ID   ARBH_FOWPN              Reviewed;         175 AA.
AC   Q9J5G4;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Apoptosis regulator Bcl-2 homolog;
GN   OrderedLocusNames=FPV039;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
RN   [2]
RP   FUNCTION, INTERACTION WITH HOST BAK1, AND SUBCELLULAR LOCATION.
RX   PubMed=17686864; DOI=10.1128/jvi.00734-07;
RA   Banadyga L., Gerig J., Stewart T., Barry M.;
RT   "Fowlpox virus encodes a Bcl-2 homologue that protects cells from apoptotic
RT   death through interaction with the proapoptotic protein Bak.";
RL   J. Virol. 81:11032-11045(2007).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HOST BAX.
RX   PubMed=19439472; DOI=10.1128/jvi.00437-09;
RA   Banadyga L., Veugelers K., Campbell S., Barry M.;
RT   "The fowlpox virus BCL-2 homologue, FPV039, interacts with activated Bax
RT   and a discrete subset of BH3-only proteins to inhibit apoptosis.";
RL   J. Virol. 83:7085-7098(2009).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-143.
RX   PubMed=28411240; DOI=10.1074/jbc.m116.768879;
RA   Anasir M.I., Caria S., Skinner M.A., Kvansakul M.;
RT   "Structural basis of apoptosis inhibition by the fowlpox virus protein
RT   FPV039.";
RL   J. Biol. Chem. 292:9010-9021(2017).
CC   -!- FUNCTION: Plays a role in the inhibition of host apoptosis by
CC       sequestering and inactivating multiple proapoptotic BCL-2 proteins,
CC       including BAK1 and BAX. {ECO:0000269|PubMed:19439472}.
CC   -!- SUBUNIT: Interacts with host BAX; this interaction inhibits BAX
CC       oligomerization and subsequent activation. Interacts with host BAK1.
CC       {ECO:0000269|PubMed:17686864, ECO:0000269|PubMed:19439472}.
CC   -!- SUBCELLULAR LOCATION: Host mitochondrion {ECO:0000269|PubMed:17686864}.
CC   -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR   EMBL; AF198100; AAF44383.1; -; Genomic_DNA.
DR   RefSeq; NP_039002.1; NC_002188.1.
DR   PDB; 5TZP; X-ray; 1.35 A; A=1-143.
DR   PDB; 5TZQ; X-ray; 1.65 A; A/B=1-143.
DR   PDBsum; 5TZP; -.
DR   PDBsum; 5TZQ; -.
DR   SASBDB; Q9J5G4; -.
DR   SMR; Q9J5G4; -.
DR   GeneID; 1486587; -.
DR   KEGG; vg:1486587; -.
DR   Proteomes; UP000008597; Genome.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0019050; P:suppression by virus of host apoptotic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.437.10; -; 1.
DR   InterPro; IPR036834; Bcl-2-like_sf.
DR   InterPro; IPR046371; Bcl-2_BH1-3.
DR   InterPro; IPR002475; Bcl2-like.
DR   InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR   Pfam; PF00452; Bcl-2; 1.
DR   SUPFAM; SSF56854; SSF56854; 1.
DR   PROSITE; PS50062; BCL2_FAMILY; 1.
DR   PROSITE; PS01080; BH1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Host mitochondrion; Host-virus interaction;
KW   Inhibition of host apoptosis by viral BCL2-like protein;
KW   Modulation of host cell apoptosis by virus; Reference proteome.
FT   CHAIN           1..175
FT                   /note="Apoptosis regulator Bcl-2 homolog"
FT                   /id="PRO_0000143093"
FT   MOTIF           75..94
FT                   /note="BH1"
FT   MOTIF           105..120
FT                   /note="BH2"
FT   HELIX           9..27
FT                   /evidence="ECO:0007829|PDB:5TZP"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:5TZP"
FT   HELIX           38..63
FT                   /evidence="ECO:0007829|PDB:5TZP"
FT   HELIX           69..76
FT                   /evidence="ECO:0007829|PDB:5TZP"
FT   HELIX           83..100
FT                   /evidence="ECO:0007829|PDB:5TZP"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:5TZP"
FT   HELIX           110..131
FT                   /evidence="ECO:0007829|PDB:5TZP"
FT   HELIX           134..141
FT                   /evidence="ECO:0007829|PDB:5TZP"
SQ   SEQUENCE   175 AA;  20458 MW;  4537425136506629 CRC64;
     MASSNMKDET YYIALNMIQN YIIEYNTNKP RKSFVIDSIS YDVLKAACKS VIKTNYNEFD
     IIISRNIDFN VIVTQVLEDK INWGRIITII AFCAYYSKKV KQDTSPQYYD GIISEAITDA
     ILSKYRSWFI DQDYWNGIRI YKNYSYIFNT ASYCIFTASL IIASLAVFKI CSFYM