ID GAG_SCVLA Reviewed; 680 AA. AC P32503; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 22-FEB-2023, entry version 86. DE RecName: Full=Major capsid protein; DE AltName: Full=Gag protein; DE AltName: Full=Major coat protein; GN Name=gag; OS Saccharomyces cerevisiae virus L-A (ScV-L-A) (ScVL1). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes; OC Ghabrivirales; Totiviridae; Totivirus. OX NCBI_TaxID=11008; OH NCBI_TaxID=4932; Saccharomyces cerevisiae (Baker's yeast). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2651431; DOI=10.1016/s0021-9258(18)83488-3; RA Icho T., Wickner R.B.; RT "The double-stranded RNA genome of yeast virus L-A encodes its own putative RT RNA polymerase by fusing two open reading frames."; RL J. Biol. Chem. 264:6716-6723(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-27. RX PubMed=6366515; DOI=10.1128/mcb.4.1.92-100.1984; RA Thiele D.J., Hannig E.M., Leibowitz M.J.; RT "Multiple L double-stranded RNA species of Saccharomyces cerevisiae: RT evidence for separate encapsidation."; RL Mol. Cell. Biol. 4:92-100(1984). RN [3] RP ACETYLATION AT MET-1. RX PubMed=1400344; DOI=10.1016/s0021-9258(19)88697-0; RA Tercero J.C., Wickner R.B.; RT "MAK3 encodes an N-acetyltransferase whose modification of the L-A gag NH2 RT terminus is necessary for virus particle assembly."; RL J. Biol. Chem. 267:20277-20281(1992). RN [4] RP FUNCTION. RX PubMed=1630453; DOI=10.1128/mcb.12.8.3390-3398.1992; RA Blanc A., Goyer C., Sonenberg N.; RT "The coat protein of the yeast double-stranded RNA virus L-A attaches RT covalently to the cap structure of eukaryotic mRNA."; RL Mol. Cell. Biol. 12:3390-3398(1992). RN [5] RP FUNCTION. RX PubMed=7739557; DOI=10.1128/mcb.15.5.2763; RA Masison D.C., Blanc A., Ribas J.C., Carroll K., Sonenberg N., Wickner R.B.; RT "Decoying the cap- mRNA degradation system by a double-stranded RNA virus RT and poly(A)- mRNA surveillance by a yeast antiviral system."; RL Mol. Cell. Biol. 15:2763-2771(1995). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS). RX PubMed=12244300; DOI=10.1038/nsb844; RA Naitow H., Tang J., Canady M., Wickner R.B., Johnson J.E.; RT "L-A virus at 3.4 A resolution reveals particle architecture and mRNA RT decapping mechanism."; RL Nat. Struct. Biol. 9:725-728(2002). CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid CC with a T=2 symmetry, 40 nm in diameter, and consisting of 60 capsid CC proteins asymmetric dimers. The capsid encapsulates the genomic dsRNA CC and the polymerase and remains intact following cell entry to protect CC the dsRNA from degradation and to prevent unfavorable antiviral CC responses in the host cell during all the replication cycle of the CC virus. Nascent transcripts are transcribed within the structural CC confines of the virion and are extruded into the cytoplasm. CC -!- FUNCTION: Binds and removes 5' cap structures from cellular mRNA. Forms CC a covalent bond with m7GMP through His-154 of the capsid protein while CC releasing the mRNA body. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Ribosomal frameshifting; Named isoforms=2; CC Name=Major capsid protein; Synonyms=Gag protein; CC IsoId=P32503-1; Sequence=Displayed; CC Name=RNA-directed RNA polymerase; Synonyms=Pol protein; CC IsoId=Q87022-1; Sequence=External; CC -!- PTM: Acetylation is necessary for viral assembly. CC {ECO:0000269|PubMed:1400344}. CC -!- MISCELLANEOUS: [Isoform Major capsid protein]: Produced by conventional CC translation. CC -!- SIMILARITY: Belongs to the totivirus major capsid protein family. CC {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=1m1c"; 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; J04692; AAA50506.1; -; Genomic_RNA. DR PIR; S26764; S26764. DR RefSeq; NP_620494.1; NC_003745.1. [P32503-1] DR PDB; 1M1C; X-ray; 3.50 A; A/B=1-680. DR PDB; 6YGD; X-ray; 2.75 A; D=1-5. DR PDBsum; 1M1C; -. DR PDBsum; 6YGD; -. DR SMR; P32503; -. DR iPTMnet; P32503; -. DR GeneID; 940477; -. DR KEGG; vg:940477; -. DR OrthoDB; 6256at10239; -. DR EvolutionaryTrace; P32503; -. DR Proteomes; UP000000351; Genome. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR Gene3D; 3.90.1840.10; Major capsid protein; 1. DR InterPro; IPR015302; Major_coat_LA-virus. DR InterPro; IPR036332; Major_coat_LA-virus_sf. DR Pfam; PF09220; LA-virus_coat; 1. DR SUPFAM; SSF82856; L-A virus major coat protein; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Capsid protein; Reference proteome; KW Ribosomal frameshifting; Virion. FT CHAIN 1..680 FT /note="Major capsid protein" FT /id="PRO_0000222991" FT MOD_RES 1 FT /note="N-acetylmethionine; by host N-acetyltransferase FT MAK3" FT /evidence="ECO:0000269|PubMed:1400344" FT CONFLICT 26..27 FT /note="FV -> LL (in Ref. 2)" FT /evidence="ECO:0000305" FT HELIX 2..5 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 6..11 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 26..38 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 41..54 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 86..95 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 101..110 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 121..138 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 208..217 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 252..256 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 269..282 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 286..298 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 313..315 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 333..336 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 340..344 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 345..356 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 359..382 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 383..385 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 394..396 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 402..414 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 416..418 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 422..425 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 439..443 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 458..463 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 470..475 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 478..481 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 486..491 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 499..505 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 506..518 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 521..525 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 528..530 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 541..543 FT /evidence="ECO:0007829|PDB:1M1C" FT HELIX 550..553 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 554..556 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 559..567 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 581..583 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 587..600 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 601..603 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 604..606 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 613..615 FT /evidence="ECO:0007829|PDB:1M1C" FT STRAND 623..627 FT /evidence="ECO:0007829|PDB:1M1C" FT TURN 631..634 FT /evidence="ECO:0007829|PDB:1M1C" SQ SEQUENCE 680 AA; 75994 MW; 32353D8B7F05C943 CRC64; MLRFVTKNSQ DKSSDLFSIC SDRGTFVAHN RVRTDFKFDN LVFNRVYGVS QKFTLVGNPT VCFNEGSSYL EGIAKKYLTL DGGLAIDNVL NELRSTCGIP GNAVASHAYN ITSWRWYDNH VALLMNMLRA YHLQVLTEQG QYSAGDIPMY HDGHVKIKLP VTIDDTAGPT QFAWPSDRST DSYPDWAQFS ESFPSIDVPY LDVRPLTVTE VNFVLMMMSK WHRRTNLAID YEAPQLADKF AYRHALTVQD ADEWIEGDRT DDQFRPPSSK VMLSALRKYV NHNRLYNQFY TAAQLLAQIM MKPVPNCAEG YAWLMHDALV NIPKFGSIRG RYPFLLSGDA ALIQATALED WSAIMAKPEL VFTYAMQVSV ALNTGLYLRR VKKTGFGTTI DDSYEDGAFL QPETFVQAAL ACCTGQDAPL NGMSDVYVTY PDLLEFDAVT QVPITVIEPA GYNIVDDHLV VVGVPVACSP YMIFPVAAFD TANPYCGNFV IKAANKYLRK GAVYDKLEAW KLAWALRVAG YDTHFKVYGD THGLTKFYAD NGDTWTHIPE FVTDGDVMEV FVTAIERRAR HFVELPRLNS PAFFRSVEVS TTIYDTHVQA GAHAVYHASR INLDYVKPVS TGIQVINAGE LKNYWGSVRR TQQGLGVVGL TMPAVMPTGE PTAGAAHEEL IEQADNVLVE //