RNA-directed RNA polymerase
     (EC 2.7.7.48)
mRNA (guanine-N(7)-)-methyltransferase
     (EC 2.1.1.56)
mRNA guanylyltransferase
     (EC 2.7.7.-)

Gene name

Name:

From

Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))

[TaxID: 11198]

Taxonomy

Viruses; ssRNA negative-strand viruses; Mononegavirales; Paramyxoviridae; Paramyxovirinae; Respirovirus.

Virus hosts

Cavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]
Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. DOI=10.1093/nar/14.4.1545; PubMed=3005975 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1016/0042-6822(90)90040-X; PubMed=2161155 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1016/0042-6822(91)90839-4; PubMed=1651590 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1006/viro.1995.1440; PubMed=7645261 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1006/viro.1995.0008; PubMed=7491760 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1006/viro.1999.9933; PubMed=10502516 [NCBI, ExPASy, EBI, Israel, Japan] 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]	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. DOI=10.1006/viro.2000.0615; PubMed=11080486 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1006/viro.2000.0234; PubMed=10753721 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1006/viro.2001.1068; PubMed=11543662 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1128/JVI.76.6.3078-3083.2002; PubMed=11861877 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1006/viro.2002.1644; PubMed=12490411 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/S0042-6822(03)00342-8; PubMed=12954219 [NCBI, ExPASy, EBI, Israel, Japan] 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]	MRNA (GUANINE-N(7)-)-METHYLTRANSFERASE ACTIVITY. DOI=10.1074/jbc.M411167200; PubMed=15574411 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Displays RNA-directed RNA polymerase, mRNA guanylyl transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A) synthetase activities. The viral mRNA guanylyl transferase displays a different biochemical reaction than the cellular enzyme. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). Functions either as transcriptase or as replicase. The transcriptase synthesizes subsequently six subgenomic RNAs, assuring their capping and polyadenylation by a stuttering mechanism. The transcriptase stutters on a specific sequence, resulting on a cotranscriptional editing of the phosphoprotein (P) mRNA. The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing the transcriptional signals. 5' GpppApGpG sequence is required for mRNA cap methylation by the enzyme.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m₇G(5')pppR-RNA.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 6 for mRNA (guanine-N⁷-)-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.
SUBCELLULAR LOCATION: Virion (Potential). 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 paramyxoviruses L protein family.
SIMILARITY: Contains 1 RdRp catalytic domain.
CAUTION: PubMed:11861877 sequence used for mutagenesis is in conflict with the sequence shown in positions 29, 210, 211, 262, 263 and 264.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X03614; CAA27272.1; ALT_INIT; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03614; CAA27273.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30202; AAB06283.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30203; AAB06289.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30204; AAB06201.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M69046; AAB06295.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A04120; ZLNZSV.

3D structure databases

ModBase

P06447.

Family and domain databases

InterPro

IPR016269; RNA-dir_RNA_pol_paramyxovir.
IPR014023; RNA_pol_cat.
IPR001016; RNA_pol_L_viral.
Graphical view of domain structure.

Pfam

PF00946; Paramyx_RNA_pol; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000830; RNA_pol_ParamyxoV; 1.

