| IED ID | IndEnz0002008526 |
| Enzyme Type ID | protease008526 |
| Protein Name |
PAN2-PAN3 deadenylation complex catalytic subunit PAN2 EC 3.1.13.4 PAB1P-dependent poly A -specific ribonuclease Poly A -nuclease deadenylation complex subunit 2 PAN deadenylation complex subunit 2 |
| Gene Name | PAN2 LELG_03597 |
| Organism | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Lodderomyces Lodderomyces elongisporus Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Enzyme Sequence | MEGWSQVALVPLKNSNNNSNSNSSSNNSSNGVLVQDPISTVTTTVFDSVQNLVWCGDTSGYVRSLSSVKTSPYSIQLYPYTKFRTNTLNQPIIQILSHREGVLSLLNDQLSIYNRRGVPRNAVNSMSFKESNGRELFKDLKTMSFNCNSFNEIVVGTELDLIKVDMNKSNLVQQFNHTGKVAMVKEAPKLLALASSTGSLELFDPTSNSSIKTFSAHNGYMSDMDIKGNYIATCGNSIRPKRYHYHQAPEYTADPLVNIFDIRTMKAVAPVAFPAGVSSVRFHPKLPNILIVTSAYGLIEFVDIFDQTNVSVYHADMSAATPPLPPAGSSAAQQQKQQQQQQQQPHLSGLEISENGDFFMFNDGFSNLHLWSITNSGTLSKNFVNFPQEIERPDIVNGPSGVLGGGSGSGDGAFIDIDADVPLSVVGMPYYKELLLSNWPNDLKFVKEKARLPEPIDPDLLSIFEKQQQQKISQTPKWIPYDSLKYGTCNIPEYYSLTSQKDTQIPKFLSEKNGGQKQRQKSIQALEDSIFQCQNDEKIPNCYSRLQIQYSKFGVKDFDFAFYNRTQEYCGLENHSDNSYINSLLQLYRFQSVFYNKVVHSLSNEWLPNDEATIETNPEGSSILNELAYLFDMMFKAKSRNVKTYNFSQVMNHDKQAAKLINLNELMNLNSHEVRELIIAFNNYLLTRLSMDFRNQFNFNFDLTELAYEIEVRGRGHSCPIYDKQMGAMFSLELITPPHNMMSKMSILVNPNTQQDQQQQQQQQQQQQQQQQPTNLANIRKNLNILTYLEYSMNQYKTIPCTQHQHFHPHTLEIRTSITKLPPVLVLNVNLTNEEFRIINSLKQWLVPDLYAVRATNNGSNRGYSFKPSMPVSGDFKKYQLLGYVCEISHQVDTSRTGGHNLVSFVKIKDEWMFFNDYLVIPIPEEEVFNLTYSWKKPVIVIYQEVDKMDKVEPFRHITHFQGNDSILYRDHFAGPIRELYQREYTLLTREKEAPQPGTLVAIDAEFVTLKPEQLEISYNGQKKLVKPKELSLARVSVLRGGREGINSNITGNNNDDNNNISGMIIDDPLFGEAFIDDYIVHKSHIYDYTTNFSGIEPNDLDIHKSSKNLVTLQTAYRKLWLLLNLGVIFVGHGLYTDFRTINLQVPEEQIRDTADFYYKSSFKRQLSLKFLAYVMLKERVQKGNHDSIEDARTALLLYKKYVELNQKSTNEFEKMLNFVYEEGNRLKYRVPEL |
| Enzyme Length | 1234 |
| Uniprot Accession Number | A5E1W0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Positively regulated by the regulatory subunit PAN3. {ECO:0000255|HAMAP-Rule:MF_03182}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; |
| DNA Binding | |
| EC Number | 3.1.13.4 |
| Enzyme Function | FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. {ECO:0000255|HAMAP-Rule:MF_03182}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Domain (2); Metal binding (4); Region (4); Repeat (3) |
| Keywords | Cytoplasm;Exonuclease;Hydrolase;Metal-binding;Nuclease;Reference proteome;Repeat;WD repeat;mRNA processing |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 141,073 |
| Kinetics | |
| Metal Binding | METAL 1004; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 1006; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 1138; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 1191; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182 |
| Rhea ID | |
| Cross Reference Brenda |