L_RABVS
ID L_RABVS Reviewed; 2127 AA.
AC P16289; A3F5M4; A3F5R9; Q6HA95;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Large structural protein;
DE Short=Protein L;
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 Rabies virus (strain SAD B19) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11300;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2139267; DOI=10.1016/0042-6822(90)90433-r;
RA Conzelmann K.-K., Cox J.H., Schneider L.G., Thiel H.-J.;
RT "Molecular cloning and complete nucleotide sequence of the attenuated
RT rabies virus SAD B19.";
RL Virology 175:485-499(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=SRV9;
RA Wang T., Zhang S., Hu R.;
RT "Analysis of the whole sequence of rabies virus vaccine strain SRV9.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate SAD Bern, Isolate SAD Bern original var 1,
RC Isolate SAD Bern original var 2, Isolate SAD Bern original var 3,
RC Isolate SAD Bern original var 4, Isolate SAD Bern original var 5,
RC Isolate SAD P5/88, Isolate SAD VA1, Isolate SAD1-3670 var 1,
RC Isolate SAD1-3670 var 2, and Isolate SAG 2;
RA Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
RA Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E.,
RA Cox J., Mueller T.;
RT "Complete nucleotide sequencing of SAD derivatives of attenuated rabies
RT virus vaccine strains.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP MUTAGENESIS OF LEU-725; ALA-726; GLN-727; GLY-728; ASP-729; ASN-730;
RP GLN-731; VAL-732 AND LEU-733.
RX PubMed=8553554; DOI=10.1006/viro.1995.0063;
RA Schnell M.J., Conzelmann K.K.;
RT "Polymerase activity of in vitro mutated rabies virus L protein.";
RL Virology 214:522-530(1995).
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}.
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:0000250|UniProtKB:P03523};
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:0000250|UniProtKB:P03523};
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 -!- SUBUNIT: May form homodimer. Interacts with the P protein.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged
CC asymmetrically towards the blunt end of the virus.
CC {ECO:0000250|UniProtKB:P03523}.
CC -!- SIMILARITY: Belongs to the rhabdoviruses protein L family.
CC {ECO:0000305}.
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DR EMBL; M31046; AAA47203.1; -; Genomic_RNA.
DR EMBL; AF499686; AAT48626.1; -; Genomic_RNA.
DR EMBL; EF206708; ABN11300.1; -; Genomic_RNA.
DR EMBL; EF206709; ABN11305.1; -; Genomic_RNA.
DR EMBL; EF206710; ABN11310.1; -; Genomic_RNA.
DR EMBL; EF206711; ABN11315.1; -; Genomic_RNA.
DR EMBL; EF206712; ABN11320.1; -; Genomic_RNA.
DR EMBL; EF206713; ABN11325.1; -; Genomic_RNA.
DR EMBL; EF206714; ABN11330.1; -; Genomic_RNA.
DR EMBL; EF206715; ABN11335.1; -; Genomic_RNA.
DR EMBL; EF206716; ABN11340.1; -; Genomic_RNA.
DR EMBL; EF206717; ABN11345.1; -; Genomic_RNA.
DR EMBL; EF206718; ABN11350.1; -; Genomic_RNA.
DR EMBL; EF206719; ABN11355.1; -; Genomic_RNA.
DR EMBL; EF206720; ABN11360.1; -; Genomic_RNA.
DR PIR; E34746; ZLVNSB.
DR PDB; 6UEB; EM; 3.30 A; A=1-2127.
DR PDBsum; 6UEB; -.
DR SMR; P16289; -.
DR PRIDE; P16289; -.
DR BRENDA; 2.1.1.375; 14818.
DR Proteomes; UP000006363; Genome.
DR Proteomes; UP000007308; Genome.
DR Proteomes; UP000100286; Genome.
DR Proteomes; UP000107382; Genome.
DR Proteomes; UP000115894; Genome.
DR Proteomes; UP000118099; Genome.
DR Proteomes; UP000123862; Genome.
DR Proteomes; UP000132522; Genome.
DR Proteomes; UP000133682; Genome.
DR Proteomes; UP000142143; Genome.
DR Proteomes; UP000151156; Genome.
DR Proteomes; UP000167748; Genome.
DR Proteomes; UP000172072; Genome.
DR Proteomes; UP000174835; Genome.
DR Proteomes; UP000175378; 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 GO; GO:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
DR InterPro; IPR039530; L_methyltransferase_rhabdo.
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; IPR017234; RNA-dir_pol_rhabdovirus.
DR Pfam; PF14314; Methyltrans_Mon; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF037546; RNA_pol_RhabdoV_sub; 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 3D-structure; ATP-binding; Host cytoplasm; Hydrolase; Methyltransferase;
KW mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-directed RNA polymerase;
KW S-adenosyl-L-methionine; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2127
FT /note="Large structural protein"
FT /id="PRO_0000222841"
FT DOMAIN 611..799
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 1674..1871
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00923"
FT REGION 1562..2127
FT /note="Interaction with P protein"
FT /evidence="ECO:0000250"
FT BINDING 1701..1710
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 26
FT /note="I -> T (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 365
FT /note="F -> Y (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 391
FT /note="L -> I (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 394
FT /note="M -> V (in strain: SRV9, Isolate SAD1-3670 var 1,
FT Isolate SAD1-3670 var 2, Isolate SAD Bern, Isolate SAD Bern
FT original var 1, Isolate SAD Bern original var 2, Isolate
FT SAD Bern original var 3, Isolate SAD Bern original var 4,
FT Isolate SAD Bern original var 5, Isolate SAD P5/88, Isolate
FT SAD VA1 and Isolate SAG 2)"
FT VARIANT 524
FT /note="R -> K (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 901
FT /note="I -> V (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 933
FT /note="Q -> H (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 1018
FT /note="I -> T (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 1100
FT /note="L -> Q (in strain: SRV9)"
FT VARIANT 1212
FT /note="A -> T (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 1450
FT /note="V -> I (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 1516
FT /note="I -> V (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 1541
FT /note="S -> T (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 1761
FT /note="L -> F (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 1990
FT /note="S -> L (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 2097
FT /note="R -> G (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT MUTAGEN 725
FT /note="L->I,M: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 726
FT /note="A->G,S,V: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 727
FT /note="Q->E,N: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 728..730
FT /note="GDN->SDD: Complete loss of polymerase activity."
FT MUTAGEN 728
FT /note="G->A: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 729
FT /note="D->E,N: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 730
FT /note="N->A,D,E,Q: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 731
FT /note="Q->E,N: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 732
FT /note="V->A: Partial loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 732
FT /note="V->S,T: Complete loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 733
FT /note="L->I: No effect on polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 733
FT /note="L->N: Partial loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT MUTAGEN 733
FT /note="L->S: Partial loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:8553554"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 162..185
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 240..260
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 271..290
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 296..313
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 326..339
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 398..418
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 447..452
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 487..496
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 507..513
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 519..527
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 559..575
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 589..598
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 599..602
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 614..618
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 622..625
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 628..632
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 633..641
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 650..657
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 700..718
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 720..737
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 745..772
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 779..781
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 783..787
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 794..797
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 806..810
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 811..813
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 823..839
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 845..864
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 867..870
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 875..878
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 883..892
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 896..899
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 906..908
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 917..930
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 936..945
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 954..958
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 959..962
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 975..989
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 991..993
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 997..1018
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1020..1022
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1025..1034
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1038..1046
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1050..1056
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1059..1080
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1094..1106
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 1118..1120
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1127..1131
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1144..1148
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1154..1157
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1176..1178
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1188..1197
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 1200..1202
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1205..1207
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1208..1219
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 1245..1248
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1260..1263
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1264..1267
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1269..1276
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1286..1301
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1311..1313
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 1341..1343
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1346..1348
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1373..1393
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1397..1400
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1407..1413
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1415..1436
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1442..1444
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1446..1462
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1466..1472
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1474..1481
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1495..1509
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 1510..1512
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 1514..1518
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1530..1532
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1535..1551
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1560..1576
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1579..1581
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1588..1594
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 1595..1598
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1599..1601
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1610..1613
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 1614..1618
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1640..1643
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1647..1650
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1656..1661
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1670..1673
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1678..1681
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1683..1692
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1698..1704
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1706..1708
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1709..1717
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1722..1726
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1737..1739
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1745..1750
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1752..1756
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1775..1786
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1793..1796
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1804..1818
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1824..1831
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1832..1835
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1843..1846
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1852..1861
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1867..1874
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1888..1895
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1896..1901
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1903..1912
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1916..1919
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1924..1927
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1930..1940
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1945..1957
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1961..1978
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 1988..1991
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 1996..2017
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 2020..2031
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 2034..2042
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 2044..2054
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 2058..2064
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 2069..2082
FT /evidence="ECO:0007829|PDB:6UEB"
FT HELIX 2092..2106
FT /evidence="ECO:0007829|PDB:6UEB"
FT TURN 2113..2118
FT /evidence="ECO:0007829|PDB:6UEB"
FT STRAND 2121..2125
FT /evidence="ECO:0007829|PDB:6UEB"
SQ SEQUENCE 2127 AA; 242979 MW; 6D74F0779CCBBDF9 CRC64;
MLDPGEVYDD PIDPIELEAE PRGTPIVPNI LRNSDYNLNS PLIEDPARLM LEWLKTGNRP
YRMTLTDNCS RSFRVLKDYF KKVDLGSLKV GGMAAQSMIS LWLYGAHSES NRSRRCITDL
AHFYSKSSPI EKLLNLTLGN RGLRIPPEGV LSCLERVDYD NAFGRYLANT YSSYLFFHVI
TLYMNALDWD EEKTILALWK DLTSVDIGKD LVKFKDQIWG LLIVTKDFVY SQSSNCLFDR
NYTLMLKDLF LSRFNSLMVL LSPPEPRYSD DLISQLCQLY IAGDQVLSMC GNSGYEVIKI
LEPYVVNSLV QRAEKFRPLI HSLGDFPVFI KDKVSQLEET FGPCARRFFR ALDQFDNIHD
LVFVFGCYRH WGHPYIDYRK GLSKLYDQVH LKKMIDKSYQ ECLASDLARR ILRWGFDKYS
KWYLDSRFLA RDHPLTPYIK TQTWPPKHIV DLVGDTWHKL PITQIFEIPE SMDPSEILDD
KSHSFTRTRL ASWLSENRGG PVPSEKVIIT ALSKPPVNPR EFLRSIDLGG LPDEDLIIGL
KPKERELKIE GRFFALMSWN LRLYFVITEK LLANYILPLF DALTMTDNLN KVFKKLIDRV
TGQGLLDYSR VTYAFHLDYE KWNNHQRLES TEDVFSVLDQ VFGLKRVFSR THEFFQKAWI
YYSDRSDLIG LREDQIYCLD ASNGPTCWNG QDGGLEGLRQ KGWSLVSLLM IDRESQIRNT
RTKILAQGDN QVLCPTYMLS PGLSQEGLLY ELERISRNAL SIYRAVEEGA SKLGLIIKKE
ETMCSYDFLI YGKTPLFRGN ILVPESKRWA RVSCVSNDQI VNLANIMSTV STNALTVAQH
SQSLIKPMRD FLLMSVQAVF HYLLFSPILK GRVYKILSAE GESFLLAMSR IIYLDPSLGG
ISGMSLGRFH IRQFSDPVSE GLSFWREIWL SSQESWIHAL CQEAGNPDLG ERTLESFTRL
LEDPTTLNIR GGASPTILLK DAIRKALYDE VDKVENSEFR EAILLSKTHR DNFILFLISV
EPLFPRFLSE LFSSSFLGIP ESIIGLIQNS RTIRRQFRKS LSKTLEESFY NSEIHGISRM
TQTPQRVGGV WPCSSERADL LREISWGRKV VGTTVPHPSE MLGLLPKSSI SCTCGATGGG
NPRVSVSVLP SFDQSFFSRG PLKGYLGSST SMSTQLFHAW EKVTNVHVVK RALSLKESIN
WFITRDSNLA QALIRNIMSL TGPDFPLEEA PVFKRTGSAL HRFKSARYSE GGYSSVCPNL
LSHISVSTDT MSDLTQDGKN YDFMFQPLML YAQTWTSELV QRDTRLRDST FHWHLRCNRC
VRPIDDVTLE TSQIFEFPDV SKRISRMVSG AVPHFQRLPD IRLRPGDFES LSGREKSHHI
GSAQGLLYSI LVAIHDSGYN DGTIFPVNIY GKVSPRDYLR GLARGVLIGS SICFLTRMTN
ININRPLELV SGVISYILLR LDNHPSLYIM LREPSLRGEI FSIPQKIPAA YPTTMKEGNR
SILCYLQHVL RYEREIITAS PENDWLWIFS DFRSAKMTYL SLITYQSHLL LQRVERNLSK
SMRDNLRQLS SLMRQVLGGH GEDTLESDDN IQRLLKDSLR RTRWVDQEVR HAARTMTGDY
SPNKKVSRKV GCSEWVCSAQ QVAVSTSANP APVSELDIRA LSKRFQNPLI SGLRVVQWAT
GAHYKLKPIL DDLNVFPSLC LVVGDGSGGI SRAVLNMFPD AKLVFNSLLE VNDLMASGTH
PLPPSAIMRG GNDIVSRVID LDSIWEKPSD LRNLATWKYF QSVQKQVNMS YDLIICDAEV
TDIASINRIT LLMSDFALSI DGPLYLVFKT YGTMLVNPNY KAIQHLSRAF PSVTGFITQV
TSSFSSELYL RFSKRGKFFR DAEYLTSSTL REMSLVLFNC SSPKSEMQRA RSLNYQDLVR
GFPEEIISNP YNEMIITLID SDVESFLVHK MVDDLELQRG TLSKVAIIIA IMIVFSNRVF
NVSKPLTDPS FYPPSDPKIL RHFNICCSTM MYLSTALGDV PSFARLHDLY NRPITYYFRK
QVIRGNVYLS WSWSNDTSVF KRVACNSSLS LSSHWIRLIY KIVKTTRLVG SIKDLSREVE
RHLHRYNRWI TLEDIRSRSS LLDYSCL
