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RNA-directed RNA polymerase L (Protein L) (Large structural protein) (Replicase) (Transcriptase) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56); GDP polyribonucleotidyltransferase (EC 2.7.7.88); Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 (EC 2.1.1.296)]

 L_SENDZ                 Reviewed;        2228 AA.
P06447; P27566; Q84185; Q98705;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
15-MAR-2017, entry version 102.
RecName: Full=RNA-directed RNA polymerase L;
Short=Protein L;
AltName: Full=Large structural protein;
AltName: Full=Replicase;
AltName: Full=Transcriptase;
Includes:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48 {ECO:0000250|UniProtKB:P03523};
Includes:
RecName: Full=mRNA (guanine-N(7)-)-methyltransferase;
EC=2.1.1.56 {ECO:0000269|PubMed:15574411};
Includes:
RecName: Full=GDP polyribonucleotidyltransferase;
EC=2.7.7.88 {ECO:0000250|UniProtKB:P03523};
Includes:
RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2;
EC=2.1.1.296 {ECO:0000250|UniProtKB:P03523};
Name=L;
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Respirovirus.
NCBI_TaxID=11198;
NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
NCBI_TaxID=36483; Cricetidae sp. (Hamster).
NCBI_TaxID=10090; Mus musculus (Mouse).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3005975; DOI=10.1093/nar/14.4.1545;
Shioda T., Iwasaki K., Shibuta H.;
"Determination of the complete nucleotide sequence of the Sendai virus
genome RNA and the predicted amino acid sequences of the F, HN and L
proteins.";
Nucleic Acids Res. 14:1545-1563(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant F1-R, and Mutant ts-f1;
PubMed=2161155; DOI=10.1016/0042-6822(90)90040-X;
Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E.,
Klenk H.-D., Rott R., Seto J.T.;
"Nucleotide sequence analyses of the genes encoding the HN, M, NP, P,
and L proteins of two host range mutants of Sendai virus.";
Virology 176:656-657(1990).
[3]
SEQUENCE REVISION TO 581 AND 971.
Middleton Y.;
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant F1-R / T-5 revertant;
PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D.,
Rott R., Seto J.T.;
"Pneumotropic revertants derived from a pantropic mutant, F1-R, of
Sendai virus.";
Virology 184:227-234(1991).
[5]
INTERACTION WITH P PROTEIN.
PubMed=1321276;
Horikami S.M., Curran J., Kolakofsky D., Moyer S.A.;
"Complexes of Sendai virus NP-P and P-L proteins are required for
defective interfering particle genome replication in vitro.";
J. Virol. 66:4901-4908(1992).
[6]
MUTAGENESIS OF CYS-1571.
PubMed=7645261; DOI=10.1006/viro.1995.1440;
Horikami S.M., Moyer S.A.;
"Alternative amino acids at a single site in the Sendai virus L
protein produce multiple defects in RNA synthesis in vitro.";
Virology 211:577-582(1995).
[7]
INTERACTION WITH P PROTEIN, AND MUTAGENESIS OF 349-THR-SER-350;
354-LYS-ALA-355; ARG-362; THR-363; HIS-366; SER-368; GLU-370 AND
376-ASP-LYS-377.
PubMed=7491760; DOI=10.1006/viro.1995.0008;
Chandrika R., Horikami S.M., Smallwood S., Moyer S.A.;
"Mutations in conserved domain I of the Sendai virus L polymerase
protein uncouple transcription and replication.";
Virology 213:352-363(1995).
[8]
MUTAGENESIS OF 533-ASP--GLU-535; 542-LEU-LYS-543; 544-ASP--LYS-548;
ARG-552; LYS-556; ARG-562 AND GLU-569.
PubMed=10502516; DOI=10.1006/viro.1999.9933;
Smallwood S., Easson C.D., Feller J.A., Horikami S.M., Moyer S.A.;
"Mutations in conserved domain II of the large (L) subunit of the
Sendai virus RNA polymerase abolish RNA synthesis.";
Virology 262:375-383(1999).
[9]
FUNCTION, AND MUTAGENESIS OF 1149-THR-TYR-1150; 1172-GLU--SER-1174;
1208-PRO--ILE-1210; 1220-ASP--ARG-1222; 1254-ASP-GLU-1255;
1293-LYS-ASP-1294; 1303-SER--THR-1305; 1333-LEU-VAL-1334 AND
1351-ARG--LYS-1354.
PubMed=11080486; DOI=10.1006/viro.2000.0615;
Cortese C.K., Feller J.A., Moyer S.A.;
"Mutations in domain V of the Sendai virus L polymerase protein
uncouple transcription and replication and differentially affect
replication in vitro and in vivo.";
Virology 277:387-396(2000).
[10]
MUTAGENESIS OF 943-MET--THR-945; 957-ALA--ALA-959; 963-ASP--ARG-966;
1004-PRO--SER-1006; 1011-THR--ILE-1013; 1023-GLN-GLU-1024;
1036-GLU-THR-1037; 1040-GLU--ASP-1042; 1051-ASP--LYS-1053;
1065-GLY-ASN-1066; 1097-TYR--ILE-1099; 1798-LYS--ARG-1800;
1815-ASP--THR-1817 AND 1838-ARG-GLU-1839.
PubMed=10753721; DOI=10.1006/viro.2000.0234;
Feller J.A., Smallwood S., Horikami S.M., Moyer S.A.;
"Mutations in conserved domains IV and VI of the large (L) subunit of
the Sendai virus RNA polymerase give a spectrum of defective RNA
synthesis phenotypes.";
Virology 269:426-439(2000).
[11]
INTERACTION WITH C PROTEIN.
PubMed=11543662; DOI=10.1006/viro.2001.1068;
Grogan C.C., Moyer S.A.;
"Sendai virus wild-type and mutant C proteins show a direct
correlation between L polymerase binding and inhibition of viral RNA
synthesis.";
Virology 288:96-108(2001).
[12]
INTERACTION WITH P PROTEIN, AND MUTAGENESIS OF 20-SER--VAL-25;
29-ILE--HIS-33; 77-GLN--LYS-81; 173-PHE--PHE-177; 209-TYR--THR-213;
235-LEU--MET-238; 262-ILE--GLY-266; 287-VAL--LEU-291 AND
345-ILE--HIS-347.
PubMed=11861877; DOI=10.1128/JVI.76.6.3078-3083.2002;
Holmes D.E., Moyer S.A.;
"The phosphoprotein (P) binding site resides in the N-terminus of the
L polymerase subunit of Sendai virus.";
J. Virol. 76:3078-3083(2002).
[13]
MUTAGENESIS OF TYR-540; LYS-543; THR-661; ASP-663; LYS-666; CYS-668;
ASN-734; ARG-736; GLY-737; GLY-738; GLU-740; GLY-741 AND GLN-744.
PubMed=12490411; DOI=10.1006/viro.2002.1644;
Smallwood S., Hoevel T., Neubert W.J., Moyer S.A.;
"Different substitutions at conserved amino acids in domains II and
III in the Sendai L RNA polymerase protein inactivate viral RNA
synthesis.";
Virology 304:135-145(2002).
[14]
OLIGOMERIZATION.
PubMed=12954219; DOI=10.1016/S0042-6822(03)00342-8;
Cevik B., Smallwood S., Moyer S.A.;
"The L-L oligomerization domain resides at the very N-terminus of the
Sendai virus L RNA polymerase protein.";
Virology 313:525-536(2003).
[15]
FUNCTION, AND MRNA (GUANINE-N(7)-)-METHYLTRANSFERASE ACTIVITY.
PubMed=15574411; DOI=10.1074/jbc.M411167200;
Ogino T., Kobayashi M., Iwama M., Mizumoto K.;
"Sendai virus RNA-dependent RNA Polymerase L protein catalyzes cap
methylation of virus-specific mRNA.";
J. Biol. Chem. 280:4429-4435(2005).
-!- FUNCTION: RNA-directed RNA polymerase that catalyzes the
transcription of viral mRNAs, their capping and polyadenylation.
The template is composed of the viral RNA tightly encapsidated by
the nucleoprotein (N). The viral polymerase binds to the genomic
RNA at the 3' leader promoter, and transcribes subsequently all
viral mRNAs with a decreasing efficiency. The first gene is the
most transcribed, and the last the least transcribed. The viral
phosphoprotein acts as a processivity factor. Capping is
concommitant with initiation of mRNA transcription. Indeed, a GDP
polyribonucleotidyl transferase (PRNTase) adds the cap structure
when the nascent RNA chain length has reached few nucleotides.
Ribose 2'-O methylation of viral mRNA cap precedes and facilitates
subsequent guanine-N-7 methylation, both activities being carried
by the viral polymerase. Polyadenylation of mRNAs occur by a
stuttering mechanism at a slipery stop site present at the end
viral genes. After finishing transcription of a mRNA, the
polymerase can resume transcription of the downstream gene.
{ECO:0000250|UniProtKB:P03523, ECO:0000269|PubMed:11080486,
ECO:0000269|PubMed:15574411}.
-!- FUNCTION: RNA-directed RNA polymerase that catalyzes the
replication of viral genomic RNA. The template is composed of the
viral RNA tightly encapsidated by the nucleoprotein (N). The
replicase mode is dependent on intracellular N protein
concentration. In this mode, the polymerase replicates the whole
viral genome without recognizing transcriptional signals, and the
replicated genome is not caped or polyadenylated.
{ECO:0000250|UniProtKB:P03523}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000269|PubMed:15574411}.
-!- CATALYTIC ACTIVITY: 5'-triphospho-mRNA + GDP = diphosphate +
guanosine 5'-triphospho-mRNA. {ECO:0000250|UniProtKB:P03523}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5'-(N(7)-methyl
5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-
(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-
methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-
ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA].
{ECO:0000250|UniProtKB:P03523}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6 for mRNA (guanine-N(7)-)-methyltransferase
activity.;
Temperature dependence:
Optimum temperature is 30 degrees Celsius.;
-!- SUBUNIT: Homooligomer. Interacts with the P and C proteins. The L
protein complexes with P protein to form the functional
polymerase. C protein binding to L has an inhibitory effect.
{ECO:0000269|PubMed:11543662, ECO:0000269|PubMed:11861877,
ECO:0000269|PubMed:1321276, ECO:0000269|PubMed:7491760}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
-!- DOMAIN: The N-terminal part (about 1-400) seems to be involved in
binding to the P protein.
-!- MISCELLANEOUS: Least abundant structural protein (approximately 50
copies per virion). Unstable in the absence of P protein.
-!- SIMILARITY: Belongs to the paramyxovirus L protein family.
{ECO:0000305}.
-!- CAUTION: PubMed:11861877 sequence used for mutagenesis is in
conflict with the sequence shown in positions 29, 210, 211, 262,
263 and 264. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA27272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X03614; CAA27272.1; ALT_INIT; Genomic_RNA.
EMBL; X03614; CAA27273.1; -; Genomic_RNA.
EMBL; M30202; AAB06283.1; -; Genomic_RNA.
EMBL; M30203; AAB06289.1; -; Genomic_RNA.
EMBL; M30204; AAB06201.1; -; Genomic_RNA.
EMBL; M69046; AAB06295.1; -; Genomic_RNA.
PIR; A04120; ZLNZSV.
Proteomes; UP000110830; Genome.
Proteomes; UP000163956; Genome.
Proteomes; UP000169749; Genome.
Proteomes; UP000181310; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
InterPro; IPR026890; Mononeg_mRNAcap.
InterPro; IPR014023; Mononeg_RNA_pol_cat.
InterPro; IPR025786; Mononega_L_MeTrfase.
InterPro; IPR016269; RNA-dir_pol_paramyxovirus.
InterPro; IPR024352; RNA-pol_paramyxovirus_C_dom.
Pfam; PF12803; G-7-MTase; 1.
Pfam; PF14318; Mononeg_mRNAcap; 1.
Pfam; PF00946; Mononeg_RNA_pol; 1.
PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PROSITE; PS51590; SAM_MT_MNV_L; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Host cytoplasm; Methyltransferase;
mRNA capping; mRNA processing; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase;
RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase;
Viral RNA replication; Virion.
CHAIN 1 2228 RNA-directed RNA polymerase L.
/FTId=PRO_0000142740.
DOMAIN 656 840 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 1771 1978 Mononegavirus-type SAM-dependent 2'-O-
MTase. {ECO:0000255|PROSITE-
ProRule:PRU00923}.
NP_BIND 1801 1810 ATP. {ECO:0000255}.
REGION 1 174 Oligomerization domain.
REGION 1756 2228 Involved in mRNA cap methylation.
COMPBIAS 2031 2034 Poly-Ser.
VARIANT 96 96 Q -> H (in strain: Mutant F1-R / T-5
revertant, Mutant ts-f1 and Mutant F1-R).
VARIANT 581 581 R -> S (in strain: Mutant F1-R / T-5
revertant, Mutant ts-f1 and Mutant F1-R).
VARIANT 625 625 E -> G (in strain: Mutant F1-R / T-5
revertant and Mutant F1-R).
VARIANT 752 752 I -> M (in strain: Mutant F1-R / T-5
revertant, Mutant ts-f1 and Mutant F1-R).
VARIANT 971 971 D -> G (in strain: Mutant F1-R / T-5
revertant, Mutant ts-f1 and Mutant F1-R).
VARIANT 1207 1207 C -> S (in strain: Mutant F1-R / T-5
revertant, Mutant ts-f1 and Mutant F1-R).
MUTAGEN 20 25 LNSPIV->ANAPAA: Complete loss of P
binding. {ECO:0000269|PubMed:11861877}.
MUTAGEN 29 33 IAQLH->AAAAA: Complete loss of P binding.
{ECO:0000269|PubMed:11861877}.
MUTAGEN 77 81 QRTIK->ASAIA: 80% loss of P binding.
{ECO:0000269|PubMed:11861877}.
MUTAGEN 173 177 FLTWF->AAAWA: Complete loss of P binding.
{ECO:0000269|PubMed:11861877}.
MUTAGEN 209 213 YTLVT->AEAAA: Complete loss of P binding.
{ECO:0000269|PubMed:11861877}.
MUTAGEN 235 238 LVLM->AAAA: Complete loss of P binding.
{ECO:0000269|PubMed:11861877}.
MUTAGEN 262 266 ITSKG->AAGRA: 80% loss of P binding.
{ECO:0000269|PubMed:11861877}.
MUTAGEN 287 291 VIALL->AAAAA: Complete loss of P binding.
{ECO:0000269|PubMed:11861877}.
MUTAGEN 345 347 IFH->AAA: Complete loss of P binding.
{ECO:0000269|PubMed:11861877}.
MUTAGEN 349 350 TS->DD: 46% loss of transcription.
Complete loss of replication.
{ECO:0000269|PubMed:7491760}.
MUTAGEN 354 355 KA->TG: 62% loss of transcription.
complete loss of replication.
{ECO:0000269|PubMed:7491760}.
MUTAGEN 362 362 R->A: Complete loss of transcription and
replication.
{ECO:0000269|PubMed:7491760}.
MUTAGEN 363 363 T->S: Complete loss of transcription and
replication.
{ECO:0000269|PubMed:7491760}.
MUTAGEN 366 366 H->A: Complete loss of transcription and
replication.
{ECO:0000269|PubMed:7491760}.
MUTAGEN 368 368 S->R: Loss of phosphoprotein binding.
Complete loss of transcription and
replication.
{ECO:0000269|PubMed:7491760}.
MUTAGEN 370 370 E->A: No effect.
{ECO:0000269|PubMed:7491760}.
MUTAGEN 376 377 DK->EN: 60% loss of transcription. 22%
loss of replication.
{ECO:0000269|PubMed:7491760}.
MUTAGEN 533 535 DEE->AAA: 75% loss of replication. No
loss of transcription.
{ECO:0000269|PubMed:10502516}.
MUTAGEN 540 540 Y->E,Q: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 540 540 Y->F: 70% loss of transcription.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 542 543 LK->AA: Complete loss of transcription
and replication. No effect on template
binding. {ECO:0000269|PubMed:10502516}.
MUTAGEN 543 543 K->H,I,L,N,P,Q,R,S,T,V: Complete loss of
transcription and replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 544 548 EKEIK->AAAIA: Complete loss of
transcription and replication. No effect
on template binding.
{ECO:0000269|PubMed:10502516}.
MUTAGEN 552 552 R->A: 50% loss of transcription; complete
loss of replication. No effect on
template binding.
{ECO:0000269|PubMed:10502516}.
MUTAGEN 556 556 K->A: Complete loss of transcription and
replication. No effect on template
binding. {ECO:0000269|PubMed:10502516}.
MUTAGEN 562 562 R->A: Complete loss of transcription and
replication. No effect on template
binding. {ECO:0000269|PubMed:10502516}.
MUTAGEN 569 569 E->A: Complete loss of transcription and
replication.
{ECO:0000269|PubMed:10502516}.
MUTAGEN 661 661 T->E,K: Complete loss od transcription
and replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 663 663 D->G,R,S,V,Y: Complete loss of
transcription and replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 666 666 K->A: 80% loss of transcription. Complete
loss of replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 666 666 K->G,L,V: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 666 666 K->R: 76% loss of transcription. 40% loss
of replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 668 668 C->K,L: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 668 668 C->Y: 40% loss of transcription.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 734 734 N->E: 26% loss of transcription. No
effect on replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 736 736 R->D,E,P: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 736 736 R->L,V: 80% loss of transcription. 50%
increase of replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 736 736 R->M: 13% loss of transcription. No
effect on replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 737 737 G->E: Complete loss of transcription. 80%
loss of replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 738 738 G->F: Complete loss of transcription and
replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 740 740 E->S: Complete loss of transcription and
replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 741 741 G->R: Complete loss of transcription and
replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 744 744 Q->K: Complete loss of transcription and
replication.
{ECO:0000269|PubMed:12490411}.
MUTAGEN 943 945 MST->LNM: No effect.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 957 959 AVA->VTS: 38% loss of transcription.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 963 966 DLKR->ALAA: Complete loss of
transcription and replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1004 1006 PHS->VCV: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1011 1013 TII->RLL: 70% loss of transcription and
replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1023 1024 QE->IH: 30% loss of transcription and
replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1036 1037 ET->DD: 25% loss of transcription. 40%
loss of replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1040 1042 EED->AAA: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1051 1053 DRK->AAA: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1065 1066 GN->DH: 14% loss of transcription. 48%
loss of replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1097 1099 YGI->SRV: 16% loss of transcription. 66%
loss of replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1149 1150 TY->AR: 70% loss of transcription.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1172 1174 EGS->RRH: 30% loss of transcription. 27%
loss of replication.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1208 1210 PAI->SSL: 80% loss of transcription.
Complete loss replication.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1220 1222 DER->AAA: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1254 1255 DE->AA: 90% loss of transcription and
replication.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1293 1294 KD->AA: 86% loss of transcription.
Complete loss of replication.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1303 1305 SAT->GTS: 15% loss of replication. 45%
loss of replication.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1333 1334 LV->FI: 77% loss of transcription. 94%
loss of replication.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1351 1354 RYKK->AAAA: Complete loss of
transcription and replication. No effect
on template binding or complex formation
with P protein.
{ECO:0000269|PubMed:11080486}.
MUTAGEN 1571 1571 C->F,L,S: Almost no effect.
{ECO:0000269|PubMed:7645261}.
MUTAGEN 1571 1571 C->F,L: Almost no effect.
{ECO:0000269|PubMed:7645261}.
MUTAGEN 1571 1571 C->G: 80% loss of transcription and
replication.
{ECO:0000269|PubMed:7645261}.
MUTAGEN 1571 1571 C->H,R: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:7645261}.
MUTAGEN 1571 1571 C->T: 30% loss of transcription.
{ECO:0000269|PubMed:7645261}.
MUTAGEN 1571 1571 C->V: 120% increase of transcription. 70%
increase of replication.
{ECO:0000269|PubMed:7645261}.
MUTAGEN 1571 1571 C->Y: 70% loss of transcription. Complete
loss of replication.
{ECO:0000269|PubMed:7645261}.
MUTAGEN 1798 1800 KDR->AAA: 80% loss of transcription. 27%
loss of replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1815 1817 DAT->KEI: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:10753721}.
MUTAGEN 1838 1839 RE->AA: Complete loss of transcription
and replication.
{ECO:0000269|PubMed:10753721}.
SEQUENCE 2228 AA; 252867 MW; 074A4DFE8F8A37B5 CRC64;
MDGQESSQNP SDILYPECHL NSPIVRGKIA QLHVLLDVNQ PYRLKDDSII NITKHKIRNG
GLSPRQIKIR SLGKALQRTI KDLDRYTFEP YPTYSQELLR LDIPEICDKI RSVFAVSDRL
TRELSSGFQD LWLNIFKQLG NIEGREGYDP LQDIGTIPEI TDKYSRNRWY RPFLTWFSIK
YDMRWMQKTR PGGPLDTSNS HNLLECKSYT LVTYGDLVMI LNKLTLTGYI LTPELVLMYC
DVVEGRWNMS AAGHLDKKSI GITSKGEELW ELVDSLFSSL GEEIYNVIAL LEPLSLALIQ
LNDPVIPLRG AFMRHVLTEL QTVLTSRDVY TDAEADTIVE SLLAIFHGTS IDEKAEIFSF
FRTFGHPSLE AVTAADKVRA HMYAQKAIKL KTLYECHAVF CTIIINGYRE RHGGQWPPCD
FPDHVCLELR NAQGSNTAIS YECAVDNYTS FIGFKFRKFI EPQLDEDLTI YMKDKALSPR
KEAWDSVYPD SNLYYKAPES EETRRLIEVF INDENFNPEE IINYVESGDW LKDEEFNISY
SLKEKEIKQE GRLFAKMTYK MRAVQVLAET LLAKGIGELF RENGMVKGEI DLLKRLTTLS
VSGVPRTDSV YNNSKSSEKR NEGMENKNSG GYWDEKKRSR HEFKATDSST DGYETLSCFL
TTDLKKYCLN WRFESTALFG QRCNEIFGFK TFFNWMHPVL ERCTIYVGDP YCPVADRMHR
QLQDHADSGI FIHNPRGGIE GYCQKLWTLI SISAIHLAAV RVGVRVSAMV QGDNQAIAVT
SRVPVAQTYK QKKNHVYEEI TKYFGALRHV MFDVGHELKL NETIISSKMF VYSKRIYYDG
KILPQCLKAL TKCVFWSETL VDENRSACSN ISTSIAKAIE NGYSPILGYC IALYKTCQQV
CISLGMTINP TISPTVRDQY FKGKNWLRCA VLIPANVGGF NYMSTSRCFV RNIGDPAVAA
LADLKRFIRA DLLDKQVLYR VMNQEPGDSS FLDWASDPYS CNLPHSQSIT TIIKNITARS
VLQESPNPLL SGLFTETSGE EDLNLASFLM DRKVILPRVA HEILGNSLTG VREAIAGMLD
TTKSLVRASV RKGGLSYGIL RRLVNYDLLQ YETLTRTLRK PVKDNIEYEY MCSVELAVGL
RQKMWIHLTY GRPIHGLETP DPLELLRGIF IEGSEVCKLC RSEGADPIYT WFYLPDNIDL
DTLTNGCPAI RIPYFGSATD ERSEAQLGYV RNLSKPAKAA IRIAMVYTWA YGTDEISWME
AALIAQTRAN LSLENLKLLT PVSTSTNLSH RLKDTATQMK FSSATLVRAS RFITISNDNM
ALKEAGESKD TNLVYQQIML TGLSLFEFNM RYKKGSLGKP LILHLHLNNG CCIMESPQEA
NIPPRSTLDL EITQENNKLI YDPDPLKDVD LELFSKVRDV VHTVDMTYWS DDEVIRATSI
CTAMTIADTM SQLDRDNLKE MIALVNDDDV NSLITEFMVI DVPLFCSTFG GILVNQFAYS
LYGLNIRGRE EIWGHVVRIL KDTSHAVLKV LSNALSHPKI FKRFWNAGVV EPVYGPNLSN
QDKILLALSV CEYSVDLFMH DWQGGVPLEI FICDNDPDVA DMRRSSFLAR HLAYLCSLAE
ISRDGPRLES MNSLERLESL KSYLELTFLD DPVLRYSQLT GLVIKVFPST LTYIRKSSIK
VLRTRGIGVP EVLEDWDPEA DNALLDGIAA EIQQNIPLGH QTRAPFWGLR VSKSQVLRLR
GYKEITRGEI GRSGVGLTLP FDGRYLSHQL RLFGINSTSC LKALELTYLL SPLVDKDKDR
LYLGEGAGAM LSCYDATLGP CINYYNSGVY SCDVNGQREL NIYPAEVALV GKKLNNVTSL
GQRVKVLFNG NPGSTWIGND ECEALIWNEL QNSSIGLVHC DMEGGDHKDD QVVLHEHYSV
IRIAYLVGDR DVVLISKIAP RLGTDWTRQL SLYLRYWDEV NLIVLKTSNP ASTEMYLLSR
HPKSDIIEDS KTVLASLLPL SKEDSIKIEK WILIEKAKAH EWVTRELREG SSSSGMLRPY
HQALQTFGFE PNLYKLSRDF LSTMNIADTH NCMIAFNRVL KDTIFEWARI TESDKRLKLT
GKYDLYPVRD SGKLKTISRR LVLSWISLSM STRLVTGSFP DQKFEARLQL GIVSLSSREI
RNLRVITKTL LDRFEDIIHS ITYRFLTKEI KILMKILGAV KMFGARQNEY TTVIDDGSLG
DIEPYDSS


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