ID   A0A427XKL8_9TREE        Unreviewed;      1265 AA.
AC   A0A427XKL8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   31-JUL-2019, entry version 4.
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   ECO:0000313|EMBL:RSH79396.1};
GN   ORFNames=EHS24_001442 {ECO:0000313|EMBL:RSH79396.1};
OS   Apiotrichum porosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Trichosporonales; Trichosporonaceae; Apiotrichum.
OX   NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH79396.1, ECO:0000313|Proteomes:UP000279236};
RN   [1] {ECO:0000313|EMBL:RSH79396.1, ECO:0000313|Proteomes:UP000279236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH79396.1,
RC   ECO:0000313|Proteomes:UP000279236};
RA   Aliyu H., Gorte O., Ochsenreither K.;
RT   "Genome sequence of Apiotrichum porosum DSM 27194.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN)
CC       deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC       involved in mRNA turnover. PAN specifically shortens poly(A) tails
CC       of RNA and the activity is stimulated by poly(A)-binding protein
CC       PAB1. PAN deadenylation is followed by rapid degradation of the
CC       shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs
CC       are then degraded by two alternative mechanisms, namely exosome-
CC       mediated 3'-5' exonucleolytic degradation, or deadenlyation-
CC       dependent mRNA decaping and subsequent 5'-3' exonucleolytic
CC       degradation by XRN1. May also be involved in post-transcriptional
CC       maturation of mRNA poly(A) tails. {ECO:0000256|HAMAP-
CC       Rule:MF_03182}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.;
CC         EC=3.1.13.4; 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
CC       exonuclease domain. {ECO:0000256|HAMAP-Rule:MF_03182};
CC   -!- ACTIVITY REGULATION: Positively regulated by the regulatory
CC       subunit 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
CC       domain is predicted to be catalytically inactive because it lacks
CC       the active site catalytic triad characteristic of thiol proteases,
CC       with residues at the equivalent structural positions that are
CC       incompatible with catalysis, and it cannot bind ubiquitin. It
CC       functions as a structural scaffold for intra- and intermolecular
CC       interactions in the complex. {ECO:0000256|HAMAP-Rule:MF_03182}.
CC   -!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the
CC       WD40 repeats and the pseudo-UCH domain mediates interaction with
CC       PAN3. {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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03182}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:RSH79396.1}.
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DR   EMBL; RSCE01000010; RSH79396.1; -; Genomic_DNA.
DR   Proteomes; UP000279236; 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_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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; IPR001680; WD40_repeat.
DR   Pfam; PF00929; RNase_T; 1.
DR   Pfam; PF13423; UCH_1; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000279236};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03182};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_03182};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03182};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03182};
KW   mRNA processing {ECO:0000256|HAMAP-Rule:MF_03182};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_03182};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279236};
KW   WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   REPEAT      298    322       WD. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00221}.
FT   DOMAIN      519    870       USP. {ECO:0000259|PROSITE:PS50235}.
FT   REGION      445    487       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1136   1265       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    451    487       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1152   1173       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS   1181   1211       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS   1218   1234       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   METAL       925    925       Divalent metal cation; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_03182}.
FT   METAL       927    927       Divalent metal cation; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_03182}.
FT   METAL      1034   1034       Divalent metal cation; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_03182}.
FT   METAL      1087   1087       Divalent metal cation; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_03182}.
SQ   SEQUENCE   1265 AA;  138984 MW;  5FCD4D802CCD7EE1 CRC64;
     MGSYNPLSLF PLPPQVSDPK PVPSVLAVDG FADMLWVGSA AGLVSAFASP LTLTRNVQFP
     AHGAAPHLSQ QREFQALPGL HGGVRQLRVN DREVWTLTDG GMGGRRRGGA PRWFVSDPTR
     SLRAMTPSPT NSHEVLAGGT GQMMLVNNSR GEVVRRFESP STVVHLGTMQ RTVVCGSGSG
     QVSLLDPRTG FRPAANITPV QAHTGGMSGA DSQNNIIATW GWTHMQGHPI PDPLVKLYDT
     RTLRPLPPIS FSSGPAFVML NPLEPSKLVI AGQQGMVQVA DISTGTNEFQ QLDVSSFITS
     MALSPRGDYL AFGDGDGQLH LWTQHPTGEG AQLDDHGNLA LPPFNGFEGI KPEWPDPVDP
     PPPIVWDDST PLNIIGMPHY EDPLLSNFSP ADYATIYSPF FNPPEPIPTS VLSSLNYQDF
     VGYGQLPKEL KGKRNLVTAR PGAGKHALRH GAIGSRRESE PRFRSEKDRH KGRHNPPPEI
     DEETPAGEVP KYYRKVEIKY SRFGVEDFDF GYYNRTQYSG LETDILNSYT NALLQALHYA
     APVRAVAKAH ICVDCQKENC LLCEAGFLFR MLEDAKGTNC QASNFSRAFS ATPQASALGL
     MDGSNDKAMV APSTLIQNFN RWVLSTFTTE AVVEGQNFSM RPPSMEAMSL SSPVSAINQV
     LGVSVKTTNT CLSCKYVSGR ESTLQAIDLL WPRKPSDATS FPETLRSAII RNSTTKATCS
     NCKSFAPLDS RRDLASNPMY SLPPVLSINA SVSSPEHLEI WKDRPEAGGK TKHYLSRRVA
     FRQGPQGEIV ADDSNEGIVY EVRSVVVQVQ TSPENPAHLV TFSRMPQLED EDEPKWIMFN
     DFLVRPVKEE EVFSFPDTWK VPAVIVLERA DCPLVVDYTR LPQELDHNVL FKDHSMAWHR
     RASEIHHQVL SPDELPKPGT LISIDAEFVA LQNEELEFRS DGTKKILRPT LMSLARVSVL
     RGPGQLEAVP FIDDYIRTTE NVSDYLTEFS GIKAGDLDPN NSIHTLVPLK VAYKKLRLLV
     DLGCIFIGHG LSKDFRTINI FVPPEQVLDT VNIYTIPGRS RKLSLRFLTW FVLKRDIQTK
     EHDSIEDARH AYLLYKEYKA FDAEGCFDDV MEDIFAEGHK TGFKPKNEAG AIIDTSSQSR
     PMTPSAFPPL QSPPQSHSLS TLGLGQGQAQ GQGQGHAHPA APASITSTAS VDGGSSMTMS
     PPPQTYSLAA HTHGAAQHAQ HAAQQQQQNM HFARRKPQQG PPSPSPAARS QWGLPPAFVP
     GQKRW
//