| IED ID | IndEnz0002008543 |
| Enzyme Type ID | protease008543 |
| 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 YALI0E29403g |
| Organism | Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Dipodascaceae Yarrowia Yarrowia lipolytica (Candida lipolytica) Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
| Enzyme Sequence | MEGWQEPPRIPLTQICRVSHTAPVATEIGQLTDTLPLTFDLAEDLVWAGDTNGIVSSYYGETLQPYSRFRAGRGRVTSLVSHDRGLVALTTDALHYSTRGGLTRKHVTDPSLGNNLCMTFTHGPTEFVVGGNPGKLVVVNSERGDVTRVVDSPGMATHMAGSSSCVVWGTENGKLVVGDNNLKELHTFQAHQGPFSDVSVQDNVVMTCGFSAASTGHRIDPLIKVWDLRMMRAMAPISYPLAAFVCQTPDSRTLITSPSGQLEFLDHATQQIKLYQAEVALVNGVKLSPRGHHFVVSDTSGQLQLWSDEPQSSFAEFSAPTAFPTPEQSYPPVSIRDTRYPLGAVGMPYYSDTLLSAMPSSIINVGMPPEEVDEDLEVRQIDFVGHAPNYKQQKRNLAQKYSNQRRTSIAAPKFLSEKEKERARRMEDIEDESFFGDEDTCTEASMSSKKVPRLYRKLEIKYSKFGISDFDFSYYNNHTGLSGLETNPFNPLLQLFRFCSPVFNFALRSVARGTPNRLLNEVGLLFDMMHKARGHVCRASNLMHCYDGIAQTRSLAPEDATNIVLFCRFLLEQIGFEQRQTPALFDSFRQLLGATVITVNTFSCGKMAQAESVWYTLELALGSTFYECLERTLDKELHTRAWCDKCRKYQSLHVSKHVESLPQVLTLSVADGNVDVAKSFLVLDGKVSPAAETDNDAYKLVGFICQIQGNGQVAFIRVGDEWYLFNDFLVTKVSEKEAFMKTPWKRTVMMVYAVGADERFDYDSWKNDMDVSALFEERLVNGNNVSRETTDYGYELIKEVPPPKTLCAIDAEFVVLKNEETEIRSDGTKVVLAPRNLCLARVTLLNEDGHPFINDYIAINEHIVDYLTAFSGIEPGDLDPSISRKPLVSLPTSYRRLWLLLNLGCVFVGHGLANDFRTINMQVPPEQVIDTVDLYYIPSERRKLSLRFLAWCVLGKKVQSGNHDSTEDSHTALLLYKKYQDCAPEEFQVLLLDVYRQGRMCNFKVPEA |
| Enzyme Length | 1008 |
| Uniprot Accession Number | Q6C462 |
| 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); Domain (2); Erroneous gene model prediction (1); Metal binding (4); Region (1); Repeat (5) |
| 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 | 112,973 |
| Kinetics | |
| Metal Binding | METAL 810; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 812; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 915; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 968; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182 |
| Rhea ID | |
| Cross Reference Brenda |