Detail Information for IndEnz0002018974
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