GAG_JEMBR
ID GAG_JEMBR Reviewed; 436 AA.
AC Q82850;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 91.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Pr53Gag;
DE Contains:
DE RecName: Full=Matrix protein p16;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p26;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p13;
DE Short=NC;
GN Name=gag;
OS Jembrana disease virus (JDV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=36370;
OH NCBI_TaxID=9906; Bos javanicus (Wild banteng).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Tabanan/87;
RX PubMed=9049370; DOI=10.1099/0022-1317-76-7-1637;
RA Chadwick B.J., Coelen R.J., Wilcox G.E., Sammels L.M., Kertayadnya G.;
RT "Nucleotide sequence analysis of Jembrana disease virus: a bovine
RT lentivirus associated with an acute disease syndrome.";
RL J. Gen. Virol. 76:1637-1650(1995).
CC -!- FUNCTION: Matrix protein p16 forms the outer shell of the core of the
CC virus, lining the inner surface of the viral membrane. {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p26 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p13 encapsulates and protects viral
CC dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
CC fingers (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p26]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p13]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=This strategy of translation probably allows the virus to
CC modulate the quantity of each viral protein.;
CC Name=Gag polyprotein;
CC IsoId=Q82850-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=Q82851-1; Sequence=External;
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. Nucleocapsid protein p13 contains one L
CC domain: a PTAP/PSAP motif, which interacts with the UEV domain of
CC TSG101 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation.
CC -!- SIMILARITY: Belongs to the bovine lentivirus group gag polyprotein
CC family. {ECO:0000305}.
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DR EMBL; U21603; AAA64388.1; -; Genomic_RNA.
DR SMR; Q82850; -.
DR Proteomes; UP000246436; Genome.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR012344; Matrix_HIV/RSV_N.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 3: Inferred from homology;
KW Capsid protein; Host-virus interaction; Metal-binding; Reference proteome;
KW Repeat; Ribosomal frameshifting; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral nucleoprotein; Viral release from host cell; Virion;
KW Virion maturation; Zinc; Zinc-finger.
FT CHAIN 1..436
FT /note="Gag polyprotein"
FT /id="PRO_0000272349"
FT CHAIN 1..125
FT /note="Matrix protein p16"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272350"
FT CHAIN 126..344
FT /note="Capsid protein p26"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272351"
FT CHAIN 345..436
FT /note="Nucleocapsid protein p13"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272352"
FT ZN_FING 368..385
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 386..403
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 400..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 428..431
FT /note="PTAP/PSAP motif"
FT COMPBIAS 404..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 125..126
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
FT SITE 344..345
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255"
SQ SEQUENCE 436 AA; 48785 MW; D57C822435006384 CRC64;
MKLSKLEKAL KKVRVTPQRD DTYTIGNVLW AIRMCRLMGL DCCIDEATAA EVAILIGRFQ
SLDLQDSPLK GKDEKAILTT LKVLWSLLAG HHPENSDMAE KYWEAWTIRE RESQKEEEGE
ITSIYPQLRK NFPAVSTSDG SPRYDPDLTK QLKIWADATE KHGVDHHAVN ILGVITANLT
QSEIRLLLQS TPQWRLDIQL IESKLNAREH AHRVWKESHP EAPKTDEIIG KGLTAAEQAT
LTTQECRDTY RQWVLEAALE VAQGKHDRPG PINIHQGPKE PYPEFVNKLV TALEGMAAPE
TTKQYLLDHL SVDHANEDCR AVLLPLGPSA PMERKLEACR AVGSSKQKMQ FLAEAFAAIN
VKGDGEVQRC YGCGKPGHIR RDCKNQKCFK CGKPGHLQRN CKSKNGRRSS APSGQRSGYH
QEKTSVTPSA PPLVLD
