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Exodeoxyribonuclease I (ExoI) (Exonuclease I) (EC 3.1.11.1) (DNA deoxyribophosphodiesterase) (dRPase)

 EX1_ECOLI               Reviewed;         475 AA.
P04995;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
25-APR-2018, entry version 167.
RecName: Full=Exodeoxyribonuclease I;
Short=ExoI {ECO:0000303|PubMed:11101894};
Short=Exonuclease I {ECO:0000303|PubMed:11101894};
EC=3.1.11.1 {ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540};
AltName: Full=DNA deoxyribophosphodiesterase;
Short=dRPase;
Name=sbcB; Synonyms=cpeA, xonA; OrderedLocusNames=b2011, JW1993;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12.
STRAIN=K12;
PubMed=3539937;
Phillips G.J., Kushner S.R.;
"Determination of the nucleotide sequence for the exonuclease I
structural gene (sbcB) of Escherichia coli K12.";
J. Biol. Chem. 262:455-459(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / BHB2600;
Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
Church G.M.;
"Automated multiplex sequencing of the E.coli genome.";
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097040; DOI=10.1093/dnares/3.6.379;
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION AS A DRPASE.
PubMed=1329027; DOI=10.1093/nar/20.18.4699;
Sandigursky M., Franklin W.A.;
"DNA deoxyribophosphodiesterase of Escherichia coli is associated with
exonuclease I.";
Nucleic Acids Res. 20:4699-4703(1992).
[7]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
DOMAIN.
STRAIN=K12 / DH5-alpha {ECO:0000303|PubMed:11101894};
PubMed=11101894; DOI=10.1038/81978;
Breyer W.A., Matthews B.W.;
"Structure of Escherichia coli exonuclease I suggests how processivity
is achieved.";
Nat. Struct. Biol. 7:1125-1128(2000).
[8]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH DTMP PRODUCT
AND MAGNESIUM, COFACTOR, AND DOMAIN.
STRAIN=K12 {ECO:0000303|PubMed:18219121};
PubMed=18219121; DOI=10.1107/S090744490706012X;
Busam R.D.;
"Structure of Escherichia coli exonuclease I in complex with thymidine
5'-monophosphate.";
Acta Crystallogr. D 64:206-210(2008).
[9]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH
SSB TAIL PEPTIDE AND MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR,
INTERACTION WITH SSB, DOMAIN, SITES, AND MUTAGENESIS OF ARG-148;
GLU-150; TYR-207; LYS-227; GLN-311; ARG-316; GLU-318; ASP-319;
ARG-327; LEU-331; ARG-338; GLN-448 AND GLN-452.
PubMed=18591666; DOI=10.1073/pnas.0800741105;
Lu D., Keck J.L.;
"Structural basis of Escherichia coli single-stranded DNA-binding
protein stimulation of exonuclease I.";
Proc. Natl. Acad. Sci. U.S.A. 105:9169-9174(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH INHIBITORS
AND MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH SSB, AND
SITE.
PubMed=20018747; DOI=10.1073/pnas.0909191107;
Lu D., Bernstein D.A., Satyshur K.A., Keck J.L.;
"Small-molecule tools for dissecting the roles of SSB/protein
interactions in genome maintenance.";
Proc. Natl. Acad. Sci. U.S.A. 107:633-638(2010).
[11]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH
SINGLE-STRANDED DNA SUBSTRATES AND ZINC.
Qiu R., Lou T., Wei J., Liu M., Gu S., Tang R., Ji C., Gong W.;
"The structures of Escherichia coli exonuclease I in complex with the
single strand DNA.";
Submitted (SEP-2012) to the PDB data bank.
[12]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH
SINGLE-STRANDED DNA SUBSTRATES AND MAGNESIUM, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT, DOMAIN, AND
MUTAGENESIS OF HIS-181.
STRAIN=K12 {ECO:0000303|PubMed:23609540};
PubMed=23609540; DOI=10.1093/nar/gkt278;
Korada S.K., Johns T.D., Smith C.E., Jones N.D., McCabe K.A.,
Bell C.E.;
"Crystal structures of Escherichia coli exonuclease I in complex with
single-stranded DNA provide insights into the mechanism of processive
digestion.";
Nucleic Acids Res. 41:5887-5897(2013).
-!- FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly
processive manner (PubMed:23609540). Also functions as a DNA
deoxyribophosphodiesterase that releases deoxyribose-phosphate
moieties following the cleavage of DNA at an apurinic/apyrimidinic
(AP) site by either an AP endonuclease or AP lyase
(PubMed:1329027). {ECO:0000269|PubMed:1329027,
ECO:0000269|PubMed:23609540}.
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
direction to yield nucleoside 5'-phosphates.
{ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747,
ECO:0000269|PubMed:23609540}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:18219121,
ECO:0000269|PubMed:18591666, ECO:0000269|PubMed:20018747,
ECO:0000269|PubMed:23609540};
Note=Binds 2 Mg(2+) ions per monomer.
{ECO:0000269|PubMed:18591666};
-!- ENZYME REGULATION: Inhibited by 10 mM EDTA.
{ECO:0000269|PubMed:23609540}.
-!- SUBUNIT: Monomer (PubMed:23609540). Interacts with ssb (via C-
terminus); this interaction stimulates the exonuclease activity by
recruiting the enzyme to its substrate (PubMed:18591666,
PubMed:20018747). {ECO:0000269|PubMed:18591666,
ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23609540}.
-!- DOMAIN: The N-terminal exonuclease domain and the exonuclease C-
terminal domain form a central positively charged groove which
binds the DNA. {ECO:0000269|PubMed:18591666,
ECO:0000269|PubMed:23609540, ECO:0000305|PubMed:11101894,
ECO:0000305|PubMed:18219121}.
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EMBL; J02641; AAA19938.1; -; Unassigned_DNA.
EMBL; U00009; AAA16417.1; -; Genomic_DNA.
EMBL; U00096; AAC75072.1; -; Genomic_DNA.
EMBL; AP009048; BAA15839.1; -; Genomic_DNA.
PIR; B64966; NCECX1.
RefSeq; NP_416515.1; NC_000913.3.
RefSeq; WP_000980589.1; NZ_LN832404.1.
PDB; 1FXX; X-ray; 2.40 A; A=1-475.
PDB; 2QXF; X-ray; 1.50 A; A=1-475.
PDB; 3C94; X-ray; 2.70 A; A=1-475.
PDB; 3C95; X-ray; 1.70 A; A=1-475.
PDB; 3HL8; X-ray; 1.55 A; A=1-475.
PDB; 3HP9; X-ray; 1.60 A; A=1-475.
PDB; 4HCB; X-ray; 2.00 A; A/B=1-475.
PDB; 4HCC; X-ray; 2.96 A; A/B=1-475.
PDB; 4JRP; X-ray; 1.95 A; A/B=1-475.
PDB; 4JRQ; X-ray; 3.00 A; A/B=1-475.
PDB; 4JS4; X-ray; 3.10 A; A/B=1-475.
PDB; 4JS5; X-ray; 3.50 A; A/B=1-475.
PDBsum; 1FXX; -.
PDBsum; 2QXF; -.
PDBsum; 3C94; -.
PDBsum; 3C95; -.
PDBsum; 3HL8; -.
PDBsum; 3HP9; -.
PDBsum; 4HCB; -.
PDBsum; 4HCC; -.
PDBsum; 4JRP; -.
PDBsum; 4JRQ; -.
PDBsum; 4JS4; -.
PDBsum; 4JS5; -.
ProteinModelPortal; P04995; -.
SMR; P04995; -.
BioGrid; 4260414; 102.
DIP; DIP-10827N; -.
IntAct; P04995; 7.
STRING; 316385.ECDH10B_2158; -.
PaxDb; P04995; -.
PRIDE; P04995; -.
EnsemblBacteria; AAC75072; AAC75072; b2011.
EnsemblBacteria; BAA15839; BAA15839; BAA15839.
GeneID; 946529; -.
KEGG; ecj:JW1993; -.
KEGG; eco:b2011; -.
EchoBASE; EB0919; -.
EcoGene; EG10926; sbcB.
eggNOG; ENOG4105CJB; Bacteria.
eggNOG; COG2925; LUCA.
HOGENOM; HOG000276591; -.
InParanoid; P04995; -.
KO; K01141; -.
OMA; RDRPAQF; -.
PhylomeDB; P04995; -.
BioCyc; EcoCyc:EG10926-MONOMER; -.
BioCyc; MetaCyc:EG10926-MONOMER; -.
BRENDA; 3.1.11.1; 2026.
EvolutionaryTrace; P04995; -.
PRO; PR:P04995; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
GO; GO:0008852; F:exodeoxyribonuclease I activity; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0006308; P:DNA catabolic process; IDA:EcoCyc.
GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
Gene3D; 2.30.30.450; -; 1.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR023607; Exodeoxyribonuclease_I.
InterPro; IPR034748; EXOI_C.
InterPro; IPR034747; EXOI_SH3.
InterPro; IPR038649; EXOI_SH3_sf.
InterPro; IPR013620; Exonuc_1_C.
InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF08411; Exonuc_X-T_C; 1.
Pfam; PF00929; RNase_T; 1.
PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
SMART; SM00479; EXOIII; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS51785; EXOI_C; 1.
PROSITE; PS51784; EXOI_SH3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
DNA damage; DNA repair; DNA-binding; Exonuclease; Hydrolase;
Magnesium; Metal-binding; Nuclease; Reference proteome; Zinc.
CHAIN 1 475 Exodeoxyribonuclease I.
/FTId=PRO_0000087110.
DOMAIN 13 192 Exonuclease. {ECO:0000255}.
DOMAIN 202 355 ExoI SH3-like. {ECO:0000255|PROSITE-
ProRule:PRU01120}.
DOMAIN 358 475 ExoI C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU01121}.
METAL 15 15 Magnesium 1.
{ECO:0000269|PubMed:11101894,
ECO:0000269|PubMed:18219121,
ECO:0000269|PubMed:18591666,
ECO:0000269|PubMed:20018747,
ECO:0000269|PubMed:23609540}.
METAL 17 17 Magnesium 2.
{ECO:0000269|PubMed:18219121}.
METAL 186 186 Magnesium 2.
{ECO:0000269|PubMed:18219121}.
BINDING 17 17 Substrate. {ECO:0000269|PubMed:18219121}.
BINDING 165 165 Substrate. {ECO:0000269|PubMed:18219121}.
SITE 18 18 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 66 66 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 113 113 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 124 124 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 128 128 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 142 142 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 148 148 Important for interaction with ssb.
{ECO:0000269|PubMed:18591666}.
SITE 164 164 Interaction with single-stranded DNA.
{ECO:0000244|PDB:4HCC,
ECO:0000269|PubMed:23609540}.
SITE 181 181 Important for activity.
{ECO:0000269|PubMed:23609540}.
SITE 207 207 Important for interaction with ssb.
{ECO:0000269|PubMed:18591666}.
SITE 214 214 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 257 257 Interaction with single-stranded DNA.
{ECO:0000244|PDB:4HCC,
ECO:0000269|PubMed:23609540}.
SITE 284 284 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 304 304 Interaction with single-stranded DNA.
{ECO:0000244|PDB:4HCC,
ECO:0000269|PubMed:23609540}.
SITE 311 311 Important for interaction with ssb.
{ECO:0000269|PubMed:18591666}.
SITE 338 338 Important for interaction with ssb.
{ECO:0000305|PubMed:20018747}.
SITE 368 368 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
SITE 371 371 Interaction with single-stranded DNA.
{ECO:0000269|PubMed:23609540}.
MUTAGEN 148 148 R->A: Strongly reduced ssb-binding.
Reduced ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 150 150 E->A: About 2-fold increased ssb-binding.
Weakly increased ssb-independent and ssb-
dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 181 181 H->A: Residual nuclease activity.
{ECO:0000269|PubMed:23609540}.
MUTAGEN 207 207 Y->A: Strongly reduced ssb-binding.
Reduced ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 227 227 K->A: 7-fold reduced ssb-binding. Reduced
ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 311 311 Q->A: 2-fold reduced ssb-binding. Weakly
reduced ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 316 316 R->A: Strongly reduced ssb-binding.
Strongly reduced ssb-dependent nuclease
activity. {ECO:0000269|PubMed:18591666}.
MUTAGEN 318 318 E->A: About 2-fold increased ssb-binding.
No effect on ssb-dependent nuclease
activity. {ECO:0000269|PubMed:18591666}.
MUTAGEN 319 319 D->A: 2-fold reduced ssb-binding. No
effect on ssb-dependent nuclease
activity. {ECO:0000269|PubMed:18591666}.
MUTAGEN 327 327 R->A: No effect on ssb-binding and on
ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 331 331 L->A: No effect on ssb-binding and on
ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 338 338 R->A: 3-fold reduced ssb-binding. Reduced
ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 448 448 Q->A: No effect on ssb-binding and on
ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
MUTAGEN 452 452 Q->A: No effect on ssb-binding and on
ssb-dependent nuclease activity.
{ECO:0000269|PubMed:18591666}.
CONFLICT 210 218 Missing (in Ref. 1; AAA19938).
{ECO:0000305}.
CONFLICT 225 225 Q -> H (in Ref. 1; AAA19938).
{ECO:0000305}.
CONFLICT 343 343 V -> E (in Ref. 1; AAA19938).
{ECO:0000305}.
CONFLICT 475 475 V -> A (in Ref. 1; AAA19938).
{ECO:0000305}.
STRAND 10 21 {ECO:0000244|PDB:2QXF}.
TURN 23 25 {ECO:0000244|PDB:2QXF}.
STRAND 28 36 {ECO:0000244|PDB:2QXF}.
STRAND 47 51 {ECO:0000244|PDB:2QXF}.
HELIX 61 67 {ECO:0000244|PDB:2QXF}.
HELIX 71 77 {ECO:0000244|PDB:2QXF}.
HELIX 81 92 {ECO:0000244|PDB:2QXF}.
STRAND 97 103 {ECO:0000244|PDB:2QXF}.
TURN 104 107 {ECO:0000244|PDB:2QXF}.
HELIX 108 118 {ECO:0000244|PDB:2QXF}.
HELIX 125 127 {ECO:0000244|PDB:2QXF}.
HELIX 129 131 {ECO:0000244|PDB:2QXF}.
STRAND 133 136 {ECO:0000244|PDB:2QXF}.
HELIX 137 147 {ECO:0000244|PDB:2QXF}.
STRAND 160 162 {ECO:0000244|PDB:2QXF}.
HELIX 166 172 {ECO:0000244|PDB:2QXF}.
HELIX 185 200 {ECO:0000244|PDB:2QXF}.
HELIX 202 210 {ECO:0000244|PDB:2QXF}.
HELIX 214 219 {ECO:0000244|PDB:2QXF}.
TURN 223 226 {ECO:0000244|PDB:2QXF}.
STRAND 229 232 {ECO:0000244|PDB:2QXF}.
HELIX 234 236 {ECO:0000244|PDB:2QXF}.
HELIX 238 240 {ECO:0000244|PDB:2QXF}.
STRAND 243 251 {ECO:0000244|PDB:2QXF}.
STRAND 258 263 {ECO:0000244|PDB:2QXF}.
HELIX 269 273 {ECO:0000244|PDB:2QXF}.
HELIX 276 285 {ECO:0000244|PDB:3HL8}.
HELIX 287 289 {ECO:0000244|PDB:4HCB}.
STRAND 298 302 {ECO:0000244|PDB:2QXF}.
HELIX 303 305 {ECO:0000244|PDB:4JRQ}.
STRAND 308 311 {ECO:0000244|PDB:2QXF}.
HELIX 312 314 {ECO:0000244|PDB:2QXF}.
HELIX 317 323 {ECO:0000244|PDB:2QXF}.
HELIX 327 339 {ECO:0000244|PDB:2QXF}.
HELIX 343 346 {ECO:0000244|PDB:2QXF}.
HELIX 363 365 {ECO:0000244|PDB:2QXF}.
HELIX 367 369 {ECO:0000244|PDB:2QXF}.
HELIX 374 385 {ECO:0000244|PDB:2QXF}.
TURN 388 390 {ECO:0000244|PDB:2QXF}.
TURN 391 393 {ECO:0000244|PDB:4HCB}.
HELIX 402 414 {ECO:0000244|PDB:2QXF}.
HELIX 416 418 {ECO:0000244|PDB:2QXF}.
HELIX 421 434 {ECO:0000244|PDB:2QXF}.
HELIX 437 453 {ECO:0000244|PDB:2QXF}.
