IED ID | IndEnz0002006008 |
Enzyme Type ID | protease006008 |
Protein Name |
Hexon protein CP-H Protein II |
Gene Name | L3 |
Organism | Human adenovirus F serotype 40 (HAdV-40) (Human adenovirus 40) |
Taxonomic Lineage | Viruses Varidnaviria Bamfordvirae Preplasmiviricota Tectiliviricetes Rowavirales Adenoviridae Mastadenovirus Human mastadenovirus F Human adenovirus F serotype 40 (HAdV-40) (Human adenovirus 40) |
Enzyme Sequence | MATPSMMPQWSYMHIAGQDASEYLSPGLVQFARATDTYFSLGNKFRNPTVAPTHDVTTDRSQRLTLRFVPVDREETAYSYKVRFTLAVGDNRVLDMASTYFDIRGVLDRGPSFKPYSGTAYNSLAPKGAPNPSQWTNQNKTNSFGQAPYIGQKITNQGVQVGSDSNNRDVFADKTYQPEPQVGQTQWNINPMQNAAGRILKQTTPMQPCYGSYARPTNEKGGQAKLVKNDDNQTTTTNVGLNFFTTATETANFSPKVVLYSEDVNLEAPDTHLVFKPDVNGTSAELLLGQQAAPNRPNYIGFRDNFIGLMYYNSTGNMGVLAGQASQLNAVVDLQDRNTELSYQLMLDALGDRSRYFSMWNQAVDSYDPDVRIIENHGVEDELPNYCFPLNGQGISNSYQGVKTDNGTNWSQNNTDVSSNNEISIGNVFAMEINLAANLWRSFLYSNVALYLPDSYKITPDNITLPDNKNTYAYMNGRVAVPSALDTYVNIGARWSPDPMDNVNPFNHHRNAGLRYRSMLLGNGRYVPFHIQVPQKFFAIKNLLLLPGSYTYEWNFRKDVNMILQSSLGNDLRVDGASVRFDSINLYANFFPMAHNTASTLEAMLRNDTNDQSFNDYLCAANMLYPIPANATSVPISIPSRNWAAFRGWSFTRLKTKETPSLGSGFDPYFTYSGSVPYLDGTFYLNHTFKKVSVMFDSSVSWPGNDRLLTPNEFEIKRTVDGEGYNVAQCNMTKDWFLIQMLSHYNIGYQGFHVPESYKDRMYSFFRNFQPMSRQVVDTTTYTEYQNVTLPFQHNNSGFVGYMGPAIREGQAYPANYPYPLIGQTAVPSLTQKKFLCDRTMWRIPFSSNFMSMGALTDLGQNMLYANSAHALDMTFEVDPMDEPTLLYVLFEVFDVVRIHQPHRGVIEAVYLRTPFSAGNATT |
Enzyme Length | 923 |
Uniprot Accession Number | P11819 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. {ECO:0000255|HAMAP-Rule:MF_04051}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Initiator methionine (1); Modified residue (2); Sequence conflict (1); Site (1) |
Keywords | Acetylation;Capsid protein;Cytoplasmic inwards viral transport;Host nucleus;Host-virus interaction;Late protein;Microtubular inwards viral transport;Phosphoprotein;T=25 icosahedral capsid protein;Virion;Virus entry into host cell |
Interact With | |
Induction | INDUCTION: Expressed in the late phase of the viral replicative cycle. {ECO:0000255|HAMAP-Rule:MF_04051}. |
Subcellular Location | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04051}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04051}. Note=Forms the capsid icosahedric shell. Present in 720 copies per virion, assembled in 240 trimers. {ECO:0000255|HAMAP-Rule:MF_04051}. |
Modified Residue | MOD_RES 2; /note=N-acetylalanine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04051; MOD_RES 911; /note=Phosphotyrosine; by host; /evidence=ECO:0000255|HAMAP-Rule:MF_04051 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 103,953 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |