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mRNA-capping enzyme catalytic subunit (Virus termination factor large subunit) (VTF large subunit) (mRNA-capping enzyme 97 kDa subunit) (mRNA-capping enzyme D1 subunit) (mRNA-capping enzyme large subunit) [Includes: Polynucleotide 5'-triphosphatase (EC 3.1.3.33) (mRNA 5'-triphosphatase) (TPase); mRNA guanylyltransferase (EC 2.7.7.50) (GTP--RNA guanylyltransferase) (GTase); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56) (mRNA cap methyltransferase)]

 MCEL_VACCW              Reviewed;         844 AA.
P04298; Q76ZS6;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
25-OCT-2017, entry version 97.
RecName: Full=mRNA-capping enzyme catalytic subunit;
AltName: Full=Virus termination factor large subunit;
Short=VTF large subunit;
AltName: Full=mRNA-capping enzyme 97 kDa subunit;
AltName: Full=mRNA-capping enzyme D1 subunit;
AltName: Full=mRNA-capping enzyme large subunit;
Includes:
RecName: Full=Polynucleotide 5'-triphosphatase;
EC=3.1.3.33;
AltName: Full=mRNA 5'-triphosphatase;
Short=TPase;
Includes:
RecName: Full=mRNA guanylyltransferase;
EC=2.7.7.50;
AltName: Full=GTP--RNA guanylyltransferase;
Short=GTase;
Includes:
RecName: Full=mRNA (guanine-N(7)-)-methyltransferase;
EC=2.1.1.56;
AltName: Full=mRNA cap methyltransferase;
OrderedLocusNames=VACWR106; ORFNames=D1R;
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
WR)).
Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
Orthopoxvirus; Vaccinia virus.
NCBI_TaxID=10254;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
"Nucleotide sequence and genetic map of the 16-kb vaccinia virus
HindIII D fragment.";
Virology 153:96-112(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M.,
Osborne J., Wohlhueter R.;
"Sequencing of the coding region of Vaccinia-WR to an average 9-fold
redundancy and an error rate of 0.16/10kb.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]
COFACTOR.
PubMed=2164022;
Shuman S.;
"Catalytic activity of vaccinia mRNA capping enzyme subunits
coexpressed in Escherichia coli.";
J. Biol. Chem. 265:11960-11966(1990).
[4]
INTERACTION WITH SMALL SUBUNIT, AND PROTEIN SEQUENCE OF 1-20 AND
498-517.
PubMed=2161527; DOI=10.1073/pnas.87.11.4023;
Guo P., Moss B.;
"Interaction and mutual stabilization of the two subunits of vaccinia
virus mRNA capping enzyme coexpressed in Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 87:4023-4027(1990).
[5]
DOMAIN METHYLTRANSFERASE.
PubMed=7929111;
Mao X., Shuman S.;
"Intrinsic RNA (guanine-7) methyltransferase activity of the vaccinia
virus capping enzyme D1 subunit is stimulated by the D12 subunit.
Identification of amino acid residues in the D1 protein required for
subunit association and methyl group transfer.";
J. Biol. Chem. 269:24472-24479(1994).
[6]
ACTIVE SITE OF TRIPHOSPHATASE ACTIVITY, AND MUTAGENESIS OF
77-ARG--LYS-79; 135-LYS-LYS-136; 160-PHE-LYS-161; 192-GLU--GLU-194;
LYS-260 AND 524-LYS--GLY-526.
PubMed=8709242;
Yu L., Shuman S.;
"Mutational analysis of the RNA triphosphatase component of vaccinia
virus mRNA capping enzyme.";
J. Virol. 70:6162-6168(1996).
[7]
CHARACTERIZATION OF TRIPHOSPHATASE ACTIVITY, AND MUTAGENESIS OF
LYS-107; GLU-126; ASP-159 AND LYS-161.
