| IED ID | IndEnz0002018974 |
| Enzyme Type ID | protease018974 |
| Protein Name |
Hexon protein CP-H Protein II |
| Gene Name | L3 |
| Organism | Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
| Taxonomic Lineage | Viruses Varidnaviria Bamfordvirae Preplasmiviricota Tectiliviricetes Rowavirales Adenoviridae Mastadenovirus Human mastadenovirus C Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
| Enzyme Sequence | MATPSMMPQWSYMHISGQDASEYLSPGLVQFARATETYFSLNNKFRNPTVAPTHDVTTDRSQRLTLRFIPVDREDTAYSYKARFTLAVGDNRVLDMASTYFDIRGVLDRGPTFKPYSGTAYNALAPKGAPNSCEWEQTEDSGRAVAEDEEEEDEDEEEEEEEQNARDQATKKTHVYAQAPLSGETITKSGLQIGSDNAETQAKPVYADPSYQPEPQIGESQWNEADANAAGGRVLKKTTPMKPCYGSYARPTNPFGGQSVLVPDEKGVPLPKVDLQFFSNTTSLNDRQGNATKPKVVLYSEDVNMETPDTHLSYKPGKGDENSKAMLGQQSMPNRPNYIAFRDNFIGLMYYNSTGNMGVLAGQASQLNAVVDLQDRNTELSYQLLLDSIGDRTRYFSMWNQAVDSYDPDVRIIENHGTEDELPNYCFPLGGIGVTDTYQAIKANGNGSGDNGDTTWTKDETFATRNEIGVGNNFAMEINLNANLWRNFLYSNIALYLPDKLKYNPTNVEISDNPNTYDYMNKRVVAPGLVDCYINLGARWSLDYMDNVNPFNHHRNAGLRYRSMLLGNGRYVPFHIQVPQKFFAIKNLLLLPGSYTYEWNFRKDVNMVLQSSLGNDLRVDGASIKFDSICLYATFFPMAHNTASTLEAMLRNDTNDQSFNDYLSAANMLYPIPANATNVPISIPSRNWAAFRGWAFTRLKTKETPSLGSGYDPYYTYSGSIPYLDGTFYLNHTFKKVAITFDSSVSWPGNDRLLTPNEFEIKRSVDGEGYNVAQCNMTKDWFLVQMLANYNIGYQGFYIPESYKDRMYSFFRNFQPMSRQVVDDTKYKEYQQVGILHQHNNSGFVGYLAPTMREGQAYPANVPYPLIGKTAVDSITQKKFLCDRTLWRIPFSSNFMSMGALTDLGQNLLYANSAHALDMTFEVDPMDEPTLLYVLFEVFDVVRVHQPHRGVIETVYLRTPFSAGNATT |
| Enzyme Length | 968 |
| Uniprot Accession Number | P03277 |
| 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, ECO:0000269|PubMed:20798312}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (49); Chain (1); Compositional bias (1); Helix (30); Initiator methionine (1); Modified residue (4); Region (1); Site (1); Turn (10) |
| Keywords | 3D-structure;Acetylation;Capsid protein;Cytoplasmic inwards viral transport;Direct protein sequencing;Host nucleus;Host-virus interaction;Late protein;Microtubular inwards viral transport;Phosphoprotein;Reference proteome;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, ECO:0000269|PubMed:20798312}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04051, ECO:0000269|PubMed:20798312}. 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, ECO:0000269|PubMed:4823869"; MOD_RES 182; /note="Phosphoserine; by host"; /evidence="ECO:0000255|HAMAP-Rule:MF_04051, ECO:0000269|PubMed:22939182"; MOD_RES 283; /note="Phosphoserine; by host"; /evidence="ECO:0000255|HAMAP-Rule:MF_04051, ECO:0000269|PubMed:22939182"; MOD_RES 956; /note="Phosphotyrosine; by host"; /evidence="ECO:0000269|PubMed:22939182" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1P2Z; |
| Mapped Pubmed ID | 12915569; |
| Motif | |
| Gene Encoded By | |
| Mass | 109,153 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |