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 05-JUN-2019, entry version 82. 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; OC 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 RP 576-600 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 RT analysis, and expression in tobacco protoplasts."; RL Arch. Virol. 130:17-31(1993). CC -!- FUNCTION: VP58: Responsible for viral RNA2 accumulation. May CC function by recruiting the RNA1-encoded polyprotein that contains CC the 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 CC any budding. The movement protein allows efficient cell to cell CC propagation, by bypassing the host cell wall barrier. Acts by CC forming a tubular structure at the host plasmodesmata, enlarging CC it enough to allow free passage of virion capsids. Binds to GTP CC and to single-stranded RNA and single-stranded DNA in a non- CC sequence-specific manner. {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 CC positive strand RNA genome, with a diameter of approximately 300 CC Angstroms. The capsid is formed from 60 copies each of the large CC and the small capsid protein. The large capsid protein interacts CC with the viral RNA. {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 CC positive strand RNA genome, with a diameter of approximately 300 CC Angstroms. The capsid is formed from 60 copies each of the large CC and the small capsid protein. The small capsid protein forms the CC turrets at the fivefold axes of the viral particle. CC {ECO:0000250|UniProtKB:P03599}. CC -!- SUBUNIT: Small capsid protein: Interacts with the large capsid CC protein. Large capsid protein: Interacts with the small capsid CC protein. Large capsid protein: Homomultimer; assembles as pentons. CC Large capsid protein: Interacts with the movement protein (via C- CC terminus). Movement protein: Interacts (via C-terminus) with the CC large capsid protein. {ECO:0000250|UniProtKB:P03599}. CC -!- SUBCELLULAR LOCATION: Movement protein: Host cell junction, host CC plasmodesma {ECO:0000250|UniProtKB:P03599}. Note=Assembles in CC tubules 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: Contain a beta-sheet structure CC called beta-barrel jelly roll. {ECO:0000250|UniProtKB:P03599}. CC -!- DOMAIN: Small capsid protein: Contain a beta-sheet structure CC called 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 CC 3C-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; KW Transport; Viral movement protein; Virion. FT CHAIN 1 1009 RNA2 polyprotein. FT /FTId=PRO_0000445854. FT CHAIN 1 90 VP58. FT /FTId=PRO_0000445855. FT CHAIN 91 451 Movement protein. FT /FTId=PRO_0000037037. FT CHAIN 452 825 Large capsid protein. FT /FTId=PRO_0000037038. FT CHAIN 826 1009 Small capsid protein. FT /FTId=PRO_0000037039. FT REGION 387 393 Involved in tubule formation by the FT movement protein. FT {ECO:0000250|UniProtKB:P03599}. FT SITE 451 452 Cleavage; by viral protease. FT {ECO:0000269|PubMed:8503782}. FT SITE 468 468 Interaction with the viral RNA. FT {ECO:0000250|UniProtKB:P03599}. FT SITE 825 826 Cleavage; by viral protease. FT {ECO:0000269|PubMed:8503782}. FT VARIANT 315 315 R -> K (in strain Melon). {ECO:0000305}. FT VARIANT 562 562 D -> N (in strain Melon). {ECO:0000305}. FT VARIANT 740 740 A -> R (in strain Melon). {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 //