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PAN2_NEOFI
ID   PAN2_NEOFI              Reviewed;        1161 AA.
AC   A1DFN6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=NFIA_081370;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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:0000250, 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; DS027696; EAW18193.1; -; Genomic_DNA.
DR   RefSeq; XP_001260090.1; XM_001260089.1.
DR   AlphaFoldDB; A1DFN6; -.
DR   SMR; A1DFN6; -.
DR   STRING; 36630.CADNFIAP00006624; -.
DR   PRIDE; A1DFN6; -.
DR   EnsemblFungi; EAW18193; EAW18193; NFIA_081370.
DR   GeneID; 4586646; -.
DR   KEGG; nfi:NFIA_081370; -.
DR   VEuPathDB; FungiDB:NFIA_081370; -.
DR   eggNOG; KOG1275; Eukaryota.
DR   HOGENOM; CLU_002369_1_0_1; -.
DR   OMA; TQELLWT; -.
DR   OrthoDB; 128953at2759; -.
DR   Proteomes; UP000006702; 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; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00929; RNase_T; 1.
DR   Pfam; PF13423; UCH_1; 1.
DR   SMART; SM00479; EXOIII; 1.
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..1161
FT                   /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT                   pan2"
FT                   /id="PRO_0000295350"
FT   REPEAT          20..59
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REPEAT          276..315
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   DOMAIN          453..822
FT                   /note="USP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   DOMAIN          871..1049
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REPEAT          1009..1060
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REGION          316..452
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REGION          1092..1161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1092..1143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         874
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         876
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         983
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         1042
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   1161 AA;  129833 MW;  B2E1FEFD4AF29BC7 CRC64;
     MEADWDELSR IPVPPPSPHG LPTAATTIAF DDVSELLWAG NEFGRITSFY GPELQRYTSV
     RAHPVSDGPV RQILFHERGV ISLSPKSVHM ITRRGLTQWH ISHEEMTDLY CMSLTAQLNK
     IIVAGCQRAM FTIDIDKGII VDKLHTDHNY TLMKKSRYLC AATDTGSVNA LSLTDFRVVK
     SWKSHGTAIN DMDARNDLLV TCGFSVRHLG SPIVDPLANV YDLKTLSPLP PIPFHAGAAY
     VRMHPKLSTT SFVASQTGQL QVVDLMNPNA INLRQANVSF MLGIDISPSG EALAINDAEC
     SIHLWGSPSK IHFNEMSKEV EFADVVPRPP PLDWSPDTPL NMIGMPYYRE RLLSAWPSHL
     VFEVGSPPAP IDQSLIPYLR PAEMGHYAPN PKKTRRYQVE NTRALTTAEP ALIAPKFLSE
     KAREQNKFKS EASVSDTAEA LAGAKLNGEA EDDPLLKYSN VEIKYSRFGV DDFDFRFYNQ
     TTFSGLETHI ANSFTNALLQ LLKFIPLVRN LALHHAASTC IYETCLLCEM GYLFDMLEKA
     NGQNCQATNL LRTFSSYREA SNLGLFEENL TTKSLSSAIQ SVNRFFLNQI AHDFRMIVPS
     SDDLDQRLST IASESIRCMF CQNEIVRPGN SLANELIYPA IDIKQARRNP AFRFSNILRA
     SIERETQNRG WCNYCRRYQQ VTIRKSIHRM PLVLILNAAL SNPICRRLWS IPGWLPEEVG
     IAVDNGQVMC FEGDELKTQL QNKLPNLVVY ELVGLVSEID IPEHQKPHLV SFINVSISSR
     ELEAKNRWHL FNDFLVTEVD KDEALRFNQP WKSPCILAYQ AKDARHAVDD SWKNVLDITL
     LFRDWSLNGG RAVETRQTLT EEEKPTPGTP VALDTEFVDL EKAEIDVKAD GSQEIVRPSK
     SGLARVSVLR GSGVHEGVPF IDDYITIKEP IVDYVTQYSG IKPGDLDPRT SQHNLVPLKV
     AYKKLWLLLN LGCVFVGHGL ASDFRKINIQ VPKSQTVDTQ YLYFHPGKNR RLSLRYLAWA
     VFKEYIQEEP ADNNQGHDSI EDARMALRLW KKFQEYEDAG IVNQILEEIF REGSKLGFRP
     PPRNGVATVL SRPGTAVTMQ NSSGRNTPST PDVGGAATAT ATTSAPATPR QAFRRSIALT
     PSNGTFGGPG AGDFFGGSPL K
 
 
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