| IED ID | IndEnz0002008522 |
| Enzyme Type ID | protease008522 |
| 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 CTHT_0042640 |
| Organism | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Chaetomium Chaetomium thermophilum Chaetomium thermophilum var. thermophilum Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
| Enzyme Sequence | MDADWDEVTRIAYPAPGTNDFPRPATAVAFDPIAELLWAGFDRGRVCSFYGRDLTRYTAFKIQPASEGPVRQFLFHDKGVIVLGTRSVHMAMRRGPALWNIRHENMKDLRCMSFTSKGTQEIIVAGWQDTMLVIDVLKGDIIKQIPAQHHYSIMKKSRYICAATKTGSVDLIDPLSFKIVRSWQAHASYINDMDAQNDFIVTCGGSLKQQAAQTYMLDPYVNVFDLKNMASMKPMPFPPLAAHVRLHPRMLTTAIVTSQHGQMHVVDIMNPNSSTVRYANISSYVKLFEIAPSGEALVIGDADCNIHLWGSPTKIHFTDMAIPIELPEPEEPAPVLDWSIETPLSSIGLPYYREPLFSAWPADIISDVGAPPLQLEPSFVATLKQAEWGLYGKNTRNVRRNQVEDTRNTNKQSNALQAPKFLSERARESALSSGGDSSSDPQVDQEPEDPNEIESLKPEAPPLYRNLEIKYSKFGVDDFDFGYYNKTRYAGLENHIPNSYANSLLQLMHYTPLLRNMALQHAATACVSDLCLLCELGFVFDMLQKAEGATCQATNMFKALSGTPQAAPLGLLEEETHVPSLATMAQNLSRFLLEKIHNEYRTIPPISTALEQSLFNFPHPPTPDELVAKVLATSAVATIKCMNCRSETTRPGTTHVIDLLYPPPKTAGRGGRASKVTFSQVLKMGVERETTSKGWCSRCQRYQNLQMRKTIHSVPAVLVVNAGVSNQEHRKLWSTPGWLPEEIGIIVDQGQFFCFEGEDLKLHLQRGIHNITVYSLIGMVINIESHSPQKSHLVGIINVAHAEATPPGENKWHLFNDFSVRPVSAAEALTFNAAWKMPAVLLFQIKSANNKSNLDWKTNLDTSILYKDTNPNTEKKTYRTLDQERERPGPDTIVALDTEFVSLKQPEIQMNSDGERETIRPMSHALARVSVVRGQGENEGSAFIDDYIAIREPVVDYLTLYSGITASDLDPRTSKHNLVSLKTAYKKLWVLLNLGCKFLGHGLKQDFRVINIQVPRAQVIDTIEVFYLKSRLRKLSLAFLAWYLLKEDIQLETHDSIEDARTALKLYRKYLEFDDAGILEAMLEDIYKAGRATNFKPPRREDREKELQRQSTPPNSTAPNDCGAKPDGNGNENGGEPATPARKTGGITAPTFGAVNVFGTPSKASSPLPK |
| Enzyme Length | 1170 |
| Uniprot Accession Number | G0SAK8 |
| 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, ECO:0000269|PubMed:24872509}; |
| 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, ECO:0000269|PubMed:24872509}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (31); Chain (1); Compositional bias (1); Domain (2); Helix (3); Metal binding (4); Mutagenesis (1); Region (3); Repeat (2); Turn (5) |
| Keywords | 3D-structure;Cytoplasm;Exonuclease;Hydrolase;Metal-binding;Nuclease;Reference proteome;Repeat;WD repeat;mRNA processing |
| Interact With | G0S0Y3 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4CYJ; 4D0K; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 130,569 |
| Kinetics | |
| Metal Binding | METAL 897; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 899; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 1006; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 1059; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182" |
| Rhea ID | |
| Cross Reference Brenda |