PAN2_ASPCL
ID PAN2_ASPCL Reviewed; 1161 AA.
AC A1CEK7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=ACLA_089990;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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 deadenlyation-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}.
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DR EMBL; DS027052; EAW11306.1; -; Genomic_DNA.
DR RefSeq; XP_001272732.1; XM_001272731.1.
DR AlphaFoldDB; A1CEK7; -.
DR SMR; A1CEK7; -.
DR STRING; 5057.CADACLAP00008452; -.
DR EnsemblFungi; EAW11306; EAW11306; ACLA_089990.
DR GeneID; 4705070; -.
DR KEGG; act:ACLA_089990; -.
DR VEuPathDB; FungiDB:ACLA_089990; -.
DR eggNOG; KOG1275; Eukaryota.
DR HOGENOM; CLU_002369_1_0_1; -.
DR OMA; TQELLWT; -.
DR OrthoDB; 128953at2759; -.
DR Proteomes; UP000006701; 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 Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03182; PAN2; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR030843; PAN2.
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 Pfam; PF00929; RNase_T; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54001; SSF54001; 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_0000295335"
FT REPEAT 20..59
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 102..145
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 276..315
FT /note="WD 3"
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 REGION 316..452
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 1094..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1147
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; 129570 MW; A4CE644E3608128F CRC64;
MEADWDELSR IPVPAPSSHG LPTIATTIAF DDVSELLWAG NEFGRITSFY GPELQRYTSV
RAHPVSDGPV RQILFHERGV ISLSPKSVHM ITRRGLSQWH IAHEEMTDLH CMSFTAQLNR
IIVAGCQSAM FTIDIDKGVI VDKLQTDHNY TMMKKSRYLC AATDTGSVNA LSLSDFQVVK
SWKAHGTAIN DMDARNDLLV TCGFSVRHLG SPIVDPLANV YDLKTLSPLP PIPFHAGAAY
VRMHPKLHTT SFVASQTGQL QVVDLMNPNA INLRQANVSF MLGIDISPSG EALAINDAEC
AIHLWGSPSK VHFNEMSKEV EFADVVPRPP SLDWSPDTPL NMIGMPYYHE RLFSAWPSHL
VFEVGNPPAS IDQSLIPYLR PAEMGHYAPN PKKTRRYQVE NTRALTTAES ALIAPKFLSE
KAREQTRAKS EGSVSDTAEA LAGAKLNGEA EDDPLLKYSN VEIKYSRFGV DDFDFRFYNQ
TIFSGLETHI ANSFTNALLQ LLKFIPLVRN LALHHAASTC IYETCLLCEM GYLFDMLEKA
NGQNCQATNL LKAFSSYREA SNLGLLEENL TTKSLSSAIQ SVNRFFLNQI AHDFRMILPS
SDDLDHRLAT IASESIRCMF CQNEIVRPGN SLANELIYPA IDIKQARRNP AFKFSNILRA
SIERETQNRG WCNYCRRYQQ VTIRKTVHRM PLVLILNAAL NNPLCRRLWS IPGWLPEEIG
IVVEGGQVMC YEGDELKAQV QNKVPNLVLY DLVGLVAEID IPEHQKAHLV SFINVSISSR
ETESKSRWHL FNDFLVTEVD KDEALRFNQP WKIPCVLAYQ ARDARHGVDD AWKDTLDTTL
LFRDWSLNGG RPVESRQTLT EEEKPTPGTP VALDTEFVDL EKAEIDVKAD GSQEIVRPNK
SGLARVSVLR GSGIHEGVPF IDDYITIKEP IVDYVTQYSG IKPGDLDPRT SQHNLVPLKV
AYKKLWLLLN LGCIFVGHGL ASDFRKINIQ VPKNQTVDTQ YLYFHPGKNR RLSLRYLAWA
VFKEYIQEES TDANQGHDSV EDARMALRLW KKFQEYEDAG IVNQILEEIF REGSRLGFRP
PPRNGVATVL SRPGTAVTMQ NNSGRNTPST PDVGGAAAAA ATTSAPATPR QAFRRSIALT
PSNGTFGGPG TGDFFGGSPL K
