POL2_CNSV
ID POL2_CNSV Reviewed; 1240 AA.
AC Q8QVU9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=RNA2 polyprotein;
DE AltName: Full=P2;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Movement protein;
DE AltName: Full=2B-MP;
DE Contains:
DE RecName: Full=Coat protein;
DE AltName: Full=2C-CP;
OS Cycas necrotic stunt virus (CNSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX NCBI_TaxID=173976;
OH NCBI_TaxID=16901; Aucuba japonica (Japanese laurel) (Spotted laurel).
OH NCBI_TaxID=3396; Cycas revoluta (Sago palm).
OH NCBI_TaxID=49747; Gladiolus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEIN SEQUENCE OF 684-695.
RX PubMed=12417954; DOI=10.1007/s00705-002-0876-5;
RA Han S.S., Karasev A.V., Ieki H., Iwanami T.;
RT "Nucleotide sequence and taxonomy of Cycas necrotic stunt virus.";
RL Arch. Virol. 147:2207-2214(2002).
CC -!- FUNCTION: [Protein 2A]: Implicated in RNA2 replication. Could also be
CC required for nematode transmission of the virus (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: [Movement protein]: Transports viral genome to neighboring
CC plant cells directly through plasmosdesmata, without any budding. The
CC movement protein allows efficient cell to cell propagation, by
CC bypassing the host cell wall barrier. Acts by forming a tubular
CC structure at the host plasmodesmata, enlarging it enough to allow free
CC passage of virion capsids (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host
CC plasmodesma {ECO:0000250}. Note=Assembles in tubules that are embedded
CC within modified plasmodesmata. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Coat protein]: Virion {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo by the P1 encoded 3C-like
CC protease yield mature proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: Virions are comprised of 60 copies of the coat protein.
CC -!- SIMILARITY: Belongs to the nepoviruses RNA2 polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AB073148; BAB89370.2; -; Genomic_RNA.
DR RefSeq; NP_620620.2; NC_003792.2.
DR SMR; Q8QVU9; -.
DR GeneID; 988024; -.
DR KEGG; vg:988024; -.
DR Proteomes; UP000008564; Genome.
DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.20; -; 2.
DR InterPro; IPR005054; Nepo_coat.
DR InterPro; IPR005305; Nepo_coat_C.
DR InterPro; IPR005306; Nepo_coat_N.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF03391; Nepo_coat; 1.
DR Pfam; PF03688; Nepo_coat_C; 1.
DR Pfam; PF03689; Nepo_coat_N; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Direct protein sequencing; Host cell junction; Transport;
KW Viral movement protein; Virion.
FT CHAIN 1..?314
FT /note="Protein 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037118"
FT CHAIN ?315..683
FT /note="Movement protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037119"
FT CHAIN 684..1240
FT /note="Coat protein"
FT /id="PRO_0000037120"
FT REGION 1193..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 138745 MW; 334E35EE5B67A0D8 CRC64;
MFAPIGAPGM GERASQNFRS ASGFRDLLVH AVKVLVLSAY QRRPCTSMLR PREQKRIKMR
LKWMCLMKFC FMQNNYWDTQ RRFTGGMHNV PELATFDAWL QHWRVVHWRL NIISEILIDF
QALVRMMKNL AGQCHFDFYP VCTHCVQLVN NWYIAEFKPH LEEETEWWKD LVKPRMGNPV
HEIEPNRKSQ YVESRRIPPP LNGDEFANFL HVCQCAKLAF DVERAATEEN FEDALDTLEE
DFYDIDSTIP KRDLLAADAR VVKRAFTLRR KRRPNRTSVY SMKGQPPVTF SASDLVSCLG
QVLSTLPTVK MDREAIEDQQ DHLEDKQGGE ILTTPQFIEV LRKKKREVRE KEFDDSTQGK
LLPAEDFTLS KHDVFLANSV LDGLRKSKLI QRFAGKCATS TKITVDLTNK EEVVRYGPKE
LASEGFRQTF NVLNRPEYNA LNKLAEAGWK EAKSVVLNLH IRSYLPQQMN AYAFCVIMWG
HSSDAQEAAL SGSYVYLGDG EATMLQLPLL CEYVGHNLQD FEAYKRSLVL STVFPEFSGI
ADGKAMFGIT SIEFTEYLPT SHAGITHERD SWDAMLRNHT EEKRRFLAGF NVVDTIEKGN
RKGFSFPDFD LKAVPRHQAV VRTFEDQDVA PILSKAKSMR VKTFGSFRAG NIPVNFLGTP
SNGQVASKHS VSENAGYSVG DMKSAENFVF TQLITVPAAS TKGNVLAGVD ILANARTTMS
GFYMRWLQKG YIDTNLKLIC HLPRAPFAGM SFFVLIDGTG YLAKDAPTSL NEEEILSYPL
HLVTTSDVSS YEFVLDWHRY IGQVPFAEEN AFLRPTLFLV ACVSSTLALS AKVEFYLEAQ
SVGEELPRTL APSPVLSYPF QNSFLEDLDL FLPPKRLTLG ERETTIIPLS FAKSKKSGDA
VLYSHAAARL AHFQGIGGVL HGVVYLVGSQ LVASQSRISM WSKEQHIQHQ AVNVHVDTDT
GVAFDLPIKD AFYASSVYGD SGAVIQVTCL CSPMSPNAIK APFDMIFKIR GFTPDAPMCR
TINFTQRFGW FAVEPTTSTG AIKLKIWPVS NHLESEDMKV TGYTNAFLQM CQTSTMHFGS
VIIHFSWTLF GGTTNAATAG GVVTIAEGFG PEEENFRGHC RNLSIYEGRA TVPLELGTFA
GPTPLKKLDF KYRNWIRFTT PKGRNISSIF CAIEVLPGFS FYGRTGSPRL SVVGTTVPPT
ADASTSNSQG GDEDIGDQYS AALGRGRGRG SRPGPSPIRG