PubMed=12726733; DOI=10.1016/S0042-6822(03)00002-3;
Gong C., Shuman S.;
"Mapping the active site of vaccinia virus RNA triphosphatase.";
Virology 309:125-134(2003).
[8]
FUNCTION.
STRAIN=IHDW, and mutant Dts36;
PubMed=18295814; DOI=10.1016/j.virol.2008.01.028;
Shatzer A.N., Kato S.E., Condit R.C.;
"Phenotypic analysis of a temperature sensitive mutant in the large
subunit of the vaccinia virus mRNA capping enzyme.";
Virology 375:236-252(2008).
[9]
FUNCTION.
PubMed=18455214; DOI=10.1016/j.virol.2008.03.031;
Christen L.A., Piacente S., Mohamed M.R., Niles E.G.;
"Vaccinia virus early gene transcription termination factors VTF and
Rap94 interact with the U9 termination motif in the nascent RNA in a
transcription ternary complex.";
Virology 376:225-235(2008).
[10]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASN-570;
LYS-573; LYS-607; TYR-608; ASP-676; PHE-679; HIS-682 AND GLU-763.
PubMed=18256245; DOI=10.1261/rna.928208;
Zheng S., Shuman S.;
"Structure-function analysis of vaccinia virus mRNA cap (guanine-N7)
methyltransferase.";
RNA 14:696-705(2008).
[11] {ECO:0000244|PDB:2VDW}
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 545-844 IN COMPLEX WITH
ADOHCY AND THE REGULATORY SUBUNIT.
PubMed=17989694; DOI=10.1038/sj.emboj.7601912;
De la Pena M., Kyrieleis O.J., Cusack S.;
"Structural insights into the mechanism and evolution of the vaccinia
virus mRNA cap N7 methyl-transferase.";
EMBO J. 26:4913-4925(2007).
[12]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GTP AND
S-ADENOSYL-L-HOMOCYSTEINE, AND COFACTOR.
PubMed=24607143; DOI=10.1016/j.str.2013.12.014;
Kyrieleis O.J., Chang J., de la Pena M., Shuman S., Cusack S.;
"Crystal structure of vaccinia virus mRNA capping enzyme provides
insights into the mechanism and evolution of the capping apparatus.";
Structure 22:452-465(2014).
-!- FUNCTION: Catalytic subunit of the mRNA capping enzyme which
catalyzes three enzymatic reactions: the 5' triphosphate end of
the pre-mRNA is hydrolyzed to a diphosphate by RNA 5'
triphosphatase; the diphosphate RNA end is capped with GMP by RNA
guanylyltransferase and the GpppN cap is methylated by RNA
(guanine-N7) methyltransferase. Heterodimeric mRNA capping enzyme
catalyzes the linkage of a N7-methyl-guanosine moiety to the first
transcribed nucleotide (cap 0 structure), whereas the polymerase
associated VP39 is responsible for a second methylation at the 2'-
O position of the ribose (cap 1 structure).
-!- FUNCTION: The heterodimeric enzyme is also involved in early viral
gene transcription termination and intermediate viral gene
transcription initiation. Early gene transcription termination
requires the termination factor VTF, the DNA-dependent ATPase NPH-
I and the Rap94 subunit of the viral RNA polymerase, as well as
the presence of a specific termination motif. Binds, together with
RAP94, to the termination motif 5'-UUUUUNU-3' in the nascent early
mRNA.
-!- CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a
polynucleotide + phosphate.
-!- CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate +
G(5')ppp-Pur-mRNA.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:2164022,
ECO:0000305|PubMed:24607143};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=23 uM for GpppA {ECO:0000269|PubMed:18256245};
Note=A-570 and A-763 mutants have 3-fold and 10-fold higher Km
values for GpppA.;
-!- SUBUNIT: Heterodimer of a catalytic and a regulatory subunit.
Intrinsic methyltransferase activity of the catalytic subunit is
weak and needs to be stimulated 30- to 50-fold by the regulatory
subunit, which is itself catalytically inert.
