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PAN2_CANGA
ID   PAN2_CANGA              Reviewed;        1093 AA.
AC   Q6FS70;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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};
GN   OrderedLocusNames=CAGL0H03025g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
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DR   EMBL; CR380954; CAG59857.1; -; Genomic_DNA.
DR   RefSeq; XP_446924.1; XM_446924.1.
DR   AlphaFoldDB; Q6FS70; -.
DR   SMR; Q6FS70; -.
DR   STRING; 5478.XP_446924.1; -.
DR   EnsemblFungi; CAG59857; CAG59857; CAGL0H03025g.
DR   GeneID; 2888907; -.
DR   KEGG; cgr:CAGL0H03025g; -.
DR   CGD; CAL0132004; CAGL0H03025g.
DR   VEuPathDB; FungiDB:CAGL0H03025g; -.
DR   eggNOG; KOG1275; Eukaryota.
DR   HOGENOM; CLU_002369_1_0_1; -.
DR   InParanoid; Q6FS70; -.
DR   OMA; TQELLWT; -.
DR   Proteomes; UP000002428; Chromosome H.
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   GO; GO:0006301; P:postreplication repair; IEA:EnsemblFungi.
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..1093
FT                   /note="PAN2-PAN3 deadenylation complex catalytic subunit
FT                   PAN2"
FT                   /id="PRO_0000295341"
FT   REPEAT          27..66
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REPEAT          154..194
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REPEAT          197..236
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REPEAT          295..334
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   DOMAIN          462..836
FT                   /note="USP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   DOMAIN          888..1058
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   REGION          336..462
FT                   /note="Linker"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03182"
FT   BINDING         891
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         893
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         1000
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         1051
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   1093 AA;  123992 MW;  A7F5CE68F766C6C9 CRC64;
     MNNWQHSFNN ARPLDEHLHK PYLQYDGIEK HLTKFIFDDH ANLVWTGDTY GCVSSYDVNF
     QPYVRQRAHI GGSPVKDLMS HSSGVLSLSS DSLHLQDRRG TTLLNLTNID IAAFNDLQTM
     CYMSADQTSK VYCAGTDIGT GLSLIDLQRG TLETNIPYFS KVNFIKSSKK LAAIGKLSGS
     IDLFDPGSNQ VIKSFISHSS CITSMDIQDY TLVTTGQSNG FYNTFADPFV NVYDLRTMRQ
     LPPISFSKST SMGTVGADFV QLHPVLPTIV MIASSSGAFD FVDMANPSLR TQFANPGNGI
     KCIRLSSNGD HLGVLESNDM FSTWKRPNSS VNFTNMPELL TYPSYPNDGP LANISIDDYN
     YPLSTVGMPY YQEKLLSTWS TVIFRSPGTV PRDIDKILTD LKNSKKSKKL VADGVNFYPY
     SVAKYGHKDA LQPYISLRDK RYQRSTGSVP DDVLITKSVD GELPPAFKNL PLVVTKYATD
     SFDFESVNKT PYCGLDNDVD NPFTNALIQL YRFIPEISNF LISTLKHEHF ESPLLTDMAY
     LFDMMRNTID GICRTTNYQM SLNDVLEKNN LSLHTISESN MLQKINSLSL NDDGGKKQLS
     IQELNDFLLS ELCEEEVKFI DQNFVLQHCY CCEFAVKTKG CMTYGQTSGS LYKPSITIGP
     NACTQKNGKV SYPHSILGYI EHGLKNSIVL NKKCEQCGIK ENLEEDISIQ ELPPILSLSL
     EFDDNAMKLA KTTKNWLPKE FYASIMKNKP LVRGSVNDIR TNTMIYKYEL HGYIARISDP
     DRGDHYVTFS RIYNEESKMF RWYLFNDYLV TEVDESIVYD LGKHWLKPEV VIYGDAEELR
     KPFNYLKDVE IDDSILYKDY FSAAIRESIQ KEYELLTRNE APRPGSLIAI DAEFVTLKNE
     KYDIDCRGAK TVVQSKVSAL ARISVVRGNE EQFGVPFIDD YIIIEKNIDD YLTKFSGILP
     GDLDPKTSNK HLVPRNVAYR KIWLLMQLGC TFIGHGLQND FKHINISVPK EQIRDTAVYF
     LQGKRYLSLR YLAYVLLDIN VQEGNHDSIE DAYTALVLYK KYLELKSNGM MDQVLNKLYE
     EGRTTNYKVP LKL
 
 
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