ID A0A3F2Y0J4_DEKBR Unreviewed; 573 AA.
AC A0A3F2Y0J4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Poly(A) polymerase {ECO:0000256|PIRNR:PIRNR018425};
DE EC=2.7.7.19 {ECO:0000256|PIRNR:PIRNR018425};
GN Name=PAP1 {ECO:0000313|EMBL:VUG16808.1};
GN ORFNames=BRETT_003083 {ECO:0000313|EMBL:QOU22895.1}, DEBR0S1_26192G
GN {ECO:0000313|EMBL:VUG16808.1}, HII12_000932
GN {ECO:0000313|EMBL:KAF6015389.1};
OS Dekkera bruxellensis (Brettanomyces custersii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=5007 {ECO:0000313|EMBL:VUG16808.1, ECO:0000313|Proteomes:UP000478008};
RN [1] {ECO:0000313|EMBL:VUG16808.1, ECO:0000313|Proteomes:UP000478008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Friedrich A., Schacherer J.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF6015389.1, ECO:0000313|Proteomes:UP000568158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1613 {ECO:0000313|EMBL:KAF6015389.1,
RC ECO:0000313|Proteomes:UP000568158};
RX PubMed=32592028;
RA Varela C., Bartel C., Onetto C., Borneman A.;
RT "Targeted gene deletion in Brettanomyces bruxellensis with an expression-
RT free CRISPR-Cas9 system.";
RL Appl. Microbiol. Biotechnol. 104:7105-7115(2020).
RN [3] {ECO:0000313|EMBL:QOU22895.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCD 2041 {ECO:0000313|EMBL:QOU22895.1};
RA Palmer J.M.;
RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QOU22895.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCD 2041 {ECO:0000313|EMBL:QOU22895.1};
RX PubMed=32122298;
RA Roach M.J., Borneman A.R.;
RT "New genome assemblies reveal patterns of domestication and adaptation
RT across Brettanomyces (Dekkera) species.";
RL BMC Genomics 21:0-0(0).
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}.
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DR EMBL; JABCYN010000010; KAF6015389.1; -; Genomic_DNA.
DR EMBL; CP063137; QOU22895.1; -; Genomic_DNA.
DR EMBL; CABFWN010000001; VUG16808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F2Y0J4; -.
DR STRING; 5007.A0A3F2Y0J4; -.
DR OMA; PAYPAMC; -.
DR OrthoDB; 1351913at2759; -.
DR Proteomes; UP000478008; Unassembled WGS sequence.
DR Proteomes; UP000568158; Unassembled WGS sequence.
DR Proteomes; UP000663131; Chromosome 9.
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:UP000478008};
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..538
FT /note="Poly(A) polymerase RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF04926"
FT REGION 531..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Basic and acidic 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 573 AA; 65639 MW; 3C4511184FB6776E CRC64;
MNSSQPKQYG VTPPVSIASP SAEEVKMNDA MIEELRNQNS FETEDGVQKR RKVLATLQTI
VQEFVYTVSR KKNMSEGMSK DAGGKLFTFG SYRLGVYGPG SDIDTLVVVP KHVTKEDFFT
VFDQLLRKRK ELQKIEPIPG AYVPIIKTVF DGIDIDIICA RLDIPQVPLD LQLNSNDLLR
NIDDQDLRAL NGTRVTDLIL KLVPQKTVFR HALRTIKLWA KKRAIYANMF GFPGGVAWAM
LVARICQLYP NAVGAVIVEK FFYIYLQWKW PQPVMLTQIE DGPLPVRVWN PRLYGGDRAH
IMPVITPAYP SMCATHNICH STQSIILAEM RRASGIIKQI KEGKKNWSAM FQKHDFFYKY
KFYLTVIAAT RESYEDHLGW SGLVKSKLRL LVQKLENIPE IALAHPYVNP FMNSYISESE
SELFKMKDLY GTIAGEKFAK EHLEEVKIDD ETNFKKVEEE VKNSGKHIIH LMKLYIGLSL
DIKGREKKID IQVPCTEFDK FCQSWPDFDE KKFSLSIRYT KIWNLPDDVY DDGEKRPVRH
KRKRESLKSE SANKRQRTIT TSVPAGAATE AEA
//
