L_SENDZ
ID L_SENDZ Reviewed; 2228 AA.
AC P06447; P27566; Q84185; Q98705;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=RNA-directed RNA polymerase L;
DE Short=Protein L;
DE AltName: Full=Large structural protein;
DE AltName: Full=Replicase;
DE AltName: Full=Transcriptase;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48 {ECO:0000250|UniProtKB:P28887};
DE Includes:
DE RecName: Full=GTP phosphohydrolase {ECO:0000250|UniProtKB:P03523};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:P03523};
DE Includes:
DE RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000305};
DE EC=2.7.7.88 {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=PRNTase {ECO:0000305};
DE Includes:
DE RecName: Full=mRNA cap methyltransferase {ECO:0000305};
DE EC=2.1.1.375 {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE Short=G-N7-MTase {ECO:0000250|UniProtKB:P03523};
DE AltName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000250|UniProtKB:P03523};
DE Short=N1-2'-O-MTase {ECO:0000250|UniProtKB:P03523};
GN Name=L;
OS Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11198;
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3005975; DOI=10.1093/nar/14.4.1545;
RA Shioda T., Iwasaki K., Shibuta H.;
RT "Determination of the complete nucleotide sequence of the Sendai virus
RT genome RNA and the predicted amino acid sequences of the F, HN and L
RT proteins.";
RL Nucleic Acids Res. 14:1545-1563(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant F1-R, and Mutant ts-f1;
RX PubMed=2161155; DOI=10.1016/0042-6822(90)90040-x;
RA Middleton Y., Tashiro M., Thai T., Oh J., Seymour J., Pritzer E.,
RA Klenk H.-D., Rott R., Seto J.T.;
RT "Nucleotide sequence analyses of the genes encoding the HN, M, NP, P, and L
RT proteins of two host range mutants of Sendai virus.";
RL Virology 176:656-657(1990).
RN [3]
RP SEQUENCE REVISION TO 581 AND 971.
RA Middleton Y.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Mutant F1-R / T-5 revertant;
RX PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
RA Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D., Rott R.,
RA Seto J.T.;
RT "Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai
RT virus.";
RL Virology 184:227-234(1991).
RN [5]
RP INTERACTION WITH P PROTEIN.
RX PubMed=1321276; DOI=10.1128/jvi.66.8.4901-4908.1992;
RA Horikami S.M., Curran J., Kolakofsky D., Moyer S.A.;
RT "Complexes of Sendai virus NP-P and P-L proteins are required for defective
RT interfering particle genome replication in vitro.";
RL J. Virol. 66:4901-4908(1992).
RN [6]
RP MUTAGENESIS OF CYS-1571.
RX PubMed=7645261; DOI=10.1006/viro.1995.1440;
RA Horikami S.M., Moyer S.A.;
RT "Alternative amino acids at a single site in the Sendai virus L protein
RT produce multiple defects in RNA synthesis in vitro.";
RL Virology 211:577-582(1995).
RN [7]
RP INTERACTION WITH P PROTEIN, AND MUTAGENESIS OF 349-THR-SER-350;
RP 354-LYS-ALA-355; ARG-362; THR-363; HIS-366; SER-368; GLU-370 AND
RP 376-ASP-LYS-377.
RX PubMed=7491760; DOI=10.1006/viro.1995.0008;
RA Chandrika R., Horikami S.M., Smallwood S., Moyer S.A.;
RT "Mutations in conserved domain I of the Sendai virus L polymerase protein
RT uncouple transcription and replication.";
RL Virology 213:352-363(1995).
RN [8]
RP MUTAGENESIS OF 533-ASP--GLU-535; 542-LEU-LYS-543; 544-ASP--LYS-548;
RP ARG-552; LYS-556; ARG-562 AND GLU-569.
RX PubMed=10502516; DOI=10.1006/viro.1999.9933;
RA Smallwood S., Easson C.D., Feller J.A., Horikami S.M., Moyer S.A.;
RT "Mutations in conserved domain II of the large (L) subunit of the Sendai
RT virus RNA polymerase abolish RNA synthesis.";
RL Virology 262:375-383(1999).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF 1149-THR-TYR-1150; 1172-GLU--SER-1174;
RP 1208-PRO--ILE-1210; 1220-ASP--ARG-1222; 1254-ASP-GLU-1255;
RP 1293-LYS-ASP-1294; 1303-SER--THR-1305; 1333-LEU-VAL-1334 AND
RP 1351-ARG--LYS-1354.
RX PubMed=11080486; DOI=10.1006/viro.2000.0615;
RA Cortese C.K., Feller J.A., Moyer S.A.;
RT "Mutations in domain V of the Sendai virus L polymerase protein uncouple
RT transcription and replication and differentially affect replication in
RT vitro and in vivo.";
RL Virology 277:387-396(2000).
RN [10]
RP MUTAGENESIS OF 943-MET--THR-945; 957-ALA--ALA-959; 963-ASP--ARG-966;
RP 1004-PRO--SER-1006; 1011-THR--ILE-1013; 1023-GLN-GLU-1024;
RP 1036-GLU-THR-1037; 1040-GLU--ASP-1042; 1051-ASP--LYS-1053;
RP 1065-GLY-ASN-1066; 1097-TYR--ILE-1099; 1798-LYS--ARG-1800;
RP 1815-ASP--THR-1817 AND 1838-ARG-GLU-1839.
RX PubMed=10753721; DOI=10.1006/viro.2000.0234;
RA Feller J.A., Smallwood S., Horikami S.M., Moyer S.A.;
RT "Mutations in conserved domains IV and VI of the large (L) subunit of the
RT Sendai virus RNA polymerase give a spectrum of defective RNA synthesis
RT phenotypes.";
RL Virology 269:426-439(2000).
RN [11]
RP INTERACTION WITH C PROTEIN.
RX PubMed=11543662; DOI=10.1006/viro.2001.1068;
RA Grogan C.C., Moyer S.A.;
RT "Sendai virus wild-type and mutant C proteins show a direct correlation
RT between L polymerase binding and inhibition of viral RNA synthesis.";
RL Virology 288:96-108(2001).
RN [12]
RP INTERACTION WITH P PROTEIN, AND MUTAGENESIS OF 20-SER--VAL-25;
RP 29-ILE--HIS-33; 77-GLN--LYS-81; 173-PHE--PHE-177; 209-TYR--THR-213;
RP 235-LEU--MET-238; 262-ILE--GLY-266; 287-VAL--LEU-291 AND 345-ILE--HIS-347.
RX PubMed=11861877; DOI=10.1128/jvi.76.6.3078-3083.2002;
RA Holmes D.E., Moyer S.A.;
RT "The phosphoprotein (P) binding site resides in the N-terminus of the L
RT polymerase subunit of Sendai virus.";
RL J. Virol. 76:3078-3083(2002).
RN [13]
RP MUTAGENESIS OF TYR-540; LYS-543; THR-661; ASP-663; LYS-666; CYS-668;
RP ASN-734; ARG-736; GLY-737; GLY-738; GLU-740; GLY-741 AND GLN-744.
RX PubMed=12490411; DOI=10.1006/viro.2002.1644;
RA Smallwood S., Hoevel T., Neubert W.J., Moyer S.A.;
RT "Different substitutions at conserved amino acids in domains II and III in
RT the Sendai L RNA polymerase protein inactivate viral RNA synthesis.";
RL Virology 304:135-145(2002).
RN [14]
RP OLIGOMERIZATION.
RX PubMed=12954219; DOI=10.1016/s0042-6822(03)00342-8;
RA Cevik B., Smallwood S., Moyer S.A.;
RT "The L-L oligomerization domain resides at the very N-terminus of the
RT Sendai virus L RNA polymerase protein.";
RL Virology 313:525-536(2003).
RN [15]
RP FUNCTION, AND MRNA (GUANINE-N(7)-)-METHYLTRANSFERASE ACTIVITY.
