IED ID | IndEnz0002013125 |
Enzyme Type ID | protease013125 |
Protein Name |
Preterminal protein pTP Bellett protein Precursor terminal protein Cleaved into: Intermediate terminal protein iTP ; Terminal protein TP |
Gene Name | PTP |
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 | MALSVNDCARLTGQSVPTMEHFLPLRNIWNRVRDFPRASTTAAGITWMSRYIYGYHRLMLEDLAPGAPATLRWPLYRQPPPHFLVGYQYLVRTCNDYVFDSRAYSRLRYTELSQPGHQTVNWSVMANCTYTINTGAYHRFVDMDDFQSTLTQVQQAILAERVVADLALLQPMRGFGVTRMGGRGRHLRPNSAAAVAIDARDAGQEEGEEEVPVERLMQDYYKDLRRCQNEAWGMADRLRIQQAGPKDMVLLSTIRRLKTAYFNYIISSTSARNNPDRHPLPPATVLSLPCDCDWLDAFLERFSDPVDADSLRSLGGGVPTQQLLRCIVSAVSLPHGSPPPTHNRDMTGGVFQLRPRENGRAVTETMRRRRGEMIERFVDRLPVRRRRRRVPPPPPPPEEEEEGEALMEEEIEEEEAPVAFEREVRDTVAELIRLLEEELTVSARNSQFFNFAVDFYEAMERLEALGDINESTLRRWVMYFFVAEHTATTLNYLFQRLRNYAVFARHVELNLAQVVMRARDAEGGVVYSRVWNEGGLNAFSQLMARISNDLAATVERAGRGDLQEEEIEQFMAEIAYQDNSGDVQEILRQAAVNDTEIDSVELSFRFKLTGPVVFTQRRQIQEINRRVVAFASNLRAQHQLLPARGADVPLPPLPAGPEPPLPPGARPRHRF |
Enzyme Length | 671 |
Uniprot Accession Number | P03269 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Protein covalently bound to the viral DNA that acts as a primer for viral genomic replication by DNA strand displacement. Assembles on the viral origin of replication in an initiation complex with viral polymerase, DBP, host NFIA and host POU2F1/OCT1. During initiation, the polymerase covalently couples the first dCTP with Ser-580 of pTP. The terminal protein stimulates the template activity over 20 fold compared to protein-free templates. Neo-synthesized viral genomes are linked to two preterminal proteins, one for each 5' end. These new genomes are encapsidated in the nucleus, and during capsid maturation by viral protease, preterminal protein is first cleaved into intermediary (iTP), then into mature TP. May play a role in host nuclear matrix localization of genomic DNA. {ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000269|PubMed:1291241}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (3); Compositional bias (1); Erroneous initiation (1); Modified residue (1); Motif (1); Mutagenesis (6); Region (2); Site (3) |
Keywords | Covalent protein-DNA linkage;DNA replication;DNA-binding;Direct protein sequencing;Host nucleus;Phosphoprotein;Reference proteome;Viral DNA replication |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000255|HAMAP-Rule:MF_04061}. |
Modified Residue | MOD_RES 580; /note="O-(5'-phospho-DNA)-serine"; /evidence="ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000269|PubMed:7142163" |
Post Translational Modification | PTM: Preterminal protein is used to replicate viral genome, upon genomic encapsidation it is processed first into iTP and finally into TP by adenovirus protease. {ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000269|PubMed:9261355}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 380..389; /note="Nuclear localization signal"; /evidence="ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000269|PubMed:3203379" |
Gene Encoded By | |
Mass | 76,543 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |