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Database: UniProt
Entry: PAPA_CANAL
LinkDB: PAPA_CANAL
Original site: 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   24-JAN-2024, entry version 122.
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   EnsemblFungi; C5_01780W_A-T; C5_01780W_A-T-p1; C5_01780W_A.
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; 1351913at2759; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IDA:CGD.
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:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
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; 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
//
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