Detail Information for IndEnz0002001194
IED ID IndEnz0002001194
Enzyme Type ID protease001194
Protein Name Replicase polyprotein 1ab
Cleaved into: Leader protease
L-Pro
EC 3.4.22.-
Papain-like cysteine proteinase
PCP
; Methyltransferase/helicase/RNA-directed RNA polymerase
EC 2.1.1.-
EC 2.7.7.48
EC 3.6.4.13
Gene Name 1a-1b
Organism Beet yellows virus (isolate Ukraine) (BYV) (Sugar beet yellows virus)
Taxonomic Lineage Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Martellivirales Closteroviridae Closterovirus Beet yellows virus Beet yellows virus (isolate Ukraine) (BYV) (Sugar beet yellows virus)
Enzyme Sequence MAFLNVSAVPSCAFAPAFAPHAGASPIVPDSFPCVPRYSDDISHFRLTLSLDFSVPRPLSLNARVHLSASTDNPLPSLPLGFHAETFVLELNGSSAPFSIPSRHIDFVVNRPFSVFPTEVLSVSSLRTPSRLFALLCDFFLYCSKPGPCVEIASFSTPPPCLVSNCVAQIPTHAEMESIRFPTKTLPAGRFLQFHKRKYTKRPETLIIHESGLALKTSALGVTSKPNSRPITVKSASGEKYEAYEISRKDFERSRRRQQTPRVRSHKPRKINKAVEPFFFPEEPKKDKRKRASLPTEDEGFITFGTLRFPLSETPKEEPRLPKFREVEIPVVKKHAVPAVVSKPVRTFRPVATTGAEYVNARNQCSRRPRNHPILRSASYTFGFKKMPLQRFMKEKKEYYVKRSKVVSSCSVTKSPLEALASILKNLPQYSYNSERLKFYDHFIGDDFEIEVHPLRGGKLSVLLILPKGEAYCVVTAATPQYHAALTIARGDRPRVGELLQYRPGEGLCYLAHAALCCALQKRTFREEDFFVGMYPTKFVFAKRLTEKLGPSALKHPVRGRQVSRSLFHCDVASAFSSPFYSLPRFIGGVEEEAPEITSSLKHKAIESVYERVSIHKDNLLARSVEKDLIDFKDEIKSLSKEKRSVTVPFYMGEAVQSGLTRAYPQFNLSFTHSVYSDHPAAAGSRLLENETLASMAKSSFSDIGGCPLFHIKRGSTDYHVCRPIYDMKDAQRRVSRELQARGLVENLSREQLVEAQARVSVCPHTLGNCNVKSDVLIMVQVYDASLNEIASAMVLKESKVAYLTMVTPGELLDEREAFAIDALGCDVVVDTRRDMVQYKFGSSCYCHKLSNIKSIMLTPAFTFSGNLFSVEMYENRMGVNYYKITRSAYSPEIRGVKTLRYRRACTEVVQVKLPRFDKTLKTFLSGYDYIYLDAKFVSRVFDYVVSNCSVVNSKTFEWVWSYIKSSKSRVVISGKVIHRDVHIDLKHSECFAAVMLAVGVRSRTTTEFLAKNLNYYTGDASCFETIRFLFREWSRRAYAEINRSFRKLMKSILSAGLDYEFLDLDNSLQHLLEYSEVEVRVSIAQNGEVDCNEENRVLTEIIAEAADRKSIAQGLSGALSSVPTQPRGGLRGGSRRSGVSFLYNLVEEVGNLFFSVGDAVRFLVKVFKTFSDSPIFRVVRMFLDLAEAASPFVSVVSLCAWLREAVSAFSSWVADRTVSESVKTFVNRTVKRFLNFMSAKTLTKKFFRFFLSASALAKTVVRKAKVILEAYWEVWFESILSDSGEYSAVEFCSSVVITLLTNSGRLLPGFSPSAIITEVLLDLATKISIEVLLKQISPADSTASSALYRRVLSEILSNFRTMGEHGIFTKVFLLCGFLPVFVRKCVALCVPGDMATYARFLEYGVDDLFFLGRSVNSIKNYLCVVAAGLVDSIVDSVVLKLSGVAKERVLGFKSKIIKNFLNVFRKAKVVTRTSSSTDLSEDEYFSCDESKPGLRGGSSRFTLSRLLDIFFNFLKSSKLVIENACFSAYERIERNMKLYFFPLNSSEEEARRLIRCAGDFDYLSDSAFDEDEMLRQAFEQYYSSDDESVTYDGKPTVLRSYLNVSRRFLETFCNGPKFFVKVSNYFKALYSRLLRVLPWVDRNLSDSPGLKGGNEKALLAKFFKTCVITACECVSQICCLRLIRLCWGTPACGLVRLFYITYSSTRVLSRVVVAVAVCPLLVRNELDGLSDGLTNMGVSVFRRLFVALRRALSAYSNSALRRKIIEFIFGNIHHPFDVAVIETNEVAPEPLSPEVDIDVDCDFGSDSESVSSDEVASNPRPGLHGGSRRSSNFLTSLVKVVFKLARRIPRLLFRLRNFVAYFVERRLASKRLKTFIGLARLFDNFSLTSVVYLLQEYDSVLNAFIDVELILLNSGSVNVLPLVSWVRGSLTKLAEAIVGSGFASFLGRMCCRVSDWCSSSSNAGCNFMSPVRTKGKFVPPSSSGSTASMYERLEALESDIREHVLSTCRVGSDEEEERPKEVTEPGIEHTSEDVVPIRSHSQPLSGGECSYSEDREENERANLLPHVSKIVSERRGLETARRNKRTLHGVSEFLNAINTSNEQPRPIIVDHSPESRALTNSVREFYYLQELALFELSCKLREYYDQLKVANFNRQECLCDKDEDMFVLRAGQGVVSGRNSRLPLKHFKGHEFCFRSGGLVPYDGTSRVDTIFHTQTNFVSANALLSGYLSYRTFTFTNLSANVLLYEAPPGGGKTTTLIKVFCETFSKVNSLILTANKSSREEILAKVNRIVLDEGDTPLQTRDRILTIDSYLMNNRGLTCKVLYLDECFMVHAGAAVACIEFTKCDSAILFGDSRQIRYGRCSELDTAVLSDLNRFVDDESRVYGEVSYRCPWDVCAWLSTFYPKTVATTNLVSAGQSSMQVREIESVDDVEYSSEFVYLTMLQSEKKDLLKSFGKRSRSSVEKPTVLTVHEAQGETYRKVNLVRTKFQEDDPFRSENHITVALSRHVESLTYSVLSSKRDDAIAQAIVKAKQLVDAYRVYPTSFGGSTLDVSVNPSTSDRSKCKASSAPYEVINSFLESVVPGTTSVDFGDVSEEMGTQVFESGADNVVIRDSAPVNKSTDHDPQRVSSIRSQAIPKRKPSLQENLYSYESRNYNFTVCERFSGPQEFGQAMAMVMLERSFDLEKVAKVRSDVIAITEKGVRTWMSKREPSQLRALSSDLQKPLNLEEEITTFKLMVKRDAKVKLDSSCLVKHPPAQNIMFHRKAVNAIFSPCFDEFKNRVITCTNSNIVFFTEMTNSTLASIAKEMLGSEHVYNVGEIDFSKFDKSQDAFIKSFERTLYSAFGFDEDLLDVWMQGEYTSNATTLDGQLSFSVDNQRKSGASNTWIGNSIETLGILSMFYYTNRFKALFVSGDDSLIFSESPIRNSADAMCTELGFETKFLTPSVPYFCSKFFVMTGHDVFFVPDPYKLLVKLGASKDEVDDEFLFEVFTSFRDLTKDLVDERVIELLTHLVHSKYGYESGDTYAALCAIHCIRSNFSSFKKLYPKVKGWVVHYGKLKFVLRKFANCFREKFDTAFGERTFLLTTKLETVL
Enzyme Length 3094
Uniprot Accession Number Q08534
Absorption
Active Site ACT_SITE 509; /note=For leader protease activity; /evidence=ECO:0000269|PubMed:8259666; ACT_SITE 569; /note=For leader protease activity; /evidence=ECO:0000269|PubMed:8259666
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}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
DNA Binding
EC Number 3.4.22.-; 2.1.1.-; 2.7.7.48; 3.6.4.13
Enzyme Function FUNCTION: L-pro is involved in systemic transport and in RNA amplification. {ECO:0000269|PubMed:12584307}.; FUNCTION: RNA-dependent RNA polymerase replicates the viral genome. {ECO:0000305}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (1); Chain (3); Coiled coil (1); Domain (4); Region (1); Site (1)
Keywords ATP-binding;Coiled coil;Direct protein sequencing;Helicase;Host cytoplasmic vesicle;Host membrane;Hydrolase;Membrane;Methyltransferase;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-directed RNA polymerase;Reference proteome;Ribosomal frameshifting;Thiol protease;Transferase;Viral RNA replication
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Leader protease]: Host cytoplasmic vesicle membrane. Note=Associates with the closterovirus-induced membranous vesicle aggregates.; SUBCELLULAR LOCATION: [Methyltransferase/helicase/RNA-directed RNA polymerase]: Host cytoplasmic vesicle membrane. Note=Associates with the closterovirus-induced membranous vesicle aggregates.
Modified Residue
Post Translational Modification PTM: The leader protease is released by autoproteolysis.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 348,277
Kinetics
Metal Binding
Rhea ID RHEA:21248; RHEA:13065
Cross Reference Brenda