ID   POL_GALV                Reviewed;        1686 AA.
AC   P21414;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 2.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Gag-Pol polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p15;
DE              Short=MA;
DE   Contains:
DE     RecName: Full=RNA-binding phosphoprotein p12;
DE     AltName: Full=pp12;
DE   Contains:
DE     RecName: Full=Capsid protein p30;
DE              Short=CA;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p10-Pol;
DE              Short=NC-pol;
DE   Contains:
DE     RecName: Full=Protease;
DE              EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
DE   Contains:
DE     RecName: Full=Reverse transcriptase/ribonuclease H;
DE              Short=RT;
DE              EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
DE              EC=2.7.7.7 {ECO:0000255|PROSITE-ProRule:PRU00405};
DE              EC=3.1.26.4 {ECO:0000255|PROSITE-ProRule:PRU00408};
DE   Contains:
DE     RecName: Full=Integrase;
DE              Short=IN;
DE              EC=2.7.7.- {ECO:0000250|UniProtKB:P03355};
DE              EC=3.1.-.- {ECO:0000250|UniProtKB:P03355};
GN   Name=pol;
OS   Gibbon ape leukemia virus (GALV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11840;
OH   NCBI_TaxID=9577; Hylobatidae (gibbons).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2683360; DOI=10.1016/0042-6822(89)90236-5;
RA   Delassus S., Sonigo P., Wain-Hobson S.;
RT   "Genetic organization of gibbon ape leukemia virus.";
RL   Virology 173:205-213(1989).
CC   -!- FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is
CC       processed by the viral protease during virion maturation outside the
CC       cell. During budding, it recruits, in a PPXY-dependent or independent
CC       manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules
CC       to Gag-Pol, or to Gag-Pol binding host factors. Interaction with HECT
CC       ubiquitin ligases probably links the viral protein to the host ESCRT
CC       pathway and facilitates release. {ECO:0000250|UniProtKB:P03332}.
CC   -!- FUNCTION: [Matrix protein p15]: Targets Gag and gag-pol polyproteins to
CC       the plasma membrane via a multipartite membrane binding signal, that
CC       includes its myristoylated N-terminus. Also mediates nuclear
CC       localization of the pre-integration complex.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-
CC       integration complex (PIC) which tethers the latter to mitotic
CC       chromosomes. This allows the integration of the viral genome into the
CC       host DNA. {ECO:0000250|UniProtKB:P03355}.
CC   -!- FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion
CC       that encapsulates the genomic RNA-nucleocapsid complex.
CC       {ECO:0000250|UniProtKB:P03336}.
CC   -!- FUNCTION: [Nucleocapsid protein p10-Pol]: Involved in the packaging and
CC       encapsidation of two copies of the genome (By similarity). Binds with
CC       high affinity to conserved UCUG elements within the packaging signal,
CC       located near the 5'-end of the genome (By similarity). This binding is
CC       dependent on genome dimerization (By similarity). Acts as a nucleic
CC       acid chaperone which is involved in rearrangement of nucleic acid
CC       secondary structures during gRNA retrotranscription (By similarity).
CC       {ECO:0000250|UniProtKB:P03332, ECO:0000250|UniProtKB:P03355}.
CC   -!- FUNCTION: [Protease]: The aspartyl protease mediates proteolytic
CC       cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC       release of the virion from the plasma membrane. Cleavages take place as
CC       an ordered, step-wise cascade to yield mature proteins. This process is
CC       called maturation. Displays maximal activity during the budding process
CC       just prior to particle release from the cell. {ECO:0000255|PROSITE-
CC       ProRule:PRU00275}.
CC   -!- FUNCTION: [Reverse transcriptase/ribonuclease H]: RT is a
CC       multifunctional enzyme that converts the viral dimeric RNA genome into
CC       dsDNA in the cytoplasm, shortly after virus entry into the cell. This
CC       enzyme displays a DNA polymerase activity that can copy either DNA or
CC       RNA templates, and a ribonuclease H (RNase H) activity that cleaves the
CC       RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5'
CC       endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires
CC       many steps. A tRNA binds to the primer-binding site (PBS) situated at
CC       the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to
CC       perform a short round of RNA-dependent minus-strand DNA synthesis. The
CC       reading proceeds through the U5 region and ends after the repeated (R)
CC       region which is present at both ends of viral RNA. The portion of the
CC       RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA
CC       product attached to the tRNA primer. This ssDNA/tRNA hybridizes with
CC       the identical R region situated at the 3' end of viral RNA. This
CC       template exchange, known as minus-strand DNA strong stop transfer, can
CC       be either intra- or intermolecular. RT uses the 3' end of this newly
CC       synthesized short ssDNA to perform the RNA-dependent minus-strand DNA
CC       synthesis of the whole template. RNase H digests the RNA template
CC       except for a polypurine tract (PPT) situated at the 5' end of the
CC       genome. It is not clear if both polymerase and RNase H activities are
CC       simultaneous. RNase H probably can proceed both in a polymerase-
CC       dependent (RNA cut into small fragments by the same RT performing DNA
CC       synthesis) and a polymerase-independent mode (cleavage of remaining RNA
CC       fragments by free RTs). Secondly, RT performs DNA-directed plus-strand
CC       DNA synthesis using the PPT that has not been removed by RNase H as
CC       primers. PPT and tRNA primers are then removed by RNase H. The 3' and
CC       5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate.
