POLS_CRPVC
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 03-AUG-2022, entry version 101.
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.
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";
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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 PRIDE; P13418; -.
DR GeneID; 944542; -.
DR KEGG; vg:944542; -.
DR EvolutionaryTrace; P13418; -.
DR Proteomes; UP000008590; Genome.
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.
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
