VF706_ASFWA
ID VF706_ASFWA Reviewed; 706 AA.
AC P0C9B2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Termination factor NPH-I homolog {ECO:0000250|UniProtKB:Q89581};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:Q89581};
GN OrderedLocusNames=War-132;
OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561444;
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; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Proteomes; UP000000858; 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 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; Late protein; Nucleotide-binding; Virion.
FT CHAIN 1..706
FT /note="Termination factor NPH-I homolog"
FT /id="PRO_0000373120"
FT DOMAIN 62..227
FT /note="Helicase ATP-binding"
FT DOMAIN 417..599
FT /note="Helicase C-terminal"
FT MOTIF 168..171
FT /note="DEAH box"
FT BINDING 75..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 80328 MW; AC325402B4E865B3 CRC64;
MSCVHNNTSF PVQTEAYLKE VFEKYKELQE 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 CMLKNIKTSP GPVLIYSQFV ELGLHVVARF LEIEGYQCLQ
PLKVLEEGHN TILLHKDGKD LMVKNFAEDG PTRTLVLSSK ITRFTLITGK ILSKERDMIQ
QLWNSPLNIH GEVIKILLVS KTGAEGLDLK YGRQVHILEP YWDKAREDQV KARIIRIGSH
DALPPEEKTV QPFLYIAVAN QKMFYSIPEG SQEQKTIDER FHERGLEKSH LNSAFRDLLK
RAAIECAFNG ESGCLMCQPT NALLFHENFE RDLRLPNPCQ PLVKAEVKAY SISYEGKQFF
YQKNKDVGLG YTFYEYNPII KAYIEIKPSN PLYIKLIKHV QAGTTA