{ECO:0000269|PubMed:17989694}.
-!- INTERACTION:
P04318:VACWR117; NbExp=3; IntAct=EBI-16095746, EBI-16095776;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes
and other proteins required to synthesize early mRNAs are packaged
within the virion core along with the DNA genome.
-!- DOMAIN: The N-terminus contains the triphosphatase and
guanylyltransferase domains, whereas the C-terminus contains the
methyltransferase domain. The N-terminus is involved in binding to
the temination motif 5'-UUUUUNU-3' in the nascent mRNA.
{ECO:0000269|PubMed:7929111}.
-!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus
mRNA guanylyltransferase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the class I-like
SAM-binding methyltransferase superfamily. mRNA cap 0
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00895}.
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EMBL; M15058; AAA48253.1; -; Genomic_DNA.
EMBL; AY243312; AAO89385.1; -; Genomic_DNA.
PIR; A03872; QQVZ1.
RefSeq; YP_232988.1; NC_006998.1.
PDB; 2VDW; X-ray; 2.70 A; A/C/E/G=545-844.
PDB; 4CKB; X-ray; 2.80 A; A/D=1-844.
PDB; 4CKC; X-ray; 2.90 A; A/D=1-844.
PDB; 4CKE; X-ray; 2.90 A; A/D=1-844.
PDBsum; 2VDW; -.
PDBsum; 4CKB; -.
PDBsum; 4CKC; -.
PDBsum; 4CKE; -.
ProteinModelPortal; P04298; -.
SMR; P04298; -.
DIP; DIP-60664N; -.
IntAct; P04298; 1.
GeneID; 3707562; -.
KEGG; vg:3707562; -.
OrthoDB; VOG0900001L; -.
SABIO-RK; P04298; -.
EvolutionaryTrace; P04298; -.
Proteomes; UP000000344; Genome.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IMP:UniProtKB.
GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0050355; F:triphosphatase activity; IMP:UniProtKB.
GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR019602; mRNA_cap_ATPase/GuylTrfase_vir.
InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF10640; Pox_ATPase-GT; 1.
Pfam; PF03291; Pox_MCEL; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51562; RNA_CAP0_MT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
GTP-binding; Hydrolase; Metal-binding; Methyltransferase;
mRNA capping; mRNA processing; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
RNA-binding; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transcription termination; Transferase;
Virion.
CHAIN 1 844 mRNA-capping enzyme catalytic subunit.
/FTId=PRO_0000210124.
DOMAIN 516 844 mRNA cap 0 methyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
REGION 1 539 Triphosphatase-guanylyltransferase.
REGION 549 550 S-adenosyl-L-methionine binding.
REGION 569 570 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
REGION 678 680 S-adenosyl-L-methionine binding.
ACT_SITE 260 260 N6-GMP-lysine intermediate.
{ECO:0000255}.
METAL 37 37 Magnesium; Catalytic; for RNA
triphosphatase activity. {ECO:0000255,
ECO:0000305|PubMed:24607143}.
METAL 39 39 Magnesium; Catalytic; for RNA
triphosphatase activity. {ECO:0000255,
ECO:0000305|PubMed:24607143}.
METAL 192 192 Magnesium; Catalytic; for RNA
triphosphatase activity. {ECO:0000255,
ECO:0000305|PubMed:24607143}.
METAL 194 194 Magnesium; Catalytic; for RNA
triphosphatase activity. {ECO:0000255,
ECO:0000305|PubMed:24607143}.
BINDING 573 573 S-adenosyl-L-methionine.
BINDING 598 598 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 620 620 S-adenosyl-L-methionine.
BINDING 682 682 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 763 763 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 836 836 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 77 77 Essential for RNA triphosphatase
activity.
SITE 107 107 Essential for RNA triphosphatase
activity.
SITE 126 126 Essential for RNA triphosphatase
activity.
