| IED ID | IndEnz0002008541 |
| Enzyme Type ID | protease008541 |
| 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 ubp13 SPAC22G7.04 |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MDAWKEITKTTENDGVSTCSLSSIAFDPYSELVWTGHKNGQIKSSFGPSLTSYTQFIGHEGPVHQVLPQERGVFSLSSKSLRLSNRKGTIRWRYQDSDCIDYRAMFYQSRNNPEVVIGGYHQKLTVVNAERGISIHKDKNVSDIFIMRRNRLLCCGSTNGEIILRDPNSFQPVNKVVAHTGTISDIDTSGNLLLSCGYSLRHGTYMLDPFVKVWDLRNLSSLVPIPFPAGPTIIRMHPKLSTTAVVCSCSGQFHIVDTGNPLDAKLMQIPLTSYLTGMDIASTGDAMVFTDVEDNIHLWSPLENPSFSDLKLPIQLPNTSTETVQLENNDPLNSIGLPYYKDELLSSWSKYLIFDVGKPILDSNLLIAKQISENSHPVPQEIKSFHRNQIIEVPWLNRKLISEGATPKFHSERQKDIMSGNDIEGSASYFEEIEDTISGPDSIPKFYQRPVIKYSKFGIEDFDFGFYNKTKYAGLETDITNSYCNSVLQLLSYVPSFSKAAISHSLGPCDLMECLLCELGFLFAMLKESTGRNCQATNFLRAFSNSSFAQSLGIVFDDYSDGTFPDSFVIQKFTKFMLTEISRIADYEDKKDGTSFPVSFLLKSFCIPEMQTYRCGICGITSQKIKSSLYIIDLHYPSQQLESILSFEWLFKMSLDRRVDLPPGWCEYCLAHQPFLLRSFIRSLPDCLFINTQVKHHEHWKLWARKNWLPKKLHLRRVNDTMQCVSQKISNLDKDQQSLSVYVLRGIIYEIRQNGEEPHFVSTIRVSDNTSSDNPDDNRWYIFNDFLVKEVTEEEALTVHGPWKIPIIVYYEKLDTKIPQWDEVSDYTLLYQPYSLNKNPPINKIQPLTTDEMLYPKMLVGIDSEFVALQQEETEVRSDGTKSTIKPSKLSLARVSVLRGEGPNKGLPFIDDYVATDDKVTDYLTEYSGIHPGDLDPDRSPYNVVPLKVAYKKLRLLVNAGCIFVGHGLQKDFRIINLLVPPEQVVDTVDLFFLSSRQRKLSLKFLAWYLLDEEIQLTEHDSIEDALTALKLYDCYDKLKSQGKLEETLDNIYEVGRRFKFRPPSVASMSLEDRNSYGDESVISNQTN |
| Enzyme Length | 1088 |
| Uniprot Accession Number | Q09798 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Positively regulated by the regulatory subunit ppk26/pan3. {ECO:0000250, 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); Metal binding (4); Region (1); Repeat (4) |
| 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, ECO:0000269|PubMed:16823372}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20473289; 23697806; 25720772; 29996109; 34250083; |
| Motif | |
| Gene Encoded By | |
| Mass | 123,874 |
| Kinetics | |
| Metal Binding | METAL 863; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 865; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 972; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 1025; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182 |
| Rhea ID | |
| Cross Reference Brenda |