Q503I9

PR
Gene name
tent2
Protein name
Poly(A) RNA polymerase GLD2
Names
PAP-associated domain-containing protein 4
Species
Danio rerio (Zebrafish) (Brachydanio rerio)
KEGG Pathway
dre:553626
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)

30-159 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q503I9

Entry ID Method Resolution Chain Position Source
AF-Q503I9-F1 Predicted AlphaFoldDB

No variants for Q503I9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q503I9

No associated diseases with Q503I9

2 regional properties for Q503I9

Type Name Position InterPro Accession
domain PAP/25A-associated 386 - 440 IPR002058
domain Polymerase, nucleotidyl transferase domain 193 - 285 IPR002934

Functions

Description
EC Number 2.7.7.19 Nucleotidyltransferases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

6 GO annotations of molecular function

Name Definition
5'-3' RNA polymerase activity Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template, via extension of the 3'-end.
adenylyltransferase activity Catalysis of the transfer of an adenylyl group to an acceptor.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
nucleotidyltransferase activity Catalysis of the transfer of a nucleotidyl group to a reactant.
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.

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.
negative regulation of miRNA catabolic process Any process that stops, prevents or reduces the frequency, rate or extent of miRNA catabolic process.
RNA 3'-end processing Any process involved in forming the mature 3' end of an RNA molecule.
RNA polyadenylation The enzymatic addition of a sequence of adenylyl residues at the 3' end of an RNA molecule.
RNA stabilization Prevention of degradation of RNA molecules.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5VYS8 TUT7 Terminal uridylyltransferase 7 Homo sapiens (Human) PR
Q5BLK4 Tut7 Terminal uridylyltransferase 7 Mus musculus (Mouse) PR
A8WHT1 C53A5.17 tRNA (guanine(37)-N1)-methyltransferase Caenorhabditis elegans PR
Q5XET5 HESO1 Protein HESO1 Arabidopsis thaliana (Mouse-ear cress) PR
Q0VFA3 tent2 Poly(A) RNA polymerase GLD2 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MLPRPYIFSH NDGPSSHLFQ HVLPHNVSQQ QRIEAHLNST NNFIGPPMNA PRFIPTYQWT
70 80 90 100 110 120
PVELSDVACS PNGPMGNNRK RRIQDNSDIN LKRQRFSCPS PHNQSARNSN FTSQPVTRPV
130 140 150 160 170 180
TGREVTCPTC SSATFIPGGC VPSLGETCHQ NAFSPSSVKD KLSQQILNLF FACEQQSDDL
190 200 210 220 230 240
EKKESCRAAL QTDIQKIFPC AKVFLGGSSL NGFGSRSSDA DLCLVIEEGP VNHRKDAVYV
250 260 270 280 290 300
LSLVRKLLYK LSYIEKPQLI RAKVPIVKFR DRISGVEFDL NFNNTVGIRN TFLLRTYAFV
310 320 330 340 350 360
EKRVRPLVLV IKKWANHHCI NDASRGTLSS YTLVLMVLHY LQTLPEPVIP CLQRDYPTCF
370 380 390 400 410 420
DPKMDIHLVP SGPSDIPAFV SRNQSSLGDL FLGFLRYYAT VFKWDKQVIS VRMARTLPKS
430 440 450 460 470 480
NCKEWKDKFI CVEEPFNRTN TARAVHERMK FEAIKAAFIE SHRLLQLRKD LNFILPKSKQ
MARPQTAPR