ID Q0NC79_VARV Unreviewed; 479 AA.
AC Q0NC79; Q0NCT0;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 08-NOV-2023, entry version 55.
DE RecName: Full=Poly(A) polymerase catalytic subunit {ECO:0000256|ARBA:ARBA00017061, ECO:0000256|PIRNR:PIRNR015693};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388, ECO:0000256|PIRNR:PIRNR015693};
DE AltName: Full=Poly(A) polymerase large subunit {ECO:0000256|PIRNR:PIRNR015693};
GN ORFNames=VARV_BOT72_143_045 {ECO:0000313|EMBL:ABF23008.1},
GN VARV_BOT73_225_045 {ECO:0000313|EMBL:ABF23210.1}, VARV_SAF65_102_045
GN {ECO:0000313|EMBL:ABF26627.1}, VARV_SAF65_103_045
GN {ECO:0000313|EMBL:ABF26827.1};
OS Variola virus.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=10255 {ECO:0000313|EMBL:ABF26827.1, ECO:0000313|Proteomes:UP000143307};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|Proteomes:UP000008171, ECO:0000313|Proteomes:UP000143307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Botswana 1972 {ECO:0000313|EMBL:ABF23008.1}, Botswana 1973
RC {ECO:0000313|EMBL:ABF23210.1}, South Africa 1965
RC {ECO:0000313|EMBL:ABF26827.1}, and Variola virus (isolate Human/South
RC Africa/102/1965) {ECO:0000313|Proteomes:UP000008171};
RX PubMed=16873609; DOI=10.1126/science.1125134;
RA Esposito J.J., Sammons S.A., Frace A.M., Osborne J.D., Olsen-Rasmussen M.,
RA Zhang M., Govil D., Damon I.K., Kline R., Laker M., Li Y., Smith G.L.,
RA Meyer H., LeDuc J.W., Wohlhueter R.M.;
RT "Genome sequence diversity and clues to the evolution of variola (smallpox)
RT virus.";
RL Science 313:807-812(2006).
CC -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
CC {ECO:0000256|ARBA:ARBA00003054, ECO:0000256|PIRNR:PIRNR015693,
CC ECO:0000256|RuleBase:RU004458}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000256|ARBA:ARBA00024620,
CC ECO:0000256|PIRNR:PIRNR015693, ECO:0000256|RuleBase:RU004458};
CC -!- SUBUNIT: Heterodimer of a large (catalytic) subunit and a small
CC (regulatory) subunit. {ECO:0000256|ARBA:ARBA00011405,
CC ECO:0000256|PIRNR:PIRNR015693, ECO:0000256|RuleBase:RU004458}.
CC -!- SIMILARITY: Belongs to the poxviridae poly(A) polymerase catalytic
CC subunit family. {ECO:0000256|ARBA:ARBA00006268,
CC ECO:0000256|PIRNR:PIRNR015693, ECO:0000256|RuleBase:RU004458}.
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DR EMBL; DQ441417; ABF23008.1; -; Genomic_DNA.
DR EMBL; DQ441418; ABF23210.1; -; Genomic_DNA.
DR EMBL; DQ441435; ABF26627.1; -; Genomic_DNA.
DR EMBL; DQ441436; ABF26827.1; -; Genomic_DNA.
DR Proteomes; UP000008171; Genome.
DR Proteomes; UP000143307; Genome.
DR Proteomes; UP000153789; Genome.
DR Proteomes; UP000158123; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd20919; polyA_pol_Pox; 1.
DR Gene3D; 1.20.1270.320; Poxvirus poly(A) polymerase, N domain; 1.
DR Gene3D; 3.30.460.60; Poxvirus poly(A) polymerase, nucleotidyltransferase domain; 1.
DR InterPro; IPR004976; PolyA_pol_cat_Poxvir.
DR InterPro; IPR037265; PolyA_pol_cat_sf.
DR InterPro; IPR024231; PolyA_pol_nucTrfase_Poxvir.
DR InterPro; IPR038419; PolyA_pol_nucTrfase_sf_Poxvir.
DR InterPro; IPR024397; Poxvirus_polyA_pol_cat_C.
DR InterPro; IPR024398; Poxvirus_polyA_pol_cat_N.
DR InterPro; IPR038337; Poxvirus_polyA_pol_cat_N_sf.
DR Pfam; PF03296; Pox_polyA_pol; 1.
DR Pfam; PF12629; Pox_polyA_pol_C; 1.
DR Pfam; PF12630; Pox_polyA_pol_N; 1.
DR PIRSF; PIRSF015693; VAC-48L_nuct; 2.
DR SUPFAM; SSF160957; Poly(A) polymerase catalytic subunit-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR015693};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Early protein {ECO:0000256|ARBA:ARBA00022518};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR015693};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR015693};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR015693};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR015693}.
FT DOMAIN 15..117
FT /note="Poxvirus poly(A) polymerase catalytic subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12630"
FT DOMAIN 132..279
FT /note="Poly(A) polymerase nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF03296"
FT DOMAIN 282..478
FT /note="Poxvirus poly(A) polymerase catalytic subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12629"
FT ACT_SITE 202
FT /evidence="ECO:0000256|PIRSR:PIRSR015693-50"
FT ACT_SITE 204
FT /evidence="ECO:0000256|PIRSR:PIRSR015693-50"
SQ SEQUENCE 479 AA; 55525 MW; 33E8870F31DE2792 CRC64;
MNRNPDHNTL PNITLKIIET YLGRLPSVNE YHMLKLQTRN IQKITVFNKD IFVSLVKKNK
KRFFSDVDTS ASEIKDRILS YFSKQTQTYN IGKLFTIIEL QSVLVTTYTD ILGVLTIKAP
NVISSKISYN VTSMEELARD MLNSMNVAVI DKAKVMGRHN VSSLVKNVNK LMEEYLRRHN
KSCICYGSYS LYLINPNIRY GDIDILQTNS RTFLIDLAFL IKFITGNNII LSKIPYLKNY
MVIKDENDNH IIDSFNIRQD TMNVVPKIFI DNIYIVDPTF QLLNMIKMFS QIDRLEDLSK
DPEKFNARMA TMLEYVRYTH GIVFDGKRNN MPMKCIIDEN NRVVTVTTKD YFSFKKCLVY
LDENVLSSDI LDLNADTSCD FESVTNSVYL IHDNIMYTYF SNTILLSDKG KVHEISARGL
CAHILLYQML TSGAYKQCLS DLLNSMMNRD KIPIYSHTER DKKHGRHGFI NIEKDIIVF
//
