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 21-SEP-2011, entry version 50. 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; dsRNA viruses; Totiviridae; Totivirus. OX NCBI_TaxID=11008; OH NCBI_TaxID=4932; Saccharomyces cerevisiae (Baker's yeast). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=89214077; PubMed=2651431; RA Icho T., Wickner R.B.; RT "The double-stranded RNA genome of yeast virus L-A encodes its own RT putative 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; 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 FUNCTION. RX PubMed=1630453; 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 [4] RP FUNCTION. RX PubMed=7739557; RA Masison D.C., Blanc A., Ribas J.C., Carroll K., Sonenberg N., RA Wickner R.B.; RT "Decoying the cap- mRNA degradation system by a double-stranded RNA RT virus and poly(A)- mRNA surveillance by a yeast antiviral system."; RL Mol. Cell. Biol. 15:2763-2771(1995). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND MASS RP SPECTROMETRY. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). 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 CC capsid with a T=2 symmetry, 40 nm in diameter, and consisting of CC 60 capsid proteins asymmetric dimers. The capsid encapsulates the CC genomic dsRNA and the polymerase and remains intact following cell CC entry to protect the dsRNA from degradation and to prevent CC unfavorable antiviral responses in the host cell during all the CC replication cycle of the virus. Nacent transcripts are transcribed CC within the structural confines of the virion and are extruded into CC the cytoplasm. CC -!- FUNCTION: Binds and removes 5' cap structures from cellular mRNA. CC Forms a covalent bond with m7GMP through His-154 of the capsid CC protein while releasing the mRNA body. CC -!- SUBCELLULAR LOCATION: Virion (Potential). 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 Note=Produced by conventional translation; CC Name=RNA-directed RNA polymerase; Synonyms=Pol protein; CC IsoId=Q87022-1; Sequence=External; CC Note=Produced by -1 ribosomal frameshifting; CC -!- PTM: Acetylation is necessary for viral assembly. CC -!- SIMILARITY: Belongs to the totivirus major capsid protein family. CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral CC capsid structure; CC URL="http://viperdb.scripps.edu/info_page.php?VDB=1m1c"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J04692; AAA50506.1; -; Genomic_RNA. DR PIR; S26764; S26764. DR RefSeq; NP_620494.1; NC_003745.1. DR PDB; 1M1C; X-ray; 3.50 A; A/B=1-680. DR PDBsum; 1M1C; -. DR ProteinModelPortal; P32503; -. DR SMR; P32503; 1-651. DR PRIDE; P32503; -. DR GeneID; 940477; -. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR InterPro; IPR015302; Major_coat_LA-virus. DR Pfam; PF09220; LA-virus_coat; 1. DR SUPFAM; SSF82856; Major_coat_LA-virus; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Capsid protein; Complete proteome; KW Phosphoprotein; Reference proteome; Ribosomal frameshifting; Virion. FT CHAIN 1 680 Major capsid protein. FT /FTId=PRO_0000222991. FT MOD_RES 1 1 N-acetylmethionine; by host N- FT acetyltransferase MAK3. FT MOD_RES 580 580 Phosphoserine. FT CONFLICT 26 27 FV -> LL (in Ref. 2). FT HELIX 2 5 FT TURN 6 11 FT STRAND 22 24 FT STRAND 26 38 FT STRAND 41 54 FT STRAND 60 64 FT HELIX 75 77 FT STRAND 80 84 FT HELIX 86 95 FT HELIX 101 110 FT HELIX 121 138 FT STRAND 153 157 FT TURN 165 167 FT TURN 178 180 FT STRAND 195 198 FT STRAND 200 202 FT HELIX 208 217 FT STRAND 225 227 FT HELIX 228 230 FT STRAND 241 243 FT HELIX 252 256 FT TURN 261 263 FT HELIX 269 282 FT HELIX 286 298 FT HELIX 309 312 FT TURN 313 315 FT STRAND 319 323 FT TURN 333 336 FT STRAND 340 344 FT HELIX 345 356 FT HELIX 359 382 FT TURN 383 385 FT TURN 394 396 FT HELIX 398 400 FT HELIX 402 414 FT STRAND 416 418 FT STRAND 422 425 FT STRAND 427 429 FT HELIX 431 433 FT STRAND 439 443 FT STRAND 458 463 FT TURN 470 475 FT STRAND 478 481 FT STRAND 486 491 FT STRAND 495 497 FT STRAND 499 505 FT HELIX 506 518 FT STRAND 521 525 FT STRAND 528 530 FT TURN 541 543 FT HELIX 550 553 FT STRAND 554 556 FT STRAND 559 567 FT TURN 581 583 FT STRAND 587 600 FT TURN 601 603 FT STRAND 604 606 FT TURN 613 615 FT STRAND 623 627 FT TURN 631 634 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 //