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 26-FEB-2020, entry version 85. 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; 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 (Jumping 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PRIDE; 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 //