POLG_MRFVC
ID POLG_MRFVC Reviewed; 2027 AA.
AC Q91TW9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Genome polyprotein;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE Includes:
DE RecName: Full=Helicase;
DE EC=3.6.4.13;
DE Includes:
DE RecName: Full=Methyltransferase;
DE EC=2.1.1.-;
DE Contains:
DE RecName: Full=RNA replication protein;
DE Contains:
DE RecName: Full=Capsid protein CP1;
DE Short=CP1;
DE AltName: Full=Coat protein;
GN ORFNames=ORF1;
OS Maize rayado fino virus (isolate Costa Rica/Guapiles) (MRFV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Tymovirales; Tymoviridae; Marafivirus.
OX NCBI_TaxID=652669;
OH NCBI_TaxID=4577; Zea mays (Maize).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11289816; DOI=10.1006/viro.2001.0859;
RA Hammond R.W., Ramirez P.;
RT "Molecular characterization of the genome of Maize rayado fino virus, the
RT type member of the genus Marafivirus.";
RL Virology 282:338-347(2001).
RN [2]
RP FUNCTION OF CAPSID PROTEINS, AND IDENTIFICATION OF SUBGENOMIC CAPSID
RP PROTEIN CP2.
RX PubMed=3721810; DOI=10.1159/000149664;
RA Falk B.W., Tsai J.H.;
RT "The two capsid proteins of maize rayado fino virus contain common peptide
RT sequences.";
RL Intervirology 25:111-116(1986).
CC -!- FUNCTION: RNA replication protein replicates the viral genomic RNA. The
CC central part of this protein possibly functions as an ATP-binding
CC helicase and/or methyltransferase (Probable).
CC {ECO:0000305|PubMed:3721810}.
CC -!- FUNCTION: Capsid protein CP1 and CP2 assemble to form an icosahedral
CC capsid, about 30 nm in diameter, and consisting of capsid proteins CP1
CC and CP2 in a 1:3 ratio. The capsid encapsulates the single-stranded RNA
CC genome. While CP1 is produced as a C-terminal fusion of the replication
CC protein, CP2 may be expressed from a 3'-co-terminal subgenomic RNA.
CC {ECO:0000269|PubMed:3721810}.
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 -!- SUBCELLULAR LOCATION: [Capsid protein CP1]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=Q91TW9-1; Sequence=Displayed;
CC Name=Subgenomic capsid protein CP2;
CC IsoId=Q91TW9-2; Sequence=VSP_040286;
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DR EMBL; AF265566; AAK52838.1; -; Genomic_RNA.
DR RefSeq; NP_115454.1; NC_002786.1.
DR PDB; 7MIA; X-ray; 1.90 A; A/B=667-815.
DR PDB; 7MIC; X-ray; 2.09 A; A=667-815.
DR PDBsum; 7MIA; -.
DR PDBsum; 7MIC; -.
DR SMR; Q91TW9; -.
DR GeneID; 921087; -.
DR KEGG; vg:921087; -.
DR Proteomes; UP000000400; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
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:0008174; F:mRNA methyltransferase 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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; 3.40.50.300; -; 1.
DR Gene3D; 3.90.70.100; -; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008043; Peptidase_C21.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR043629; Salyut_dom.
DR InterPro; IPR000574; Tymo_coat.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR InterPro; IPR043181; TYMV_endopept_dom.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF05381; Peptidase_C21; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF19227; Salyut; 1.
DR Pfam; PF00983; Tymo_coat; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51738; PEPTIDASE_C21; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; ATP-binding; Capsid protein;
KW Hydrolase; Methyltransferase; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..2027
FT /note="Genome polyprotein"
FT /id="PRO_0000402496"
FT CHAIN 1..1799
FT /note="RNA replication protein"
FT /id="PRO_0000402497"
FT CHAIN 1800..2027
FT /note="Capsid protein CP1"
FT /id="PRO_0000402498"
FT DOMAIN 65..226
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 668..823
