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PAN2_CRYNB
ID   PAN2_CRYNB              Reviewed;        1183 AA.
AC   P0CQ09; Q55UG2; Q5KHY2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
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}; OrderedLocusNames=CNBD1450;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
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DR   EMBL; AAEY01000019; EAL21450.1; -; Genomic_DNA.
DR   RefSeq; XP_776097.1; XM_771004.1.
DR   AlphaFoldDB; P0CQ09; -.
DR   SMR; P0CQ09; -.
DR   PRIDE; P0CQ09; -.
DR   EnsemblFungi; AAW43174; AAW43174; CND04900.
DR   EnsemblFungi; EAL21450; EAL21450; CNBD1450.
DR   GeneID; 4935534; -.
DR   KEGG; cnb:CNBD1450; -.
DR   VEuPathDB; FungiDB:CNBD1450; -.
DR   HOGENOM; CLU_002369_1_0_1; -.
DR   Proteomes; UP000001435; Chromosome 4.
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; 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   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50998; SSF50998; 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; Repeat; WD repeat.
FT   CHAIN           1..1183
FT                   /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT                   PAN2"
FT                   /id="PRO_0000410214"
FT   REPEAT          150..189
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REPEAT          289..328
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   DOMAIN          479..864
FT                   /note="USP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   DOMAIN          916..1085
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REGION          331..478
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REGION          439..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1169..1183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         919
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         921
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         1028
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         1081
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   1183 AA;  130525 MW;  CDBABDC093D24627 CRC64;
     MNYNPLHLLP LPPTALDPKP IPTSLTLDPF SDVLWVGASS GIVSALCSPL TLARNVHFPA
     HGCKIGGGGF SAQGVSAVRE VRVTDRDVWT LTEGGIGGRK RGGAPKWIVS DVTRSLRTMS
     PNPTNSHELI TGGSGSLLLA NTARGEVVRS IENSSPVVKL APLHRTVLAA GLSGQVTVLD
     PRTGFKAAQN ISPVQAHTGG LSGADVQGNI VATWGWTHMQ GHPLPDPLIR LYDVRALRPL
     PPISFSSGPA FVLLHPSSSS HIVVSSQQGM LQTIDMSLGP SATVFQQLDV SSYITSMALS
     SRGDYLAFGD GDGQLHVWTT NETGENAAVD ENGSIVLPPF NGYDGVKPEW PDQVDPLPTI
     AWEESTPLNL VGMPYYNEAL LSQFPSECYA TSTSPLFNPP ATIPQPVLSS MKMVDFVGYA
     PNPKELRGKR YVLRAVPGAE GRARGKGRRD SGPRFRSEKD KKGTYKDKEE IEEELNDGEV
     PKYYRKVEIK YSKFGIEDFD FEFYNRTNYS GLETDILNSY TNSLLQALHY TLPLRAIATA
     HICVDCKKEH CLLCEAGFLF RMLEDAKGRN CQASNFSRAF SATSQAYALG LMDENTNSKS
     TAPYGSLIQN FNRWLLSTFS TESIVDGETF HLRPFPQKTS GLDGLSMNDG PSAIDQVLGV
     KIKTTNTCRH CGFVSSRDST LHVVDLVYPK KMNPRLSFSD ILRSSLIRDS TTKAICSSCK
     AFAPLDSRRS LSPSSGHPLP PVLSVNAMVT NSDVYGFWKD KKDVKEKDGV RRFLPKRVTI
     REVGKLENGQ EEGVKYSIRS MVVQIQESPD AVAHLVSFVK MPSKDGSSAW IMFNDFLVRP
     VSEDEVLSFP DQWKVPAVII LERENAEELL NLEVLPKELD REILFKDVSI AWNRKQDMIK
     HKILQREEMP KRGTLVAIDA EFVALQQEEM EFRSDGTKNI LRPSHMSLAR VSVLRGEGEM
     EGKPFIDDYI HTSEAVVDYL TEFSGIKAGD LDPNNSPHTL VPLKVAYKKL RLLVDLGCIF
     VGHGLSKDFR TINIFVPPEQ VMDTVLIYTL PGSQRKLSLR FLAWYLLHQD IQTNSHDSIE
     DAHFALLLCK LWMDYASESE EAFEIVMEDI FAEGKKLAFK PPSSAGNMMA EQQLSPVSFP
     PLSNGDQTVA RAVVKSRMAT PPPPTKLGLP QWASQNSPSP LRR
 
 
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