CC       Strand displacement synthesis by RT to the PBS and PPT ends produces a
CC       blunt ended, linear dsDNA copy of the viral genome that includes long
CC       terminal repeats (LTRs) at both ends. {ECO:0000255}.
CC   -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host
CC       chromosome, by performing a series of DNA cutting and joining
CC       reactions. This enzyme activity takes place after virion entry into a
CC       cell and reverse transcription of the RNA genome in dsDNA. The first
CC       step in the integration process is 3' processing. This step requires a
CC       complex comprising the viral genome, matrix protein and integrase. This
CC       complex is called the pre-integration complex (PIC). The integrase
CC       protein removes 2 nucleotides from each 3' end of the viral DNA,
CC       leaving recessed CA OH's at the 3' ends. In the second step that
CC       requires cell division, the PIC enters cell nucleus. In the third step,
CC       termed strand transfer, the integrase protein joins the previously
CC       processed 3' ends to the 5' ends of strands of target cellular DNA at
CC       the site of integration. The last step is viral DNA integration into
CC       host chromosome. {ECO:0000250|UniProtKB:P03355}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00405};
CC       Note=The RT polymerase active site binds 2 magnesium ions.
CC       {ECO:0000255|PROSITE-ProRule:PRU00405};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P03355};
CC       Note=Binds 1 magnesium ion for ribonuclease H (RNase H) activity.
CC       {ECO:0000250|UniProtKB:P03355};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P03355};
CC       Note=Magnesium ions are required for integrase activity. Binds at least
CC       1, maybe 2 magnesium ions. {ECO:0000250|UniProtKB:P03355};
CC   -!- ACTIVITY REGULATION: [Protease]: Most efficiently inhibited by
CC       Amprenavir, which is able to block Gag-Pol processing in infected
CC       cells. {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBUNIT: [Capsid protein p30]: Homohexamer; further associates as
CC       homomultimer (By similarity). The virus core is composed of a lattice
CC       formed from hexagonal rings, each containing six capsid monomers (By
CC       similarity). {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBUNIT: [Gag-Pol polyprotein]: Interacts (via PPXY motif) with host
CC       NEDD4 (By similarity). Interacts (via PSAP motif) with host TSG101 (By
CC       similarity). {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBUNIT: [Reverse transcriptase/ribonuclease H]: The reverse
CC       transcriptase is a monomer (Potential). Interacts (via RNase domains)
CC       with host release factor ETF1; this interaction is essential for
CC       translational readthrough of amber codon between viral gag and pol
CC       genes, as well as for viral replication (By similarity).
CC       {ECO:0000250|UniProtKB:P03355, ECO:0000305}.
CC   -!- SUBUNIT: [Integrase]: Homodimer (By similarity).
CC       {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion
CC       {ECO:0000250|UniProtKB:P03332}. Host cell membrane
CC       {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane
CC       {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body
CC       {ECO:0000250|UniProtKB:P26807}. Note=These locations are probably
CC       linked to virus assembly sites. {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion
CC       {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion
CC       {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10-Pol]: Virion
CC       {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBCELLULAR LOCATION: [Protease]: Virion
CC       {ECO:0000250|UniProtKB:P03355}.
CC   -!- SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm
CC       {ECO:0000250|UniProtKB:P03355}. Note=Localizes to the host cytoplasm
CC       early in infection and binds to the mitotic chromosomes later on.
CC       {ECO:0000250|UniProtKB:P03355}.
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. RNA-binding
CC       phosphoprotein p12 contains one L domain: a PPXY motif which
CC       potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC       ligase. Matrix protein p15 contains one L domain: a PTAP/PSAP motif,
CC       which potentially interacts with the UEV domain of TSG101.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral
CC       protease yield mature proteins. The protease is released by
CC       autocatalytic cleavage. The polyprotein is cleaved during and after
CC       budding, this process is termed maturation.
CC       {ECO:0000250|UniProtKB:P03355}.
CC   -!- PTM: [RNA-binding phosphoprotein p12]: Phosphorylated on serine
CC       residues. {ECO:0000250|UniProtKB:P03355}.
