Annotation

PREDICTED:_glypican-5_[Papilio_xuthus]

Description

Cell surface proteoglycan that bears heparan sulfate.      

Annotation

minichromosome_maintenance_complex_component_7_[Bombyx_mori]

Description

Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.       + More
Acts as component of the Mcm2-7 complex (Mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the Mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.      

Annotation

minichromosome_maintenance_complex_component_7_[Bombyx_mori]

Description

Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.       + More
Acts as component of the Mcm2-7 complex (Mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the Mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.      
Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development (By similarity).      
Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development.      

Annotation

PREDICTED:_DNA_polymerase_alpha_catalytic_subunit_isoform_X2_[Bombyx_mori]

Description

Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes (By similarity).       + More
Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. In the cytosol, responsible for a substantial proportion of the physiological concentration of cytosolic RNA:DNA hybrids, which are necessary to prevent spontaneous activation of type I interferon responses.      

Annotation

PREDICTED:_LOW_QUALITY_PROTEIN:_uncharacterized_protein_CG7065-like_[Bombyx_mori]

Description

F:nucleic acid binding

Annotation

PREDICTED:_LOW_QUALITY_PROTEIN:_uncharacterized_protein_CG7065-like_[Bombyx_mori]

Description

F:nucleic acid binding

Annotation

PREDICTED:_LOW_QUALITY_PROTEIN:_uncharacterized_protein_CG7065-like_[Bombyx_mori]

Description

F:nucleic acid binding

Annotation

PREDICTED:_LOW_QUALITY_PROTEIN:_uncharacterized_protein_CG7065-like_[Bombyx_mori]

Description

Zinc finger C2H2-type

Annotation

ribosomal_protein_S8_[Bombyx_mori]

Description

ribosomal_protein_S8_[Bombyx_mori]

Annotation

PREDICTED:_serine_protease_inhibitor_34_isoform_X1_[Bombyx_mori]

Description

PREDICTED:_serine_protease_inhibitor_34_isoform_X1_[Bombyx_mori]

Annotation

mago_nashi_[Bombyx_mori]

Description

mago_nashi_[Bombyx_mori]

Annotation

PREDICTED:_maternal_protein_pumilio-like_[Bombyx_mori]

Description

PREDICTED:_maternal_protein_pumilio-like_[Bombyx_mori]

Annotation

PREDICTED:_pumilio_homolog_2_isoform_X1_[Bombyx_mori]

Description

PREDICTED:_pumilio_homolog_2_isoform_X1_[Bombyx_mori]

Annotation

hypothetical_protein_KGM_08054_[Danaus_plexippus]