GAG_SCVLA
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 03-AUG-2022, entry version 84.
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";
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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 PRIDE; P32503; -.
DR GeneID; 940477; -.
DR KEGG; vg:940477; -.
DR EvolutionaryTrace; P32503; -.
DR Proteomes; UP000000351; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1840.10; -; 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; SSF82856; 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