PROSITE

PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Cytoplasm; Methyltransferase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase; RNA replication; RNA-directed RNA polymerase; S-adenosyl-L-methionine; Transferase; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 2228`	`2228`	`Large structural protein.`	`PRO_0000142740`
`DOMAIN`	`656 840`	`185`	`RdRp catalytic.`
`NP_BIND`	`1801 1810`	`10`	`ATP (Potential).`
`REGION`	`1 174`	`174`	`Oligomerization domain.`
`REGION`	`1756 2228`	`473`	`Involved in mRNA cap methylation.`
`COMPBIAS`	`2031 2034`	`4`	`Poly-Ser.`
`VARIANT`	`96 96`	`1`	`Q -> H (in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R).`
`VARIANT`	`581 581`	`1`	`R -> S (in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R).`
`VARIANT`	`625 625`	`1`	`E -> G (in strain: Mutant F1-R / T-5 revertant and Mutant F1-R).`
`VARIANT`	`752 752`	`1`	`I -> M (in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R).`
`VARIANT`	`971 971`	`1`	`D -> G (in strain: Mutant F1-R / T-5 revertant, Mutant ts-f1 and Mutant F1-R).`
`VARIANT`	`1207 1207`	`1`	`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.`
`MUTAGEN`	`29 33`		`IAQLH->AAAAA: Complete loss of P binding.`
`MUTAGEN`	`77 81`		`QRTIK->ASAIA: 80% loss of P binding.`
`MUTAGEN`	`173 177`		`FLTWF->AAAWA: Complete loss of P binding.`
`MUTAGEN`	`209 213`		`YTLVT->AEAAA: Complete loss of P binding.`
`MUTAGEN`	`235 238`		`LVLM->AAAA: Complete loss of P binding.`
`MUTAGEN`	`262 266`		`ITSKG->AAGRA: 80% loss of P binding.`
`MUTAGEN`	`287 291`		`VIALL->AAAAA: Complete loss of P binding.`
`MUTAGEN`	`345 347`		`IFH->AAA: Complete loss of P binding.`
`MUTAGEN`	`349 350`		`TS->DD: 46% loss of transcription. Complete loss of replication.`
`MUTAGEN`	`354 355`		`KA->TG: 62% loss of transcription. complete loss of replication.`
`MUTAGEN`	`362 362`		`R->A: Complete loss of transcription and replication.`
`MUTAGEN`	`363 363`		`T->S: Complete loss of transcription and replication.`
`MUTAGEN`	`366 366`		`H->A: Complete loss of transcription and replication.`
`MUTAGEN`	`368 368`		`S->R: Loss of phosphoprotein binding. Complete loss of transcription and replication.`
`MUTAGEN`	`370 370`		`E->A: No effect.`
`MUTAGEN`	`376 377`		`DK->EN: 60% loss of transcription. 22% loss of replication.`
`MUTAGEN`	`533 535`		`DEE->AAA: 75% loss of replication. No loss of transcription.`
`MUTAGEN`	`540 540`		`Y->E,Q: Complete loss of transcription and replication.`
`MUTAGEN`	`540 540`		`Y->F: 70% loss of transcription.`
`MUTAGEN`	`542 543`		`LK->AA: Complete loss of transcription and replication. No effect on template binding.`
`MUTAGEN`	`543 543`		`K->H,I,L,N,P,Q,R,S,T,V: Complete loss of transcription and replication.`
`MUTAGEN`	`544 548`		`EKEIK->AAAIA: Complete loss of transcription and replication. No effect on template binding.`
`MUTAGEN`	`552 552`		`R->A: 50% loss of transcription; complete loss of replication. No effect on template binding.`
`MUTAGEN`	`556 556`		`K->A: Complete loss of transcription and replication. No effect on template binding.`
`MUTAGEN`	`562 562`		`R->A: Complete loss of transcription and replication. No effect on template binding.`
`MUTAGEN`	`569 569`		`E->A: Complete loss of transcription and replication.`
`MUTAGEN`	`661 661`		`T->E,K: Complete loss od transcription and replication.`
`MUTAGEN`	`663 663`		`D->G,R,S,V,Y: Complete loss of transcription and replication.`
`MUTAGEN`	`666 666`		`K->A: 80% loss of transcription. Complete loss of replication.`
`MUTAGEN`	`666 666`		`K->G,L,V: Complete loss of transcription and replication.`
`MUTAGEN`	`666 666`		`K->R: 76% loss of transcription. 40% loss of replication.`
`MUTAGEN`	`668 668`		`C->K,L: Complete loss of transcription and replication.`
`MUTAGEN`	`668 668`		`C->Y: 40% loss of transcription.`
`MUTAGEN`	`734 734`		`N->E: 26% loss of transcription. No effect on replication.`
`MUTAGEN`	`736 736`		`R->D,E,P: Complete loss of transcription and replication.`
`MUTAGEN`	`736 736`		`R->L,V: 80% loss of transcription. 50% increase of replication.`
`MUTAGEN`	`736 736`		`R->M: 13% loss of transcription. No effect on replication.`
`MUTAGEN`	`737 737`		`G->E: Complete loss of transcription. 80% loss of replication.`
`MUTAGEN`	`738 738`		`G->F: Complete loss of transcription and replication.`
`MUTAGEN`	`740 740`		`E->S: Complete loss of transcription and replication.`
`MUTAGEN`	`741 741`		`G->R: Complete loss of transcription and replication.`
`MUTAGEN`	`744 744`		`Q->K: Complete loss of transcription and replication.`
`MUTAGEN`	`943 945`		`MST->LNM: No effect.`
`MUTAGEN`	`957 959`		`AVA->VTS: 38% loss of transcription.`
`MUTAGEN`	`963 966`		`DLKR->ALAA: Complete loss of transcription and replication.`
`MUTAGEN`	`1004 1006`		`PHS->VCV: Complete loss of transcription and replication.`
`MUTAGEN`	`1011 1013`		`TII->RLL: 70% loss of transcription and replication.`
`MUTAGEN`	`1023 1024`		`QE->IH: 30% loss of transcription and replication.`
`MUTAGEN`	`1036 1037`		`ET->DD: 25% loss of transcription. 40% loss of replication.`
`MUTAGEN`	`1040 1042`		`EED->AAA: Complete loss of transcription and replication.`
`MUTAGEN`	`1051 1053`		`DRK->AAA: Complete loss of transcription and replication.`
`MUTAGEN`	`1065 1066`		`GN->DH: 14% loss of transcription. 48% loss of replication.`
`MUTAGEN`	`1097 1099`		`YGI->SRV: 16% loss of transcription. 66% loss of replication.`
`MUTAGEN`	`1149 1150`		`TY->AR: 70% loss of transcription.`
`MUTAGEN`	`1172 1174`		`EGS->RRH: 30% loss of transcription. 27% loss of replication.`
`MUTAGEN`	`1208 1210`		`PAI->SSL: 80% loss of transcription. Complete loss replication.`
`MUTAGEN`	`1220 1222`		`DER->AAA: Complete loss of transcription and replication.`
`MUTAGEN`	`1254 1255`		`DE->AA: 90% loss of transcription and replication.`
`MUTAGEN`	`1293 1294`		`KD->AA: 86% loss of transcription. Complete loss of replication.`
`MUTAGEN`	`1303 1305`		`SAT->GTS: 15% loss of replication. 45% loss of replication.`
`MUTAGEN`	`1333 1334`		`LV->FI: 77% loss of transcription. 94% loss of replication.`
`MUTAGEN`	`1351 1354`		`RYKK->AAAA: Complete loss of transcription and replication. No effect on template binding or complex formation with P protein.`
`MUTAGEN`	`1571 1571`		`C->F,L,S: Almost no effect.`
`MUTAGEN`	`1571 1571`		`C->F,L: Almost no effect.`
`MUTAGEN`	`1571 1571`		`C->G: 80% loss of transcription and replication.`
`MUTAGEN`	`1571 1571`		`C->H,R: Complete loss of transcription and replication.`
`MUTAGEN`	`1571 1571`		`C->T: 30% loss of transcription.`
`MUTAGEN`	`1571 1571`		`C->V: 120% increase of transcription. 70% increase of replication.`
`MUTAGEN`	`1571 1571`		`C->Y: 70% loss of transcription. Complete loss of replication.`
`MUTAGEN`	`1798 1800`		`KDR->AAA: 80% loss of transcription. 27% loss of replication.`
`MUTAGEN`	`1815 1817`		`DAT->KEI: Complete loss of transcription and replication.`
`MUTAGEN`	`1838 1839`		`RE->AA: Complete loss of transcription and replication.`

