| IED ID | IndEnz0002008530 |
| Enzyme Type ID | protease008530 |
| 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 | par-1 pan2 NCU04792 NCU10733 |
| Organism | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora Neurospora crassa Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
| Enzyme Sequence | MDSRDWTQLGCVAYPSPIHPDYHAGPASTIAFDNQDELLWIGTQKGFAGSFIGRELKRFTAFRIHPETDGPLRQFLFVDKGVIFLGSRSVYMAARSGVPIWSIRHESMQDLRAMSFTSKGTSEILVAGWQNKMLVIDVNKGEVVKELPTQDQYSFLKMSRYICAATNKGTVNILDPITFTIKKQWQAHGAFINDLDTSNDFIVTCGGSHRQTHNTPAILDPYVKVFDLKNMSAMNPVPFAPLAAHVRMHPRMLTTAIVVNQAGQIHVTDLLNPSNSQVCYTQPQGVVLHFDVSRTGEGKALADNKHNTYVWGSPNKIQFTEIGIPPRLPDPPQPSLLPPDPDMLEELPLSRIGLPYYREQLFSALPPDIISDVGAPPQQIDPNILSTLTKTDWGYIGPNKTGLQRNQYMDTRSTMKTSNTIRAPKFLSEKARESQTGSEDNTLATNETAMMTPNNDHWSLRPEAPPEYRICEIKYSKFGVDDFDFGFFNNTPYPGLENNITNSYANSLLQVMHYTPLLRNMALQHAATACLADPCLLCELGYVFDMLQKGEGPSCHATNMLRALNHTSNASVSGVLEDIAKDKNPSTLVKNLTMFLFDKISQDYKGTPPISTELERTLFKLNQPPNPLDLVKRLLETDARYQIKCMHCQHVSPRTATTFVNKLCYPAAKPNIRGMKAQRITFSQVLKAGLENEAVNKGYCTKCQRYQNLDQRKIIFNIPAVLALCTEITTAEHRKLWSTPGWLPEEIGIIVDQGHVYCYEGDDLKLHLNRGIHNITVYSLVGTVVNVETKSPQKSHLVATVNVGRAEPESKDQDRWHLFNDFSVRGISKVEALTFNAAWKMPVVVMFQVKAANHRFNMDWKTRLDTSVLFRDNNPHALKTYELLDRETEIPGPDTVIAIDTEFIRLKEREIHIDEDGKSKTIRPISHAIARASVVRGQGSREGVAFIDDYIHIKETIVDYLTEWSGITPTDLDPINSQRNLVSPKTAYKKLWVLVNLGCKFLGHGLSQDFRVINIQVPRNQVIDTSIIFMKPPSQRKISLAFLAWYLLKEDIQQNTHDSIEDAQTALKLYRKYEEFMANGSFHDVLEALYKKGKTLNFKPPRISTGAAKDAGFGAVHRVGTPPVPAPGTTEGSFEISNSSTATTGGSALSATGGMGSASASSSMPSTPVRKPIGLGGPFTVAGVVKPSPATSLDNFGAGAVGTGITTAAATMGGGYGGYGTDGAYWGGPNDMAPTSMIGGSAFIPAKFPPGPPETRGFIPYRPQVLLAEREAAAAAAAAAAAAAANNDVGGRGGVACGNGGAGGEQGKQE |
| Enzyme Length | 1310 |
| Uniprot Accession Number | P0C581 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Positively regulated by the regulatory subunit par-2/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 pabp-1. 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 rgb-30/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 | Beta strand (51); Chain (1); Compositional bias (1); Domain (2); Helix (29); Metal binding (12); Region (2); Repeat (4); Turn (17) |
| Keywords | 3D-structure;Cytoplasm;Exonuclease;Hydrolase;Metal-binding;Nuclease;Reference proteome;Repeat;WD repeat;mRNA processing |
| Interact With | Q7SDP4 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 4CZV; 4CZW; 4CZX; 4CZY; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 143,936 |
| Kinetics | |
| Metal Binding | METAL 525; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:24880343, ECO:0007744|PDB:4CZW"; METAL 530; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:24880343, ECO:0007744|PDB:4CZW"; METAL 535; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:24880343, ECO:0007744|PDB:4CZW"; METAL 538; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:24880343, ECO:0007744|PDB:4CZW"; METAL 645; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:24880343, ECO:0007744|PDB:4CZW"; METAL 648; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:24880343, ECO:0007744|PDB:4CZW"; METAL 700; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:24880343, ECO:0007744|PDB:4CZW"; METAL 703; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:24880343, ECO:0007744|PDB:4CZW"; METAL 900; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 902; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 1009; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182"; METAL 1062; /note="Divalent metal cation; catalytic"; /evidence="ECO:0000250|UniProtKB:O95453, ECO:0000255|HAMAP-Rule:MF_03182" |
| Rhea ID | |
| Cross Reference Brenda |