Detail Information for IndEnz0002015664
IED ID IndEnz0002015664
Enzyme Type ID protease015664
Protein Name Non-structural polyprotein 1AB
Cleaved into: VPg; Protein p19; Transmembrane protein 1A; Serine protease p27
p27
EC 3.4.21.-
; Protein p20; RNA-directed RNA polymerase p57
p57
EC 2.7.7.48
Gene Name ORF1
Organism Human astrovirus-5 (HAstV-5)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Stelpaviricetes Stellavirales Astroviridae Mamastrovirus Mamastrovirus 1 Human astrovirus-5 (HAstV-5)
Enzyme Sequence MAHGEPYYSSKPDKDFNFGSTMARRQMTPTMVTKLPKFVRNSPQVYDWIVRGLIFPTTGKTYFQRVVVITGGFEDGTYGSFAFDGREWVEIYPIEHLNLMSSLKLIHKANALQERLRLSQEEKATLTLDVQFLQHENVRLKELISKPEPRKIQMKWIIVGAVLTFLSLIPGGYAQSQTNNTIFTDVIAACKYSTETLTENLDLRIKLALANITISDKLDAVRQILNFAFVPRSHWLRTVFYYIHYYEMWNIFMFVLAIGTVMRSTRPGTDLITLATSHLSGFRMAVLPTIPFHTTMTLWVMNTLMVCYYFDNLLAITMAILAPILGIIFLCFMEDSNYVSQIRGLIATAVLIAGGHACLTLTGTTTSLFVVILTCRFVRMATIFIGTRFEIRDANGKVVATVPTRIKNAAFDFFQRLKQSGVRVGVNEFVVIKPGALCVIDTPEGKGTGFFSGNDIVTAAHVVGNNTFVNVCYEGLMYEAKVRYMPEKDIAFITCPGDLHPTARLKLSKNPDYSCVTVMAYVNEDLVVSTAAAMVHGNTLSYAVRTQDGMSGAPVCDKYGRVLAVHQTNTGYTGGAVIIDPADFHPVKAPSQVELLKEEIERLKAQLNSAAENPSTVITQQPTATLEQKSVNDSDVVDLVRTAMEREMKILRDEINGILAPFLQKKKGKTKHGRGRVRRNLRKGVKLLTEEEYRELLEKGLDRETFLDLIDRIIGERSGYPDYDDEDYYDEDDDGWGMVGDDVEFDYTEVINFDQAKPTPAPRTTKPKPCPEPEAETQPLDLSQKKDKQLEHEQQVVKPTKPQKNDPQPYSQTYGKAPIWESYDFDWDEDDAKFILPAPPRLTKADEIVLGSKIVKLRTIIETAIKTQNYSALPEAVFELDKAAYEAGLEGFLQRVKSKNKAPKKLQRAPEDQGAQNYHSLDAWKSLLEPPRERRCVPANFPLLGHLPIDRPIFDDKKPRDDLLGLLPEPTWHAFEEYGPTTWGPQAFIKSFDKFFYAEPIDFFSEYPQLCAFADWATYREFRYLEDTRVIHITATEKNTDSTPAYPKMNYFDTEEKYLESYGWAPYIREFTRVFKGDKPEVLWYLFLKKEIIKEEKIRNSDIRQIVCADPIYTRIGACLEAHQNALMKQHTETSVGQCGWSPMEGGFKKTMQRLVNKGNKYFIEFDWTRYDGTIPPSLFRHIKEIRWNFINKDQREKYRHVHEWYVDNLLNRHVLLPSGEVTLQTRGNPSGQFSTTMDNNMINFWLQAFEFAYFNGPNKDLWKTYDTVVYGDDRLSTTPSVPENYEERVIDMYRDIFGMWVKPGKVICRESIVGLSFCGFTVNADLEPVPTSPEKLMASLLKPYKILPDLESLHGKLLCYQLLAAFMAEDHPFKVYVEHCLSRTAKQLRDSGLPARLTEEQLHRIWRGGPKKCDG
Enzyme Length 1416
Uniprot Accession Number Q4TWH8
Absorption
Active Site ACT_SITE 461; /note=Charge relay system; for serine protease activity; /evidence=ECO:0000250; ACT_SITE 489; /note=Charge relay system; for serine protease activity; /evidence=ECO:0000250; ACT_SITE 551; /note=Charge relay system; for serine protease activity; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
DNA Binding
EC Number 3.4.21.-; 2.7.7.48
Enzyme Function FUNCTION: [Non-structural polyprotein 1AB]: Contains the viral protease participating in the cleavage of the polyprotein into functional products. It contains also the activities necessary for replication of genomic RNA, as well as transcription of subgenomic mRNA.; FUNCTION: [VPg]: Protein covalently attached to the 5' extremity of the genomic and subgenomic RNAs. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (7); Coiled coil (2); Compositional bias (1); Domain (1); Region (1); Site (5); Transmembrane (5)
Keywords ATP-binding;Coiled coil;Host membrane;Hydrolase;Membrane;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Ribosomal frameshifting;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification PTM: Cleaved presumably by viral and host proteases. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 161,728
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda