POL_SINV3
ID POL_SINV3 Reviewed; 2580 AA.
AC C1JCT1;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Polyprotein;
DE Contains:
DE RecName: Full=Helicase {ECO:0000303|PubMed:19403154};
DE EC=3.6.4.13 {ECO:0000305};
DE Contains:
DE RecName: Full=3C-like protease {ECO:0000303|PubMed:19403154};
DE Short=3CL-PRO;
DE EC=3.4.22.- {ECO:0000305};
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE Contains:
DE RecName: Full=Capsid protein VP1 {ECO:0000303|PubMed:24686475};
OS Solenopsis invicta virus 3 (SINV-3).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Solinviviridae; Invictavirus.
OX NCBI_TaxID=631345;
OH NCBI_TaxID=13686; Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND ACTIVE SITE (3C-LIKE PROTEASE).
RC STRAIN=DM {ECO:0000312|EMBL:ACO37271.1};
RX PubMed=19403154; DOI=10.1016/j.virol.2009.03.028;
RA Valles S.M., Hashimoto Y.;
RT "Isolation and characterization of Solenopsis invicta virus 3, a new
RT positive-strand RNA virus infecting the red imported fire ant, Solenopsis
RT invicta.";
RL Virology 388:354-361(2009).
RN [2]
RP RIBOSOMAL FRAMESHIFTING, FUNCTION (CAPSID PROTEIN VP1), SUBCELLULAR
RP LOCATION (CAPSID PROTEIN VP1), ACETYLATION AT MET-2346, AND PROTEOLYTIC
RP CLEAVAGE (POLYPROTEIN).
RX PubMed=24686475; DOI=10.1371/journal.pone.0093497;
RA Valles S.M., Bell S., Firth A.E.;
RT "Solenopsis invicta virus 3: mapping of structural proteins, ribosomal
RT frameshifting, and similarities to Acyrthosiphon pisum virus and Kelp fly
RT virus.";
RL PLoS ONE 9:E93497-E93497(2014).
CC -!- FUNCTION: [Capsid protein VP1]: Assembles with VP1-FSD and VP2 to form
CC an icosahedral capsid. VP1 is about 5 time more abundant than VP1-FSD
CC in the virion. {ECO:0000269|PubMed:24686475}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates genomic and
CC antigenomic RNA. {ECO:0000250|UniProtKB:Q6UP17, ECO:0000255|PROSITE-
CC ProRule:PRU00539}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q6UP17};
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000269|PubMed:24686475}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Polyprotein;
CC IsoId=C1JCT1-1; Sequence=Displayed;
CC Name=Polyprotein-FSD;
CC IsoId=C1JCT2-1; Sequence=External;
CC -!- PTM: [Capsid protein VP1]: N-acetylated. {ECO:0000269|PubMed:24686475}.
CC -!- PTM: [Polyprotein]: Proteolytic cleavages of the polyprotein yield
CC mature proteins. {ECO:0000305|PubMed:24686475}.
CC -!- MISCELLANEOUS: [Capsid protein VP1]: A sgRNA is also expressed which
CC encloses the VP1 capsid protein and probably a leader protein.
CC {ECO:0000269|PubMed:24686475}.
CC -!- MISCELLANEOUS: [Isoform Polyprotein]: Produced by conventional
CC translation. {ECO:0000269|PubMed:24686475}.
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DR EMBL; FJ528584; ACO37271.1; -; Genomic_RNA.
DR RefSeq; YP_002790879.1; NC_012531.1. [C1JCT1-1]
DR SMR; C1JCT1; -.
DR iPTMnet; C1JCT1; -.
DR GeneID; 7751223; -.
DR KEGG; vg:7751223; -.
DR BRENDA; 2.7.7.48; 11653.
DR Proteomes; UP000207613; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:UniProtKB-EC.
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; 2.60.120.20; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; Reference proteome;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2580
FT /note="Polyprotein"
FT /id="PRO_0000442440"
FT CHAIN 1..?
FT /note="Helicase"
FT /id="PRO_0000442441"
FT CHAIN ?..?1432
FT /note="3C-like protease"
FT /id="PRO_0000442442"
FT CHAIN ?1433..2345
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000442443"
FT CHAIN 2346..2580
FT /note="Capsid protein VP1"
FT /id="PRO_0000442444"
FT DOMAIN 369..543
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1206..1423
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1914..2042
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1258
FT /note="For 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000305|PubMed:19403154"
FT ACT_SITE 1295
FT /note="For 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000305|PubMed:19403154"
FT ACT_SITE 1381
FT /note="For 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000305|PubMed:19403154"
FT BINDING 396..403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 1432..1433
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT SITE 2345..2346
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:24686475"
FT MOD_RES 2346
FT /note="N-acetylmethionine; by host"
FT /evidence="ECO:0000269|PubMed:24686475"
SQ SEQUENCE 2580 AA; 299117 MW; 238B7E9621BEAD60 CRC64;
MSEKTQTFVQ NETHVLDMTS DFKSDLSLEK VTSSVEQTDD LVSKIINNND LDIKDLSFLR
NLLLSTLQYL GIAKFVAINI TLSILSILML LINSCAKFTR IVNLSSHILN IITTLGLYFQ
VSSMEIEEIT QTFENEFGTY DDDKILSHYI KICNLPNRKD VYEYISLNDL KYKIKLPDIS
FYELKNDILS KNKNLHLWIF QKFTDEFLAM WFGVQPYRIS NLREMLVISR QGFIPKDLFN
EIRKLCNMGV SVIISFIQSK LFDEPFKKRD CTQALKDASV ISSPFDTLWN LISKQVCDNS
AEERFTQTIL DFTSEFDNFL GIPNYKFAKN QKLVNTISKS LDACAKFIRD CPKDKQTEIF
PLQGLHTATV KRRNEILTNV MPKFARQEPF VVLFQGPGGI GKTHLVQQLA TKCVNSFYQD
HEDDYIEISP DDKYWPPLSG QRVAFFDEAG NLNDLTEDLL FRNIKSICSP AYFNCAAADI
EHKISPCPFE LVFATVNTDL DTLQSKISST FGQASVFPIW RRCIVVECSW NEKELGPFNY
KNPSGHRSDY SHITMNYMSY DDKTQKLALE KEINFDTLFD MIRLRFRKKQ QEHDTKISIL
NNEIQRQSNS KQHFSVCLYG EPGQGKTYNL NKLITTFANA TNLKIGSEEK PSIHIFDDYI
KDENDENCSK FMDIYNNKLP NNSVIFSATN VYPKTHFFPT FFLTNLIYAF IQPFKQVGLY
RRLGFDGYTD IPNSSVNAPI FVQNFKFYER KQHICYFLSL EFLKNIICYI FFFLYFPLKF
IKKIDLIEIK DVNKYVYDRY INFLSLSKQI EIVEYPPNLE NVEFDFRFNM NKFHRVSFNN
PFELDKYIHF NKNSYENLLH FDWKMYLSPR VKHRLALSYE KFFITISEVN KEIIIEELKR
YVLLFKQFNI DPNMEINLGE YGSFYYINGK IHLMTINIES NVSEIPVFTD GDYVYISEHK
IPVIDLFDNI NINSKYNLSF DQSIALNSFK TGDSFYSNAK VRKSLSKFVL LNYQTKFKLY
LKEAKDKVKN FIETPIGHLL SILLTIFVIC YASFKIYSKF SNFFSKDQAI EDQRKGEKKI
KKITNYDSDG VQPQRKGEKK IKKVTNYDSD GVQPQSNVKV EEEIKLVFDP TGQKLLFGND
FTSELETLVE LEKDDEEFTK SKIDNKSMAG LRREVRRRRY ARSKKAQIEK QEVLTLPDVN
GFEGGKPYFQ IAEEKARKNL CQIYMIANNE NCIASKFSDH IVCYGLFVFK KRLASVGHIV
EALKCAPGYN LYAGCDQFNG KLYKMNLVRN YRKRELSVWD VDCPNDFVDL TSFFIPKEEL
YDAENCNTVL GRFGMNKREV YLYGNCEFIQ EFFKVDNKGA QEFGYIDWAT VDITLTTGGD
CGLPYYICER KKFHNKIMGL HFAGNNVNHK TIGMSALIYK EDLVVWKGAE RQSKCKFCDV
KDIIIAQPDI PKEKYKGYNH EIVWNSLHES SPTTLNEELE HYLNIFPKFT GTIIKHSGDK
FYGSVKHSHT QFISKFKTEL TVTNGWKLST AGDCQFESNH ISPNTEVMYR VVDVQFNSIF
KAFKSQPYIK NFRLIANVYE KDGKQRVTIL TIIPVSDFNV KQQTVRQALV PLHLNEDEEV
YVTEDVSDIF KTAIKRKQRG ILPDVPYETV ENETVEILGI THRNMTPEPA QMYKPTPFYK
LALKFNLDHK LPVNFNMKDC PQEQKDMMVL DRLGQPNPRI TQSLKWAHKD YSPDYELRKY
VKEQYMCNIM EYYAGCNLLT EEQILKGYGP NHRLYGALGG MEIDSSIGWT MKELYRVTKK
SDVINLDSNG NYSFLNNEAA QYTQELLKIS MEQAHNGQRY YTAFNELMKM EKLKPSKNFI
PRTFTAQDLN GVLMERWILG EFTARALAWD ENCAVGCNPY ATFHKFATKF FKFKNFFSCD
YKNFDRTIPK CVFEDFRDML IQANPHMKNE IYACFQTIID RIQVSGNSIL LVHGGMPSGC
VPTAPLNSKV NDIMIYTAYV NILRRADRGD ITSYRYYRDL VCRLFYGDDV IIAVDDSIAD
IFNCQTLSEE MKILFGMNMT DGSKSDIIPK FETIETLSFI SRFFRPLKHQ ENFIVGALKK
ISIQTHFYYA TDDTPEHFGQ VFKTIQEEAA LWEEEYFNKI QSYIQEIIRK FPEISKFFNF
ESYKSIQKRY IMNGWNEFVK LEKLDLNLNK KKSSKVTGIH SKQYSKFLKF LSRIENEKAA
LEGNFNKESV NTWYFKMSKA MHLNEIFQKG LISKPLAEFY FNEGQKMWDC NITFRRSKDD
LPFTFSGSGT TKACAREQAA EEALVLFSQE DEIVRQINDI QSDCKFCKKM IRYKKLLSGV
SIQRQMNVSK ITENHVPSAG MMATDPSVAP DSGIATNTQT PSISRVLNPI ARALDNPAGT
GAPFDKHTYV YNVFTRWPEM STVVNKSLAA GAEVFKISLD PNKLPKRILQ YIQFHKTIIP
QIEVQILIGG AAGTVGWLKV GWVPDASTAK KYSLDDLQLV ASETINLNST ITMSMIINDS
RRNGMFRLTK SDPEPWPGIV CLVEHPITNV QRNDDVNYPV IVSVRLGPDC QLMQPYNDLN
