Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O42617 (PAP_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) polymerase PAPalpha

EC=2.7.7.19
Alternative name(s):
Polynucleotide adenylyltransferase alpha
Gene names
Name:PAPALPHA
Synonyms:PAP1
ORF Names:CaO19.10713
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor By similarity.

Catalytic activity

ATP + RNA(n) = diphosphate + RNA(n+1).

Cofactor

Binds 2 magnesium ions. Also active with manganese By similarity.

Subcellular location

Nucleus.

Miscellaneous

The C.albicans mating-type-like (MTL) locus contains, in addition to the genes for the regulatory proteins (MTLA1, MTLA2, MTLALPHA1 and MTLALPHA2), a and alpha idiomorphs of a phosphatidylinositol kinase (PIKA and PIKALPHA), a poly(A) polymerase (PAPA and PAPALPHA) and an oxysterol binding protein-like protein (OBPA and OBPALPHA).

Sequence similarities

Belongs to the poly(A) polymerase family.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA polyadenylation

Inferred from electronic annotation. Source: InterPro

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

polynucleotide adenylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Poly(A) polymerase PAPalpha
PRO_0000051618

Regions

Nucleotide binding86 – 883ATP By similarity
Nucleotide binding99 – 1013ATP By similarity
Nucleotide binding232 – 2332ATP By similarity

Sites

Metal binding991Magnesium 1; catalytic By similarity
Metal binding991Magnesium 2; catalytic By similarity
Metal binding1011Magnesium 1; catalytic By similarity
Metal binding1011Magnesium 2; catalytic By similarity
Metal binding1531Magnesium 2; catalytic By similarity
Binding site1531ATP By similarity
Binding site2141ATP By similarity
Binding site2231ATP By similarity
Site1441Interaction with RNA By similarity
Site3131Interaction with RNA By similarity
Site3141Interaction with RNA By similarity
Site3861Interaction with RNA By similarity
Site3911Interaction with RNA By similarity
Site4841Interaction with RNA By similarity

Sequences

Sequence LengthMass (Da)Tools
O42617 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 8F9B5CA8B64CC106

FASTA55863,268
        10         20         30         40         50         60 
MNTKTYGVTE PISTNGPTPK ENILNDALIQ ELKNRGSFES EQATKKRVEV LTLFQRLVQE 

        70         80         90        100        110        120 
FVYTVSKSKN MSDSMAQDAG GKVFTFGSYR LGVYGPGSDI DTLVVVPKHV TRDDFFSVFA 

       130        140        150        160        170        180 
DIIRKRPELE EIACVPDAYV PIIKLEFDGI SIDLIMARLN IPRVPLDLTL DDKNLLKNLD 

       190        200        210        220        230        240 
EKDLRSLNGT RVTDEILQLV PKPTVFKHAL RCIKLWAQQR AVYGNIFGFP GGVAWAMLVA 

       250        260        270        280        290        300 
RICQLYPNAV SSAIVEKFFN IYTKWNWPEP VLLKSIEDGP LQVRVWNPRL YPHDRLHRMP 

       310        320        330        340        350        360 
VITPAYPSMC ATHNITSSTQ KVILAELSRG SSIMQEIHAG KKTWSDLFEK HSFFYKYKFY 

       370        380        390        400        410        420 
LCVVAASIDS AEEHKKWSGF IESKLRQLVL KLEVAEGVEI AHPYVKDFSN TFILDDKNAE 

       430        440        450        460        470        480 
DIINSYGTLS GEDFLRTLHS SDSDKDDEEF KKIRLTKYYI GLDLNLTKSS DGVRKLDIQY 

       490        500        510        520        530        540 
PCAEFYSICK GSTSFTEGVN FIQIKNVKLH ELSNDVYEDG EERPKKSGKK RKKVIKEDGQ 

       550 
KRVRNESPAS SASVNGSS 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a mating type-like locus in the asexual pathogenic yeast Candida albicans."
Hull C.M., Johnson A.D.
Science 285:1271-1275(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[2]"Molecular cloning of Candida albicans poly(A) polymerase gene."
Ishii N., Aoki Y., Arisawa M.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060.
[3]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF167163 Genomic DNA. Translation: AAD51412.1.
AB009394 Genomic DNA. Translation: BAA23802.1.
AACQ01000097 Genomic DNA. Translation: EAK95706.1.
RefSeqXP_714750.1. XM_709657.1.

3D structure databases

ProteinModelPortalO42617.
SMRO42617. Positions 4-526.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3643608.
KEGGcal:CaO19.10713.

Organism-specific databases

CGDCAL0006627. PAPALPHA.

Phylogenomic databases

KOK14376.
OrthoDBEOG7M6DHG.

Family and domain databases

Gene3D3.30.70.590. 1 hit.
InterProIPR002934. Nucleotidyltransferase.
IPR011068. NuclTrfase_I_C.
IPR007012. PolA_pol_cen_dom.
IPR007010. PolA_pol_RNA-bd_dom.
IPR014492. PolyA_polymerase.
[Graphical view]
PfamPF01909. NTP_transf_2. 1 hit.
PF04928. PAP_central. 1 hit.
PF04926. PAP_RNA-bind. 1 hit.
[Graphical view]
PIRSFPIRSF018425. PolyA_polymerase. 1 hit.
SUPFAMSSF55003. SSF55003. 1 hit.
ProtoNetSearch...

Entry information

Entry namePAP_CANAL
AccessionPrimary (citable) accession number: O42617
Secondary accession number(s): Q59YW5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: November 13, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Candida albicans

Candida albicans: entries and gene names