PAN2_PICGU
ID PAN2_PICGU Reviewed; 1098 AA.
AC A5DAD0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 79.
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=PGUG_00235;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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=EDK36137.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH408155; EDK36137.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001486858.1; XM_001486808.1.
DR AlphaFoldDB; A5DAD0; -.
DR SMR; A5DAD0; -.
DR STRING; 4929.XP_001486858.1; -.
DR PRIDE; A5DAD0; -.
DR EnsemblFungi; EDK36137; EDK36137; PGUG_00235.
DR GeneID; 5129459; -.
DR KEGG; pgu:PGUG_00235; -.
DR eggNOG; KOG1275; Eukaryota.
DR HOGENOM; CLU_002369_1_0_1; -.
DR InParanoid; A5DAD0; -.
DR OrthoDB; 128953at2759; -.
DR Proteomes; UP000001997; 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; IPR001680; WD40_repeat.
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 SMART; SM00320; WD40; 5.
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..1098
FT /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT PAN2"
FT /id="PRO_0000295353"
FT REPEAT 19..58
FT /note="WD 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 150..190
FT /note="WD 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 253..293
FT /note="WD 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REPEAT 300..338
FT /note="WD 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 466..839
FT /note="USP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT DOMAIN 894..1067
FT /note="Exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 340..466
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT REGION 417..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 897
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 899
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 1006
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 1059
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 1098 AA; 123106 MW; 4D01CA09F572FD77 CRC64;
MEGWEEVSIL AAILYSFPAS KDPVTSLLFD SVHNLLWCGD SSGSARSFTP NAGYPFQLYP
YTKFPATTSP LPVVQQRNHS RGILSLSQNC VNLNSRRGLS QATFTAASVT DSANVLRNLS
CMTTLGTGND IIVGGTHSLG SLDMQKCVAT GFDHSGNLSF VDSVAKTLVL GTTDGTVELF
DTASNSSVKS FPAHSGLLSD MAVQGNYIAT CGYSARRRYD HKNSSAAGGT SYITDPLVHL
IDTRMMKSLS PIPFPNGASF VRFHPKLPNI VIVASSTGVL EFVDIFDQSK LNVYQVNMSP
ASPGISRMEI SDNGEYICCS EGRSLHLWSF TSDTNFVNFP APLEEQDIPA PLPPPFEVDD
PVPLSSVGMP YYKDYLLSNY ATDMVFTKEL SKVPAEVDTS LGHGAFVPYD RTAHGPRNIS
QPYQSLREPP GSNSNAPRFI SERDGESNEN MIHAENSIFH LKSPTSVPHC YSRLQIQYSK
FGVDDFDFDY YNKSNGACSG LENHLDNSYT NALLQLYRAA PAFYNSVVES LLPEYLPNGP
EIISWNPQGS SLLIELGYLF DMMHKAEGRN VKIANFSQLL TQSASAASAG VINTDEEKSL
NADGLREIII RFNHYLLSEL TSNQRERRHT NSEKIEDIMG IKLEMQIKSQ CTETETHTGS
QLIFDLTSPP EQYLNKLAML RRAEKTEITI LSYMDYFMDQ YKSASCRECE ARGRPHAVNA
RQRVVRLPKV LSINLSMTNF ELQQIHNCRG WLVPEFHIGE DERFVDAGRG RKYELLGYVC
EISHGPGVKR GAHNLVSFVK IKGQWYLFND FLVMPIAQEE ALNLSYSWKK PVIIVYSEPG
QDFSYFETST FKKIQDLDTS IIYRDHFVRA AREGHRQEYK LLTKQEAPEI GTLIAIDAEF
VVSEPEQLEI RYTGTRKLIK PKKLTLARVS VLRGNGPNIG VPFIDDYIVW TGHIEDYLTS
FSGIEPGDLD PEVSKKALVT LQTVYRKLWL LLNMGCVFVG HGLQNDFRCI NLVVPKTQVR
DTADLFYLPE FKRKLSLKFL AYVLLKEKVQ TGNHDSVEDA YTALMLFQKH EELTRTGDLE
TVLYQVYMEG QQRRFRAP
