ID   RAP94_FOWPN             Reviewed;         798 AA.
AC   Q9J589;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-SEP-2021, entry version 59.
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=FPV141;
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: 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 (By similarity). {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- DOMAIN: Interacts with ETF via its N-terminus and with DNA-directed RNA
CC       polymerase via its C-terminus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the poxviridae protein RAP94 family.
CC       {ECO:0000305}.
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DR   EMBL; AF198100; AAF44485.1; -; Genomic_DNA.
DR   RefSeq; NP_039104.1; NC_002188.1.
DR   SMR; Q9J589; -.
DR   GeneID; 1486689; -.
DR   KEGG; vg:1486689; -.
DR   Proteomes; UP000008597; Genome.
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   InterPro; IPR004974; Pox_Rap94.
DR   Pfam; PF03294; Pox_Rap94; 1.
PE   2: Evidence at transcript level;
KW   Late protein; Reference proteome; Transcription; Transcription regulation;
KW   Transcription termination; Virion.
FT   CHAIN           1..798
FT                   /note="RNA polymerase-associated transcription-specificity
FT                   factor RAP94"
FT                   /id="PRO_0000099123"
FT   REGION          1..195
FT                   /note="Interaction with NPH-I; required for transcription
FT                   termination"
FT                   /evidence="ECO:0000250"
FT   REGION          234..254
FT                   /note="Interaction with J3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   798 AA;  95221 MW;  2A3ED2D453537BD3 CRC64;
     MENKESVLLE LVPKIKAYIK DDTVKEKSYQ DFIEKNKELF ICNLYNVNMI TDEDIKLLYI
     TIEQNIDIDD KSLVAIFSYI GYNFEKNIHD DNSSIDLGDR MTGDMNYNMY DTFFSTLDFI
     IRQKHVNILV NDEGNNDFNI NYRSFTTSLS YKEDKYEQVV NEIPFNMKEL LSYVSKNLDQ
     LRFSKKYLDF AYLCRNIGIK ISKRKYNVRY IFNYVIDELT IPIVIKDYLD VKYVYLEETN
     KAYRNNFDND NKYFYEWGKV IIPKFKNPRL YSYFFLSNYG LCDLFMELIN IKQVTFEPRK
     NPIEYIYVSE LKFWEEGGSV DFVPCEHEIA IIDAKKVSLE YYENINKFIA KYIYYEDGLA
     YCNLCGINIQ ELNLDATDVT KISLINVTYN KSIFMSEPYN YFSHSQRFIF NTIMSFDTIM
     KSQMWNMKYN INRLILNFLI DINSKRHEYE KQFATEIKKG IFFLRLSANL FDIQMSSMEL
     FYSAKILNIH FIVALVIVLN SGADFIMYYM TNKKEETNYS DLNHIISVIV FDFLKKTRTV
     DSKQFNTIEL FTETYMKIAT EELIVHYNRI KLEMERLIAI KKDRKTPNYD ISIYRQIQRT
     DEIAFFPSCI TSTKLFITYE KVVAENTEII TIKHPVRIKE GTDEDKEIFE DIMKKTTKVL
     IRVNDTNAYN ASFFTTHIKL EVEKKKIIIP LTSLFVYNVL KYYSSNVDFY VFKFGDPFPF
     HYDLISQEHT NHKITGYNML RQELLPNSNV FTYFSDSLNR QELEFSFYMF LASYVNVTEW
     IEENSKKIKE LYIINFNN