Detail Information for IndEnz0002008516
IED ID IndEnz0002008516
Enzyme Type ID protease008516
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 An11g04210
Organism Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Enzyme Sequence MEADWDELSRIPVPAPSVHALPTIATAIAFDDVMELLWGRITSFFGPELQRYTSVRAHPATEPVRQIIFHDRGVISLSPKSVHMITRRGLTQWHIAHEEMTDLRCMSFTAQTNRIIVAGCQKSMFTIDIDKGIIIDKLHTEYNYTIMKKSRYLCAATDTGSVNALSLNDFSVVKSWKAHGTAVNDMDARNDLLVTCGFSVRHLGSPIVDPLANVYDLKTLSPLPPIPFHAGAAYVRMHPKLHTTSFVASQTGQLQVVDLMNPNAINLRQANVSFMLGIDLSPSGEALAINDAECAIHLWGSPAKVHFNEMSKEAEFGDVAPRPPTLDWSPETPLSMIGMPYYHERLFSAWPSHLVFEVGSPPPQVDQALIPYLRPAELGHHAPNPKKTRRYQVENTRALASAEPALIAPKFLSEKAREQNKAKSEGAISDAAEALAGAKINGETDDDPLLKYSNVEIKYSRFGVDDFDFRFYNQTTFSGLETHIANSFTNALLQLFKFIPYIRNVALHHAASSCIFETCLLCEMGYLFDMLEKASGQNCQATNLLKTFSSYREASNLGLFEENLTNKSLSAAIQAVNRFFLGQISHDFRMISPSSDDLDHRLATVASESIRCMFCQNEIVRPGNSLVNELNYPAIDIKQARRNPAFRFSNILRASIEREAQNRGWCNYCRRYQQVAIRKSVHRMPQVLMLNAALTNPICRRLWAIPGWLPEEVGIVIEGGQILCFEGEDLKLRVQAKMPGLVVYDLVGLVCEIDIPEHQKAHLVSFINVSISSREPETKNKWHLFNDFLVTEVDKEEALRFNQPWKIPCVLAYQVQDGRHAMDDTWKDALDTTLLFRDWSLNGGRPVESRVTLSEEEKPTPGTPVALDTEFVDLEKAEIDVKADGSQEIVRPSKSGLARVSVLRGSGIREGVPFIDDYITIKENIVDYVTQYSGIKPGDLDPRVSQHNLVPLKVAYKKLWLLLNLGCVFVGHGLASDFRKVNIQVPKSQTVDTQYLFFHPGKNRRLSLRYLAWAVFKEYIQEEPADDSQGHDSIEDARMALRLWKKFKEYEDAGIVSQILEEIFREGSKLGFRPPPRNGVPTVLSRPGTAVTMQNNSGRNTPSTSDVAGAAASAPATPRQAFRRSIALTPSNGSFAGPGTGDFFSGSPLK
Enzyme Length 1150
Uniprot Accession Number A2QW83
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Positively regulated by the regulatory subunit 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); Compositional bias (2); Domain (2); Metal binding (4); Region (2); Repeat (2)
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 128,444
Kinetics
Metal Binding METAL 868; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 870; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 977; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182; METAL 1036; /note=Divalent metal cation; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03182
Rhea ID
Cross Reference Brenda