Sequence information

Length: 2228 AA [This is the length of the unprocessed precursor]

Molecular weight: 252867 Da [This is the MW of the unprocessed precursor]

CRC64: 074A4DFE8F8A37B5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDGQESSQNP SDILYPECHL NSPIVRGKIA QLHVLLDVNQ PYRLKDDSII NITKHKIRNG 

        70         80         90        100        110        120 
GLSPRQIKIR SLGKALQRTI KDLDRYTFEP YPTYSQELLR LDIPEICDKI RSVFAVSDRL 

       130        140        150        160        170        180 
TRELSSGFQD LWLNIFKQLG NIEGREGYDP LQDIGTIPEI TDKYSRNRWY RPFLTWFSIK 

       190        200        210        220        230        240 
YDMRWMQKTR PGGPLDTSNS HNLLECKSYT LVTYGDLVMI LNKLTLTGYI LTPELVLMYC 

       250        260        270        280        290        300 
DVVEGRWNMS AAGHLDKKSI GITSKGEELW ELVDSLFSSL GEEIYNVIAL LEPLSLALIQ 

       310        320        330        340        350        360 
LNDPVIPLRG AFMRHVLTEL QTVLTSRDVY TDAEADTIVE SLLAIFHGTS IDEKAEIFSF 

       370        380        390        400        410        420 
FRTFGHPSLE AVTAADKVRA HMYAQKAIKL KTLYECHAVF CTIIINGYRE RHGGQWPPCD 

       430        440        450        460        470        480 
FPDHVCLELR NAQGSNTAIS YECAVDNYTS FIGFKFRKFI EPQLDEDLTI YMKDKALSPR 

       490        500        510        520        530        540 
KEAWDSVYPD SNLYYKAPES EETRRLIEVF INDENFNPEE IINYVESGDW LKDEEFNISY 

       550        560        570        580        590        600 
SLKEKEIKQE GRLFAKMTYK MRAVQVLAET LLAKGIGELF RENGMVKGEI DLLKRLTTLS 

       610        620        630        640        650        660 
VSGVPRTDSV YNNSKSSEKR NEGMENKNSG GYWDEKKRSR HEFKATDSST DGYETLSCFL 

       670        680        690        700        710        720 
TTDLKKYCLN WRFESTALFG QRCNEIFGFK TFFNWMHPVL ERCTIYVGDP YCPVADRMHR 

       730        740        750        760        770        780 
QLQDHADSGI FIHNPRGGIE GYCQKLWTLI SISAIHLAAV RVGVRVSAMV QGDNQAIAVT 

