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PAN2_ASPOR
ID   PAN2_ASPOR              Reviewed;        1155 AA.
AC   Q2ULU6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=AO090003000263;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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: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; AP007155; BAE57469.1; -; Genomic_DNA.
DR   RefSeq; XP_001819471.1; XM_001819419.2.
DR   AlphaFoldDB; Q2ULU6; -.
DR   SMR; Q2ULU6; -.
DR   STRING; 510516.Q2ULU6; -.
DR   EnsemblFungi; BAE57469; BAE57469; AO090003000263.
DR   GeneID; 5991454; -.
DR   KEGG; aor:AO090003000263; -.
DR   VEuPathDB; FungiDB:AO090003000263; -.
DR   HOGENOM; CLU_002369_1_0_1; -.
DR   OMA; TQELLWT; -.
DR   Proteomes; UP000006564; Chromosome 2.
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   Pfam; PF00929; RNase_T; 1.
DR   Pfam; PF13423; UCH_1; 1.
DR   SMART; SM00479; EXOIII; 1.
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; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..1155
FT                   /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT                   pan2"
FT                   /id="PRO_0000295338"
FT   REPEAT          102..145
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   REGION          316..452
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REGION          1095..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1095..1142
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   1155 AA;  129302 MW;  5D1090DD313F64B7 CRC64;
     MEADWDELSR IQVPPPSPHG MPTIATAIAF DDVMELLWVG NEYGRITSFC GPELQRYTSV
     RAHPVSEGPV RQILFHDRGV ISLSSKSVHM ITRRGLTQWH ITHEDMTDLR CMSFTAQLNK
     VIVAGCQKAM FTIDIDKGHI VDKLPTEYNY TMMKKSRYLC AATDTGSVNA LSLTDFRVVK
     SWKAHGTAVN DMDARNDLLV TCGFSVRHLG SPIVDPLANV YDLKTLSPLP PIPFHAGAAY
     VRMHPKLHTT SFVASQTGQL QVVDLMNPNA INLRQANVSF MLGIDLSPSG EALAINDAEC
     AIHLWGSPSK VHFNEMSKEV EFADVPARPP PLDWSPDTPL SMIGMPYYHE RLFSAWPSHL
     VFEIGSPPAP IDQALIPYLR PAEIGHYAPN PKKTRRNQVE NTRALANSEP ALIAPKFLSE
     KAREQSKAKS DGLVTDAAET LAGTKLNGEA EDDPLLKYSN VEIKYSRFGV DDFDFRFYNQ
     TKFSGLETHI ANSFTNALLQ LFKFIPLIRN VALQHAASAC IFENCLLCEM GYLFDMLEKA
     DGQNCQATNL LKTFGSFREA SSLGLLEENL TNKSLSTSIQ SVNRFFLGQI SHDFRMILPS
     SDDLDHKLAT VASESIRCMF CQKEIVRPGN SLVNELIYPA IDIKQIRRNP AYRFSNILRA
     SIERETQNRG WCNYCRRYQQ VAIRKTVHRM PLVMMLNTAL NNPIYRRLWA IPGWLPEAVG
     LVVDAGQILC FEGEDLRMRM QNNMPGLVVY ELVGVVSEID IPEHQKAHLV SFINVSISSR
     EPETTNKWHL FNDFLVTEVD KDEALRFNQP WKVPCVLAYQ VKDARHAMDD NWKNVLDTTL
     LYRDWSLNGG RSVESLATLS EEEKPTPGTP VALDTEFVDL EKAEIDVKAD GSQEIVRPSK
     SGLARVSVLR GSGTREGVPF IDDYITIKET IVDYVTQYSG IKPGDLDPRT SQHNLVPLKV
     AYKKLWLLLN LGCVFVGHGL ASDFRKINIQ VPKCQTVDTQ YLFFHPGKNR RLSLRYLAWA
     VFKEYIQEEP TDNNQGHDSI EDARMALRLW KKFQEYEDAG VVSQILEELF REGSKLGFRP
     PARNGATAVL SRPGTAVTMQ NNSGRNTPST PEVTAPTASA PTTPRQGFRR SVALTPSNGS
     FAPGTGDFFG GSPLK
 
 
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