ID A0A0K6G8U5_9AGAM Unreviewed; 1749 AA.
AC A0A0K6G8U5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ORFNames=RSOLAG22IIIB_01533 {ECO:0000313|EMBL:CUA74901.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA74901.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA74901.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA74901.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
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DR EMBL; CYGV01001511; CUA74901.1; -; Genomic_DNA.
DR Proteomes; UP000044841; 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:0006270; P:DNA replication initiation; IEA:InterPro.
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 CDD; cd06143; PAN2_exo; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03182; PAN2; 1.
DR InterPro; IPR003874; CDC45.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR030843; PAN2.
DR InterPro; IPR048841; PAN2_N.
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 PANTHER; PTHR15728; DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1.
DR PANTHER; PTHR15728:SF0; PAN2-PAN3 DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1.
DR Pfam; PF02724; CDC45; 1.
DR Pfam; PF20770; PAN2_N; 1.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF101908; Putative isomerase YbhE; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW 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:UP000044841};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 152..165
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 481..809
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1248..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 864
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT BINDING 866
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT BINDING 969
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
FT BINDING 1022
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182"
SQ SEQUENCE 1749 AA; 193623 MW; 1A7BF87213768774 CRC64;
MDSSQTQPKS TYYALPSLHL THPVPVSALS FDPVSDVLWT GSAAGLVTGY FGNVTVNGYA
GSLTRGVTFP VRGETGVLKI LTGEKDIKAL GSGGFGSWTK GGAGRWQFIP QEHLSTFTPH
PTIPNTFVVA VQSPGSGFHI VNAISGASLR RVSSPFNVSH LAHVGTLLVS GTVDGMLRTH
DFRTRGREDT AAESSCIAHT GGIQALEAAG NYIFTAGWGI RQSHPHAEHF VKVFDMRTLR
PLSPIPFADL PSFIKVHPKK PTTLVVASSQ GFVNVIDVAQ PGGTPDFVPT ISPEGDYVAL
GDAEGFVHLL SSVPENTTEP VPFNGFEGEP VVWAHKPDLP DIHWTVETPL STIGLPYYKT
ALLSSQVPLA VPHGIQAYPP PAKIPPKVLD TMRTVDFVGY AQLPKDLVGR RNVAPTSQVE
SGRFRSTRTT RKASDVDAVT EHFGDTSISE IPRHYRRVEI MYSKFGVEDF DFAYYNKTVY
SGLETHIVNS YTNALLQALH YVHSVRRVAQ SHITTPCQTE HCLLCEFGFL TRMLEDAKGV
NCQASNFCKT IPKIQQAGAL GVVDYQAEGP KRDYGAIIQV FNRFLLEEMS VRSDVPDGNP
WLTRVAENET AANGANKSTI TQLMGIDAQS IVMCSACGAT TEKDTLSHVV DLTFRKPQSN
ITFSSLLSAS ILRETTHRSV CQSCKQQATF RTQRIVPANA LPPVLAVNTA ILTDEAGSIW
RTKGQNFLTP DVTVACGRDG NEMVEYELRS MVVEVKNETH APHLVALTKI PRDGWYLFND
FVVQSVTEAE ALSFAGTWKT PCVLYLERTD NASTLDFSML PMKMDPAILC NIDNISWRMN
KAKLAHEPLT PDELPTPGTL VAIDAEFVSL QKEENEMRSD GTKKVIRPSQ LCLARVSVLR
EDGKAFIDDY IHTSDTIVDY LTEFSGIKPG DLDPYSSEHA LVPLKTAYKK LRLLIDLGCI
FIGHGLSKDF RIINITVPKE QVIDTVDIYF LKERQRRIGL RFLSWYLLRQ TIQIDTHNSI
EDARAALFLY NLHVQLETEG QFEDTLEEIY REGRKLNWKT PGDPTSPKPA KAQVAAMSPS
ISGTFTPPYG SPSTGGGHTK GIYPIDLNHI LHAKSASSIV IISSPDVDAL CATRILVTMF
RNENVLHRVT PISGYPDLTE YREELLKSPE LQTIILVNIG AILDLLSEEW FADFPKDVAI
HVIDSTRPQN LSNLFTPGRE GERVCVWDNG EALKLEKQKE AYETFLYAVD SSSDESDDDD
EDDEELEEME EDGFEDGENS DNDRPRQRRK LNTGKPSAKQ RREQRHIRER HRQIIEIIAL
EQVMLAVNET LWLAIIGLTY QYTSSRISRD DYDYWQVVYA DEVARLNPRI DLSASTALHA
DDTGIRSCQE LRFTLYRHWT LYDSMFHSPY VAGKMNIWKE RGRRNLAAMF AKMGISLQEG
QQDYSHMDRN FRKELPDLLE TIGPEYGLVE LQYPSFVRAY GFSAQPFAAA DCVEAISALL
DAGTGVRLEV EVDGGRGGGE WFGGARIWNA GDGTSKSKSS TTTGGAGKEN LGIDGPSDTK
NEEDEKNKAW RKKFWLAYDA LGSDADSTRA LQRAIPLAKS LHQIILSQGS ELIERSGAIK
TYRKFRMAIL TQGAHLALFS QPGPLSRLAL WLVDALRDKV VSVKGPRGRE TLPFVVACLN
ERAGSYLVVG VTGAVEFGDV RHNLFGLAFL KAKGESNART RHGTFDTSVV EVNMDDLQLF
TEALAMHAS
//
