ID   A0A427XKL8_9TREE        Unreviewed;      1265 AA.
AC   A0A427XKL8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   19-JAN-2022, entry version 11.
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; Tremellomycetes;
OC   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) 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:RSH79396.1}.
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DR   EMBL; RSCE01000010; RSH79396.1; -; Genomic_DNA.
DR   STRING; 105984.A0A427XKL8; -.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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|HAMAP-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:UP000279236};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          298..322
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          519..870
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          445..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1152..1173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1181..1211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           925
FT                   /note="Divalent metal cation; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT   METAL           927
FT                   /note="Divalent metal cation; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT   METAL           1034
FT                   /note="Divalent metal cation; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT   METAL           1087
FT                   /note="Divalent metal cation; catalytic"
FT                   /evidence="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
//