ID   GAG_AVIMD               Reviewed;         453 AA.
AC   P06444;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   23-FEB-2022, entry version 88.
DE   RecName: Full=Gag polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p19;
DE   Contains:
DE     RecName: Full=p2A;
DE   Contains:
DE     RecName: Full=p2B;
DE   Contains:
DE     RecName: Full=p10;
DE   Contains:
DE     RecName: Full=Capsid protein p27, truncated;
GN   Name=gag;
OS   Avian myelocytomatosis virus HBI.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae.
OX   NCBI_TaxID=11915;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2999450; DOI=10.1128/jvi.56.3.969-977.1985;
RA   Smith D.R., Vennstrom B., Hayman M.J., Enrietto P.J.;
RT   "Nucleotide sequence of HBI, a novel recombinant MC29 derivative with
RT   altered pathogenic properties.";
RL   J. Virol. 56:969-977(1985).
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC   -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC       sequence motifs essential for viral particle budding. They recruit
CC       proteins of the host ESCRT machinery (Endosomal Sorting Complex
CC       Required for Transport) or ESCRT-associated proteins. Gag contains one
CC       L domain: a PPXY motif which potentially interacts with the WW domain 3
CC       of NEDD4 E3 ubiquitin ligase (Potential). {ECO:0000305}.
CC   -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. {ECO:0000250|UniProtKB:P03322}.
CC   -!- MISCELLANEOUS: [Gag polyprotein]: This protein is synthesized as a Gag-
CC       vMyc polyprotein. {ECO:0000305}.
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DR   EMBL; M11784; AAA42406.1; -; Genomic_DNA.
DR   PIR; A03924; FOFVHB.
DR   SMR; P06444; -.
DR   GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
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; IPR004028; Gag_M.
DR   InterPro; IPR000721; Gag_p24_N.
DR   InterPro; IPR012344; Matrix_HIV/RSV_N.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF02813; Retro_M; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
DR   SUPFAM; SSF47943; SSF47943; 1.
PE   3: Inferred from homology;
KW   Host-virus interaction; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral matrix protein;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..453
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000442121"
FT   CHAIN           1..155
FT                   /note="Matrix protein p19"
FT                   /id="PRO_0000040818"
FT   CHAIN           156..166
FT                   /note="p2A"
FT                   /id="PRO_0000442122"
FT   CHAIN           167..177
FT                   /note="p2B"
FT                   /id="PRO_0000442123"
FT   CHAIN           178..239
FT                   /note="p10"
FT                   /id="PRO_0000040819"
FT   CHAIN           240..453
FT                   /note="Capsid protein p27, truncated"
FT                   /id="PRO_0000040820"
FT   REGION          100..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           172..175
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   COMPBIAS        114..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            155..156
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            166..167
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            177..178
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            239..240
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
SQ   SEQUENCE   453 AA;  47563 MW;  B16F1F92DE62991E CRC64;
     MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS WDPITAALSQ
     RAMVLGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ESIEKPATER
     RIDKGEEVGE TTVQRDAKMA PEETATPKTV GTSCYHCGTA IGCNCATASA PPPPYVGSGL
     YPSLAGVGEL QGQGGDTPRG AEQPRAEPGH AGLAPGPALT DWARVGEELA STGPPVVAMP
     VVIKTEGPAW TPLEPKLITR LADTVRAKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL
     GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLDRLKGLAD GMVGNPQGQA
     ALLRPGELVA ITASALQAFR EVARLAEPAG PWADITQGPS ESFVDFANRL IKAVEGSDLP
     PSARAPVIID CFRQKSQPDI QQLIRAAPST VHG