ID POLN_ABPVR Reviewed; 1906 AA. AC Q9DSN9; DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 13-SEP-2023, entry version 88. DE RecName: Full=Replicase polyprotein; DE EC=2.7.7.48; DE EC=3.4.22.-; GN ORFNames=ORF1; OS Acute bee paralysis virus (strain Rothamsted) (ABPV). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Dicistroviridae; Aparavirus; Aparavirus apisacutum. OX NCBI_TaxID=1217067; OH NCBI_TaxID=7460; Apis mellifera (Honeybee). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=11080493; DOI=10.1006/viro.2000.0616; RA Govan V.A., Leat N., Allsopp M., Davison S.; RT "Analysis of the complete genome sequence of acute bee paralysis virus RT shows that it belongs to the novel group of insect-infecting RNA viruses."; RL Virology 277:457-463(2000). CC -!- FUNCTION: Replicase polyprotein contains helicase, VPg, protease and CC RNA-directed RNA polymerase functions. CC -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and CC antigenomic RNA and transcribes the vial genome. CC -!- FUNCTION: The protease generates mature viral proteins from the CC precursor polyprotein. CC -!- FUNCTION: VPg is covalently linked to the 5'-end of genomic RNA. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CC -!- PTM: Specific enzymatic cleavages in vivo by the viral protease yield a CC variety of precursors and mature proteins. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF150629; AAG13118.1; -; Genomic_RNA. DR RefSeq; NP_066241.1; NC_002548.1. DR GeneID; 911837; -. DR KEGG; vg:911837; -. DR Proteomes; UP000006040; Segment. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR CDD; cd23194; Dicistroviridae_RdRp; 1. DR Gene3D; 1.20.960.20; -; 1. DR Gene3D; 3.30.70.270; -; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir. DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir. DR InterPro; IPR044067; PCV_3C_PRO. DR InterPro; IPR024387; Pept_C3G_Picornavir. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR Pfam; PF12381; Peptidase_C3G; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF00910; RNA_helicase; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS51874; PCV_3C_PRO; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51218; SF3_HELICASE_2; 1. PE 4: Predicted; KW ATP-binding; Hydrolase; Nucleotide-binding; Nucleotidyltransferase; KW Protease; Reference proteome; RNA-directed RNA polymerase; Thiol protease; KW Transferase; Viral RNA replication. FT CHAIN 1..1906 FT /note="Replicase polyprotein" FT /id="PRO_0000423158" FT DOMAIN 513..692 FT /note="SF3 helicase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551" FT DOMAIN 1126..1343 FT /note="Peptidase C3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222" FT DOMAIN 1638..1772 FT /note="RdRp catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539" FT REGION 1124..1350 FT /note="Protease" FT ACT_SITE 1171 FT /note="For picornain 3C-like protease activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222" FT ACT_SITE 1213 FT /note="For picornain 3C-like protease activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222" FT ACT_SITE 1305 FT /note="For picornain 3C-like protease activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222" FT BINDING 544..551 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551" SQ SEQUENCE 1906 AA; 219430 MW; 5A48F79063235FE4 CRC64; MNFTKQPASL KYLSSMKLIT SQDQDFFNFG EVSREFILEQ AYVNGYDFHM LHQDMNCIGF VLSIFDEDAR DEYEYKDLNC EYHENLFDAV VDSEFDKIWP HLVLKYITYY PCSLNWRGMP TIPIVYVSKH FWYELYRTGF LNKLYHCGSW TDILLLLSGD VETNPGPVET YKDLCRRKNI RKRKSRIREE IKMQQHIDKI IGQENEEYKI INVNMQGIFS FNEEKEIIKS TAWKFNSTLD KTNSIIDNLI PQLEETLAGF RKTYSKCESK IFGTISVVDV CVDLISALLQ VSFAKPAMKI ASLAVEVFRL IKKYVSNINI NIDKIKELLS YGKVALNNNN PIIHVTMQSN SPILEVLLQP NIIVSAIFIA LSVVFHKKFT YKKLGIEAMI KRLGDLGRAA KGCSDLNVVL NQAITNHMLE HFGKNVLGLK QEDELKVLVE GYRNWCDEVR DLVGHKINSD GELDSKSIVE NIMKDVYEIQ RIENMYKKGL EISRNIAELK LPTKLTISFN THMRYLTEVF KSVDTSGAFG NKPRTQPIVI WLFGESGRGK SGMTWPLAID LNNSLLDNVD EMRNFSKNIY MRNVEQEFWD NYQGQNIVCX DDFGQMRDSS SNPNPEFMEL IRTANIAPYP LHMAHLEDKR KTKFTSKVII MTSNVFEQDV NSLTFPDAFR RRVDLCAEVK NKDEFTKMCW SKSAGKMVQR LDKGKVKKIT GDIHSTVPYI VDLIDPESGE VYKTGLEYEE FLDMCLEKTS QCRDDSAKLN DFLMDYAEKR ANRSREIDEV CARTMDEAFV DAYDDVIDVN MQIETVDEME LIEPNKLREM IEQCSNKIVY TYEGIAVKIT SLAFKLATLN YEEQWEQIKE MKYYVKVSSG VNYLKRVLSQ GMKVCEEWMK EMINYVKEHP WMTVSLILGT LIGILTVVGF WKWLCSGDKK KNPIKRHFIN TGNVLILPDR ELNTFWKNQE SLDLRDMYIN RVEEHIISLL KLQHKVVLVP KVTKYILTTV ENHAKISDKI ILITRNRYLN YQGKFVELIC GEINQFFIDP ETLDTNVEAF ASADLKTFVQ RKPIVIEGPE FVEAQTSGDQ ITLRKQTQKV IEAFASSDAI TMARKTPKFV ESDDVVEVSM QMWKDQVAQK LITNRVLTNL YKICLVKENG DMVPLLNGLF VRSNIMLAPG HLVGFLSDSD TIEIRNLFDV VFRVPWKDVK KVDVVNAFGE SKEAVLLCFP KFVCQHTDLV KHFQDSESMS KFKRCEVTLP VLRYSDKMNR FLATLIECDK VEAYDRPYTL NDSSKGQYIL RQGLEYTMPT TNGDCGAPLV INETQVIRKI AGIHVAGDAR GKAYAESISQ KDLIRAFSKI DVSMQIQLDL DQTLNFNQQQ XIIPPNAEFG PEDLDFCDLP SLKMIPVGRL SEPLFEPGKT DIRPSLVYGK ISEIKTKPAI LRNVIVDGKI VNIKHKNLKK CAMDTPYVSK EMTEEAFQLV KSVWLKGMRN ELKKVLTYEE AICGNDSSEF ISAINRSSSP GFPWIRDRIK GTKGKQGWFG AEGEYILDED VFEAVKTRIQ NAKNGVRTPV MWVDTLKDER RPIEKVDQLK TRVFSNGPMD FSITFRMYYL GFIAHLMENR ITNEVSIGTN VYSQDWNKTV RKLKTMGPKV IAGDFSTFDG SLNVCIMEKF ADLANEFYDD GSENALIRHV LLMDVYNSTH ICGDSVYMMT HSQPSGNPAT TPLNCFINSM GLRMVFELCS KKYSALNGTK CYVMKDFSKH VSIVSYGDDN VINFSDEVSE WFNMETITEA FEKLGFTYTD ELKGKNGEVP KWRTIEDVQY LKRKFRYDSK RKVWEAPLCM DTILEMPNWC RGSLDIQEGT KVNCENAIME LSMHEEYVFD KWSKVISKAY QKATGDCLDI STYNGYAQER FLNYYL //