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Decapping and exoribonuclease protein 1 (EC 3.1.13.-) (EC 3.6.1.-)

 DXO1_KLULA              Reviewed;         403 AA.
Q6CPU0;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
18-JUL-2018, entry version 66.
RecName: Full=Decapping and exoribonuclease protein 1;
EC=3.1.13.-;
EC=3.6.1.-;
Name=DXO1; OrderedLocusNames=KLLA0E02245g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
[2]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MANGANESE,
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-161; HIS-163 AND
ASP-167.
PubMed=22961381; DOI=10.1038/nsmb.2381;
Chang J.H., Jiao X., Chiba K., Oh C., Martin C.E., Kiledjian M.,
Tong L.;
"Dxo1 is a new type of eukaryotic enzyme with both decapping and 5'-3'
exoribonuclease activity.";
Nat. Struct. Mol. Biol. 19:1011-1017(2012).
-!- FUNCTION: Ribonuclease that specifically degrades pre-mRNAs with a
defective 5' end cap and is part of a pre-mRNA capping quality
control. Has decapping and 5'-3' exonuclease activities. Has
decapping activity toward incomplete 5' end cap mRNAs such as
unmethylated 5' end-capped RNA to release GpppN and 5' end
monophosphate RNA. The 5' end monophosphate RNA is then degraded
by the 5'-3' exoribonuclease activity, enabling this enzyme to
decap and degrade incompletely capped mRNAs.
{ECO:0000269|PubMed:22961381}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Divalent metal cation. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the DXO/Dom3Z family. {ECO:0000305}.
-!- CAUTION: In contrast to canonical decapping enzymes which release
m(7)pppG (m(7)GDP), the decapping activity releases the entire cap
structure GpppN and a 5' end monophosphate RNA.
{ECO:0000305|PubMed:22961381}.
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EMBL; CR382125; CAG99136.1; -; Genomic_DNA.
RefSeq; XP_454049.1; XM_454049.1.
PDB; 4GPS; X-ray; 2.40 A; A=1-403.
PDB; 4GPU; X-ray; 2.80 A; A=1-403.
PDBsum; 4GPS; -.
PDBsum; 4GPU; -.
SMR; Q6CPU0; -.
PRIDE; Q6CPU0; -.
EnsemblFungi; CAG99136; CAG99136; KLLA0_E02245g.
GeneID; 2894233; -.
KEGG; kla:KLLA0E02245g; -.
eggNOG; ENOG410IK9Z; Eukaryota.
eggNOG; ENOG4111D9P; LUCA.
InParanoid; Q6CPU0; -.
OMA; TELKCYA; -.
OrthoDB; EOG092C4JGE; -.
Proteomes; UP000000598; Chromosome E.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:GOC.
GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:UniProtKB.
InterPro; IPR039039; RAI1-like_fam.
PANTHER; PTHR12395; PTHR12395; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Exonuclease; Hydrolase;
Metal-binding; Nuclease; Nucleotide-binding; Reference proteome;
RNA-binding.
CHAIN 1 403 Decapping and exoribonuclease protein 1.
/FTId=PRO_0000422597.
METAL 223 223 Divalent metal cation.
METAL 262 262 Divalent metal cation.
METAL 273 273 Divalent metal cation.
METAL 274 274 Divalent metal cation; via carbonyl
oxygen.
MUTAGEN 161 161 L->W: Reduced decapping activity without
affecting the exonuclease activity.
Reduced decapping and exonuclease
activities; when associated with G-163.
{ECO:0000269|PubMed:22961381}.
MUTAGEN 163 163 H->G: Does not affect the exonuclease
activity. Reduced decapping and
exonuclease activities; when associated
with W-161. Reduced decapping and
exonuclease activities; when associated
with K-167.
{ECO:0000269|PubMed:22961381}.
MUTAGEN 167 167 D->K: Does not affect the decapping and
exonuclease activities. Reduced decapping
and exonuclease activities; when
associated with G-163.
{ECO:0000269|PubMed:22961381}.
STRAND 40 43 {ECO:0000244|PDB:4GPS}.
STRAND 62 75 {ECO:0000244|PDB:4GPS}.
TURN 76 79 {ECO:0000244|PDB:4GPS}.
STRAND 80 83 {ECO:0000244|PDB:4GPS}.
HELIX 84 86 {ECO:0000244|PDB:4GPS}.
HELIX 94 102 {ECO:0000244|PDB:4GPS}.
HELIX 108 111 {ECO:0000244|PDB:4GPS}.
TURN 112 116 {ECO:0000244|PDB:4GPS}.
TURN 119 122 {ECO:0000244|PDB:4GPS}.
HELIX 136 147 {ECO:0000244|PDB:4GPS}.
HELIX 148 150 {ECO:0000244|PDB:4GPS}.
STRAND 155 161 {ECO:0000244|PDB:4GPS}.
HELIX 162 170 {ECO:0000244|PDB:4GPS}.
HELIX 171 173 {ECO:0000244|PDB:4GPS}.
STRAND 178 184 {ECO:0000244|PDB:4GPS}.
STRAND 190 193 {ECO:0000244|PDB:4GPS}.
HELIX 213 226 {ECO:0000244|PDB:4GPS}.
STRAND 239 248 {ECO:0000244|PDB:4GPS}.
STRAND 250 260 {ECO:0000244|PDB:4GPS}.
STRAND 263 265 {ECO:0000244|PDB:4GPS}.
TURN 266 269 {ECO:0000244|PDB:4GPS}.
STRAND 270 277 {ECO:0000244|PDB:4GPS}.
HELIX 285 299 {ECO:0000244|PDB:4GPS}.
STRAND 301 303 {ECO:0000244|PDB:4GPS}.
STRAND 305 311 {ECO:0000244|PDB:4GPS}.
TURN 313 315 {ECO:0000244|PDB:4GPS}.
STRAND 317 324 {ECO:0000244|PDB:4GPS}.
HELIX 326 333 {ECO:0000244|PDB:4GPS}.
HELIX 338 340 {ECO:0000244|PDB:4GPS}.
HELIX 346 348 {ECO:0000244|PDB:4GPS}.
HELIX 350 373 {ECO:0000244|PDB:4GPS}.
STRAND 378 384 {ECO:0000244|PDB:4GPS}.
STRAND 389 394 {ECO:0000244|PDB:4GPS}.
SEQUENCE 403 AA; 46312 MW; D2E6DA0EE3FE4894 CRC64;
MTTVSCDKDE NKVDQLGESL SQLRISTRKN NKPSQKKGSL VLSCKKFPHV SVNYVVDKTP
KLLTDCKEVH NCSYIINDAT LLWNEASRKP RLRPEVCTYI KDSKWENKAV KDSFIGIDLT
KGYDDYVPLD RNVLNSLVIL KEAYQRYEKT LNPEKTTFVS LRHHIIDIIM CPFLDEPLSL
LMTVQPDKNI LISVDKSKDK PNGIHETRNS FNKKICYTGF ALEDLLIESP TEGHILEHEL
YYSIVHGSLN DEIDLLIQAE MDSINTLTDT YTEIKSSVHF KLGNTYHRRK LLRMWIQTNL
LPKSDLLIGF RNSYSNELEQ LKAYKIQDIY HKINNSSIVG KPGKFYKFNP NVANDWFQHI
FQVLKQNLLL LSQESTSTTF KVQIDTNLTL SISPASQFVT ALG


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