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Conserved domains on  [gi|568815671|ref|NP_001275597|]
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host cell factor C1 regulator 1 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HPIP super family cl21090
HCF-1 beta-propeller-interacting protein family; HPIP is a small cellular polypeptide that ...
 1-71 2.24e-39

HCF-1 beta-propeller-interacting protein family; HPIP is a small cellular polypeptide that binds to the beta-propeller domain of HCF-1. HPIP regulates HCF-1 activity by modulating its subcellular localization. HCF-1 is a cellular protein required by VP16 to activate the herpes simplex virus- immediate-early genes. VP16 is a component of the viral tegument and, after release into the cell, binds to HCF-1 and translocates to the nucleus to form a complex with the POU domain protein Oct-1 and a VP16-responsive DNA sequence. HPIP-mediated export may provide the pool of cytoplasmic HCF-1 required for import of virion-derived VP16 into the nucleus.


The actual alignment was detected with superfamily member pfam15226:

Pssm-ID: 373659  Cd Length: 133  Bit Score: 126.25  E-value: 2.24e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568815671    1 MATHFSQLSLHNDHPYCSPPMTFSPALPPLRSPCSELLLWRYPGSLIPEALRLLRLGDTPSPPYPATPAGD 71
Cdd:pfam15226  63 MATHFSRLSLHNDHPYCSPPMAFPPALPPLRSPCSELLLWRYPGSLIPEALRLLRLGDTPTPPYPATPAGD 133
 
Name Accession Description Interval E-value
HPIP pfam15226
HCF-1 beta-propeller-interacting protein family; HPIP is a small cellular polypeptide that ...
 1-71 2.24e-39

HCF-1 beta-propeller-interacting protein family; HPIP is a small cellular polypeptide that binds to the beta-propeller domain of HCF-1. HPIP regulates HCF-1 activity by modulating its subcellular localization. HCF-1 is a cellular protein required by VP16 to activate the herpes simplex virus- immediate-early genes. VP16 is a component of the viral tegument and, after release into the cell, binds to HCF-1 and translocates to the nucleus to form a complex with the POU domain protein Oct-1 and a VP16-responsive DNA sequence. HPIP-mediated export may provide the pool of cytoplasmic HCF-1 required for import of virion-derived VP16 into the nucleus.


Pssm-ID: 373659  Cd Length: 133  Bit Score: 126.25  E-value: 2.24e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568815671    1 MATHFSQLSLHNDHPYCSPPMTFSPALPPLRSPCSELLLWRYPGSLIPEALRLLRLGDTPSPPYPATPAGD 71
Cdd:pfam15226  63 MATHFSRLSLHNDHPYCSPPMAFPPALPPLRSPCSELLLWRYPGSLIPEALRLLRLGDTPTPPYPATPAGD 133
 
Name Accession Description Interval E-value
HPIP pfam15226
HCF-1 beta-propeller-interacting protein family; HPIP is a small cellular polypeptide that ...
 1-71 2.24e-39

HCF-1 beta-propeller-interacting protein family; HPIP is a small cellular polypeptide that binds to the beta-propeller domain of HCF-1. HPIP regulates HCF-1 activity by modulating its subcellular localization. HCF-1 is a cellular protein required by VP16 to activate the herpes simplex virus- immediate-early genes. VP16 is a component of the viral tegument and, after release into the cell, binds to HCF-1 and translocates to the nucleus to form a complex with the POU domain protein Oct-1 and a VP16-responsive DNA sequence. HPIP-mediated export may provide the pool of cytoplasmic HCF-1 required for import of virion-derived VP16 into the nucleus.


Pssm-ID: 373659  Cd Length: 133  Bit Score: 126.25  E-value: 2.24e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568815671    1 MATHFSQLSLHNDHPYCSPPMTFSPALPPLRSPCSELLLWRYPGSLIPEALRLLRLGDTPSPPYPATPAGD 71
Cdd:pfam15226  63 MATHFSRLSLHNDHPYCSPPMAFPPALPPLRSPCSELLLWRYPGSLIPEALRLLRLGDTPTPPYPATPAGD 133
 
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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