L_BUNLC
ID L_BUNLC Reviewed; 2263 AA.
AC A5HC98;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=RNA-directed RNA polymerase L;
DE Short=Protein L;
DE EC=2.7.7.48 {ECO:0000250|UniProtKB:I0DF35};
DE AltName: Full=Large structural protein;
DE AltName: Full=Replicase;
DE AltName: Full=Transcriptase;
DE Includes:
DE RecName: Full=cap-snatching endonuclease;
DE EC=3.1.-.- {ECO:0000269|PubMed:20862319};
GN Name=L;
OS Bunyavirus La Crosse.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus;
OC La Crosse orthobunyavirus.
OX NCBI_TaxID=11577;
OH NCBI_TaxID=9850; Cervidae (deer).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=7162; Ochlerotatus triseriatus (Eastern treehole mosquito) (Aedes triseriatus).
OH NCBI_TaxID=13712; Tamias.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17488515; DOI=10.1186/1743-422x-4-41;
RA Bennett R.S., Ton D.R., Hanson C.T., Murphy B.R., Whitehead S.S.;
RT "Genome sequence analysis of La Crosse virus and in vitro and in vivo
RT phenotypes.";
RL Virol. J. 4:41-41(2007).
RN [2]
RP REVIEW.
RX PubMed=28418734; DOI=10.1080/1040841x.2017.1307805;
RA Amroun A., Priet S., de Lamballerie X., Querat G.;
RT "Bunyaviridae RdRps: structure, motifs, and RNA synthesis machinery.";
RL Crit. Rev. Microbiol. 43:753-778(2017).
RN [3]
RP REVIEW.
RX PubMed=31948728; DOI=10.1016/j.tim.2019.12.006;
RA Olschewski S., Cusack S., Rosenthal M.;
RT "The Cap-Snatching Mechanism of Bunyaviruses.";
RL Trends Microbiol. 28:293-303(2020).
RN [4] {ECO:0007744|PDB:2XI5, ECO:0007744|PDB:2XI7}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-183 IN COMPLEX WITH MANGANESE,
RP DISULFIDE BONDS, FUNCTION, MUTAGENESIS OF HIS-34; ASP-52; ASP-79; ASP-92
RP AND LYS-94, DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=20862319; DOI=10.1371/journal.ppat.1001101;
RA Reguera J., Weber F., Cusack S.;
RT "Bunyaviridae RNA polymerases (L-protein) have an N-terminal, influenza-
RT like endonuclease domain, essential for viral cap-dependent
RT transcription.";
RL PLoS Pathog. 6:E1001101-E1001101(2010).
RN [5] {ECO:0007744|PDB:5AMQ, ECO:0007744|PDB:5AMR}
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS), RNA-BINDING, DOMAIN, AND FUNCTION.
RX PubMed=26004069; DOI=10.1016/j.cell.2015.05.006;
RA Gerlach P., Malet H., Cusack S., Reguera J.;
RT "Structural insights into bunyavirus replication and its regulation by the
RT vRNA promoter.";
RL Cell 161:1267-1279(2015).
RN [6] {ECO:0007744|PDB:6Z6B, ECO:0007744|PDB:6Z6G, ECO:0007744|PDB:6Z8K}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.02 ANGSTROMS) IN COMPLEX WITH ZINC, AND
RP DOMAIN.
RX PubMed=32681014; DOI=10.1038/s41467-020-17349-4;
RA Arragain B., Effantin G., Gerlach P., Reguera J., Schoehn G., Cusack S.,
RA Malet H.;
RT "Pre-initiation and elongation structures of full-length La Crosse virus
RT polymerase reveal functionally important conformational changes.";
RL Nat. Commun. 11:3590-3590(2020).
CC -!- FUNCTION: RNA-dependent RNA polymerase, which is responsible for the
CC replication and transcription of the viral RNA genome using antigenomic
CC RNA as an intermediate (By similarity). During transcription,
CC synthesizes subgenomic RNAs and assures their capping by a cap-
CC snatching mechanism, which involves the endonuclease activity cleaving
CC the host capped pre-mRNAs (PubMed:20862319). These short capped RNAs
CC are then used as primers for viral transcription. The 3'-end of
CC subgenomic mRNAs molecules are not polyadenylated. During replication,
CC the polymerase binds the 5' and 3' vRNA extremities at distinct sites
CC (By similarity). In turn, significant conformational changes occur in
CC the polymerase and in vRNA to initiate active RNA synthesis
CC (PubMed:26004069). As a consequence of the use of the same enzyme for
CC both transcription and replication, these mechanisms need to be well
CC coordinated (PubMed:20862319). {ECO:0000250|UniProtKB:I0DF35,
CC ECO:0000250|UniProtKB:P27316, ECO:0000269|PubMed:20862319,
CC ECO:0000269|PubMed:26004069}.
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:0000250|UniProtKB:P20470};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20862319};
CC Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site
CC (PubMed:20862319). The divalent metal ions are crucial for catalytic
CC activity (PubMed:31948728). {ECO:0000269|PubMed:20862319,
CC ECO:0000269|PubMed:31948728};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A2SZS3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A2SZS3};
CC Note=For polymerase activity. Initiation activity is stronger in the
CC presence of Mn(2+) than in the presence of Mg(2+).
CC {ECO:0000250|UniProtKB:A2SZS3};
CC -!- SUBUNIT: Homomultimer (By similarity). Interacts with the glycoprotein
CC N; this interaction allows efficient polymerase packaging into virus
CC particles (By similarity). Interacts with nucleoprotein N (By
CC similarity). {ECO:0000250|UniProtKB:P27316}.
CC -!- SUBCELLULAR LOCATION: Host Golgi apparatus
CC {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250|UniProtKB:I0DF35}. Virion
CC {ECO:0000250|UniProtKB:P20470}.
CC -!- DOMAIN: The N-terminus contains the endonuclease activity (endoN)
CC (PubMed:32681014, PubMed:20862319). The central region contains the
CC RdRp activity (By similarity). The C-terminus contains the cap-binding
CC region (By similarity). {ECO:0000250|UniProtKB:A2SZS3,
CC ECO:0000250|UniProtKB:I0DF35, ECO:0000269|PubMed:20862319,
CC ECO:0000269|PubMed:32681014}.
CC -!- MISCELLANEOUS: Classified as His(+) endonuclease since it has a
CC histidine upstream of the active site that coordinates the first
CC cation. {ECO:0000303|PubMed:31948728}.
CC -!- SIMILARITY: Belongs to the Bunyavirales RNA polymerase family.
CC {ECO:0000305}.
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DR EMBL; EF485038; ABQ12639.1; -; Viral_cRNA.
DR PDB; 2XI5; X-ray; 2.20 A; A/B/C/D=1-183.
DR PDB; 2XI7; X-ray; 2.20 A; A/B/C/D=1-183.
DR PDB; 5AMQ; X-ray; 3.00 A; A=1-2263.
DR PDB; 5AMR; X-ray; 2.57 A; A=1-2263.
DR PDB; 6Z6B; X-ray; 3.96 A; EEE/PPP=1-2263.
DR PDB; 6Z6G; EM; 3.06 A; A=1-2263.
DR PDB; 6Z8K; EM; 3.02 A; A=1-2263.
DR PDB; 7ORI; EM; 3.90 A; A=1-2263.
DR PDB; 7ORJ; EM; 3.90 A; A=1-2263.
DR PDB; 7ORK; EM; 3.10 A; A=1-2263.
DR PDB; 7ORL; EM; 3.60 A; A=1-2263.
DR PDB; 7ORM; EM; 3.30 A; A=1-2263.
DR PDB; 7ORN; EM; 2.80 A; A=1-2263.
DR PDB; 7ORO; EM; 2.90 A; A=1-2263.
DR PDBsum; 2XI5; -.
DR PDBsum; 2XI7; -.
DR PDBsum; 5AMQ; -.
DR PDBsum; 5AMR; -.
DR PDBsum; 6Z6B; -.
DR PDBsum; 6Z6G; -.
DR PDBsum; 6Z8K; -.
DR PDBsum; 7ORI; -.
DR PDBsum; 7ORJ; -.
DR PDBsum; 7ORK; -.
DR PDBsum; 7ORL; -.
DR PDBsum; 7ORM; -.
DR PDBsum; 7ORN; -.
DR PDBsum; 7ORO; -.
DR SMR; A5HC98; -.
DR EvolutionaryTrace; A5HC98; -.
DR Proteomes; UP000126351; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR DisProt; DP02521; -.
DR InterPro; IPR029124; L_protein_N.
DR InterPro; IPR007099; RNA-dir_pol_NSvirus.
DR InterPro; IPR014384; RNA-dir_pol_orthobunyavirus.
DR InterPro; IPR007322; RNA_pol_bunyavir.
DR Pfam; PF04196; Bunya_RdRp; 1.
DR Pfam; PF15518; L_protein_N; 1.
DR PIRSF; PIRSF000824; L_OrthobunV; 1.
DR PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host endoplasmic reticulum; Host Golgi apparatus; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW Transferase; Viral RNA replication; Virion; Zinc.
FT CHAIN 1..2263
FT /note="RNA-directed RNA polymerase L"
FT /id="PRO_0000445739"
FT DOMAIN 1042..1230
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1..185
FT /note="Endonuclease"
FT /evidence="ECO:0000269|PubMed:32681014"
FT REGION 1841..1977
FT /note="Cap-binding"
FT /evidence="ECO:0000269|PubMed:32681014"
FT BINDING 34
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20862319"
FT BINDING 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20862319"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20862319"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20862319"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20862319"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20862319"
FT BINDING 1188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RdRp activity"
FT /evidence="ECO:0000305|PubMed:26004069"
FT BINDING 2064
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:32681014,
FT ECO:0007744|PDB:6Z6B"
FT BINDING 2169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:32681014,
FT ECO:0007744|PDB:6Z6B"
FT BINDING 2178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:32681014,
FT ECO:0007744|PDB:6Z6B"
FT BINDING 2182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:32681014,
FT ECO:0007744|PDB:6Z6B"
FT MUTAGEN 34
FT /note="H->A: Complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:20862319"
FT MUTAGEN 52
FT /note="D->A: Complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:20862319"
FT MUTAGEN 79
FT /note="D->A: Complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:20862319"
FT MUTAGEN 92
FT /note="D->A: Complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:20862319"
FT MUTAGEN 94
FT /note="K->A: Complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:20862319"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:2XI5"
FT HELIX 19..45
FT /evidence="ECO:0007829|PDB:2XI5"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:2XI5"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5AMQ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2XI5"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2XI5"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:2XI5"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2XI5"
FT HELIX 100..120
FT /evidence="ECO:0007829|PDB:2XI5"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:2XI5"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2XI5"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2XI5"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:2XI5"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2XI5"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:2XI5"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2XI5"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 274..291
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 357..371
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 408..416
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 448..465
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 490..500
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 503..522
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 556..567
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 586..591
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 594..597
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 598..619
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:5AMQ"
FT HELIX 627..639
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 643..659
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 666..672
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 681..699
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 701..704
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:6Z6G"
FT HELIX 714..721
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 738..746
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 747..750
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 759..780
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 785..788
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 796..812
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 817..824
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 827..830
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 835..837
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 840..847
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 850..869
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 893..899
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 906..910
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 911..920
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 926..928
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 929..939
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 944..947
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 953..956
FT /evidence="ECO:0007829|PDB:5AMQ"
FT STRAND 961..964
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 965..984
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 985..988
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 996..1019
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1021..1029
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1035..1037
FT /evidence="ECO:0007829|PDB:5AMQ"
FT HELIX 1040..1047
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1051..1063
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 1064..1066
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1072..1078
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1085..1098
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1102..1104
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1107..1115
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1124..1127
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 1128..1133
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1134..1138
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 1145..1148
FT /evidence="ECO:0007829|PDB:5AMQ"
FT HELIX 1149..1172
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 1173..1175
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1177..1185
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1188..1200
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1202..1219
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 1226..1228
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1230..1238
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1241..1244
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1247..1249
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1253..1257
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1258..1260
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1268..1284
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1289..1306
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1318..1320
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1326..1328
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 1331..1334
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1341..1347
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1348..1350
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1351..1364
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1367..1369
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1370..1372
FT /evidence="ECO:0007829|PDB:6Z6G"
FT HELIX 1374..1379
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1380..1383
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1386..1388
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1391..1402
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 1403..1405
FT /evidence="ECO:0007829|PDB:5AMQ"
FT HELIX 1442..1452
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1456..1466
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1468..1471
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1478..1488
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1492..1497
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1503..1512
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1514..1516
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1521..1525
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1526..1528
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1549..1561
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1567..1577
FT /evidence="ECO:0007829|PDB:5AMR"
FT TURN 1578..1580
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1582..1593
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1594..1600
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1606..1609
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1623..1630
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1631..1634
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1644..1658
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1662..1676
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1681..1699
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1708..1713
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1718..1728
FT /evidence="ECO:0007829|PDB:5AMR"
FT STRAND 1735..1742
FT /evidence="ECO:0007829|PDB:5AMR"
FT HELIX 1761..1777
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1785..1792
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1802..1811
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1815..1818
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1819..1822
FT /evidence="ECO:0007829|PDB:6Z8K"
FT TURN 1823..1826
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1830..1839
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1862..1867
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1870..1876
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1881..1890
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1893..1903
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1905..1907
FT /evidence="ECO:0007829|PDB:6Z6G"
FT STRAND 1925..1927
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1930..1932
FT /evidence="ECO:0007829|PDB:6Z8K"
FT TURN 1933..1935
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1936..1938
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1941..1943
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1944..1954
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1956..1960
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 1968..1975
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 1984..1990
FT /evidence="ECO:0007829|PDB:6Z8K"
FT TURN 1991..1993
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2001..2005
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2007..2009
FT /evidence="ECO:0007829|PDB:6Z6G"
FT HELIX 2015..2020
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2033..2037
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2040..2042
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2045..2047
FT /evidence="ECO:0007829|PDB:6Z6G"
FT HELIX 2048..2051
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2055..2058
FT /evidence="ECO:0007829|PDB:6Z8K"
FT TURN 2059..2061
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2070..2073
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2083..2085
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2086..2090
FT /evidence="ECO:0007829|PDB:6Z6G"
FT STRAND 2092..2094
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2097..2099
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2101..2103
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2110..2128
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2132..2134
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2136..2138
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2139..2153
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2159..2174
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2178..2182
FT /evidence="ECO:0007829|PDB:6Z8K"
FT STRAND 2192..2196
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2201..2209
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2219..2237
FT /evidence="ECO:0007829|PDB:6Z8K"
FT HELIX 2246..2250
FT /evidence="ECO:0007829|PDB:6Z8K"
SQ SEQUENCE 2263 AA; 263029 MW; B1EBA368F8D20FDD CRC64;
MDYQEYQQFL ARINTARDAC VAKDIDVDLL MARHDYFGRE LCKSLNIEYR NDVPFIDIIL
DIRPEVDPLT IDAPHITPDN YLYINNVLYI IDYKVSVSNE SSVITYDKYY ELTRDISDRL
SIPIEIVIIR IDPVSRDLHI NSDRFKELYP TIVVDINFNQ FFDLKQLLYE KFGDDEEFLL
KVAHGDFTLT APWCKTGCPE FWKHPIYKEF KMSMPVPERR LFEESVKFNA YESERWNTNL
VKIREYTKKD YSEHISKSAK NIFLASGFYK QPNKNEISEG WTLMVERVQD QREISKSLHD
QKPSIHFIWG AHNPGNSNNA TFKLILLSKS LQSIKGISTY TEAFKSLGKM MDIGDKAIEY
EEFCMSLKSK ARSSWKQIMN KKLEPKQINN ALVLWEQQFM INNDLIDKSE KLKLFKNFCG
IGKHKQFKNK MLEDLEVSKP KILDFDDANM YLASLTMMEQ SKKILSKSNG LKPDNFILNE
FGSRIKDANK ETYDNMHKIF ETGYWQCISD FSTLMKNILS VSQYNRHNTF RIAMCANNNV
FAIVFPSADI KTKKATVVYS IIVLHKEEEN IFNPGCLHGT FKCMNGYISI SRAIRLDKER
CQRIVSSPGL FLTTCLLFKH DNPTLVMSDI MNFSIYTSLS ITKSVLSLTE PARYMIMNSL
AISSNVKDYI AEKFSPYTKT LFSVYMTRLI KNACFDAYDQ RQRVQLRDIY LSDYDITQKG
IKDNRELTSI WFPGSVTLKE YLTQIYLPFY FNAKGLHEKH HVMVDLAKTI LEIECEQREN
IKEIWSTNCT KQTVNLKILI HSLCKNLLAD TSRHNHLRNR IENRNNFRRS ITTISTFTSS
KSCLKIGDFR KEKELQSVKQ KKILEVQSRK MRLANPMFVT DEQVCLEVGH CNYEMLRNAM
PNYTDYISTK VFDRLYELLD KKVLTDKPVI EQIMDMMIDH KKFYFTFFNK GQKTSKDREI
FVGEYEAKMC MYAVERIAKE RCKLNPDEMI SEPGDGKLKV LEQKSEQEIR FLVETTRQKN
REIDEAIEAL ATEGYESNLG KIEKLSLGKA KGLKMEINAD MSKWSAQDVF YKYFWLIALD
PILYPQEKER ILYFMCNYMD KELILPDELL FNLLDQKVAY QNDIIATMTN QLNSNTVLIK
RNWLQGNFNY TSSYVHSCAM SVYKEILKEA ITLLDGSILV NSLVHSDDNQ TSITIVQDKM
ENDKIIDFAM KEFERACLTF GCQANMKKTY VTNCIKEFVS LFNLYGEPFS IYGRFLLTSV
GDCAYIGPYE DLASRISSAQ TAIKHGCPPS LAWVSIAISH WMTSLTYNML PGQSNDPIDY
FPAENRKDIP IELNGVLDAP LSMISTVGLE SGNLYFLIKL LSKYTPVMQK RESVVNQIAE
VKNWKVEDLT DNEIFRLKIL RYLVLDAEMD PSDIMGETSD MRGRSILTPR KFTTAGSLRK
LYSFSKYQDR LSSPGGMVEL FTYLLEKPEL LVTKGEDMKD YMESVIFRYN SKRFKESLSI
QNPAQLFIEQ ILFSHKPVID FSGIRDKYIN LHDSRALEKE PDILGKVTFT EAYRLLMRDL
SSLELTNDDI QVIYSYIILN DPMMITIANT HILSIYGSPQ RRMGMSCSTM PEFRNLKLIH
HSPALVLRAY SKNNPDIQGA DPTEMARDLV HLKEFVENTN LEEKMKVRIA MNEAEKGQRD
IVFELKEMTR FYQVCYEYVK STEHKIKVFI LPAKSYTTTD FCSLMQGNLI KDKEWYTVHY
LKQILSGGHK AIMQHNATSE QNIAFECFKL ITHFADSFID SLSRSAFLQL IIDEFSYKDV
KVSKLYDIIK NGYNRTDFIP LLFRTGDLRQ ADLDKYDAMK SHERVTWNDW QTSRHLDMGS
INLTITGYNR SITIIGEDNK LTYAELCLTR KTPENITISG RKLLGSRHGL KFENMSKIQT
YPGNYYITYR KKDRHQFVYQ IHSHESITRR NEEHMAIRTR IYNEITPVCV VNVAEVDGDQ
RILIRSLDYL NNDIFSLSRI KVGLDEFATI KKAHFSKMVS FEGPPIKTGL LDLTELMKSQ
DLLNLNYDNI RNSNLISFSK LICCEGSDNI NDGLEFLSDD PMNFTEGEAI HSTPIFNIYY
SKRGERHMTY RNAIKLLIER ETKIFEEAFT FSENGFISPE NLGCLEAVVS LIKLLKTNEW
STVIDKCIHI CLIKNGMDHM YHSFDVPKCF MGNPITRDIN WVMFREFINS LPGTDIPPWN
VMTENFKKKC IALINSKFET QRDFSEFTKL MKKEGGRSNI EFD
