P29468
Gene name |
PAP1 (YKR002W) |
Protein name |
Poly(A) polymerase |
Names |
PAP, Polynucleotide adenylyltransferase |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YKR002W |
EC number |
2.7.7.19: Nucleotidyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
4 variants for P29468
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s11-442918 | 15 | T>I | No | SGRP | |
| s11-443005 | 44 | E>G | No | SGRP | |
| s11-444063 | 397 | A>T | No | SGRP | |
| s11-444178 | 435 | T>K | No | SGRP |
No associated diseases with P29468
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.19 | Nucleotidyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mRNA cleavage and polyadenylation specificity factor complex | A multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| polynucleotide adenylyltransferase activity | Catalysis of the template-independent extension of the 3'- end of an RNA or DNA strand by addition of one adenosine molecule at a time. Cannot initiate a chain 'de novo'. The primer, depending on the source of the enzyme, may be an RNA or DNA fragment, or oligo(A) bearing a 3'-OH terminal group. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| mRNA polyadenylation | The enzymatic addition of a sequence of 40-200 adenylyl residues at the 3' end of a eukaryotic mRNA primary transcript. |
| pre-mRNA cleavage required for polyadenylation | The targeted, endonucleolytic cleavage of a pre-mRNA, required for polyadenylation of the 3' end. This cleavage is directed by binding sites near the 3' end of the mRNA and leaves a 3' hydoxyl end which then becomes a target for adenylation. |
| RNA polyadenylation | The enzymatic addition of a sequence of adenylyl residues at the 3' end of an RNA molecule. |
| sno(s)RNA polyadenylation | The enzymatic addition of a sequence of adenylyl residues at the 3' end of snoRNA class molecule (referred to as an sRNA in Archaea). In eukaryotes, this occurs in conjunction with termination of transcription of precursor snoRNA molecules and may occur post-transcriptionally on incorrectly processed molecules targeted for degradation. |
| termination of RNA polymerase II transcription, poly(A)-coupled | An RNA polymerase II transcription termination process in which cleavage and polyadenylylation of the mRNA 3' end are coupled to transcription termination. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9LMT2 | PAPS1 | Nuclear poly(A) polymerase 1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSQKVFGIT | GPVSTVGATA | AENKLNDSLI | QELKKEGSFE | TEQETANRVQ | VLKILQELAQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RFVYEVSKKK | NMSDGMARDA | GGKIFTYGSY | RLGVHGPGSD | IDTLVVVPKH | VTREDFFTVF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DSLLRERKEL | DEIAPVPDAF | VPIIKIKFSG | ISIDLICARL | DQPQVPLSLT | LSDKNLLRNL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DEKDLRALNG | TRVTDEILEL | VPKPNVFRIA | LRAIKLWAQR | RAVYANIFGF | PGGVAWAMLV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ARICQLYPNA | CSAVILNRFF | IILSEWNWPQ | PVILKPIEDG | PLQVRVWNPK | IYAQDRSHRM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PVITPAYPSM | CATHNITEST | KKVILQEFVR | GVQITNDIFS | NKKSWANLFE | KNDFFFRYKF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YLEITAYTRG | SDEQHLKWSG | LVESKVRLLV | MKLEVLAGIK | IAHPFTKPFE | SSYCCPTEDD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YEMIQDKYGS | HKTETALNAL | KLVTDENKEE | ESIKDAPKAY | LSTMYIGLDF | NIENKKEKVD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IHIPCTEFVN | LCRSFNEDYG | DHKVFNLALR | FVKGYDLPDE | VFDENEKRPS | KKSKRKNLDA |
| 550 | 560 | ||||
| RHETVKRSKS | DAASGDNING | TTAAVDVN |