ID   RAP94_VACCW             Reviewed;         795 AA.
AC   P68438; P07241; P08584; P21094; Q80HW2;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   29-SEP-2021, entry version 57.
DE   RecName: Full=RNA polymerase-associated transcription-specificity factor RAP94;
DE   AltName: Full=Protein H4;
DE   AltName: Full=RPO-associated protein of 94 kDa;
GN   Name=RAP94; OrderedLocusNames=VACWR102; ORFNames=H4L;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3021979; DOI=10.1128/jvi.60.2.436-449.1986;
RA   Rosel J.L., Earl P.L., Weir J.P., Moss B.;
RT   "Conserved TAAATG sequence at the transcriptional and translational
RT   initiation sites of vaccinia virus late genes deduced by structural and
RT   functional analysis of the HindIII H genome fragment.";
RL   J. Virol. 60:436-449(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION, AND PROTEIN SEQUENCE OF 17-27 AND 544-553.
RX   PubMed=1565650; DOI=10.1073/pnas.89.8.3536;
RA   Ahn B.-Y., Moss B.;
RT   "RNA polymerase-associated transcription specificity factor encoded by
RT   vaccinia virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:3536-3540(1992).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH NPH-I.
RX   PubMed=11279216; DOI=10.1074/jbc.m101641200;
RA   Mohamed M.R., Niles E.G.;
RT   "The viral RNA polymerase H4L subunit is required for Vaccinia virus early
RT   gene transcription termination.";
RL   J. Biol. Chem. 276:20758-20765(2001).
RN   [5]
RP   INTERACTION WITH J3.
RX   PubMed=11162828; DOI=10.1006/viro.2000.0749;
RA   Mohamed M.R., Latner D.R., Condit R.C., Niles E.G.;
RT   "Interaction between the J3R subunit of vaccinia virus poly(A) polymerase
RT   and the H4L subunit of the viral RNA polymerase.";
RL   Virology 280:143-152(2001).
RN   [6]
RP   REVIEW.
RX   PubMed=12917449; DOI=10.1099/vir.0.18942-0;
RA   Broyles S.S.;
RT   "Vaccinia virus transcription.";
RL   J. Gen. Virol. 84:2293-2303(2003).
RN   [7]
RP   FUNCTION, AND RNA-BINDING.
RX   PubMed=18455214; DOI=10.1016/j.virol.2008.03.031;
RA   Christen L.A., Piacente S., Mohamed M.R., Niles E.G.;
RT   "Vaccinia virus early gene transcription termination factors VTF and Rap94
RT   interact with the U9 termination motif in the nascent RNA in a
RT   transcription ternary complex.";
RL   Virology 376:225-235(2008).
RN   [8]
RP   FUNCTION, INDUCTION, AND IDENTIFICATION IN A COMPLEX WITH THE EARLY
RP   TRANSCRIPTION FACTOR HETERODIMER AND THE RNA POLYMERASE.
RX   PubMed=19759131; DOI=10.1128/jvi.01653-09;
RA   Yang Z., Moss B.;
RT   "Interaction of the vaccinia virus RNA polymerase-associated 94-kilodalton
RT   protein with the early transcription factor.";
RL   J. Virol. 83:12018-12026(2009).
CC   -!- FUNCTION: DNA-directed RNA polymerase-associated factor required for
CC       the transcription of viral early genes as well as for transcription
CC       termination. Within minutes after virus entry, recruits the core RNA
CC       polymerase, the early transcription factor (ETF) and other enzymes
CC       needed for transcription initiation, elongation, and termination
CC       thereby allowing synthesis of early mRNAs which are extruded through
CC       pores in the core particle. Recruits the multifunctional J3 protein,
CC       with poly(A) polymerase-stimulatory, cap nucleoside-2'-O-
CC       methyltransferase, and transcription elongation activities. Interacts
CC       with NPH-I, a DNA-dependent ATPase required for the termination of
CC       early transcripts. Acts as a transcription termination factor by
CC       binding, together with the capping enzyme/VTF, to the termination motif
CC       5'-UUUUUNU-3' in the nascent mRNA. Involved as well in the packaging of
CC       RNA polymerase and other components needed for early transcription in
CC       assembling virus particles. {ECO:0000269|PubMed:11279216,
CC       ECO:0000269|PubMed:18455214, ECO:0000269|PubMed:19759131}.
