POL2_SQMVM
ID POL2_SQMVM Reviewed; 1009 AA.
AC P36341; A0A1Z2TIL5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 3.
DT 23-FEB-2022, entry version 89.
DE RecName: Full=RNA2 polyprotein;
DE AltName: Full=Genome polyprotein M;
DE AltName: Full=M RNA polyprotein;
DE AltName: Full=Middle component RNA polyprotein;
DE AltName: Full=P2;
DE Contains:
DE RecName: Full=VP58;
DE Contains:
DE RecName: Full=Movement protein;
DE Short=MP;
DE Contains:
DE RecName: Full=Large capsid protein;
DE Short=LCP;
DE AltName: Full=42k coat protein;
DE AltName: Full=Coat protein VP42;
DE AltName: Full=L subunit;
DE AltName: Full=Large coat protein;
DE Contains:
DE RecName: Full=Small capsid protein;
DE Short=SCP;
DE AltName: Full=22k coat protein;
DE AltName: Full=Coat protein VP22;
DE AltName: Full=S subunit;
OS Squash mosaic virus (strain melon) (SqMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX NCBI_TaxID=36401;
OH NCBI_TaxID=3559; Chenopodium album (Fat-hen).
OH NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH NCBI_TaxID=3679; Ecballium elaterium (Squirting cucumber) (Momordica elaterium).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate 697K2, and Isolate 702K2;
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 220-1009, PROTEIN SEQUENCE OF 576-600
RP AND 825-835, AND PROTEOLYTIC CLEAVAGE (RNA2 POLYPROTEIN).
RC STRAIN=Melon;
RX PubMed=8503782; DOI=10.1007/bf01318993;
RA Hu J.S., Pang S.Z., Nagpala P.G., Siemieniak D.R., Slightom J.L.,
RA Gonsalves D.;
RT "The coat protein genes of squash mosaic virus: cloning, sequence analysis,
RT and expression in tobacco protoplasts.";
RL Arch. Virol. 130:17-31(1993).
CC -!- FUNCTION: [VP58]: Responsible for viral RNA2 accumulation. May function
CC by recruiting the RNA1-encoded polyprotein that contains the
CC replication protein to RNA2 and enable its replication.
CC {ECO:0000250|UniProtKB:P23009}.
CC -!- FUNCTION: [Movement protein]: Transports the viral genome to
CC neighboring plant cells directly through plasmosdesmata, without any
CC budding. The movement protein allows efficient cell to cell
CC propagation, by bypassing the host cell wall barrier. Acts by forming a
CC tubular structure at the host plasmodesmata, enlarging it enough to
CC allow free passage of virion capsids. Binds to GTP and to single-
CC stranded RNA and single-stranded DNA in a non-sequence-specific manner.
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- FUNCTION: [Large capsid protein]: Together with the small capsid
CC protein, forms an icosahedral capsid (T=3) enclosing the viral positive
CC strand RNA genome, with a diameter of approximately 300 Angstroms. The
CC capsid is formed from 60 copies each of the large and the small capsid
CC protein. The large capsid protein interacts with the viral RNA.
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- FUNCTION: [Small capsid protein]: Together with the large capsid
CC protein, forms an icosahedral capsid (T=3) enclosing the viral positive
CC strand RNA genome, with a diameter of approximately 300 Angstroms. The
CC capsid is formed from 60 copies each of the large and the small capsid
CC protein. The small capsid protein forms the turrets at the fivefold
CC axes of the viral particle. {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBUNIT: [Small capsid protein]: Interacts with the large capsid
CC protein. {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBUNIT: [Large capsid protein]: Interacts with the small capsid
CC protein. Homomultimer; assembles as pentons. Interacts with the
CC movement protein (via C-terminus). {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBUNIT: [Movement protein]: Interacts (via C-terminus) with the large
CC capsid protein. {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host
CC plasmodesma {ECO:0000250|UniProtKB:P03599}. Note=Assembles in tubules
CC that are embedded within modified plasmodesmata.
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBCELLULAR LOCATION: [Large capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- SUBCELLULAR LOCATION: [Small capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- DOMAIN: [Large capsid protein]: Contains a beta-sheet structure called
CC beta-barrel jelly roll. {ECO:0000250|UniProtKB:P03599}.
CC -!- DOMAIN: [Small capsid protein]: Contains a beta-sheet structure called
CC beta-barrel jelly roll. {ECO:0000250|UniProtKB:P03599}.
CC -!- DOMAIN: [Movement protein]: The C-terminus is involved in binding to
CC the large capsid protein, and hence to the virion.
CC {ECO:0000250|UniProtKB:P03599}.
