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PAN2_CHAGB
ID   PAN2_CHAGB              Reviewed;        1102 AA.
AC   Q2GSV2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
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=CHGG_08952;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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: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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAQ84938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAQ84938.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CH408034; EAQ84938.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001226879.1; XM_001226878.1.
DR   AlphaFoldDB; Q2GSV2; -.
DR   SMR; Q2GSV2; -.
DR   STRING; 38033.XP_001226879.1; -.
DR   EnsemblFungi; EAQ84938; EAQ84938; CHGG_08952.
DR   GeneID; 4395014; -.
DR   eggNOG; KOG1275; Eukaryota.
DR   HOGENOM; CLU_002369_1_0_1; -.
DR   InParanoid; Q2GSV2; -.
DR   OrthoDB; 128953at2759; -.
DR   Proteomes; UP000001056; 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..1102
FT                   /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT                   PAN2"
FT                   /id="PRO_0000295342"
FT   REPEAT          20..59
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REPEAT          104..144
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REPEAT          269..308
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   DOMAIN          446..833
FT                   /note="USP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   DOMAIN          881..1054
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REGION          308..445
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REGION          423..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         884
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         886
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         993
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         1046
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   1102 AA;  123849 MW;  7120EABD2C771F76 CRC64;
     MDADWDEVTR IAFPAPGSND YPRPATALAF DTIAELLWAG NDRGRVVSFY GRDLQRYTAF
     KIHPPSEGPV RQFLFHDKGV IALGTRSVHM AMRRGPTLWN IRHDEMENLQ CMSFTSKGAS
     EIIVAGFQDT MFVIDVVKGE IVKQKSKYIC AATRTGCVDL LDPITFKTVR SWQAHASYIN
     DMDAQNDFIV TCGGSLKQQA AQTYMLDPYV NVFDLKNMTS MKPMPFPPLA AHVRLHPRML
     TTSIVTSQHG QMHVVDIMNP NTSNVRYANV MSFINLFEIA PSGEALAMAD TECNIHLWGS
     PSKIHFTDMA IPIEMPKAEE PAPMLDWSPD TPLSSIGMPY YREQLFSAWP SDIISDIGAP
     PVQLDPSFLA SLKQMEWGFY GRNSRGLRRN QVEDTRACMK PSMQPPKFLS EKARESAMSY
     SAAVPDPKVE QVPESSTDEL ESLKPEAPPI YRNLEIKYSK FGVDDFDFGY YNKTQYAGLE
     NHIPNSYANS LLQLIHYTPL LRNMALQHAA TACVTDLCLL CELGFVFDML QKAEGSTCQA
     TNMFKALGAT PQAAPLGLLE EETHVPSLST MSQGLSRFLF DRINHDYRSI NPISTTLEQT
     LFNLPQPPTP DELVSRVLAT SAVVTIKCMN CRSETTRPGT AQVNDLMYPP PKGSARGGRM
     HKTTFSQVLK TGVERETASK GWCSRCQRYQ NLQMRKTIHS VPAVLAINSA ISSQEHRKLW
     ATPGWLPEEI GIIVDQGQFF CFEGEDLKLH LQRGMHNITV YSLIGMVVNI ESSSPQKTHL
     VSVINVAHAD AAPSAESKWH LFNDFSVRPI STAEALTFNA AWKLPAVLLF QVKAANNKTN
     MDWKTKLDTS LLYQDLTPHS DEKTYHVLDL EAEPPGPDTI VGLDTEFVSL KQPEIQMNSD
     GERETIRPMS HALARVSVVR GQGEHEGEAF IDDYIAIREP VVDYLTLYSG ITPGDLDPRT
     TKHNLVSLKV AYKKLWVLLN LGCKFLGHGL RQDFRVINIQ VPRAQVIDTI QVFYLKARLR
     KLSLAFLAWF LLKEDIQLET HDSIEDARTA LKLYRKYLEF EDAGILEAML EDIYKVGRAT
     NFKPPRKDDQ VIQRTDTPFL SR
 
 
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