FT /note="Peptidase C21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT DOMAIN 881..1038
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1039..1171
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1507..1613
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 542..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1823..1853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..601
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 722
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT ACT_SITE 805
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT VAR_SEQ 1..1827
FT /note="Missing (in isoform Subgenomic capsid protein CP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040286"
FT HELIX 672..676
FT /evidence="ECO:0007829|PDB:7MIA"
FT STRAND 680..686
FT /evidence="ECO:0007829|PDB:7MIA"
FT HELIX 687..690
FT /evidence="ECO:0007829|PDB:7MIA"
FT TURN 697..700
FT /evidence="ECO:0007829|PDB:7MIA"
FT STRAND 702..707
FT /evidence="ECO:0007829|PDB:7MIA"
FT HELIX 718..720
FT /evidence="ECO:0007829|PDB:7MIC"
FT HELIX 722..731
FT /evidence="ECO:0007829|PDB:7MIA"
FT HELIX 735..745
FT /evidence="ECO:0007829|PDB:7MIA"
FT HELIX 748..751
FT /evidence="ECO:0007829|PDB:7MIA"
FT HELIX 756..759
FT /evidence="ECO:0007829|PDB:7MIA"
FT HELIX 763..773
FT /evidence="ECO:0007829|PDB:7MIA"
FT STRAND 775..781
FT /evidence="ECO:0007829|PDB:7MIA"
FT STRAND 784..790
FT /evidence="ECO:0007829|PDB:7MIA"
FT STRAND 794..800
FT /evidence="ECO:0007829|PDB:7MIA"
FT STRAND 805..811
FT /evidence="ECO:0007829|PDB:7MIC"
SQ SEQUENCE 2027 AA; 223738 MW; 77B46DC9950B0BF7 CRC64;
MSSFLRGGHL LSGVESLTPT THRDTITAPI VESLATPLRR SLERYPWSIP KEFHSFLHTC
GVDISGFGHA AHPHPVHKTI ETHLLLDVWP NYARGPSDVM FIKPEKFAKL QSRQPNFAHL
INYRLVPKDT TRYPSTSTNL PDCETVFMHD ALMYYTPGQI ADLFFLCPQL QKIYASVVVP
AESSFTHLSL HPEIYRFRFQ GSDLVYEPEG NPAANYTQPR SALDWLQTTG FTVGHEFFSV
TLLDSFGPVH SLLIQRGRPP VFQAEDIASF RVPDAVALPA PASLHQDLRH RLVPRKVYDA
LFNYVRAVRL RVTDPAGFVR TQVGKPEYSW VTSSAWDNLQ HFALQTAAVR PNTSHPLFQS
PFARLSHWLR THTWALWCLA SPSASVSAWA TASALGRLLP LHTDRLRLFG FDIIGRRFWP
RLPFHGPEPR FLWETHPACR PPVLFADSAF ECQILAGLAN RCSPSPFWSR LFPTASPPSW
VAYSALALAA VPLAALALRW FYGPDSPQAL HDQYHATFHP DPWTLDLPRR LRRFERESFM
RTGSAPLPQS LPPPEGSLLP VEPPPVPSDP EPALEPSPPA ASVPAPAPAL ASEPPPSPES
VAPSRRRRRA RRAAARAPSP SPALLGADLR FGDLPPVSAW DSDPEISKLG ESTQGTVFAV
TPGPRAPEPD TARLDADPSA SGPVMEFREL QKGAYIEPTG AFLTRARNSV SSSIPYPTRA
ACLLVAVSQA TGLPTRTLWA ALCANLPDSV LDDGSLATLG LTTDHFAVLA RIFSLRCRFV
SEHGDVELGL HDATSRFTIR HTPGHFELVA DNFSLPALVG ASSVPGADLA EACKRFVAPD
RTVLPFRDVH IHRTDVRRAK NLISNMKNGF DGVMAQANPL DPKSARERFL MLDSCLDIAA
PRRVRLIHIA GFAGCGKSWP ISHLLRTPAF RVFKLAVPTT ELRDEWKALM DPRDQDKWRF
GTWESSLLKT ARVLVIDEVY KMPRGYLDLA IHADAAIQFV ILLGDPIQGE YHSTHPSSSN
ARLSPEHRYL RPYVDFYCFW SRRIPQNVAR VLDVPTTSTE MGFARYSQQF PFSGKILISA
RDSAKSLADC GYHAVTIASS QGSTIAGPAY VHLDNHSRRL SHQHSLVAIT RSKSGIVFTG
DKAAADGTSS ANLLFSAVLL DRRLSVRSLF SALLPCCPFV TEPPTSRAVL LRGAGYGIAR
PLRARDAPPL GPDYVGDVIL DSSAPILGDG SANAPQVSTH FLPETRRPLH FDIPSARHQV
ADHPLAPDHS ACAIEPVYPG ESFESLASLF LPPTDAESKE TYFRGEMSNQ FPHLDKPFEL
GAQTSSLLAP LHNSKHDPTL LPASIGKRLR FRHSEAPYVI APRDEILGSL LYEAWCRAYH
RSPRDVEPFD PDLYAECINL NEFAQLSSKT QATIMANANR SDPDWRWSAV RIFAKTQHKV
NEGSLFGSWK ACQTLALMHD AVVLLLGPVK KYQRFFDQRD RPSTLYVHAG HTPFEMADWC
RAHLTPAVKL ANDYTAFDQS QHGEAVVFER YKMNRLSIPA ELVDLHVYLK TNVSTQFGPL
TCMRLTGEPG TYDDNTDYNI AVLHLEYAVG STPLMVSGDD SLLDSEPPVR DQWSAIAPML
ALTFKKERGR YATFCGYYVG FTGAVRSPPA LFAKLMIAVD DGSISDKLIA YLTEFTVGHS
SGDAFWTILP VEAVPYQSAC FDFFCRRAPA QAKVMLRLGE APESLLSLAF EGLKWASHSV
YALMNSSHRR QLLHSSRRPR SLPEDPEVSQ LQGELLHQFQ SLHLPLRGGH MPNPLAAPFR
LLQQSSSLGP TYAVAPIARA PQVPPPSMAD NATQVGPVPP RDDRVDRQPP LPDPPRVLET
APSHFLDLPF QWKVTDFTGY AAYHGTDDLV ASAVLTTLCA PYRHAELLYV EISVAPCPPS
FSKPIMFTVV WTPATLSPRD GKETDYYGGR QITVGGPVML SSTTAVPADL ARMNPFIKSS
VSYNDTPRWT MSVPAVTGGD TKIPLATAFV RGIVRVRAPS GAATPSA
