PAN2_PHANO
ID PAN2_PHANO Reviewed; 1129 AA.
AC Q0UPL5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=SNOG_06299;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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: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 -!- SEQUENCE CAUTION:
CC Sequence=EAT86130.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445333; EAT86130.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001796676.1; XM_001796624.1.
DR AlphaFoldDB; Q0UPL5; -.
DR SMR; Q0UPL5; -.
DR STRING; 13684.SNOT_06299; -.
DR GeneID; 5973555; -.
DR KEGG; pno:SNOG_06299; -.
DR eggNOG; KOG1275; Eukaryota.
DR InParanoid; Q0UPL5; -.
DR OMA; TQELLWT; -.
DR OrthoDB; 128953at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0031251; C:PAN complex; IBA:GO_Central.
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; IBA:GO_Central.
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..1129
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT PAN2"
FT /id="PRO_0000295352"
FT REPEAT 20..60
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 104..146
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 148..183
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 186..226
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 280..319
FT /note="WD 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 458..830
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 880..1052
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 320..457
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 396..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 883
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 885
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 992
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 1045
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 1129 AA; 126472 MW; 8AB531580BE94E65 CRC64;
MEADWNELVT AQLSPPGSHP PAVPISTFAF DTTQELLWTG NNQGRVTSLY GPSLERYTSY
RGHATSDGPV KQFLFTDKGV LSISRQSVHY SHRRGLTQWH LTSPDFKDLK CMNFTSKGTR
EILIAGCQEQ MFKVDVEKGI VVDTLPVDAQ YTIMKRAGQY LCAATKTGGI HILDSNSLSV
IKVFEGHTGS ISDMDAKGDF LATCGWSPRQ QYAYMLDPFT NVFSLKTLKQ LAPVPFHTGA
AFVRMHPRMS TTAIIASQNG QMQVIDLMNP DSANLRQLNL YDSYLAGFEM APSGEAFALA
DSNSNVHLWG SPAKVHFPEY SNPTEFADHV IPPASMDWSL DTPLNTIGMP YYKETLLSGW
PSHMVFEVGA PPPKIDGAIL SNMTRTDMGF FAKNPRTKRR NQIEVTRQTD RSSDSLTPPK
FLSEKSRASL SLSEANAKAV ETMETLTDLH LDDVTRKDVP AMYGNVEIKY SKFGVDDFDF
AYYNQTPFSG LETHITNSYA NSLLQLFRFT PLIRNLALQH TASPCLFESC LLCELGFLID
MLEKAAGLNC QASNFLKTFS GLSNAVSLNL LEEFAPNVAL TSMIQNLNRF LLDKISEEFR
QMLPSHGGTS LMDQVLETQA RASMRCAQCA NETIRGGKNF VNELVYPAKH VMKNTRIPRP
TFSQILKASV ERQDQTRGWC TKCNRYQQMV QRKTIQSVPG VLMLNAAIQT HEAKLLWSIP
NWLPHEIGII VDQGQFYCFE GQDLKLHLQR GVFDIMVYEL VGVVADINSG EHQKPHLVAT
INTGPSSREP DAEDKWHLFN DFLVRPIPRE EALRFEPSWK LPSVLTFQTK SARNKIDDSW
KENLDTSILY RWWSSNPTPP DDKFKLLQVS TEAPRPGYPV AIDAEFIRLQ AEEIEMKADG
TRQTIRPDRK GLARVSVCRG EGEHAGLPFI DDYIAVTEQV VDYLTEWSGI SPGDLNRETS
PHAPVSLKHA YKKLWLLLNL GCVFVGHSLA NDFRTINIHV PRSQVVDTSN LFFLPDFKRK
LNLKFLAWCV LKEQIQQDTH DSIEDATTAL KLWRKYEEFV DAGVLEPMLN DIYATGSQVK
FKAPGSGNRN SMPAGMTATG AGRDTPEPMT TPKKGGAFGG VGFRSPMRR