CC   -!- MISCELLANEOUS: [Gag-Pol polyprotein]: This protein is translated as a
CC       gag-pol fusion protein by episodic readthrough of the gag protein
CC       termination codon. Readthrough of the terminator codon TAG occurs
CC       between the codons for 520-Asp and 522-Gly.
CC       {ECO:0000250|UniProtKB:P03355}.
CC   -!- MISCELLANEOUS: [Nucleocapsid protein p10-Pol]: Nucleocapsid protein
CC       p10-Pol released from Pol polyprotein (NC-pol) is a few amino acids
CC       shorter than the nucleocapsid protein p10 released from Gag polyprotein
CC       (NC-gag). {ECO:0000250|UniProtKB:P03355}.
CC   -!- MISCELLANEOUS: [Reverse transcriptase/ribonuclease H]: The reverse
CC       transcriptase is an error-prone enzyme that lacks a proof-reading
CC       function. High mutations rate is a direct consequence of this
CC       characteristic. RT also displays frequent template swiching leading to
CC       high recombination rate. Recombination mostly occurs between homologous
CC       regions of the two copackaged RNA genomes. If these two RNA molecules
CC       derive from different viral strains, reverse transcription will give
CC       rise to highly recombinated proviral DNAs. {ECO:0000255|PROSITE-
CC       ProRule:PRU00405}.
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; M26927; AAA46810.1; -; Genomic_RNA.
DR   PIR; B32595; GNLJGL.
DR   RefSeq; NP_056790.1; NC_001885.2.
DR   GeneID; 1491893; -.
DR   KEGG; vg:1491893; -.
DR   Proteomes; UP000008231; Genome.
DR   GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
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:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR   GO; GO:0019068; P:virion assembly; IEA:InterPro.
DR   CDD; cd09273; RNase_HI_RT_Bel; 1.
DR   CDD; cd06095; RP_RTVL_H_like; 1.
DR   CDD; cd03715; RT_ZFREV_like; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 2.30.30.850; -; 1.
DR   Gene3D; 3.10.20.370; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 1.10.150.180; Gamma-retroviral matrix domain; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000840; G_retro_matrix.
DR   InterPro; IPR036946; G_retro_matrix_sf.
DR   InterPro; IPR003036; Gag_P30.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR040643; MLVIN_C.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR018061; Retropepsins.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR041577; RT_RNaseH_2.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   InterPro; IPR015416; Znf_H2C2_histone_UAS-bd.
DR   PANTHER; PTHR33166:SF1; CORE SHELL PROTEIN GAG P30 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01140; Gag_MA; 1.
DR   Pfam; PF02093; Gag_p30; 1.
DR   Pfam; PF18697; MLVIN_C; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF17919; RT_RNaseH_2; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00077; RVP; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   Pfam; PF09337; zf-H2C2; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease; Capsid protein; Coiled coil; DNA integration;
KW   DNA recombination; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW   Host cell membrane; Host cytoplasm; Host endosome; Host membrane;
KW   Host-virus interaction; Hydrolase; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
KW   Nucleotidyltransferase; Phosphoprotein; Protease;
KW   RNA suppression of termination; RNA-binding; RNA-directed DNA polymerase;
KW   Transferase; Viral genome integration; Viral matrix protein;
KW   Viral nucleoprotein; Virion; Virus entry into host cell; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..1686
FT                   /note="Gag-Pol polyprotein"
FT                   /id="PRO_0000259719"
FT   CHAIN           2..125
FT                   /note="Matrix protein p15"
FT                   /id="PRO_0000442883"
FT   CHAIN           126..195
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /id="PRO_0000442884"
FT   CHAIN           196..454
FT                   /note="Capsid protein p30"
FT                   /id="PRO_0000442885"
FT   CHAIN           455..516
FT                   /note="Nucleocapsid protein p10-Pol"
FT                   /id="PRO_0000442886"
FT   CHAIN           517..640
FT                   /note="Protease"
FT                   /id="PRO_0000026128"
FT   CHAIN           641..1309
FT                   /note="Reverse transcriptase/ribonuclease H"
FT                   /id="PRO_0000259720"
FT   CHAIN           1310..1686
