Detail Information for IndEnz0002019370
IED ID IndEnz0002019370
Enzyme Type ID protease019370
Protein Name Pre-hexon-linking protein VIII
Pre-protein VIII
pVIII

Cleaved into: Hexon-linking protein-N
12.1 kDa protein VIII
Protein VIII-N
; Hexon-linking protein-C
7.6 kDa protein VIII
Protein VIII-C
Gene Name L4
Organism Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Taxonomic Lineage Viruses Varidnaviria Bamfordvirae Preplasmiviricota Tectiliviricetes Rowavirales Adenoviridae Mastadenovirus Human mastadenovirus C Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Enzyme Sequence MSKEIPTPYMWSYQPQMGLAAGAAQDYSTRINYMSAGPHMISRVNGIRAHRNRILLEQAAITTTPRNNLNPRSWPAALVYQESPAPTTVVLPRDAQAEVQMTNSGAQLAGGFRHRVRSPGQGITHLTIRGRGIQLNDESVSSSLGLRPDGTFQIGGAGRPSFTPRQAILTLQTSSSEPRSGGIGTLQFIEEFVPSVYFNPFSGPPGHYPDQFIPNFDAVKDSADGYD
Enzyme Length 227
Uniprot Accession Number P24936
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: [Hexon-linking protein-N]: Structural component of the virion that acts as a cement protein on the capsid interior and which glue the peripentonal hexons and group-of-nine hexons together. {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:25071205}.; FUNCTION: [Hexon-linking protein-C]: Structural component of the virion that acts as a cement protein on the capsid interior and which glue the peripentonal hexons and group-of-nine hexons together. {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:25071205}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (2); Chain (1); Helix (3); Modified residue (3); Peptide (2); Propeptide (1); Sequence conflict (1); Site (2)
Keywords 3D-structure;Capsid protein;Host nucleus;Late protein;Phosphoprotein;Virion
Interact With
Induction INDUCTION: Expressed in the late phase of the viral replicative cycle. {ECO:0000255|HAMAP-Rule:MF_04049}.
Subcellular Location SUBCELLULAR LOCATION: [Hexon-linking protein-C]: Virion {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:25071205}. Note=Located on the inner side of the capsid shell. Present in 120 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:25071205}.; SUBCELLULAR LOCATION: [Pre-hexon-linking protein VIII]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000305}.; SUBCELLULAR LOCATION: [Hexon-linking protein-N]: Virion {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:25071205}. Note=Located on the inner side of the capsid shell. Present in 120 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:25071205}.
Modified Residue MOD_RES 64; /note=Phosphothreonine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04049; MOD_RES 118; /note=Phosphoserine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04049; MOD_RES 174; /note=Phosphoserine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04049
Post Translational Modification PTM: Cleaved by the viral protease during virion maturation. May cause the middle segment to be shed from the capsid. {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:17005667, ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}.
Signal Peptide
Structure 3D Electron microscopy (1); X-ray crystallography (1)
Cross Reference PDB 6B1T; 6CGV;
Mapped Pubmed ID 28978703; 30121295;
Motif
Gene Encoded By
Mass 24,687
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda