ID A0A1B9G654_9TREE Unreviewed; 1219 AA.
AC A0A1B9G654;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=I302_04201 {ECO:0000313|EMBL:OCF26515.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF26515.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF26515.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF26515.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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; KI894020; OCF26515.1; -; Genomic_DNA.
DR RefSeq; XP_019047585.1; XM_019190837.1.
DR AlphaFoldDB; A0A1B9G654; -.
DR STRING; 1296100.A0A1B9G654; -.
DR GeneID; 30208600; -.
DR VEuPathDB; FungiDB:I302_04201; -.
DR OrthoDB; 9810at2759; -.
DR Proteomes; UP000092730; 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 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; 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; 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_rpt.
DR PANTHER; PTHR15728; DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1.
DR PANTHER; PTHR15728:SF0; PAN2-PAN3 DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1.
DR Pfam; PF20770; PAN2_N; 1.
DR Pfam; PF13423; UCH_1; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 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:UP000092730};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 304..328
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 552..892
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 440..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 947
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 949
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 1056
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 1109
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 1219 AA; 134811 MW; B50E31ECB95BB6FD CRC64;
MTYNPLHLLT LPPTSIDPKP ISTSLTIDSF SDTLWLGTSS GSITALCTPL TLTRNVQFPA
HGSKLSSHPL GGYLNLPGGI NMSVRELRVT DRDVWSLTEG GVCGRKRGGV VKWSVDDPSR
SLRSMTPNPI NSHEVIAGGT GPLIIANTSR GGDIVRKVDI PNSPIVKLSP SLSSRSVLSA
SLSGQINLLD PRLGFRSVNT VVAVQAHTGG LNGADVQGNL VCTWGWTHMQ GHPLPDPLVK
IYDIRTLRPL PPISFPAGPA FALLHPTDPS KLVISSQQGM LQSVDMSSGA AGSMFQQLDV
NSYVTSMALS PRGDYLAFGD ADGNLHLWTD HDTGEGAQLD ENGQMILPTF NGYDGIKPEW
PDQAEALPPI VWEDTTPLSL IGMPYYSESL LSNFPPDLYA TDASPFFNPP TPIPTSVLNT
MKMVDFVGYA TTPKELKGKR YVIPSRPGAS GVHKNKNGND RTGGALSGRR NSEPRFRSEK
EKLEKKNKSS KRSKKNVDQD GMEVDDGDEQ VEDDNVQEQG EIPKYYRKVE IKYSKFGIED
FDFEYYNRTA YSGLETDILN SYTNSLLQAI HYIQPIRAVA TAHICVDCKK EHCLLCEAGF
LFRMLEDAKG RNCQASNFSR AFSATPQASA LGLMDDNEKS TAPYGSLIQN FNRWLLSTFS
TESIFEGETF DLRIKDIQDL SLQSSSSTPS AIDQVLGVEI KTTNTCRSCG FVSERDTTLH
AVDLIYPKKT TTQPKFNDVL KSSIFRESTT KAVCSNCKSF APLDSKRTLN SDRNQLPPVL
SVNAMMTSSD LFEVWKTDNG KSKERFLEPT VQFEMDGDGG GRIEYEVKSL VVQIQEDEGT
PAHLVSFVKM SNDSTSNWIM FNDFLVRSIS EKEVFNFPDQ WKVPSVIILQ RVDSSDLLDL
SGLPREVDKS VLFKDVSIAW NRRNALIKHK VLDEIELPKP GTLIAIDAEF VALQQEEMEF
RSDGTKNILR PSHMSLARVS VLRGEGEKEG IPFIDDYIHT SEAVVDYLTE FSGIKAGDLD
PNNSPHTLVP LKVAYKKLRL LVDLGCIFIG HGLSKDFRTI NIFIPPSQVM DTVNIFTIPG
RHRKLSLKFL AWFLLKKDIQ THTHDSIEDS KFALLLYKLW REYEDRGDED GFEGLMNDVF
TEGFKTNFKP PTDRPPSPNA FPPLRAPQIT GKQPKSRKGS NKNNNNNNNQ SNWNSESGGS
TSGSAGGGGR GRGKSSRQW
//
