CAPSD_GLVWB
ID CAPSD_GLVWB Reviewed; 886 AA.
AC Q67652;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 41.
DE RecName: Full=Major capsid protein;
DE AltName: Full=Gag protein;
DE AltName: Full=Major coat protein;
GN Name=gag;
OS Giardia lamblia virus (isolate Wang) (GLV).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes;
OC Ghabrivirales; Totiviridae; Giardiavirus.
OX NCBI_TaxID=649893;
OH NCBI_TaxID=5741; Giardia intestinalis (Giardia lamblia).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8378334; DOI=10.1073/pnas.90.18.8595;
RA Wang A.L., Yang H.M., Shen K.A., Wang C.C.;
RT "Giardiavirus double-stranded RNA genome encodes a capsid polypeptide and a
RT gag-pol-like fusion protein by a translation frameshift.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8595-8599(1993).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=2 symmetry, 35 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 (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Binds and removes 5' cap structures from cellular mRNA.
CC {ECO:0000250}.
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=Q67652-1; Sequence=Displayed;
CC Name=RNA-directed RNA polymerase; Synonyms=Pol protein;
CC IsoId=Q67653-1; Sequence=External;
CC -!- PTM: Acetylation is necessary for viral assembly. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Major capsid protein]: Produced by conventional
CC translation.
CC -!- SIMILARITY: Belongs to the totivirus major capsid protein family.
CC {ECO:0000305}.
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DR EMBL; L13218; AAB01578.1; -; Genomic_RNA.
DR RefSeq; NP_619551.1; NC_003555.1.
DR GeneID; 940170; -.
DR KEGG; vg:940170; -.
DR Proteomes; UP000000350; Genome.
DR GO; GO:0039616; C:T=2 icosahedral viral capsid; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Acetylation; Capsid protein; Reference proteome; Ribosomal frameshifting;
KW T=2 icosahedral capsid protein; Virion.
FT CHAIN 1..886
FT /note="Major capsid protein"
FT /id="PRO_0000404513"
FT REGION 42..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 886 AA; 98424 MW; C290976C75BA4423 CRC64;
MVWGTGYGNP SPLNPYGFAS LHRGGLNPLI LAPENITFDT LNTHNDHEET HGESPEVPKA
SIAPAGRQNV PVLQQNQENE DNHALGGSED AKDEREIRFS AIKTLYNYYS EGPSTPIMPH
LVNRLRGLDA LAKIDATLTK VDMNAAYIFA LRPTFPYSYG YKQRFSNRRL TTSALCYART
GLSSFLTVDK TYTSNSPLKG GSRGWPIFNV DVSSHVAEPH MRTLSPIGLE VFNLATSQFS
KTLLTASSKV FTQSLYTADI LSIFGEVFLP HVMQPVSNYT PILVRALLAL IHILGPGSGN
CSLSSSIFES SIPQFLTVSH STNMSNRTRY CLHTRSAYKD MFRNGIPPQS TLPPTLAPEG
SSARVLIPEA LVTSPMFPWL LILVSSGPQF FLYSKDASIN TVDIGSRGRI TSPIPDVAKL
DLHRLWNLFR FDGYRYIDVV IVGADRDYVW PYQNGVYVHG GKGPNGTGNY GNADVHDGIG
TIFSSFNNNV NVQTSDLMLG LLTLWNHITT TYATEEEVTM AIKIAAAFAL VYPVQPIVYS
GCPKAFQRHT SYYQPSSENC YATDTAEVKS VWDTVELSVQ VNNAMVLGMT LPFGQPTLSS
AQWYNNIDKA EISMFKVGNL PLQNLDYLSL DMMEFYAPTT GQLYDIRSDN LILSAHRTVN
LGIGYTALAD FFAYLASVPA QSFYHDRMVT SPISKQTYSV YERFIERFID DFVGWDRCDL
FNLDTLLGAK HIAGVASSPI PWHCSLQRCP LPIIMHYTGL TFGQEHITVR DVAGVEGLQQ
IVMRDFQGRI VVERLGTAAP SRIAVKLDWS RLSAWYSDTT CAIPLSDRVM EIVNYAAIWD
PTQERHAQVS CTHTLAPISF RALTCLSLYS IRVSTLHHLM TTRAKL