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Database: UniProt
Entry: A0A317V4X1_9EURO
LinkDB: A0A317V4X1_9EURO
Original site: A0A317V4X1_9EURO 
ID   A0A317V4X1_9EURO        Unreviewed;      1155 AA.
AC   A0A317V4X1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit PAN2 {ECO:0000256|HAMAP-Rule:MF_03182};
DE            EC=3.1.13.4 {ECO:0000256|HAMAP-Rule:MF_03182};
DE   AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000256|HAMAP-Rule:MF_03182};
DE   AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000256|HAMAP-Rule:MF_03182};
DE            Short=PAN deadenylation complex subunit 2 {ECO:0000256|HAMAP-Rule:MF_03182};
GN   Name=PAN2 {ECO:0000256|HAMAP-Rule:MF_03182};
GN   ORFNames=BO94DRAFT_628756 {ECO:0000313|EMBL:PWY68128.1};
OS   Aspergillus sclerotioniger CBS 115572.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY68128.1, ECO:0000313|Proteomes:UP000246702};
RN   [1] {ECO:0000313|EMBL:PWY68128.1, ECO:0000313|Proteomes:UP000246702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY68128.1,
RC   ECO:0000313|Proteomes:UP000246702};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_03182};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03182};
CC       Note=Binds 2 metal cations per subunit in the catalytic exonuclease
CC       domain. {ECO:0000256|HAMAP-Rule:MF_03182};
CC   -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit
CC       PAN3. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03182}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03182}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03182}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03182}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWY68128.1}.
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DR   EMBL; MSFK01000045; PWY68128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317V4X1; -.
DR   STRING; 1450535.A0A317V4X1; -.
DR   OrthoDB; 9810at2759; -.
DR   Proteomes; UP000246702; 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 {ECO:0000256|HAMAP-Rule:MF_03182};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_03182}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_03182};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03182};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP-
KW   Rule:MF_03182};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03182};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246702};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT   DOMAIN          483..821
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1134..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         873
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT   BINDING         875
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT   BINDING         982
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT   BINDING         1041
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
SQ   SEQUENCE   1155 AA;  128858 MW;  E347EC383615BADB CRC64;
     MEADWDELSR IPVPAPSVHA MPTIATAIAF DDVMELLWAG NEYGRITSFC GPELQRYTSV
     RAHPATEAVR QIIFHERGVI SLSPKSVHMI TRRGLTQWHI AHEEMTDLRC MSFTAQTNRI
     IVAGCQKVMF TIDIDKGVIV DKLGTEYNYT MMKKSRYLCA ATDTGSVNAL SLNDFSVVKS
     WKAHGTAVND MDARNDLLVT CGFSVRHLGA PIVDPLANVY DLKTLSPLPP IPFHAGAAYV
     RMHPKLHTTS FVASQTGQLQ VVDLMNPNAI NLRQANVSFM LGIDLSPSGE ALAINDAECA
     IHLWGSPAKV HFNELSKEAE FADVAPRPPT FDWSADTPLS MVGMPYYHER LFSAWPSHLV
     FEVGSPPAQV DQALIPYLRP AEMGHHAPNP KKTRRYQVEN TRALASAEPA LIAPKFLSEK
     AREQNKAKSE GAIIDAVEAL AGAKINGETE DDPLLKYSNV EIKYSRFGVD DFDFRFYNQT
     TFSGLETHIA NSFTNALLQL FKFIPYIRNV ALQHAASSCI FENCLLCEMG YLFDMLEKAN
     GQNCQATNLL KTFSSYREAS NLGLFEENLT NKSLSAAIQA VNRFFLGQIS HDFRMISPSS
     DDLDHKLATV ASESIRCMFC QNEIVRPGNS LVNELNYPAI DIKQARRNPA FRFSNILRSS
     IERETQNRGW CNYCRRYQQV AIRKSVHRMP HVLILNAALS NPLCRRLWAI PGWLPEEVGI
     AIDGGQISCF EGEELKMRIQ AKMPGLVIYE LVGLVCEIDI PEHQKAHLVS FINVSISSRE
     PETKNKWHLF NDFLVTEVDK DEALRFNQPW KLPCVVAFQV RDGRHAMDDT WKSALDTTLL
     FRDWSLNGGR PVESRATLTE DEKPTPGTPV ALDTEFVDLE KAEIDVKADG SQEIVRPSKS
     GLARVSVLRG SGLREGVPFI DDYITIKETI VDYVTQYSGI KPGDLDPRTS QHNLVPLKVA
     YKKLWLLLNL GCVFVGHGLA SDFRKVNIQV PKSQTVDTQY LFFHPGKNRR LSLRYLAWAV
     FKEYIQEEPA EDNQGHDSIE DARMALRLWK KFKEYKDAGI VSQMLEEIFR EGSKLGFRPP
     PRNGIPTVLS RPGTAVTMQN NSGRNTPSTA DVAGAAASAP ATPRQAFRRS IALTPSNGSF
     AGPGAGDFFS GSPLK
//
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