ID   TFNPH_ASFB7             Reviewed;         706 AA.
AC   Q89581;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Termination factor NPH-I homolog {ECO:0000303|PubMed:23041356, ECO:0000303|PubMed:32725217};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P05807};
GN   OrderedLocusNames=Ba71V-122; ORFNames=Q706L;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [2]
RP   REVIEW.
RX   PubMed=23041356; DOI=10.1016/j.virusres.2012.09.014;
RA   Rodriguez J.M., Salas M.L.;
RT   "African swine fever virus transcription.";
RL   Virus Res. 173:15-28(2013).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
RN   [4]
RP   REVIEW.
RX   PubMed=32725217; DOI=10.1042/bst20191108;
RA   Cackett G., Sykora M., Werner F.;
RT   "Transcriptome view of a killer: African swine fever virus.";
RL   Biochem. Soc. Trans. 48:1569-1581(2020).
RN   [5]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
CC   -!- FUNCTION: Putative DNA-dependent ATPase required for providing the
CC       needed energy to achieve the termination of early transcripts.
CC       {ECO:0000250|UniProtKB:P05807}.
CC   -!- SUBUNIT: Part of the viral DNA-directed RNA polymerase that consists of
CC       8 polII-like subunits (RPB1, RPB2, RPB3, RPB5, RPB6, RPB7, RPB9,
CC       RPB10), a capping enzyme and a termination factor.
CC       {ECO:0000303|PubMed:32725217}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30185597}. Note=Found
CC       in association with viral nucleoid. {ECO:0000269|PubMed:30185597}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:32075923}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U18466; AAA65350.1; -; Genomic_DNA.
DR   EMBL; X69952; CAA49573.1; -; Genomic_DNA.
DR   PIR; S42174; S42174.
DR   RefSeq; NP_042814.1; NC_001659.2.
DR   GeneID; 22220351; -.
DR   KEGG; vg:22220351; -.
DR   Proteomes; UP000000624; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Late protein; Nucleotide-binding;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Transcription termination; Virion.
FT   CHAIN           1..706
FT                   /note="Termination factor NPH-I homolog"
FT                   /id="PRO_0000373117"
FT   DOMAIN          62..227
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          378..599
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           168..171
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         75..82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   706 AA;  80376 MW;  9E313D2FF800F39D CRC64;
     MSCVHNNTSF PVQIEAYLKE VYEKYKELQE SKDTSLTARF ARALKYYQFL IYTAFSDPKF
     GIGQGENTRG LLIYHQMGMG KTILSLSLAI SLSHIYNPIL IAPKSLHSNF QQSLLKLIKL
     LYPETTDHSK ELQKISRRFR FVSLDAYNMG QQIIKAGGSL NGCLLIVDEA HNLFRGIINS
     ANDKTNARQL YNNIMQAKNI RILFLTGTPC SKDPFEMVPC FNMLSGRILL PLHYERFYTA
     YVNKTTNSPL NADKLLNRLV GMISYAGNQN ELNKLFPTEL PLIIEKVEMS PEQYRQYLLA
     RDVENAEKHA SSGMYEKINA AALCLPGSEQ ESGSSYYVRS RMISIFASEM LTVKEDEKLS
     EAVQQLPKEA FTENSSPKIV RMLKNIKTSP GPVLIYSQFV ELGLHVVARF LEIEGYQCLQ
     PLKVLEEGHN TILLHKDGKD LMVKNFAEDG PTHTLVLSSK ITRFTLITGK ILSKERDMIQ
     QVWNSPLNIH GEVIKILLVS KTGAEGLDLK YGRQVHILEP YWDKAREDQV KARIIRIGSH
     DALPPEEKTV QPFLYIAVAN QKMFYSIPEG SQEQKTIDER FHERGLEKSH LNSAFRDLLK
     RAAIECAFNG ESGCLMCQPT NALLFHENFE RDLRLPNPCQ PLVKAEVKAY SISYEGKQFF
     YQKNKDVGLG YTFYEYNPII KAYIEIKPSN PLYIKLIKHV QAGTTA