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

6 structures for P29468

Entry ID Method Resolution Chain Position Source
1FA0 X-ray 260 A A/B 1-537 PDB
2HHP X-ray 180 A A 1-530 PDB
2O1P X-ray 270 A A/B 1-538 PDB
2Q66 X-ray 180 A A 5-529 PDB
3C66 X-ray 260 A A/B 1-526 PDB
AF-P29468-F1 Predicted AlphaFoldDB

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

3 regional properties for P29468

Type Name Position InterPro Accession
domain Polymerase, nucleotidyl transferase domain 81 - 154 IPR002934
domain Poly(A) polymerase, RNA-binding domain 353 - 531 IPR007010
domain Poly(A) polymerase, central domain 8 - 351 IPR007012

Functions

Description
EC Number 2.7.7.19 Nucleotidyltransferases
Subcellular Localization
  • Nucleus
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