A18_VACCC
ID A18_VACCC Reviewed; 493 AA.
AC P20534;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Transcript termination protein A18;
DE EC=3.6.4.-;
DE AltName: Full=56 kDa abortive late protein;
GN ORFNames=A18R;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
RN [3]
RP SIMILARITY TO HELICASES.
RX PubMed=1321883; DOI=10.1099/0022-1317-73-4-989;
RA Koonin E.V., Senkevich T.G.;
RT "Vaccinia virus encodes four putative DNA and/or RNA helicases distantly
RT related to each other.";
RL J. Gen. Virol. 73:989-993(1992).
CC -!- FUNCTION: DNA helicase which seems to act as a postreplicative
CC transcription termination factor. Involved in ATP-dependent release of
CC nascent RNA. Forms a stable complex with single-stranded DNA, and to a
CC lesser extent RNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with G2. Might be part of a transcription complex
CC composed at least of G2, A18, and H5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Localizes to the
CC virion core. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. Poxviruses subfamily.
CC {ECO:0000305}.
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DR EMBL; M35027; AAA48140.1; -; Genomic_DNA.
DR PIR; B42519; B42519.
DR SMR; P20534; -.
DR Proteomes; UP000008269; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Late protein;
KW Nucleotide-binding; Reference proteome; Transcription; Virion.
FT CHAIN 1..493
FT /note="Transcript termination protein A18"
FT /id="PRO_0000102176"
FT DOMAIN 100..256
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 309..456
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 206..209
FT /note="DESH box"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 493 AA; 56737 MW; C8F189FA7EFE14AF CRC64;
MSLLKMEYNL YAELKKMTCG QPLSLFNEDG DFVEVEPGSS FKFLIPKGFY ASPSVKTSLV
FETLTTTDNK ITSINPTNAP KLYPLQRKVV SEVVSNMRKM IESKRPLYIT LHLACGFGKT
ITTCYLMATH GRKTVICVPN KMLIHQWKTQ VEAVGLEHKI SIDGVSSLLK ELKTQSPDVL
IVVSRHLTND AFCKYINKHY DLFILDESHT YNLMNNTAVT RFLAYYPPMM CYFLTATPRP
ANRIYCNSII NIAKLSDLKK TIYAVDSFFE PYSTDNIRHM IKRLDGPSNK YHIYTEKLLS
VDEPRNQLIL DTLVEEFKSG TINRILVITK LREHMVFFYK RLLDLFGPEV VFIGDAQNRR
TPDMVKSIKE LNRFIFVSTL FYSGTGLDIP SLDSLFICSA VINNMQIEQL LGRVCRETEL
LDRTVYVFPS TSIKEIKYMI GNFMQRIISL SVDKLGFKQK SYRKHQESDP TSVCTTSSRE
ERVLNRIFNS QNR