CC -!- PTM: [RNA2 polyprotein]: Specific enzymatic cleavages by picornain 3C-
CC like protease in vivo yield mature proteins.
CC {ECO:0000305|PubMed:8503782}.
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DR EMBL; M96148; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; MF166754; ASA69625.1; -; Genomic_RNA.
DR EMBL; MF166755; ASA69626.1; -; Genomic_RNA.
DR PIR; A48356; A48356.
DR SMR; P36341; -.
DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; 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; IPR003181; Como_LCP.
DR InterPro; IPR003182; RNA2_polyprotein.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF02247; Como_LCP; 1.
DR Pfam; PF02248; Como_SCP; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Direct protein sequencing; DNA-binding; GTP-binding;
KW Host cell junction; Nucleotide-binding; RNA-binding;
KW Suppressor of RNA silencing; T=3 icosahedral capsid protein; Transport;
KW Viral movement protein; Virion.
FT CHAIN 1..1009
FT /note="RNA2 polyprotein"
FT /id="PRO_0000445854"
FT CHAIN 1..90
FT /note="VP58"
FT /id="PRO_0000445855"
FT CHAIN 91..451
FT /note="Movement protein"
FT /id="PRO_0000037037"
FT CHAIN 452..825
FT /note="Large capsid protein"
FT /id="PRO_0000037038"
FT CHAIN 826..1009
FT /note="Small capsid protein"
FT /id="PRO_0000037039"
FT REGION 387..393
FT /note="Involved in tubule formation by the movement
FT protein"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT SITE 451..452
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:8503782"
FT SITE 468
FT /note="Interaction with the viral RNA"
FT /evidence="ECO:0000250|UniProtKB:P03599"
FT SITE 825..826
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000269|PubMed:8503782"
FT VARIANT 315
FT /note="R -> K (in strain: Melon)"
FT /evidence="ECO:0000305"
FT VARIANT 562
FT /note="D -> N (in strain: Melon)"
FT /evidence="ECO:0000305"
FT VARIANT 740
FT /note="A -> R (in strain: Melon)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1009 AA; 111788 MW; EDA33BB41F01B628 CRC64;
MWHFCEQVYE CFEGYHRDYS VQTVPVEYLA SHYIVNKFRP DPLAVLWLFC LGIWWEIIQI
LHHLFQYKEP ALFVGSCQNL AAFLEKKYSM EVIQKEGLAA SALKDKERLT EKAVVNQPLS
NLIPHSNKMY ERSKSLLSGL KRGLIKQKEI AFDKLMGGST IDFQHIPTGT LTPGENKVLD
IPIVPQHLLT STNITDYHQA NKKNANGATA LHVGAIEVIM DCFTSPDSNI CGGMLLVDTA
HLNPDNAIRS VFVAPFIGGR PIRVLLFPDT LVEIAPNMNS RFKLLCTTSN GDVAPDFNLA
MVKVNVAGCA VSLTRTYTPT AYLEQELIKE KGAIVQYLNR HTFSMHRNNQ MTKEEMQKQR
LSFRLESALT LQEKHPLHAT FCKSTNFVYK IGGDAKEGSN GNLTVNESQL SSHSPSAHVL
HKHNNSGDNE VEFSEIGVVV PGAGRTKAYG QNELDLAQLS LDDTSSLRGT ALQTKLATSR
IILSKTMVGN TVLREDLLAT FLQDSNERAA IDLIRTHVIR GKIRCVASIN VPENTGCALA
ICFNSGITGA ADTDIYTTSS QDAIVWNPAC EKAVELTFNP NPCGDAWNFV FLQQTKAHFA
VQCVTGWTTT PLTDLALVLT WHIDRSLCVP KTLTISSAHA SFPINRWMGK LSFPQGPARV
LKRMPLAIGG GAGTKDAILM NMPNAVISLH RYFRGDFVFE ITKMSSPYIK ATIAFFIAFG
DITEEMTNLE SFPHKLVQFA EIQGRTTITF TQSEFLTAWS TQVLSTVNPQ KDGCPHLYAL
LHDSATSTIE GNFVIGVKLL DIRNYRAYGH NPGFEGARLL GISGQSTMVQ QLGTYNPIWM
VRTPLESTAQ QNFASFTADL MESTISGDST GNWNITVYPS PIANLLKVAA WKKGTIRFQL
ICRGAAVKQS DWAASARIDL INNLSNKALP ARSWYITKPR GGDIEFDLEI AGPNNGFEMA
NSSWAFQTTW YLEIAIDNPK QFTLFELNAC LMEDFEVAGN TLNPPILLS