RX PubMed=15574411; DOI=10.1074/jbc.m411167200;
RA Ogino T., Kobayashi M., Iwama M., Mizumoto K.;
RT "Sendai virus RNA-dependent RNA Polymerase L protein catalyzes cap
RT methylation of virus-specific mRNA.";
RL J. Biol. Chem. 280:4429-4435(2005).
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC of viral mRNAs, their capping and polyadenylation. The template is
CC composed of the viral RNA tightly encapsidated by the nucleoprotein
CC (N). The viral polymerase binds to the genomic RNA at the 3' leader
CC promoter, and transcribes subsequently all viral mRNAs with a
CC decreasing efficiency. The first gene is the most transcribed, and the
CC last the least transcribed. The viral phosphoprotein acts as a
CC processivity factor. Capping is concommitant with initiation of mRNA
CC transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase)
CC adds the cap structure when the nascent RNA chain length has reached
CC few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and
CC facilitates subsequent guanine-N-7 methylation, both activities being
CC carried by the viral polymerase. Polyadenylation of mRNAs occur by a
CC stuttering mechanism at a slipery stop site present at the end viral
CC genes. After finishing transcription of a mRNA, the polymerase can
CC resume transcription of the downstream gene.
CC {ECO:0000250|UniProtKB:P03523, ECO:0000269|PubMed:11080486,
CC ECO:0000269|PubMed:15574411}.
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of
CC viral genomic RNA. The template is composed of the viral RNA tightly
CC encapsidated by the nucleoprotein (N). The replicase mode is dependent
CC on intracellular N protein concentration. In this mode, the polymerase
CC replicates the whole viral genome without recognizing transcriptional
CC signals, and the replicated genome is not caped or polyadenylated.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl
CC 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375;
CC Evidence={ECO:0000269|PubMed:15574411};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-
CC triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156482, ChEBI:CHEBI:156484;
CC Evidence={ECO:0000269|PubMed:15574411};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in
CC mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-
CC adenylyl-cytidylyl-adenosine in mRNA + diphosphate;
CC Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88;
CC Evidence={ECO:0000250|UniProtKB:P28887};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a
CC 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482,
CC ChEBI:CHEBI:156483; Evidence={ECO:0000250|UniProtKB:P03523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P28887};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6 for mRNA (guanine-N(7)-)-methyltransferase activity.;
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.;
CC -!- SUBUNIT: Homooligomer. Interacts with the P and C proteins. The L
CC protein complexes with P protein to form the functional polymerase. C
CC protein binding to L has an inhibitory effect.
CC {ECO:0000269|PubMed:11543662, ECO:0000269|PubMed:11861877,
CC ECO:0000269|PubMed:1321276, ECO:0000269|PubMed:7491760}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
CC -!- DOMAIN: The N-terminal part (about 1-400) seems to be involved in
CC binding to the P protein.
CC -!- MISCELLANEOUS: Least abundant structural protein (approximately 50
CC copies per virion). Unstable in the absence of P protein.
CC -!- SIMILARITY: Belongs to the paramyxovirus L protein family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:11861877 sequence used for mutagenesis is in conflict
CC with the sequence shown in positions 29, 210, 211, 262, 263 and 264.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27272.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X03614; CAA27272.1; ALT_INIT; Genomic_RNA.
DR EMBL; X03614; CAA27273.1; -; Genomic_RNA.
DR EMBL; M30202; AAB06283.1; -; Genomic_RNA.
DR EMBL; M30203; AAB06289.1; -; Genomic_RNA.
DR EMBL; M30204; AAB06201.1; -; Genomic_RNA.
DR EMBL; M69046; AAB06295.1; -; Genomic_RNA.
DR PIR; A04120; ZLNZSV.
DR SMR; P06447; -.
DR PRIDE; P06447; -.
DR Proteomes; UP000110830; Genome.
DR Proteomes; UP000163956; Genome.
DR Proteomes; UP000169749; Genome.
DR Proteomes; UP000181310; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR024352; L_methyltrans_paramyxo.
DR InterPro; IPR039736; L_poly_C.
DR InterPro; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR InterPro; IPR025786; Mononega_L_MeTrfase.
DR InterPro; IPR016269; RNA-dir_pol_paramyxovirus.
DR Pfam; PF12803; G-7-MTase; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
DR TIGRFAMs; TIGR04198; paramyx_RNAcap; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Host cytoplasm; Hydrolase; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2228
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000142740"
FT DOMAIN 656..840
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1771..1978
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT REGION 1..174
FT /note="Oligomerization domain"
FT REGION 610..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1756..2228
FT /note="Involved in mRNA cap methylation"
FT COMPBIAS 613..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1801..1810
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 96
FT /note="Q -> H (in strain: Mutant F1-R / T-5 revertant,
FT Mutant ts-f1 and Mutant F1-R)"
FT VARIANT 581
FT /note="R -> S (in strain: Mutant F1-R / T-5 revertant,
FT Mutant ts-f1 and Mutant F1-R)"
FT VARIANT 625
FT /note="E -> G (in strain: Mutant F1-R / T-5 revertant and
FT Mutant F1-R)"
FT VARIANT 752
FT /note="I -> M (in strain: Mutant F1-R / T-5 revertant,
FT Mutant ts-f1 and Mutant F1-R)"
FT VARIANT 971
FT /note="D -> G (in strain: Mutant F1-R / T-5 revertant,
FT Mutant ts-f1 and Mutant F1-R)"
FT VARIANT 1207
FT /note="C -> S (in strain: Mutant F1-R / T-5 revertant,
FT Mutant ts-f1 and Mutant F1-R)"
FT MUTAGEN 20..25
FT /note="LNSPIV->ANAPAA: Complete loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 29..33
FT /note="IAQLH->AAAAA: Complete loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 77..81
FT /note="QRTIK->ASAIA: 80% loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 173..177
FT /note="FLTWF->AAAWA: Complete loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 209..213
FT /note="YTLVT->AEAAA: Complete loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 235..238
FT /note="LVLM->AAAA: Complete loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 262..266
FT /note="ITSKG->AAGRA: 80% loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 287..291
FT /note="VIALL->AAAAA: Complete loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 345..347
FT /note="IFH->AAA: Complete loss of P binding."
FT /evidence="ECO:0000269|PubMed:11861877"
FT MUTAGEN 349..350
FT /note="TS->DD: 46% loss of transcription. Complete loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:7491760"
FT MUTAGEN 354..355
FT /note="KA->TG: 62% loss of transcription. complete loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:7491760"
FT MUTAGEN 362
FT /note="R->A: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:7491760"
FT MUTAGEN 363
FT /note="T->S: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:7491760"
FT MUTAGEN 366
FT /note="H->A: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:7491760"
FT MUTAGEN 368
FT /note="S->R: Loss of phosphoprotein binding. Complete loss
FT of transcription and replication."
FT /evidence="ECO:0000269|PubMed:7491760"
FT MUTAGEN 370
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:7491760"
FT MUTAGEN 376..377
FT /note="DK->EN: 60% loss of transcription. 22% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:7491760"
FT MUTAGEN 533..535
FT /note="DEE->AAA: 75% loss of replication. No loss of
FT transcription."
FT /evidence="ECO:0000269|PubMed:10502516"
FT MUTAGEN 540
FT /note="Y->E,Q: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 540
FT /note="Y->F: 70% loss of transcription."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 542..543
FT /note="LK->AA: Complete loss of transcription and
FT replication. No effect on template binding."
FT /evidence="ECO:0000269|PubMed:10502516"
FT MUTAGEN 543
FT /note="K->H,I,L,N,P,Q,R,S,T,V: Complete loss of
FT transcription and replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 544..548
FT /note="EKEIK->AAAIA: Complete loss of transcription and
FT replication. No effect on template binding."
FT /evidence="ECO:0000269|PubMed:10502516"
FT MUTAGEN 552
FT /note="R->A: 50% loss of transcription; complete loss of
FT replication. No effect on template binding."
FT /evidence="ECO:0000269|PubMed:10502516"
FT MUTAGEN 556
FT /note="K->A: Complete loss of transcription and
FT replication. No effect on template binding."
FT /evidence="ECO:0000269|PubMed:10502516"
FT MUTAGEN 562
FT /note="R->A: Complete loss of transcription and
FT replication. No effect on template binding."
FT /evidence="ECO:0000269|PubMed:10502516"
FT MUTAGEN 569
FT /note="E->A: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:10502516"
FT MUTAGEN 661
FT /note="T->E,K: Complete loss od transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 663
FT /note="D->G,R,S,V,Y: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 666
FT /note="K->A: 80% loss of transcription. Complete loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 666
FT /note="K->G,L,V: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 666
FT /note="K->R: 76% loss of transcription. 40% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 668
FT /note="C->K,L: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 668
FT /note="C->Y: 40% loss of transcription."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 734
FT /note="N->E: 26% loss of transcription. No effect on
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 736
FT /note="R->D,E,P: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 736
FT /note="R->L,V: 80% loss of transcription. 50% increase of
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 736
FT /note="R->M: 13% loss of transcription. No effect on
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 737
FT /note="G->E: Complete loss of transcription. 80% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 738
FT /note="G->F: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 740
FT /note="E->S: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 741
FT /note="G->R: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 744
FT /note="Q->K: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:12490411"
FT MUTAGEN 943..945
FT /note="MST->LNM: No effect."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 957..959
FT /note="AVA->VTS: 38% loss of transcription."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 963..966
FT /note="DLKR->ALAA: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1004..1006
FT /note="PHS->VCV: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1011..1013
FT /note="TII->RLL: 70% loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1023..1024
FT /note="QE->IH: 30% loss of transcription and replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1036..1037
FT /note="ET->DD: 25% loss of transcription. 40% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1040..1042
FT /note="EED->AAA: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1051..1053
FT /note="DRK->AAA: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1065..1066
FT /note="GN->DH: 14% loss of transcription. 48% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1097..1099
FT /note="YGI->SRV: 16% loss of transcription. 66% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1149..1150
FT /note="TY->AR: 70% loss of transcription."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1172..1174
FT /note="EGS->RRH: 30% loss of transcription. 27% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1208..1210
FT /note="PAI->SSL: 80% loss of transcription. Complete loss
FT replication."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1220..1222
FT /note="DER->AAA: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1254..1255
FT /note="DE->AA: 90% loss of transcription and replication."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1293..1294
FT /note="KD->AA: 86% loss of transcription. Complete loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1303..1305
FT /note="SAT->GTS: 15% loss of replication. 45% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1333..1334
FT /note="LV->FI: 77% loss of transcription. 94% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1351..1354
FT /note="RYKK->AAAA: Complete loss of transcription and
FT replication. No effect on template binding or complex
FT formation with P protein."
FT /evidence="ECO:0000269|PubMed:11080486"
FT MUTAGEN 1571
FT /note="C->F,L,S: Almost no effect."
FT /evidence="ECO:0000269|PubMed:7645261"
FT MUTAGEN 1571
FT /note="C->F,L: Almost no effect."
FT /evidence="ECO:0000269|PubMed:7645261"
FT MUTAGEN 1571
FT /note="C->G: 80% loss of transcription and replication."
FT /evidence="ECO:0000269|PubMed:7645261"
FT MUTAGEN 1571
FT /note="C->H,R: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:7645261"
FT MUTAGEN 1571
FT /note="C->T: 30% loss of transcription."
FT /evidence="ECO:0000269|PubMed:7645261"
FT MUTAGEN 1571
FT /note="C->V: 120% increase of transcription. 70% increase
FT of replication."
FT /evidence="ECO:0000269|PubMed:7645261"
FT MUTAGEN 1571
FT /note="C->Y: 70% loss of transcription. Complete loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:7645261"
FT MUTAGEN 1798..1800
FT /note="KDR->AAA: 80% loss of transcription. 27% loss of
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1815..1817
FT /note="DAT->KEI: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
FT MUTAGEN 1838..1839
FT /note="RE->AA: Complete loss of transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:10753721"
SQ 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
