ID POL2_SQMVM Reviewed; 803 AA. AC P36341; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 2. DT 03-APR-2013, entry version 59. DE RecName: Full=Genome polyprotein M; DE AltName: Full=RNA2 polyprotein; DE Contains: DE RecName: Full=Movement protein; DE Short=MP; DE Contains: DE RecName: Full=Large coat protein; DE Short=LCP; DE AltName: Full=Coat protein VP37; DE Contains: DE RecName: Full=Small coat protein; DE Short=SCP; DE AltName: Full=Coat protein VP23; DE Flags: Fragment; OS Squash mosaic virus (strain melon) (SqMV). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; OC Secoviridae; Comovirinae; Comovirus. OX NCBI_TaxID=36401; OH NCBI_TaxID=3559; Chenopodium album (Lamb's-quarters). 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). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEIN SEQUENCE OF 357-381 AND RP 606-616. 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: The movement protein is assembled into tubules that CC allow the transport of virions from cell to cell. Binds to GTP and CC to single-stranded RNA and single-stranded DNA in a non-sequence- CC specific manner (By similarity). CC -!- SUBCELLULAR LOCATION: Movement protein: Host cell junction, host CC plasmodesma (By similarity). Note=Assembles in tubules that are CC embedded within modified plasmodesmata (By similarity). CC -!- SUBCELLULAR LOCATION: Large coat protein: Virion (Potential). CC -!- PTM: Specific enzymatic cleavages by RNA1 encoded picornain 3C- CC like protease in vivo yield mature proteins (By similarity). CC -!- PTM: The N-terminus of the 42 kDa coat protein is blocked. CC -!- MISCELLANEOUS: The virus capsid is composed of 60 icosahedral CC units, each of which is composed of one copy each of the two coat CC proteins. CC -!- SIMILARITY: Belongs to the comoviridae genome polyprotein M CC family. 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 PIR; A48356; A48356. DR ProteinModelPortal; P36341; -. DR SMR; P36341; 247-619. DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C: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:spread of virus in host, cell to cell; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR003181; Como_LCP. DR InterPro; IPR003182; Como_SCP. 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; Transport; KW Viral movement protein; Virion. FT CHAIN <1 245 Movement protein (By similarity). FT /FTId=PRO_0000037037. FT CHAIN 246 619 Large coat protein (By similarity). FT /FTId=PRO_0000037038. FT CHAIN 620 803 Small coat protein (By similarity). FT /FTId=PRO_0000037039. FT SITE 245 246 Cleavage (By similarity). FT SITE 619 620 Cleavage (By similarity). FT NON_TER 1 1 SQ SEQUENCE 803 AA; 88415 MW; 66ABF5522CA5213C CRC64; NQKAIIITPF YVSMDCFTSP DSNICGGMLL VDTAHLNPDN AIRSVFVAPF IGGRPIRVLL FPDTLVEIAP NMNSRFKLLC TTSNGDVAPD FNLAMVKVNV AGCAVSLTKT YTPTAYLEQE LIKEKGAIVQ YLNRHTFSMH RNNQMTKEEM QKQRLSFRLE SALTLQEKHP LHATFCKSTN FVYKIGGDAK EGSNGNLTVN ESQLSSHSPS AHVLHKHNNS GDNEVEFSEI GVVVPGAGRT KAYGQNELDL AQLSLDDTSS LRGTALQTKL ATSRIILSKT MVGNTVLRED LLATFLQDSN ERAAIDLIRT HVIRGKIRCV ASINVPENTG CALAICFNSG ITGAADTDIY TTSSQNAIVW NPACEKAVEL TFNPNPCGDA WNFVFLQQTK AHFAVQCVTG WTTTPLTDLA LVLTWHIDRS LCVPKTLTIS SAHASFPINR WMGKLSFPQG PARVLKRMPL AIGGGAGTKD AILMNMPNAV ISLHRYFRGD FVFEITKMSS PYIKATIAFF IAFGDITEEM TNLESFPHKL VQFREIQGRT TITFTQSEFL TAWSTQVLST VNPQKDGCPH LYALLHDSAT STIEGNFVIG VKLLDIRNYR AYGHNPGFEG ARLLGISGQS TMVQQLGTYN PIWMVRTPLE STAQQNFASF TADLMESTIS GDSTGNWNIT VYPSPIANLL KVAAWKKGTI RFQLICRGAA VKQSDWAASA RIDLINNLSN KALPARSWYI TKPRGGDIEF DLEIAGPNNG FEMANSSWAF QTTWYLEIAI DNPKQFTLFE LNACLMEDFE VAGNTLNPPI LLS //