ID   D13_SWPVK               Reviewed;         551 AA.
AC   Q08517;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   12-AUG-2020, entry version 42.
DE   RecName: Full=Scaffold protein D13 ortholog;
DE   AltName: Full=62 kDa protein;
DE   AltName: Full=Rifampicin resistance protein;
OS   Swinepox virus (strain Kasza) (SWPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Suipoxvirus.
OX   NCBI_TaxID=10277;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8249275; DOI=10.1006/viro.1993.1625;
RA   Massung R.F., Jayarama V., Moyer R.W.;
RT   "DNA sequence analysis of conserved and unique regions of swinepox virus:
RT   identification of genetic elements supporting phenotypic observations
RT   including a novel G protein-coupled receptor homologue.";
RL   Virology 197:511-528(1993).
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}.
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DR   EMBL; L22012; AAA16176.1; -; Unassigned_DNA.
DR   SMR; Q08517; -.
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.
FT   CHAIN           1..551
FT                   /note="Scaffold protein D13 ortholog"
FT                   /id="PRO_0000099130"
SQ   SEQUENCE   551 AA;  62427 MW;  92C2E9682B568BFB CRC64;
     MNNTVINSII GNDDIVKRHN VFGVDVQNPT LYMPQYITIN GITSTDSNCD QHVVSTFEIR
     DQYITALSHV MLSIELPEVK GVGRFGYVPY VGYLCIQHVS ISSYDDILWE SSGEDLYNSC
     LDNDTALTNS GYSHELNTIS TGLTPNDTIK ESTTVYVYIK TPFDVEKTFS SLKLADTKIV
     ITVTFNPVSD IIIRDITFNY DNFVKDFVYV TELSCIGYMV KNIQIKPSYI ERPRRVFGQL
     NQSTAVISDV HSVSSLSVYI KPYYGNADNK FISYPGYSQS EKDYICVFVE RLLDDLVTVC
     DTSPKWFPET AELVEVPNSG IVTIQDVDIF VRIDNVPCNM KVYFHTNILV FGTRKNSVTY
     NLSKKFTTIT GTYSESTNRI MFSHVSHSIN ITDVSIPVSV WTCQRNIYNG DNRSESSKNK
     DLFINDPFIK GIDFKNKTDI ISRLEVRFGN DVLYSETSPI SKVYNDLLSN HKCGMRTLRF
     NFTPPTFFKP TTIVANPSRG KDKLSVRVVF TSLDPNNPIY YISKQLVLVC KDLYKVTNDD
     GINVTKIIGE L