CC   -!- SUBUNIT: Part of the early transcription complex composed of ETF,
CC       RAP94, and the DNA-directed RNA polymerase. Interacts (via N-terminus)
CC       with NPH-I. Interacts with J3. Interacts with ETF heterodimer.
CC       {ECO:0000269|PubMed:11162828, ECO:0000269|PubMed:11279216,
CC       ECO:0000269|PubMed:19759131}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and
CC       other proteins required to synthesize early mRNAs are packaged within
CC       the virion core along with the DNA genome.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:19759131}.
CC   -!- DOMAIN: Interacts with ETF via its N-terminus and with DNA-directed RNA
CC       polymerase via its C-terminus.
CC   -!- SIMILARITY: Belongs to the poxviridae protein RAP94 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB59840.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M13209; AAB59840.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY243312; AAO89381.1; -; Genomic_DNA.
DR   PIR; D42514; QQVZH4.
DR   PIR; E24481; QQVZH5.
DR   RefSeq; YP_232984.1; NC_006998.1.
DR   SMR; P68438; -.
DR   PRIDE; P68438; -.
DR   DNASU; 3707558; -.
DR   GeneID; 3707558; -.
DR   KEGG; vg:3707558; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0044423; C:virion component; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR   InterPro; IPR004974; Pox_Rap94.
DR   Pfam; PF03294; Pox_Rap94; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Late protein; Reference proteome; Transcription;
KW   Transcription regulation; Transcription termination; Virion.
FT   CHAIN           1..795
FT                   /note="RNA polymerase-associated transcription-specificity
FT                   factor RAP94"
FT                   /id="PRO_0000099121"
FT   REGION          1..196
FT                   /note="Interaction with NPH-I; required for transcription
FT                   termination"
FT                   /evidence="ECO:0000269|PubMed:11279216"
FT   REGION          235..256
FT                   /note="Interaction with J3"
FT                   /evidence="ECO:0000269|PubMed:11162828"
FT   CONFLICT        623..624
FT                   /note="YI -> CV (in Ref. 1; AAB59840)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   795 AA;  93633 MW;  113DE9F977B9FCF4 CRC64;
     MDSKETILIE IIPKIKAYLL DANISPKSYD DFISRNKNIF VINLYNVSTI TEEDIRLLYT
     TIEQNIDADD QTLVAIFSYI GYKFEQAVKE EISTSLSFND KNTTDEMTYN LYDLFFNTLD
     MYLRQKKISI LVNDDVRGDV IVSYKNSDLV SSFNAELEPE IKKIPFNMKN LLPYLEKNLD
     QLRFSKKYLD FAYLCRHIGI PISKKKYNVR YVFLYKIDGL SIPIIIKDFL DVKYVYLENT
     GKIYKNSFSE DHNNSLSDWG KVIIPLLKDR HLYSYIFLSS YHLHSYYTDL IARDEPVFVK
     RKKLDIIEID EPEAWKRDVR VEFAPCEHQI RLKEAMKVDA NYFTKINNFA NEFIYYEDGV
     AYCRVCGINI PIFNLDAADV IKNTVIVSTF NKTIFLSEPY SYFVHSQRFI FNIIMSFDNI
     MKSQTWVMKY NINRLILNFL IDINSRRQEY EKKFSSEIKR GLFFLRLSAN LFESQVSSTE
     LFYVSKMLNL NYIVALVIIL NSSADFIVSY MTSKNKTVEE STLKYAISVV IYDFLVKTRI
     CEKGSLDTIV LFTDVYTSIM PEELDLHFQR ITLELRKLVS IQRSALEPNY DVESRGEELP
     LSALKFFDTS TIIVKTMAPV HTYIEQKIVA PTPSVEPTDA SLKNFKELTC DEDIKILIRV
     HDTNATKLVI FPSHLKIEIE RKKLIIPLKS LYITNTLKYY YSNSYLYVFR FGDPMPFEEE
     LIDHEHVQYK INCYNILRYH LLPDSDVFVY FSNSLNREAL EYAFYIFLSK YVNVKQWIDE
     NITRIKELYM INFNN