PAN3_MAGO7
ID PAN3_MAGO7 Reviewed; 680 AA.
AC Q2KFH6; A4RBC4; G4NLE2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=PAN2-PAN3 deadenylation complex subunit PAN3 {ECO:0000255|HAMAP-Rule:MF_03181};
DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000255|HAMAP-Rule:MF_03181};
DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
DE Short=PAN deadenylation complex subunit 3 {ECO:0000255|HAMAP-Rule:MF_03181};
GN Name=PAN3 {ECO:0000255|HAMAP-Rule:MF_03181};
GN ORFNames=MGCH7_ch7g710, MGG_02939;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN)
CC deadenylation complex, one of two cytoplasmic mRNA deadenylases
CC involved in mRNA turnover. PAN specifically shortens poly(A) tails of
CC RNA and the 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. PAN3
CC acts as a positive regulator for PAN activity, recruiting the catalytic
CC subunit PAN2 to mRNA via its interaction with RNA and with PAB1.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- SUBUNIT: Homodimer. Forms a heterotrimer with a catalytic subunit PAN2
CC to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts
CC (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain),
CC conferring substrate specificity of the enzyme complex.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- DOMAIN: The N-terminal zinc finger binds to poly(A) RNA.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
CC -!- DOMAIN: Contains a pseudokinase domain. The protein kinase domain is
CC predicted to be catalytically inactive because some of the residues
CC important for catalytic activity are substituted and it lacks the
CC equivalent of the binding site for a peptide substrate. However, it has
CC retained an ATP-binding site and ATP-binding is required for mRNA
CC degradation, stimulating the activity of the PAN2 nuclease in vitro.
CC The nucleotide-binding site is juxtaposed to the RNase active site of
CC PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA
CC rather than ATP, feeding the poly(A)-tail to the active site of the
CC deadenylase and thus increasing the efficiency with which this
CC distributive enzyme degrades oligo(A) RNAs. {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- DOMAIN: The pseudokinase domain, the coiled-coil (CC), and C-terminal
CC knob domain (CK) form a structural unit (PKC) that forms an extensive
CC high-affinity interaction surface for PAN2. {ECO:0000255|HAMAP-
CC Rule:MF_03181}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03181}.
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DR EMBL; CM000230; EAQ71303.1; -; Genomic_DNA.
DR EMBL; CM001237; EHA46026.1; -; Genomic_DNA.
DR RefSeq; XP_003720769.1; XM_003720721.1.
DR AlphaFoldDB; Q2KFH6; -.
DR SMR; Q2KFH6; -.
DR STRING; 318829.MGG_02939T0; -.
DR EnsemblFungi; MGG_02939T0; MGG_02939T0; MGG_02939.
DR GeneID; 2682492; -.
DR KEGG; mgr:MGG_02939; -.
DR VEuPathDB; FungiDB:MGG_02939; -.
DR eggNOG; KOG3741; Eukaryota.
DR HOGENOM; CLU_016423_1_0_1; -.
DR InParanoid; Q2KFH6; -.
DR OMA; IGPHSQN; -.
DR OrthoDB; 1515085at2759; -.
DR Proteomes; UP000009058; Chromosome 7.
DR GO; GO:0031251; C:PAN complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; 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 GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR HAMAP; MF_03181; PAN3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030844; PAN3.
DR InterPro; IPR041332; Pan3_PK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12272; PTHR12272; 1.
DR Pfam; PF18101; Pan3_PK; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; Metal-binding; mRNA processing;
KW Nucleotide-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..680
FT /note="PAN2-PAN3 deadenylation complex subunit PAN3"
FT /id="PRO_0000295371"
FT ZN_FING 25..54
FT /note="C3H1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..522
FT /note="Pseudokinase domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 562..680
FT /note="Knob domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT REGION 655..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 523..561
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT MOTIF 62..82
FT /note="PABPC-interacting motif-2 (PAM-2)"
FT /evidence="ECO:0000305"
FT COMPBIAS 63..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 360..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
FT BINDING 422..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03181"
SQ SEQUENCE 680 AA; 75267 MW; BDC97AFDBB9053CF CRC64;
MATTRYNSND FRRQLGSPRP KGRADTKDTL CRNILIYGHC RYEDAGCAFN HDQTKKSPKP
DATTRKTLNV DSAPFTPAVS SQPSKKTFSS SHAASAAVFT PRATAATPTG TPTAQETDIP
PAANTPSAFS NIAAIREFTP QQQNYDLTTN GAAAATQDAS LNYDPFTMSS VASALPAAQY
NPYASTDHTG LVAHGGAYFP SAQAGYQSLI PPSFHLYAPI GPYREDLQPW QRSTYDFFMP
ENLRLELQNK SHAALQTMTG TAALQMPQVG NYHTLVTLDK TSNRKSSSLF GYVTWVYKAV
SGKTSRLYSL RRLEGFTVSN DQILRPVKEW KKITNGNIVA MQDAFTTRAW GDSSLMFSFE
YYPLAETLME HHFPNAQHKT SFRSNTNHQA SETVLWSYIV QISNALNSIH SNGLAARCID
ATKIIITGKN HIRLSSCGIL DVINYEKSKP MTELQEEDFV AFGKLIVSLA TNTPPTGLNL
GKAIEQMGRN HSSTLKDMVL WLLNPPQASG QKTVKNLVAG INEHVMTAFD AQQRQSDMLY
SELYREVENG RVLRLLMKLA TINERTEYDK DAGWSENGDR YMLKLFRDYV FHQVDAQGRP
VLDPGHMLRC LSKLDVGTEE RIKLTSRDCE TDFLVTYKDL KGAVQSAFGE LLKGSGNGRG
GPVASGSGHG VHHPSHRDRF
