ID PAN2_NEOFI Reviewed; 1161 AA.
AC A1DFN6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit pan2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE EC=3.1.13.4 {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03182};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
DE Short=PAN deadenylation complex subunit 2 {ECO:0000255|HAMAP-Rule:MF_03182};
GN Name=pan2 {ECO:0000255|HAMAP-Rule:MF_03182}; ORFNames=NFIA_081370;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC complex, one of two cytoplasmic mRNA deadenylases involved in mRNA
CC turnover. PAN specifically shortens poly(A) tails of RNA and the
CC activity is stimulated by poly(A)-binding protein pab1. PAN
CC deadenylation is followed by rapid degradation of the shortened mRNA
CC tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by
CC two alternative mechanisms, namely exosome-mediated 3'-5'
CC exonucleolytic degradation, or deadenylation-dependent mRNA decaping
CC and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be
CC involved in post-transcriptional maturation of mRNA poly(A) tails.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03182};
CC Note=Binds 2 metal cations per subunit in the catalytic exonuclease
CC domain. {ECO:0000255|HAMAP-Rule:MF_03182};
CC -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit
CC pan3. {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the
CC regulatory subunit pan3 to form the poly(A)-nuclease (PAN)
CC deadenylation complex. {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal
CC hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain
CC is predicted to be catalytically inactive because it lacks the active
CC site catalytic triad characteristic of thiol proteases, with residues
CC at the equivalent structural positions that are incompatible with
CC catalysis, and it cannot bind ubiquitin. It functions as a structural
CC scaffold for intra- and intermolecular interactions in the complex.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the WD40
CC repeats and the pseudo-UCH domain mediates interaction with pan3.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03182}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027696; EAW18193.1; -; Genomic_DNA.
DR RefSeq; XP_001260090.1; XM_001260089.1.
DR AlphaFoldDB; A1DFN6; -.
DR SMR; A1DFN6; -.
DR STRING; 331117.A1DFN6; -.
DR EnsemblFungi; EAW18193; EAW18193; NFIA_081370.
DR GeneID; 4586646; -.
DR KEGG; nfi:NFIA_081370; -.
DR VEuPathDB; FungiDB:NFIA_081370; -.
DR eggNOG; KOG1275; Eukaryota.
DR HOGENOM; CLU_002369_1_0_1; -.
DR OMA; TQELLWT; -.
DR OrthoDB; 9810at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0031251; C:PAN complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:UniProtKB-UniRule.
DR CDD; cd06143; PAN2_exo; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03182; PAN2; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR030843; PAN2.
DR InterPro; IPR048841; PAN2_N.
DR InterPro; IPR028881; PAN2_UCH_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15728; DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1.
DR PANTHER; PTHR15728:SF0; PAN2-PAN3 DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1.
DR Pfam; PF20770; PAN2_N; 1.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Metal-binding; mRNA processing;
KW Nuclease; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1161
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT pan2"
FT /id="PRO_0000295350"
FT REPEAT 20..59
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 276..315
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 453..822
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 871..1049
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 1009..1060
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 316..452
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 1092..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 874
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 876
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 983
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT BINDING 1042
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
SQ SEQUENCE 1161 AA; 129833 MW; B2E1FEFD4AF29BC7 CRC64;
MEADWDELSR IPVPPPSPHG LPTAATTIAF DDVSELLWAG NEFGRITSFY GPELQRYTSV
RAHPVSDGPV RQILFHERGV ISLSPKSVHM ITRRGLTQWH ISHEEMTDLY CMSLTAQLNK
IIVAGCQRAM FTIDIDKGII VDKLHTDHNY TLMKKSRYLC AATDTGSVNA LSLTDFRVVK
SWKSHGTAIN DMDARNDLLV TCGFSVRHLG SPIVDPLANV YDLKTLSPLP PIPFHAGAAY
VRMHPKLSTT SFVASQTGQL QVVDLMNPNA INLRQANVSF MLGIDISPSG EALAINDAEC
SIHLWGSPSK IHFNEMSKEV EFADVVPRPP PLDWSPDTPL NMIGMPYYRE RLLSAWPSHL
VFEVGSPPAP IDQSLIPYLR PAEMGHYAPN PKKTRRYQVE NTRALTTAEP ALIAPKFLSE
KAREQNKFKS EASVSDTAEA LAGAKLNGEA EDDPLLKYSN VEIKYSRFGV DDFDFRFYNQ
TTFSGLETHI ANSFTNALLQ LLKFIPLVRN LALHHAASTC IYETCLLCEM GYLFDMLEKA
NGQNCQATNL LRTFSSYREA SNLGLFEENL TTKSLSSAIQ SVNRFFLNQI AHDFRMIVPS
SDDLDQRLST IASESIRCMF CQNEIVRPGN SLANELIYPA IDIKQARRNP AFRFSNILRA
SIERETQNRG WCNYCRRYQQ VTIRKSIHRM PLVLILNAAL SNPICRRLWS IPGWLPEEVG
IAVDNGQVMC FEGDELKTQL QNKLPNLVVY ELVGLVSEID IPEHQKPHLV SFINVSISSR
ELEAKNRWHL FNDFLVTEVD KDEALRFNQP WKSPCILAYQ AKDARHAVDD SWKNVLDITL
LFRDWSLNGG RAVETRQTLT EEEKPTPGTP VALDTEFVDL EKAEIDVKAD GSQEIVRPSK
SGLARVSVLR GSGVHEGVPF IDDYITIKEP IVDYVTQYSG IKPGDLDPRT SQHNLVPLKV
AYKKLWLLLN LGCVFVGHGL ASDFRKINIQ VPKSQTVDTQ YLYFHPGKNR RLSLRYLAWA
VFKEYIQEEP ADNNQGHDSI EDARMALRLW KKFQEYEDAG IVNQILEEIF REGSKLGFRP
PPRNGVATVL SRPGTAVTMQ NSSGRNTPST PDVGGAATAT ATTSAPATPR QAFRRSIALT
PSNGTFGGPG AGDFFGGSPL K
//