       790        800        810        820        830        840 
SRVPVAQTYK QKKNHVYEEI TKYFGALRHV MFDVGHELKL NETIISSKMF VYSKRIYYDG 

       850        860        870        880        890        900 
KILPQCLKAL TKCVFWSETL VDENRSACSN ISTSIAKAIE NGYSPILGYC IALYKTCQQV 

       910        920        930        940        950        960 
CISLGMTINP TISPTVRDQY FKGKNWLRCA VLIPANVGGF NYMSTSRCFV RNIGDPAVAA 

       970        980        990       1000       1010       1020 
LADLKRFIRA DLLDKQVLYR VMNQEPGDSS FLDWASDPYS CNLPHSQSIT TIIKNITARS 

      1030       1040       1050       1060       1070       1080 
VLQESPNPLL SGLFTETSGE EDLNLASFLM DRKVILPRVA HEILGNSLTG VREAIAGMLD 

      1090       1100       1110       1120       1130       1140 
TTKSLVRASV RKGGLSYGIL RRLVNYDLLQ YETLTRTLRK PVKDNIEYEY MCSVELAVGL 

      1150       1160       1170       1180       1190       1200 
RQKMWIHLTY GRPIHGLETP DPLELLRGIF IEGSEVCKLC RSEGADPIYT WFYLPDNIDL 

      1210       1220       1230       1240       1250       1260 
DTLTNGCPAI RIPYFGSATD ERSEAQLGYV RNLSKPAKAA IRIAMVYTWA YGTDEISWME 

      1270       1280       1290       1300       1310       1320 
AALIAQTRAN LSLENLKLLT PVSTSTNLSH RLKDTATQMK FSSATLVRAS RFITISNDNM 

      1330       1340       1350       1360       1370       1380 
ALKEAGESKD TNLVYQQIML TGLSLFEFNM RYKKGSLGKP LILHLHLNNG CCIMESPQEA 

      1390       1400       1410       1420       1430       1440 
NIPPRSTLDL EITQENNKLI YDPDPLKDVD LELFSKVRDV VHTVDMTYWS DDEVIRATSI 

      1450       1460       1470       1480       1490       1500 
CTAMTIADTM SQLDRDNLKE MIALVNDDDV NSLITEFMVI DVPLFCSTFG GILVNQFAYS 

      1510       1520       1530       1540       1550       1560 
LYGLNIRGRE EIWGHVVRIL KDTSHAVLKV LSNALSHPKI FKRFWNAGVV EPVYGPNLSN 

      1570       1580       1590       1600       1610       1620 
QDKILLALSV CEYSVDLFMH DWQGGVPLEI FICDNDPDVA DMRRSSFLAR HLAYLCSLAE 

      1630       1640       1650       1660       1670       1680 
ISRDGPRLES MNSLERLESL KSYLELTFLD DPVLRYSQLT GLVIKVFPST LTYIRKSSIK 

      1690       1700       1710       1720       1730       1740 
VLRTRGIGVP EVLEDWDPEA DNALLDGIAA EIQQNIPLGH QTRAPFWGLR VSKSQVLRLR 

      1750       1760       1770       1780       1790       1800 
GYKEITRGEI GRSGVGLTLP FDGRYLSHQL RLFGINSTSC LKALELTYLL SPLVDKDKDR 

      1810       1820       1830       1840       1850       1860 
LYLGEGAGAM LSCYDATLGP CINYYNSGVY SCDVNGQREL NIYPAEVALV GKKLNNVTSL 

      1870       1880       1890       1900       1910       1920 
GQRVKVLFNG NPGSTWIGND ECEALIWNEL QNSSIGLVHC DMEGGDHKDD QVVLHEHYSV 

      1930       1940       1950       1960       1970       1980 
IRIAYLVGDR DVVLISKIAP RLGTDWTRQL SLYLRYWDEV NLIVLKTSNP ASTEMYLLSR 

      1990       2000       2010       2020       2030       2040 
HPKSDIIEDS KTVLASLLPL SKEDSIKIEK WILIEKAKAH EWVTRELREG SSSSGMLRPY 

      2050       2060       2070       2080       2090       2100 
HQALQTFGFE PNLYKLSRDF LSTMNIADTH NCMIAFNRVL KDTIFEWARI TESDKRLKLT 

      2110       2120       2130       2140       2150       2160 
GKYDLYPVRD SGKLKTISRR LVLSWISLSM STRLVTGSFP DQKFEARLQL GIVSLSSREI 

      2170       2180       2190       2200       2210       2220 
RNLRVITKTL LDRFEDIIHS ITYRFLTKEI KILMKILGAV KMFGARQNEY TTVIDDGSLG 


DIEPYDSS

P06447 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools