ID POLS_CRPVC Reviewed; 895 AA. AC P13418; Q9IJX3; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 2. DT 13-SEP-2023, entry version 104. DE RecName: Full=Structural polyprotein; DE Contains: DE RecName: Full=Capsid protein 1; DE AltName: Full=CP1; DE Contains: DE RecName: Full=Capsid protein 4; DE AltName: Full=CP4; DE Contains: DE RecName: Full=Capsid protein 2; DE AltName: Full=CP2; DE Contains: DE RecName: Full=Capsid protein 3; DE AltName: Full=CP3; OS Cricket paralysis virus (isolate Teleogryllus OS commodus/Australia/CrPVVIC/1968) (CrPV). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Dicistroviridae; Cripavirus; Cripavirus grylli. OX NCBI_TaxID=928300; OH NCBI_TaxID=128161; Teleogryllus oceanicus (black field cricket). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=10866656; DOI=10.1128/mcb.20.14.4990-4999.2000; RA Wilson J.E., Powell M.J., Hoover S.E., Sarnow P.; RT "Naturally occurring dicistronic cricket paralysis virus RNA is regulated RT by two internal ribosome entry sites."; RL Mol. Cell. Biol. 20:4990-4999(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 444-895. RA King L.A., Pullin J.S.K., Stanway G., Almond J.W., Moore N.F.; RT "Cloning of the genome of cricket paralysis virus: sequence of the 3' RT end."; RL Virus Res. 6:331-344(1987). RN [3] RP NON-METHIONINE TRANSLATION INITIATION. RX PubMed=15992743; DOI=10.1016/j.crvi.2005.02.004; RA Pisarev A.V., Shirokikh N.E., Hellen C.U.; RT "Translation initiation by factor-independent binding of eukaryotic RT ribosomes to internal ribosomal entry sites."; RL C. R. Biol. 328:589-605(2005). RN [4] RP NON-METHIONINE TRANSLATION INITIATION. RX PubMed=19299549; DOI=10.1261/rna.1315109; RA Deniz N., Lenarcic E.M., Landry D.M., Thompson S.R.; RT "Translation initiation factors are not required for Dicistroviridae IRES RT function in vivo."; RL RNA 15:932-946(2009). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 8-895, AND POLYPROTEIN PROTEOLYTIC RP CLEAVAGES. RX PubMed=10426956; DOI=10.1038/11543; RA Tate J., Liljas L., Scotti P., Christian P., Lin T., Johnson J.E.; RT "The crystal structure of cricket paralysis virus: the first view of a new RT virus family."; RL Nat. Struct. Biol. 6:765-774(1999). CC -!- FUNCTION: [Structural polyprotein]: Precursor of all the viral capsid CC proteins. CC -!- FUNCTION: Capsid protein 1, together with capsid proteins 2 and 3, form CC an icosahedral capsid protecting the viral RNA genome. The icosahedral CC capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 CC Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 CC is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at CC the quasi-sixfold axes. All these proteins contain a beta-sheet CC structure called beta-barrel jelly roll. CC -!- FUNCTION: Capsid protein 4 is a tstructural component of the CC icosahedral capsid protecting the genomic RNA. It may play an important CC role in capsid assembly. CC -!- FUNCTION: Capsid protein 2, together with capsid proteins 1 and 3, form CC an icosahedral capsid protecting the viral RNA genome. The icosahedral CC capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 CC Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 CC is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at CC the quasi-sixfold axes. All these proteins contain a beta-sheet CC structure called beta-barrel jelly roll. CC -!- FUNCTION: Capsid protein 3, together with capsid proteins 1 and 2, form CC an icosahedral capsid protecting the viral RNA genome. The icosahedral CC capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 CC Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 CC is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at CC the quasi-sixfold axes. All these proteins contain a beta-sheet CC structure called beta-barrel jelly roll. CC -!- SUBCELLULAR LOCATION: [Capsid protein 1]: Virion. Host cytoplasm CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Capsid protein 4]: Virion. Host cytoplasm CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Capsid protein 2]: Virion. Host cytoplasm CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Capsid protein 3]: Virion. Host cytoplasm CC {ECO:0000305}. CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family. CC {ECO:0000305}. CC -!- CAUTION: Translation initiates on an Ala codon through an unusual CC Internal Ribosome Entry Site (IRES). {ECO:0000305}. CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid CC structure; CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1b35"; 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; AF218039; AAF80999.1; -; Genomic_RNA. DR EMBL; M21938; AAA42889.1; -; Genomic_RNA. DR PIR; S28374; S28374. DR RefSeq; NP_647482.1; NC_003924.1. DR PDB; 1B35; X-ray; 2.40 A; A=636-895, B=8-243, C=341-622, D=284-340. DR PDBsum; 1B35; -. DR SMR; P13418; -. DR GeneID; 944542; -. DR KEGG; vg:944542; -. DR EvolutionaryTrace; P13418; -. DR Proteomes; UP000008590; Segment. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR CDD; cd00205; rhv_like; 2. DR Gene3D; 2.60.120.20; -; 3. DR InterPro; IPR014872; Dicistrovirus_capsid-polyPr_C. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR033703; Rhv-like. DR InterPro; IPR029053; Viral_coat. DR InterPro; IPR024343; VP4_dicistrovir. DR Pfam; PF08762; CRPV_capsid; 1. DR Pfam; PF11492; Dicistro_VP4; 1. DR Pfam; PF00073; Rhv; 2. DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 3. PE 1: Evidence at protein level; KW 3D-structure; Capsid protein; Host cytoplasm; Reference proteome; Virion. FT CHAIN 1..895 FT /note="Structural polyprotein" FT /id="PRO_0000123825" FT CHAIN 1..283 FT /note="Capsid protein 1" FT /id="PRO_0000398368" FT CHAIN 284..340 FT /note="Capsid protein 4" FT /id="PRO_0000398369" FT CHAIN 341..635 FT /note="Capsid protein 2" FT /id="PRO_0000398370" FT CHAIN 636..895 FT /note="Capsid protein 3" FT /id="PRO_0000398371" FT SITE 283..284 FT /note="Cleavage" FT SITE 340..341 FT /note="Cleavage" FT SITE 635..636 FT /note="Cleavage" FT CONFLICT 445..447 FT /note="THM -> HTH (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 451 FT /note="A -> T (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 556 FT /note="V -> T (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 579 FT /note="S -> N (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 594..595 FT /note="YV -> MY (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 601 FT /note="L -> D (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 641..642 FT /note="QQ -> HE (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 648 FT /note="A -> G (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 678..683 FT /note="VSIRQL -> IDSTT (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 746 FT /note="A -> V (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 854..855 FT /note="SP -> A (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT CONFLICT 861..895 FT /note="ATNHHITASFMRAPGDDFSFMYLLEVPPLVNVARA -> TTHTRSYACAW FT (in Ref. 2; AAA42889)" FT /evidence="ECO:0000305" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 19..24 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 27..33 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 53..56 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 72..80 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 88..94 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 96..99 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 102..108 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 111..125 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 131..140 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 146..153 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 169..171 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 174..179 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 190..193 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 198..209 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 211..213 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 217..234 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 285..293 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 320..323 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 331..337 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 356..359 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 384..387 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 396..400 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 404..412 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 420..425 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 431..437 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 440..444 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 446..451 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 455..459 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 461..468 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 473..483 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 488..490 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 491..493 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 497..499 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 500..509 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 512..517 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 522..524 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 534..536 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 542..545 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 546..548 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 552..564 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 570..580 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 593..597 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 603..617 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 637..639 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 645..648 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 649..651 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 667..672 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 680..683 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 688..696 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 702..705 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 716..718 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 725..729 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 730..732 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 733..737 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 740..751 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 756..758 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 763..768 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 770..772 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 773..778 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 785..789 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 793..795 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 801..805 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 807..810 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 811..817 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 822..824 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 831..834 FT /evidence="ECO:0007829|PDB:1B35" FT HELIX 838..842 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 850..857 FT /evidence="ECO:0007829|PDB:1B35" FT TURN 861..863 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 864..874 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 879..883 FT /evidence="ECO:0007829|PDB:1B35" FT STRAND 889..891 FT /evidence="ECO:0007829|PDB:1B35" SQ SEQUENCE 895 AA; 100298 MW; 92DA9084DDA850EE CRC64; ATFQDKQENS HIENEDKRLM SEQKEIVHFV SEGITPSTTA LPDIVNLSTN YLDMTTREDR IHSIKDFLSG PIIIATNLWS SSDPVEKQLY TANFPEVLIS NAMYQDKLKG FVGLRATLVV KVQVNSQPFQ QGRLMLQYIP YAQYMPNRVT LINETLQGRS GCPTTDLELS VGTEVEMRIP YVSPHLYYNL ITGQGSFGSI YVVVYSQLHD QVSGTGSIEY TVWAHLEDVD VQYPTGANIF TGNSPNYLSI AERIATGDFT ETEMRKLWIH KTYLKRPARI YAQAAKELKQ LETNNSPSTA LGQISEGLTT LSHIPVLGNI FSTPAWISAK AADLAKLFGF SKPTVQGKIG ECKLRGQGRM ANFDGMDMSH KMALSSTNEI ETKEGLAGTS LDEMDLSRVL SIPNYWDRFT WKTSDVTNTV LWDNYVSPFK VKPYSATITD RFRCTHMGYV ANAFTYWRGS IVYTFKFVKT QYHSGRLRIS FIPYYYNTTI STGTPDVSRT QKIVVDLRTS TEVSFTVPYI ASRPWLYCIR PESSWLSKDN KDGALMYNCV SGIVRVEVLN QLVAAQNVFS EIDVICEVSG GPDLEFAGPT CPSYVPYAGD LTLADTRKIE AERTQEYSNN EDNRITTQCS RIVAQVMGED QQIPRNEAQH GVHPISIDTH RISNNWSPQA MCIGEKIVSI RQLIKRFGIF GDANTLQADG SSFVVAPFTV TSPTKTLTST RNYTQFDYYY YLYAFWRGSM RIKMVAETQD GTGTPRKKTN FTWFVRMFNS LQDSFNSLIS TSSSAVTTTV LPSGTINMGP STQVIDPTVE GLIEVEVPYY NISHITPAVT IDDGTPSMED YLKGHSPPCL LTFSPRDSIS ATNHHITASF MRAPGDDFSF MYLLEVPPLV NVARA //