ID   TFNPH_ASFK5             Reviewed;         706 AA.
AC   P0C9B3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Termination factor NPH-I homolog {ECO:0000250|UniProtKB:Q89581};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P05807};
GN   OrderedLocusNames=Ken-134;
OS   African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561445;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q89581}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:Q89581}. Note=Found
CC       in association with viral nucleoid. {ECO:0000250|UniProtKB:Q89581}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000000861; 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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Transcription;
KW   Transcription regulation; Transcription termination; Virion.
FT   CHAIN           1..706
FT                   /note="Termination factor NPH-I homolog"
FT                   /id="PRO_0000373121"
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:PRU00541"
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;  80328 MW;  5CDC84D8877EE4D8 CRC64;
     MSCVHNNTSF PVQIEAYLKE VFEKYKELQE SKDTSLTARF ARALKYYQFL IYTAFSDPKF
     GIGQGENTRG LLIYHQMGMG KTILSLSLAI SLSHIYNPIL IAPKSLHSNF QQSLLKLIKL
     LYPETTDPSK ELQKISRRFR FVSLDAYNMG QQIIKAGGSL NGCLLIVDEA HNLFRGIINS
     ANDKTNARQL YNNIMQAKNI RILFLTGTPC SKDPFEMVPC FNMLSGRILL PLHYERFYTA
     YVNKTTNSPL NADKLLNRLV GMISYAGNQN ELNKLFPTEL PLIIEKVEMS PEQYRQYLLA
     RDVENAEKHA SSGMHEKINT AALCLPGSEQ ESGSSYYVRS RMISIFASEM LTIKEDEKLS
     EAVQQLPKEA FTETSSPKIV CMLKNIKTSP GPVLIYSQFV ELGLHVVARF LEIEGYQCLQ
     PLKVLEEGHN AILLHKDGKD LMVKNFAEDE PTHTLVLSSK ITRFTLITGK ILSKERDMIQ
     QLWNSPLNIH GEVIKILLVS KTGAEGLDLK YGRQVHILEP YWDKAREDQV KARIIRIGSH
     DALPPEEKTV QPFLYIAVAN QKMFYSIPEG SQEQKTIDER FHERGLEKSH LNSAFRDLLK
     RAAIECAFNG ESGCLMCQPT NALLFHENFE RDLRLPNPCQ PLVKTEVKAY SISYEGKQFF
     YQKNKGVGLG YTFYEYNPII KAYIEIKPSN PLYIKLIKHV QAGTTV