ID   PAP_CANAL               Reviewed;         558 AA.
AC   O42617; Q59YW5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Poly(A) polymerase PAPalpha;
DE            EC=2.7.7.19;
DE   AltName: Full=Polynucleotide adenylyltransferase alpha;
GN   Name=PAPALPHA; Synonyms=PAP1;
GN   OrderedLocusNames=C5_01745W_B {ECO:0000312|CGD:CAL0000202028};
GN   ORFNames=CaO19.10713;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=10455055; DOI=10.1126/science.285.5431.1271;
RA   Hull C.M., Johnson A.D.;
RT   "Identification of a mating type-like locus in the asexual pathogenic yeast
RT   Candida albicans.";
RL   Science 285:1271-1275(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060;
RA   Ishii N., Aoki Y., Arisawa M.;
RT   "Molecular cloning of Candida albicans poly(A) polymerase gene.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. May
CC       acquire specificity through interaction with a cleavage and
CC       polyadenylation factor (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: The C.albicans mating-type-like (MTL) locus contains, in
CC       addition to the genes for the regulatory proteins (MTLA1, MTLA2,
CC       MTLALPHA1 and MTLALPHA2), a and alpha idiomorphs of a
CC       phosphatidylinositol kinase (PIKA and PIKALPHA), a poly(A) polymerase
CC       (PAPA and PAPALPHA) and an oxysterol binding protein-like protein (OBPA
CC       and OBPALPHA). PAPALPHA is not represented in the genomic sequence of
CC       strain SC5314 because that haploid assembly includes the mating type a
CC       allele of this locus. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR   EMBL; AF167163; AAD51412.1; -; Genomic_DNA.
DR   EMBL; AB009394; BAA23802.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42617; -.
DR   SMR; O42617; -.
DR   PRIDE; O42617; -.
DR   CGD; CAL0000202028; PAPALPHA.
DR   eggNOG; KOG2245; Eukaryota.
DR   HOGENOM; CLU_011511_4_1_1; -.
DR   InParanoid; O42617; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:CGD.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:InterPro.
DR   GO; GO:0043631; P:RNA polyadenylation; IEA:InterPro.
DR   GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR011068; NuclTrfase_I-like_C.
DR   InterPro; IPR007012; PolA_pol_cen_dom.
DR   InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR   InterPro; IPR014492; PolyA_polymerase.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF04926; PAP_RNA-bind; 1.
DR   PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR   SUPFAM; SSF55003; SSF55003; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing;
KW   Nucleotide-binding; Nucleus; RNA-binding; Transferase.
FT   CHAIN           1..558
FT                   /note="Poly(A) polymerase PAPalpha"
FT                   /id="PRO_0000051618"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         99..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         232..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            144
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            313
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            314
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            386
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            391
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            484
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   558 AA;  63268 MW;  8F9B5CA8B64CC106 CRC64;
     MNTKTYGVTE PISTNGPTPK ENILNDALIQ ELKNRGSFES EQATKKRVEV LTLFQRLVQE
     FVYTVSKSKN MSDSMAQDAG GKVFTFGSYR LGVYGPGSDI DTLVVVPKHV TRDDFFSVFA
     DIIRKRPELE EIACVPDAYV PIIKLEFDGI SIDLIMARLN IPRVPLDLTL DDKNLLKNLD
     EKDLRSLNGT RVTDEILQLV PKPTVFKHAL RCIKLWAQQR AVYGNIFGFP GGVAWAMLVA
     RICQLYPNAV SSAIVEKFFN IYTKWNWPEP VLLKSIEDGP LQVRVWNPRL YPHDRLHRMP
     VITPAYPSMC ATHNITSSTQ KVILAELSRG SSIMQEIHAG KKTWSDLFEK HSFFYKYKFY
     LCVVAASIDS AEEHKKWSGF IESKLRQLVL KLEVAEGVEI AHPYVKDFSN TFILDDKNAE
     DIINSYGTLS GEDFLRTLHS SDSDKDDEEF KKIRLTKYYI GLDLNLTKSS DGVRKLDIQY
     PCAEFYSICK GSTSFTEGVN FIQIKNVKLH ELSNDVYEDG EERPKKSGKK RKKVIKEDGQ
     KRVRNESPAS SASVNGSS