PAPA_CANAL
ID PAPA_CANAL Reviewed; 555 AA.
AC Q9UW26; A0A1D8PN98; O93834; Q59YI3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Poly(A) polymerase PAPa;
DE EC=2.7.7.19;
DE AltName: Full=Polynucleotide adenylyltransferase a;
GN Name=PAPA; Synonyms=PAP99; OrderedLocusNames=CAALFM_C501780WA;
GN ORFNames=CaO19.3197;
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 Nagahashi S., Ishii N., Aoki Y., Arisawa M.;
RT "Candida albicans PAP99 gene, a putative homolog of the C.albicans PAP1
RT gene.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 {ECO:0000250}.
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).
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR EMBL; AF167162; AAD51407.1; -; Genomic_DNA.
DR EMBL; AB021667; BAA36217.1; -; Genomic_DNA.
DR EMBL; CP017627; AOW29609.1; -; Genomic_DNA.
DR RefSeq; XP_714613.1; XM_709520.1.
DR AlphaFoldDB; Q9UW26; -.
DR SMR; Q9UW26; -.
DR STRING; 237561.Q9UW26; -.
DR GeneID; 3643763; -.
DR KEGG; cal:CAALFM_C501780WA; -.
DR CGD; CAL0000194576; PAP1.
DR VEuPathDB; FungiDB:C5_01780W_A; -.
DR HOGENOM; CLU_011511_4_1_1; -.
DR InParanoid; Q9UW26; -.
DR OrthoDB; 326577at2759; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0033620; C:Mei2 nuclear dot complex; IEA:EnsemblFungi.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR GO; GO:1990251; C:nuclear exosome focus; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:EnsemblFungi.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:CGD.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IDA:CGD.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:CGD.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IEA:EnsemblFungi.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:EnsemblFungi.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR GO; GO:0071050; P:sno(s)RNA polyadenylation; IEA:EnsemblFungi.
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; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..555
FT /note="Poly(A) polymerase PAPa"
FT /id="PRO_0000051619"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..555
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 139
FT /note="Interaction with RNA"
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 487
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT CONFLICT 447
FT /note="N -> K (in Ref. 2; BAA36217)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="Q -> R (in Ref. 2; BAA36217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 63289 MW; 5C76DA500616042A CRC64;
MNNQAYGVTP PISVANSTPK ENELNDSLIK ELKSRGSFES ETATKKRVEV LNILQSMTEE
FVYKVSIKKN ISEGMARDVG GKIFTFGSYR LGVYGPGSDI DTLVVVPKHV SRNDFFEVFY
ELLKGRSELE EIAPVPDAFV PIIKIEFAGI SIDLIFARLD IPRVPRDLTL DDKNLLKNID
EKDLRALNGT RVTDEILQLV PKPTVFKHAL RCIKMWAQQR AVYGNIFGFP GGVAWAMLVA
RICQLYPNAV SAVIVEKFFH IYSQWAWPQP VLLKQIEDGP LQVRVWNPRL YALDRQHRMP
VITPAYPSMC ATHNITSSTQ KVILSEFQRG IELMNDINVG KKSWSDLLER HDFFFRYKFY
LCIVAATRST YAEHLKYSGM VESKLRLLVQ KLELVEGIEL AHPYVKSFEN GYYCDNAEEA
HEIMNLYGTS KGDDRVKGVL HAENNDNNKE NVENKVELHM TKLFIGLKLD LSKEGEKKLD
IQYPCAEFFN ICKGWQDFDS EKHFIQIKNV KLYDLSDDVY VDGETRPIKI AKRKRAVSKN
EGKKKPKSVG TVSAA