SITE 159 159 Essential for RNA triphosphatase
activity.
SITE 161 161 Essential for RNA triphosphatase
activity.
SITE 607 607 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 632 632 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
VARIANT 705 705 G -> D (in strain: mutant Dts36).
MUTAGEN 77 79 RTK->ATA: Almost complete loss of RNA
triphosphatase activity, 70% loss of
guanylyltransferase activity.
{ECO:0000269|PubMed:8709242}.
MUTAGEN 107 107 K->A: Complete loss of triphosphatase
activity, no effect on
guanylyltransferase activity.
{ECO:0000269|PubMed:12726733}.
MUTAGEN 126 126 E->A: Complete loss of triphosphatase
activity, no effect on
guanylyltransferase activity.
{ECO:0000269|PubMed:12726733}.
MUTAGEN 135 136 KK->AA: 70% loss of RNA triphosphatase
activity, 40% loss of guanylyltransferase
activity. {ECO:0000269|PubMed:8709242}.
MUTAGEN 159 159 D->A: Complete loss of triphosphatase
activity, no effect on
guanylyltransferase activity.
{ECO:0000269|PubMed:12726733}.
MUTAGEN 161 161 K->A: Complete loss of triphosphatase
activity, no effect on
guanylyltransferase activity.
{ECO:0000269|PubMed:12726733}.
MUTAGEN 192 194 EIE->AIA: Complete loss of RNA
triphosphatase activity, 50% loss of
guanylyltransferase activity.
{ECO:0000269|PubMed:8709242}.
MUTAGEN 260 260 K->A: Complete loss of
guanylyltransferase activity, no effect
on RNA triphosphatase activity.
{ECO:0000269|PubMed:8709242}.
MUTAGEN 524 526 KIG->AIA: 50% loss of RNA triphosphatase
activity and 40% loss of
guanylyltransferase activity.
{ECO:0000269|PubMed:8709242}.
MUTAGEN 570 570 N->A: Retains substantial
methyltransferase activity in vitro;
lethal in vivo.
{ECO:0000269|PubMed:18256245}.
MUTAGEN 573 573 K->A: Complete loss of methyltransferase
activity; lethal in vivo.
{ECO:0000269|PubMed:18256245}.
MUTAGEN 607 607 K->A: Retains substantial
methyltransferase activity in vitro;
lethal in vivo.
{ECO:0000269|PubMed:18256245}.
MUTAGEN 608 608 Y->A: Almost complete loss of
methyltransferase activity; lethal in
vivo. {ECO:0000269|PubMed:18256245}.
MUTAGEN 676 676 D->A: Complete loss of methyltransferase
activity; lethal in vivo.
{ECO:0000269|PubMed:18256245}.
MUTAGEN 679 679 F->A: Almost complete loss of
methyltransferase activity; lethal in
vivo. {ECO:0000269|PubMed:18256245}.
MUTAGEN 682 682 H->A: Complete loss of methyltransferase
activity; lethal in vivo.
{ECO:0000269|PubMed:18256245}.
MUTAGEN 763 763 E->A: Retains substantial
methyltransferase activity in vitro;
lethal in vivo.
{ECO:0000269|PubMed:18256245}.
HELIX 3 5 {ECO:0000244|PDB:4CKB}.
HELIX 11 24 {ECO:0000244|PDB:4CKB}.
STRAND 36 44 {ECO:0000244|PDB:4CKB}.
HELIX 48 54 {ECO:0000244|PDB:4CKB}.
STRAND 58 69 {ECO:0000244|PDB:4CKB}.
STRAND 71 78 {ECO:0000244|PDB:4CKB}.
HELIX 82 84 {ECO:0000244|PDB:4CKB}.
STRAND 87 89 {ECO:0000244|PDB:4CKB}.
HELIX 92 97 {ECO:0000244|PDB:4CKB}.
STRAND 103 116 {ECO:0000244|PDB:4CKB}.
STRAND 119 130 {ECO:0000244|PDB:4CKB}.
HELIX 134 140 {ECO:0000244|PDB:4CKB}.
STRAND 142 152 {ECO:0000244|PDB:4CKB}.
STRAND 154 170 {ECO:0000244|PDB:4CKB}.
HELIX 175 181 {ECO:0000244|PDB:4CKB}.
STRAND 182 185 {ECO:0000244|PDB:4CKE}.
STRAND 188 195 {ECO:0000244|PDB:4CKB}.
STRAND 198 200 {ECO:0000244|PDB:4CKB}.
HELIX 205 220 {ECO:0000244|PDB:4CKB}.
STRAND 226 229 {ECO:0000244|PDB:4CKB}.
STRAND 236 241 {ECO:0000244|PDB:4CKB}.
HELIX 244 247 {ECO:0000244|PDB:4CKB}.
STRAND 255 259 {ECO:0000244|PDB:4CKB}.
STRAND 262 271 {ECO:0000244|PDB:4CKB}.
STRAND 274 279 {ECO:0000244|PDB:4CKB}.
TURN 280 282 {ECO:0000244|PDB:4CKB}.
STRAND 283 288 {ECO:0000244|PDB:4CKB}.
STRAND 298 318 {ECO:0000244|PDB:4CKB}.
HELIX 327 337 {ECO:0000244|PDB:4CKB}.
TURN 338 340 {ECO:0000244|PDB:4CKB}.
STRAND 343 349 {ECO:0000244|PDB:4CKB}.
HELIX 359 369 {ECO:0000244|PDB:4CKB}.
TURN 370 372 {ECO:0000244|PDB:4CKB}.
STRAND 377 384 {ECO:0000244|PDB:4CKB}.
HELIX 385 388 {ECO:0000244|PDB:4CKB}.
STRAND 389 393 {ECO:0000244|PDB:4CKB}.
STRAND 398 405 {ECO:0000244|PDB:4CKB}.
STRAND 422 432 {ECO:0000244|PDB:4CKB}.
STRAND 435 445 {ECO:0000244|PDB:4CKB}.
STRAND 447 453 {ECO:0000244|PDB:4CKB}.
TURN 454 457 {ECO:0000244|PDB:4CKB}.
STRAND 458 465 {ECO:0000244|PDB:4CKB}.
HELIX 466 468 {ECO:0000244|PDB:4CKB}.
STRAND 470 484 {ECO:0000244|PDB:4CKB}.
STRAND 489 492 {ECO:0000244|PDB:4CKB}.
HELIX 494 502 {ECO:0000244|PDB:4CKB}.
STRAND 508 510 {ECO:0000244|PDB:4CKB}.
HELIX 511 522 {ECO:0000244|PDB:4CKB}.
HELIX 525 527 {ECO:0000244|PDB:4CKB}.
HELIX 563 580 {ECO:0000244|PDB:2VDW}.
TURN 583 585 {ECO:0000244|PDB:2VDW}.
STRAND 593 596 {ECO:0000244|PDB:2VDW}.
TURN 600 604 {ECO:0000244|PDB:2VDW}.
HELIX 605 610 {ECO:0000244|PDB:2VDW}.
STRAND 614 621 {ECO:0000244|PDB:2VDW}.
HELIX 623 636 {ECO:0000244|PDB:2VDW}.
STRAND 646 651 {ECO:0000244|PDB:2VDW}.
STRAND 656 658 {ECO:0000244|PDB:2VDW}.
HELIX 659 664 {ECO:0000244|PDB:2VDW}.
STRAND 672 679 {ECO:0000244|PDB:2VDW}.
HELIX 681 683 {ECO:0000244|PDB:2VDW}.
TURN 687 689 {ECO:0000244|PDB:2VDW}.
HELIX 690 700 {ECO:0000244|PDB:2VDW}.
STRAND 701 712 {ECO:0000244|PDB:2VDW}.
HELIX 714 717 {ECO:0000244|PDB:2VDW}.
STRAND 724 727 {ECO:0000244|PDB:2VDW}.
STRAND 730 732 {ECO:0000244|PDB:2VDW}.
TURN 734 736 {ECO:0000244|PDB:2VDW}.
STRAND 737 741 {ECO:0000244|PDB:2VDW}.
STRAND 743 745 {ECO:0000244|PDB:2VDW}.
STRAND 748 752 {ECO:0000244|PDB:2VDW}.
TURN 754 756 {ECO:0000244|PDB:2VDW}.
STRAND 757 759 {ECO:0000244|PDB:2VDW}.
STRAND 761 764 {ECO:0000244|PDB:2VDW}.
HELIX 768 777 {ECO:0000244|PDB:2VDW}.
STRAND 780 787 {ECO:0000244|PDB:2VDW}.
HELIX 788 793 {ECO:0000244|PDB:2VDW}.
HELIX 796 800 {ECO:0000244|PDB:2VDW}.
HELIX 802 805 {ECO:0000244|PDB:2VDW}.
HELIX 809 823 {ECO:0000244|PDB:2VDW}.
STRAND 826 828 {ECO:0000244|PDB:4CKB}.
HELIX 829 833 {ECO:0000244|PDB:2VDW}.
STRAND 836 843 {ECO:0000244|PDB:2VDW}.
SEQUENCE 844 AA; 96734 MW; 8B9FD3DE836FA6E7 CRC64;
MDANVVSSST IATYIDALAK NASELEQRST AYEINNELEL VFIKPPLITL TNVVNISTIQ
ESFIRFTVTN KEGVKIRTKI PLSKVHGLDV KNVQLVDAID NIVWEKKSLV TENRLHKECL
LRLSTEERHI FLDYKKYGSS IRLELVNLIQ AKTKNFTIDF KLKYFLGSGA QSKSSLLHAI
NHPKSRPNTS LEIEFTPRDN ETVPYDELIK ELTTLSRHIF MASPENVILS PPINAPIKTF
MLPKQDIVGL DLENLYAVTK TDGIPITIRV TSNGLYCYFT HLGYIIRYPV KRIIDSEVVV
FGEAVKDKNW TVYLIKLIEP VNAINDRLEE SKYVESKLVD ICDRIVFKSK KYEGPFTTTS
EVVDMLSTYL PKQPEGVILF YSKGPKSNID FKIKKENTID QTANVVFRYM SSEPIIFGES
SIFVEYKKFS NDKGFPKEYG SGKIVLYNGV NYLNNIYCLE YINTHNEVGI KSVVVPIKFI
AEFLVNGEIL KPRIDKTMKY INSEDYYGNQ HNIIVEHLRD QSIKIGDIFN EDKLSDVGHQ
YANNDKFRLN PEVSYFTNKR TRGPLGILSN YVKTLLISMY CSKTFLDDSN KRKVLAIDFG
NGADLEKYFY GEIALLVATD PDADAIARGN ERYNKLNSGI KTKYYKFDYI QETIRSDTFV
SSVREVFYFG KFNIIDWQFA IHYSFHPRHY ATVMNNLSEL TASGGKVLIT TMDGDKLSKL
TDKKTFIIHK NLPSSENYMS VEKIADDRIV VYNPSTMSTP MTEYIIKKND IVRVFNEYGF
VLVDNVDFAT IIERSKKFIN GASTMEDRPS TRNFFELNRG AIKCEGLDVE DLLSYYVVYV
FSKR


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29-247 U2 auxiliary factor (U2AF), comprised of a large and a small subunit, is a non-snRNP protein required for the binding of U2 snRNP to the pre-mRNA branch site. U2AF2 is the U2AF large subunit which con 0.1 mg
26-565 DCP1B may play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It may remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5' 0.05 mg
29-510 DCP2 is necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. DCP2 removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-pho 0.05 mg
25-352 UPF1 is a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA surveillance. mRNA surveillance detects exported mRNAs with truncated open reading 0.05 mg
18-003-44208 Insulin-like growth factor 2 mRNA-binding protein 1 - IGF2 mRNA-binding protein 1; IGF-II mRNA-binding protein 1; IMP-1; Coding region determinant-binding protein; CRD-BP; VICKZ family member 1 Polycl 0.05 mg Aff Pur
EIAAB38001 Mouse,Mus musculus,Pre-mRNA-splicing factor SF3b 155 kDa subunit,SAP 155,Sap155,Sf3b1,SF3b155,Spliceosome-associated protein 155,Splicing factor 3B subunit 1
EIAAB38003 Kiaa0017,Mouse,Mus musculus,Pre-mRNA-splicing factor SF3b 130 kDa subunit,SAP 130,SF3b130,Sf3b3,Spliceosome-associated protein 130,Splicing factor 3B subunit 3
EIAAB38000 Homo sapiens,Human,Pre-mRNA-splicing factor SF3b 155 kDa subunit,SAP 155,SAP155,SF3B1,SF3b155,Spliceosome-associated protein 155,Splicing factor 3B subunit 1
EIAAB38006 Homo sapiens,Human,Pre-mRNA-splicing factor SF3b 49 kDa subunit,SAP 49,SAP49,SF3B4,SF3b50,Spliceosome-associated protein 49,Splicing factor 3B subunit 4
EIAAB38002 Homo sapiens,Human,Pre-mRNA-splicing factor SF3b 145 kDa subunit,SAP 145,SAP145,SF3b145,SF3b150,SF3B2,Spliceosome-associated protein 145,Splicing factor 3B subunit 2
EIAAB38005 Bos taurus,Bovine,Pre-mRNA-splicing factor SF3b 130 kDa subunit,SAP 130,SF3b130,SF3B3,Spliceosome-associated protein 130,Splicing factor 3B subunit 3
EIAAB09112 Cleavage and polyadenylation specificity factor 73 kDa subunit,Cleavage and polyadenylation specificity factor subunit 3,CPSF 73 kDa subunit,CPSF3,CPSF73,Homo sapiens,Human,mRNA 3'-end-processing endo
EIAAB38004 Homo sapiens,Human,KIAA0017,Pre-mRNA-splicing factor SF3b 130 kDa subunit,SAP 130,SAP130,SF3b130,SF3B3,Spliceosome-associated protein 130,Splicing factor 3B subunit 3,STAF130
EIAAB09110 Bos taurus,Bovine,Cleavage and polyadenylation specificity factor 73 kDa subunit,Cleavage and polyadenylation specificity factor subunit 3,CPSF 73 kDa subunit,CPSF3,CPSF73,mRNA 3'-end-processing endon
18-003-44198 Splicing factor 3B subunit 4 - Spliceosome-associated protein 49; SAP 49; SF3b50; Pre-mRNA-splicing factor SF3b 49 kDa subunit Polyclonal 0.05 mg Aff Pur
18-003-44215 Splicing factor 3B subunit 1 - Spliceosome-associated protein 155; SAP 155; SF3b155; Pre-mRNA-splicing factor SF3b 155 kDa subunit Polyclonal 0.1 mg Protein A
18-003-43556 Splicing factor 3B subunit 1 - Spliceosome-associated protein 155; SAP 155; SF3b155; Pre-mRNA-splicing factor SF3b 155 kDa subunit Polyclonal 0.1 mg Protein A
18-003-43613 Splicing factor 3B subunit 4 - Spliceosome-associated protein 49; SAP 49; SF3b50; Pre-mRNA-splicing factor SF3b 49 kDa subunit Polyclonal 0.1 mg Protein A


 

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