POLN_ABPVR
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 03-AUG-2022, entry version 83.
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.
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}.
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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; Genome.
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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.30.70.270; -; 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 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
