ID   D13_FOWPN               Reviewed;         552 AA.
AC   P0DTA5; O72909; Q70HA0; Q9J5F4;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   12-AUG-2020, entry version 5.
DE   RecName: Full=Scaffold protein;
DE   AltName: Full=62 kDa protein;
DE   AltName: Full=D13 ortholog;
DE   AltName: Full=N3L protein;
DE   AltName: Full=Rifampicin resistance protein;
GN   OrderedLocusNames=FPV050, fp9.050; ORFNames=FP-D13, FPD13;
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).
CC   -!- FUNCTION: Scaffold protein which forms a transitory spherical honeycomb
CC       lattice providing curvature and rigidity to the convex membrane of
CC       crescent and immature virions (IV). This association occurs
CC       concomitantly with viral membrane formation. Targeted by the drug
CC       rifampicin, which prevents the formation of this lattice, and hence
CC       virus morphogenesis. In the presence of rifampicin, irregularly shaped
CC       membranes that lack the honeycomb layer accumulate around areas of
CC       electron-dense viroplasm. This layer is lost from virions during
CC       maturation from IV to mature virion (MV), through the proteolysis of
CC       A17 N-terminus (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Self-assembles to form a layer.
CC       Interacts with A17 (via N-terminus); this interaction is necessary for
CC       D13 association with membranes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC       Note=Associates transitorily with crescent and IV membranes.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Displays structure similarities to capsid proteins.
CC   -!- SIMILARITY: Belongs to the poxviridae protein D13 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF44394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF198100; AAF44394.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S42253; S42253.
DR   SMR; P0DTA5; -.
DR   Proteomes; UP000008597; Genome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   InterPro; IPR005008; Poxvirus_Rif-R.
DR   Pfam; PF03340; Pox_Rif; 1.
PE   3: Inferred from homology;
KW   Membrane; Reference proteome.
FT   CHAIN           1..552
FT                   /note="Scaffold protein"
FT                   /id="PRO_0000099129"
SQ   SEQUENCE   552 AA;  62413 MW;  899E55999D02A245 CRC64;
     MNNSIISSVI NSIDSSSKRT NIFSFDVQQP TAYMPQYISV NGYHNKKDND ANQVCSVSFD
     IRDQHIAAIN YFFISIQLPE VSGEGKFAYV PYVGYKCIQH VAITCGDITI WETDGEELFD
     KCVDDKIASL SGYSPELNDI STGYTPNDTI KDPTTLYVYI KSPFDADKTI SSLKLVNNKI
     TVTITFRSIN DVIVYDSKFQ VERFVKDFVY STELHLIAYA VSDIKPKSAY IELDRRVVSC
     SSTPTPIPVI SDVYACTAMS VYVKPYYGMM ENKFISYPGY KQTESDYVRC MVNRLLDDLV
     VVADTVPKGF PSTATFVKVP VDGQINLQDV DIIVKIDNVP DDKDIYYHTN LLIFGTRKNS
     FVYNISKKFS SIIGMYSPNT DSINFSKVNH TISITDASIP VSFWVSQKNV YQGDNRSNYS
     KSKDLVVNDP FRKGIDMVNK TDVISRLEVR FGNDPIYSEI SPITKVFNML LTGSSINMRK
     IIFNMNPANI FRPTTLNANT KRGKDKLTVR ISYIDTDPNN PIHYVAKQLV VICTDLYRID
     YDGNINITKI TE