ID   D13_VACCA               Reviewed;         551 AA.
AC   Q76ZR4;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-JUN-2021, entry version 50.
DE   RecName: Full=Scaffold protein D13;
DE   AltName: Full=62 kDa protein;
DE   AltName: Full=Rifampicin resistance protein;
GN   OrderedLocusNames=MVA110L, ACAM3000_MVA_110;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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; U94848; AAB96453.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10508.1; -; Genomic_DNA.
DR   RefSeq; YP_233000.1; NC_006998.1.
DR   SMR; Q76ZR4; -.
DR   DNASU; 3707516; -.
DR   GeneID; 3707516; -.
DR   KEGG; vg:3707516; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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   Late protein; Membrane.
FT   CHAIN           1..551
FT                   /note="Scaffold protein D13"
FT                   /id="PRO_0000099124"
SQ   SEQUENCE   551 AA;  61891 MW;  5E75F14646330A0B CRC64;
     MNNTIINSLI GGDDSIKRSN VFAVDSQIPT LYMPQYISLS GVMTNDGPDN QAIASFEIRD
     QYITALNHLV LSLELPEVKG MGRFGYVPYV GYKCINHVSI SSCNGVIWEI EGEELYNNCI
     NNTIALKHSG YSSELNDISI GLTPNDTIKE PSTVYVYIKT PFDVEDTFSS LKLSDSKITV
     TVTFNPVSDI VIRDSSFDFE TFNKEFVYVP ELSFIGYMVK NVQIKPSFIE KPRRVIGQIN
     QPTATVTEVH AATSLSVYTK PYYGNTDNKF ISYPGYSQDE KDYIDAYVSR LLDDLVIVSD
     GPPTGYPESA EIVEVPEDGI VSIQDADVYV KIDNVPDNMS VYLHTNLLMF GTRKNSFIYN
     ISKKFSAITG TYSDATKRTI FAHISHSINI IDTSIPVSLW TSQRNVYNGD NRSAESKAKD
     LFINDPFIKG IDFKNKTDII SRLEVRFGND VLYSENGPIS RIYNELLTKS NNGTRTLTFN
     FTPKIFFRPT TITANVSRGK DKLSVRVVYS TMDVNHPIYY VQKQLVVVCN DLYKVSYDQG
     VSITKIMGDN N