ID A0A2T9YKX9_9FUNG Unreviewed; 685 AA.
AC A0A2T9YKX9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Poly(A) polymerase {ECO:0000256|PIRNR:PIRNR018425};
DE EC=2.7.7.19 {ECO:0000256|PIRNR:PIRNR018425};
GN ORFNames=BB559_003529 {ECO:0000313|EMBL:PVU92924.1}, BB559_006105
GN {ECO:0000313|EMBL:PVU87312.1}, BB559_007028
GN {ECO:0000313|EMBL:PVU85428.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU92924.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU92924.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU92924.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
CC -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
CC {ECO:0000256|PIRNR:PIRNR018425}.
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|PIRNR:PIRNR018425};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR018425-2};
CC Note=Binds 2 magnesium ions. Also active with manganese.
CC {ECO:0000256|PIRSR:PIRSR018425-2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR018425}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family.
CC {ECO:0000256|ARBA:ARBA00010912, ECO:0000256|PIRNR:PIRNR018425}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVU92924.1}.
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DR EMBL; MBFT01001086; PVU85428.1; -; Genomic_DNA.
DR EMBL; MBFT01000766; PVU87312.1; -; Genomic_DNA.
DR EMBL; MBFT01000341; PVU92924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9YKX9; -.
DR STRING; 61424.A0A2T9YKX9; -.
DR Proteomes; UP000245699; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:InterPro.
DR CDD; cd05402; NT_PAP_TUTase; 1.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR048840; PolA_pol_NTPase.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR014492; PolyA_polymerase.
DR PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR PANTHER; PTHR10682:SF10; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF20750; PAP_NTPase; 1.
DR Pfam; PF04926; PAP_RNA-bind; 1.
DR PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR018425};
KW Magnesium {ECO:0000256|PIRSR:PIRSR018425-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR018425-2};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR018425};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR018425};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR018425};
KW Reference proteome {ECO:0000313|Proteomes:UP000245699};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018425}.
FT DOMAIN 10..203
FT /note="Poly(A) polymerase nucleotidyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20750"
FT DOMAIN 208..353
FT /note="Poly(A) polymerase central"
FT /evidence="ECO:0000259|Pfam:PF04928"
FT DOMAIN 355..536
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT REGION 539..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 102..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT BINDING 235..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
SQ SEQUENCE 685 AA; 77402 MW; D9D737AABC24A63A CRC64;
MALNGVVHYG VTPPISLEKA TQDDINLTKK MIETLVEAGQ FEDEKASKNR EIVLGQLDKL
TQEFVYRASI KHGLSESTAK DCRGKIYTFG SYRLGVHGAG ADIDTLCVVP AHVTREDFFE
IMHRLLSQRS DVKELSAVPD AYVPVIKMEF GNVPIDLTFA SLHLPSIPED LELLDTKVLR
NLDEQCIRSI NGSRVTDDIL RLVPDVKTFR ESLRCIKLWA KKRGVYSNSM GFLGGVAWAM
LVARVCQLYP NAAAGSIISR FFRIMYRWNW PQPVLLKPIE DGPLRARVWN PKLYIQDRAH
KMPIITPAYP SMCATHNVSQ STLTIMTAEF KRGVEILDKI IDNQCEWKEL FAKYNFFSRY
KHYLHVVVST NDPESQLKVH GFVESKLRHL VMKLENVEHV VLAHPFVGSL DQTFMCENED
VATKIKTGHF PNKMFSEESI RVSSGSLLDN SEESLDEKFG DDQIGVYTSS FFVGLLISKK
PADHIGNRRV DLSWPAQEFL MLVKQTDMWD SEKMSINIKF YKNTELPIFV FEGGTNPSVT
LTKNQKTPVK HGFSNDSGTD SQVQKKIRLE SPQNGTESDK KQDPSPQKTG KGDDTEKKTD
SINLEQKTDN NIGKNVDKQQ NGNQMPIDID DESVKKVAEQ QYFRAQQQPV SDFSKTNQNM
RIPGLPPAPP PGGIKLRLAD PQYNA
//
