ID   GAG_AVIMA               Reviewed;         124 AA.
AC   P26315;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Proteinase p15;
DE            EC=3.4.23.-;
GN   Name=gag;
OS   Avian myeloblastosis associated virus (MAV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC   unclassified Alpharetrovirus.
OX   NCBI_TaxID=11960;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 1-8.
RX   PubMed=1733789; DOI=10.1016/0020-711x(92)90252-v;
RA   Pichova I., Strop P., Sedlacek J., Kapralek F., Benes V., Travnicek M.,
RA   Pavlickova L., Soucek M., Kostka V., Foundling S.;
RT   "Isolation, biochemical characterization and crystallization of the p15gag
RT   proteinase of myeloblastosis associated virus expressed in E. coli.";
RL   Int. J. Biochem. 24:235-242(1992).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE.
RX   PubMed=6268146; DOI=10.1021/bi00516a018;
RA   Sauer R.T., Allen D.W., Niall H.D.;
RT   "Amino acid sequence of p15 from avian myeloblastosis virus complex.";
RL   Biochemistry 20:3784-3791(1981).
RN   [3]
RP   SPECIFICITY STUDIES.
RX   PubMed=2026269; DOI=10.1016/0014-5793(91)80447-b;
RA   Konvalinka J., Blaha I., Skrabana R., Sedlacek J., Pichova I., Kapralek F.,
RA   Kostka V., Strop P.;
RT   "Subsite specificity of the proteinase from myeloblastosis associated
RT   virus.";
RL   FEBS Lett. 282:73-76(1991).
RN   [4]
RP   SPECIFICITY STUDIES.
RX   PubMed=1849425; DOI=10.1021/bi00228a013;
RA   Strop P., Konvalinka J., Stys D., Pavlickova L., Blaha I., Velek J.,
RA   Travnicek M., Kostka V., Sedlacek J.;
RT   "Specificity studies on retroviral proteinase from myeloblastosis-
RT   associated virus.";
RL   Biochemistry 30:3437-3443(1991).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=1332025; DOI=10.1002/prot.340140307;
RA   Ohlendorf D.H., Foundling S.I., Wendoloski J.J., Sedlacek J., Strop P.,
RA   Salemme F.R.;
RT   "Structural studies of the retroviral proteinase from avian myeloblastosis
RT   associated virus.";
RL   Proteins 14:382-391(1992).
CC   -!- FUNCTION: Specifically liberates the five major structural proteins
CC       from the common gag precursor, as well as reverse transcriptase and
CC       integrase from the gag-pol precursor.
CC   -!- SUBUNIT: The protease is active as a homodimer.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Pol polyprotein.
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DR   PDB; 1MVP; X-ray; 2.20 A; A/B=1-124.
DR   PDBsum; 1MVP; -.
DR   SMR; P26315; -.
DR   BRENDA; 3.4.23.B13; 592.
DR   EvolutionaryTrace; P26315; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05482; HIV_retropepsin_like; 1.
DR   Gene3D; 2.40.70.10; -; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR034170; Retropepsin-like_cat_dom.
DR   InterPro; IPR018061; Retropepsins.
DR   Pfam; PF00077; RVP; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aspartyl protease; Direct protein sequencing; Hydrolase;
KW   Protease.
FT   CHAIN           1..124
FT                   /note="Proteinase p15"
FT                   /id="PRO_0000199554"
FT   DOMAIN          32..113
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   ACT_SITE        37
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          12..19
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   HELIX           111..116
FT                   /evidence="ECO:0007829|PDB:1MVP"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:1MVP"
SQ   SEQUENCE   124 AA;  13596 MW;  3B8FF451AF43BBB1 CRC64;
     LAMTMEHKDR PLVRVILTNT GSHPVKQRSV YITALLDSGA DITIISEEDW PTDWPVMEAA
     NPQIHGIGGG IPMRKSRDMI EVGVINRDGS LERPLLLFPA VAMVRGSILG RDCLQGLGLR
     LTNL