FT                   /note="Integrase"
FT                   /id="PRO_0000259721"
FT   DOMAIN          543..613
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   DOMAIN          720..911
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   DOMAIN          1152..1298
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   DOMAIN          1393..1551
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   ZN_FING         489..506
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         1338..1376
FT                   /note="HHCC-type"
FT                   /evidence="ECO:0000250|UniProtKB:P03355"
FT   REGION          111..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1304..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          407..444
FT                   /evidence="ECO:0000255"
FT   MOTIF           116..119
FT                   /note="PTAP/PSAP motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03332"
FT   MOTIF           139..142
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03332"
FT   COMPBIAS        136..156
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        548
FT                   /note="Protease; shared with dimeric partner"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT   BINDING         788
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         862
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         863
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT   BINDING         1161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1199
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT   BINDING         1404
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   BINDING         1463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   SITE            125..126
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03355"
FT   SITE            195..196
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03355"
FT   SITE            454..455
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03355"
FT   SITE            516..517
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03355"
FT   SITE            640..641
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03355"
FT   SITE            1309..1310
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03355"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1686 AA;  188090 MW;  09E371779382C400 CRC64;
     MGQDNSTPIS LTLNHWRDVR TRAHNLSVEI KKGKWQTFCS SEWPTFGVGW PPEGTFNLSV
     IFAVKKIVFQ ENGGHPDQVP YIVVWQDLAQ NPPPWVPASA KVAVVSDTRR PVAGRPSAPP
     RPPIYPATDD LLLLSEPTPP PYPAALPPPL APQAIGPPSG QMPDSSDPEG PAAGTRSRRA
     RSPADNSGPD STVILPLRAI GPPAEPNGLV PLQYWPFSSA DLYNWKSNHP SFSENPAGLT
     GLLESLMFSH QPTWDDCQQL LQILFTTEER ERILLEARKN VLGDNGAPTQ LENLINEAFP
     LNRPHWDYNT AAGRERLLVY RRTLVAGLKG AARRPTNLAK VREVLQGPAE PPSVFLERLM
     EAYRRYTPFD PSSEGQQAAV AMAFIGQSAP DIKKKLQRLE GLQDYSLQDL VKEAEKVYHK
     RETEEERQER EKKEAEEKER RRDRPKKKNL TKILAAVVSR EGSTGRQTGN LSNQAKKTPR
     DGRPPLDKDQ CAYCKEKGHW ARECPRKKHV REAKVLALDN XGSQGSDPLP EPRVTLTVEG
     TPIEFLVDTG AEHSVLTQPM GKVGSRRTVV EGATGSKVYP WTTKRLLKIG HKQVTHSFLV
     IPECPAPLLG RDLLTKLKAQ IQFSAEGPQV TWGERPTMCL VLNLEEEYRL HEKPVPSSID
     PSWLQLFPTV WAERAGMGLA NQVPPVVVEL RSGASPVAVR QYPMSKEARE GIRPHIQKFL
     DLGVLVPCRS PWNTPLLPVK KPGTNDYRPV QDLREINKRV QDIHPTVPNP YNLLSSLPPS
     YTWYSVLDLK DAFFCLRLHP NSQPLFAFEW KDPEKGNTGQ LTWTRLPQGF KNSPTLFDEA
     LHRDLAPFRA LNPQVVLLQY VDDLLVAAPT YEDCKKGTQK LLQELSKLGY RVSAKKAQLC
     QREVTYLGYL LKEGKRWLTP ARKATVMKIP VPTTPRQVRE FLGTAGFCRL WIPGFASLAA
     PLYPLTKESI PFIWTEEHQQ AFDHIKKALL SAPALALPDL TKPFTLYIDE RAGVARGVLT
     QTLGPWRRPV AYLSKKLDPV ASGWPTCLKA VAAVALLLKD ADKLTLGQNV TVIASHSLES
     IVRQPPDRWM TNARMTHYQS LLLNERVSFA PPAVLNPATL LPVESEATPV HRCSEILAEE
     TGTRRDLEDQ PLPGVPTWYT DGSSFITEGK RRAGAPIVDG KRTVWASSLP EGTSAQKAEL
     VALTQALRLA EGKNINIYTD SRYAFATAHI HGAIYKQRGL LTSAGKDIKN KEEILALLEA
     IHLPRRVAII HCPGHQRGSN PVATGNRRAD EAAKQAALST RVLAGTTKPQ EPIEPAQEKT
     RPRELTPDRG KEFIKRLHQL THLGPEKLLQ LVNRTSLLIP NLQSAVREVT SQCQACAMTN
     AVTTYRETGK RQRGDRPGVY WEVDFTEIKP GRYGNKYLLV FIDTFSGWVE AFPTKTETAL
     IVCKKILEEI LPRFGIPKVL GSDNGPAFVA QVSQGLATQL GINWKLHCAY RPQSSGQVER
     MNRTIKETLT KLALETGGKD WVTLLPLALL RARNTPGRFG LTPYEILYGG PPPILESGET
     LGPDDRFLPV LFTHLKALEI VRTQIWDQIK EVYKPGTVTI PHPFQVGDQV LVRRHRPSSL
     EPRWKGPYLV LLTTPTAVKV DGIAAWVHAS HLKPAPPSAP DESWELEKTD HPLKLRIRRR
     RDESAK
//