TURN 454 456 {ECO:0000244|PDB:2QXF}.
HELIX 458 473 {ECO:0000244|PDB:2QXF}.
SEQUENCE 475 AA; 54501 MW; A6A02AC17922C313 CRC64;
MMNDGKQQST FLFHDYETFG THPALDRPAQ FAAIRTDSEF NVIGEPEVFY CKPADDYLPQ
PGAVLITGIT PQEARAKGEN EAAFAARIHS LFTVPKTCIL GYNNVRFDDE VTRNIFYRNF
YDPYAWSWQH DNSRWDLLDV MRACYALRPE GINWPENDDG LPSFRLEHLT KANGIEHSNA
HDAMADVYAT IAMAKLVKTR QPRLFDYLFT HRNKHKLMAL IDVPQMKPLV HVSGMFGAWR
GNTSWVAPLA WHPENRNAVI MVDLAGDISP LLELDSDTLR ERLYTAKTDL GDNAAVPVKL
VHINKCPVLA QANTLRPEDA DRLGINRQHC LDNLKILREN PQVREKVVAI FAEAEPFTPS
DNVDAQLYNG FFSDADRAAM KIVLETEPRN LPALDITFVD KRIEKLLFNY RARNFPGTLD
YAEQQRWLEH RRQVFTPEFL QGYADELQML VQQYADDKEK VALLKALWQY AEEIV


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29-514 THEX1 contains 1 SAP domain and 1 exonuclease domain. It is an RNA exonuclease that binds to the 3' end of histone mRNAs and probably degrades them, suggesting that it plays an essential role in histo 0.1 mg
29-513 THEX1 contains 1 SAP domain and 1 exonuclease domain. It is an RNA exonuclease that binds to the 3' end of histone mRNAs and probably degrades them, suggesting that it plays an essential role in histo 0.05 mg
EIAAB13234 3'-5' exonuclease ERI1,3'-5' exoribonuclease 1,3'exo,Eri1,Eri-1 homolog,Histone mRNA 3'-exonuclease 1,Mouse,Mus musculus,Thex1
EIAAB43821 3'-5' exonuclease TREX1,DNase III,Homo sapiens,Human,Three prime repair exonuclease 1,TREX1
EIAAB43824 3'-5' exonuclease TREX2,Homo sapiens,Human,Three prime repair exonuclease 2,TREX2
EIAAB43822 3'-5' exonuclease TREX1,Bos taurus,Bovine,Three prime repair exonuclease 1,TREX1
EIAAB43823 3'-5' exonuclease TREX1,Mouse,Mus musculus,Three prime repair exonuclease 1,Trex1
EIAAB43825 3'-5' exonuclease TREX2,Mouse,Mus musculus,Three prime repair exonuclease 2,Trex2
EIAAB13444 C14orf114,EXD2,EXDL2,Exonuclease 3'-5' domain-containing protein 2,Exonuclease 3'-5' domain-like-containing protein 2,Homo sapiens,Human
EIAAB13442 EXD1,EXDL1,Exonuclease 3'-5' domain-containing protein 1,Exonuclease 3'-5' domain-like-containing protein 1,Homo sapiens,Human
EIAAB13443 Exd1,Exdl1,Exonuclease 3'-5' domain-containing protein 1,Exonuclease 3'-5' domain-like-containing protein 1,Mouse,Mus musculus
EIAAB13445 Exd2,Exdl2,Exonuclease 3'-5' domain-containing protein 2,Exonuclease 3'-5' domain-like-containing protein 2,Mouse,Mus musculus
18-003-44239 Histone mRNA 3'-exonuclease 1 - EC 3.1.-.-; 3'-5' exonuclease ERI1; Eri-1 homolog; Histone mRNA 3'-end-specific exoribonuclease; Protein 3'hExo; HEXO Polyclonal 0.1 mg Protein A
EIAAB13233 3'-5' exonuclease ERI1,3'-5' exoribonuclease 1,3'EXO,ERI1,Eri-1 homolog,HEXO,Histone mRNA 3'-end-specific exoribonuclease,Histone mRNA 3'-exonuclease 1,Homo sapiens,Human,Protein 3'hExo,THEX1
9217-500 Exonuclease I 500 UN
E345 Exonuclease III 4000 Package u.a.


 

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