLLQSGIISFETFIMLDSFLNIIEEHDKH----DNIIWSSYS 186
Cdd:pfam08994   1 FEEDILNIFTFIKKVENKAFKDIFRgeGHPKVQSSVIFKLLLRNIISFETFIILDRFLNFVPIIDKHdeqsDDIFWHEFK 80

                          90       100
                  ....*....|....*....|....*....
gi 1864381942 187 VRLKAYRKIFIVSSDECKAKFISAIKAAK 215
Cdd:pfam08994  81 IKAKAYDKILKIDEEKAKELFIETKKQCK 109
 
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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