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Genome polyprotein [Cleaved into: Leader protein; Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Rho) (Virion protein 4); Protein VP2 (Beta) (P1B) (Virion protein 2); Protein VP3 (Gamma) (P1C) (Virion protein 3); Protein VP1 (Alpha) (P1D) (Virion protein 1); Protein 2A (P2A) (G); Protein 2B (I) (P2B); Protein 2C (C) (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B (P3B) (H) (VPg); Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C) (p22); RNA-directed RNA polymerase 3D-POL (E) (P3D-POL) (EC 2.7.7.48)]

 POLG_ENMGO              Reviewed;        2293 AA.
P12296; Q2V6G9;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 3.
22-NOV-2017, entry version 144.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Leader protein;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Protein VP4;
AltName: Full=P1A;
AltName: Full=Rho;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Protein VP2;
AltName: Full=Beta;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Protein VP3;
AltName: Full=Gamma;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1;
AltName: Full=Alpha;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
AltName: Full=G;
Contains:
RecName: Full=Protein 2B;
Short=I;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B;
Short=P3B;
AltName: Full=H;
AltName: Full=VPg;
Contains:
RecName: Full=Protease 3C;
Short=P3C;
EC=3.4.22.28;
AltName: Full=Picornain 3C;
AltName: Full=p22;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=E;
Short=P3D-POL;
EC=2.7.7.48;
Flags: Precursor;
Mengo encephalomyocarditis virus.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Cardiovirus.
NCBI_TaxID=12107;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=10090; Mus musculus (Mouse).
NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Medium plague;
PubMed=16103157; DOI=10.1128/JVI.79.17.11062-11070.2005;
Fata-Hartley C.L., Palmenberg A.C.;
"Dipyridamole reversibly inhibits mengovirus RNA replication.";
J. Virol. 79:11062-11070(2005).
[2]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-901.
PubMed=3026048; DOI=10.1126/science.3026048;
Luo M., Vriend G., Kamer G., Minor I., Arnold E., Rossmann M.G.,
Boege U., Scraba D.G., Duke G.M., Palmenberg A.C.;
"The atomic structure of Mengo virus at 3.0-A resolution.";
Science 235:182-191(1987).
[3]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SEQUENCE REVISION TO 451
AND 669.
PubMed=2156078; DOI=10.1016/0022-2836(90)90077-Y;
Krishnaswamy S., Rossmann M.G.;
"Structural refinement and analysis of Mengo virus.";
J. Mol. Biol. 211:803-844(1990).
-!- FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed
capsid enclosing the viral positive strand RNA genome. VP4 lies on
the inner surface of the protein shell formed by VP1, VP2 and VP3.
All the three latter proteins contain a beta-sheet structure
called beta-barrel jelly roll. Together they form an icosahedral
capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with
a diameter of approximately 300 Angstroms. VP1 is situated at the
12 fivefold axes, whereas VP2 and VP3 are located at the quasi-
sixfold axes (By similarity). {ECO:0000250}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of immature
procapsids. {ECO:0000250}.
-!- FUNCTION: Protein 2B: Affects membrane integrity and cause an
increase in membrane permeability. {ECO:0000250}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. It displays RNA-
binding, nucleotide binding and NTPase activities (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as
membrane anchor. {ECO:0000250}.
-!- FUNCTION: Protease 3C: cysteine protease that generates mature
viral proteins from the precursor polyprotein. In addition to its
proteolytic activity, it binds to viral RNA, and thus influences
viral genome replication. RNA and substrate bind cooperatively to
the protease (By similarity). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- FUNCTION: Protein 2A: is involved in host translation shutoff.
Nuclear localization is required for this function (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
poliovirus polyprotein. In other picornavirus reactions Glu may be
substituted for Gln, and Ser or Thr for Gly.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- SUBCELLULAR LOCATION: Protein 2A: Host nucleus {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein VP2: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3B: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Note=Probably localizes to the surface of intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. These vesicles are derived from the
endoplasmic reticulum (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Genome polyprotein;
IsoId=P12296-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=2B*;
IsoId=P0DJX8-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting.;
-!- PTM: Specific enzymatic cleavages by the viral protease in vivo
yield a variety of precursors and mature proteins. Polyprotein
processing intermediates such as VP0 which is a VP4-VP2 precursor
are produced. During virion maturation, non-infectious particles
are rendered infectious following cleavage of VP0. This maturation
cleavage is followed by a conformational change of the particle.
The polyprotein seems to be cotranslationally cleaved at the 2A/2B
junction by a ribosomal skip from one codon to the next without
formation of a peptide bond. This process would release the L-P1-
2A peptide from the translational complex (By similarity).
{ECO:0000250}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
linked to the 5'-end of genomic RNA. This uridylylated form acts
as a nucleotide-peptide primer for the polymerase (By similarity).
{ECO:0000250}.
-!- PTM: Myristoylation of VP4 is required during RNA encapsidation
and formation of the mature virus particle. {ECO:0000250}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2mev";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1mec";
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EMBL; DQ294633; ABB97066.1; -; Genomic_RNA.
PDB; 1MEC; X-ray; 3.20 A; 1=625-898, 2=138-393, 3=394-624, 4=68-137.
PDB; 2M7Y; NMR; -; A=1-67.
PDB; 2MEV; X-ray; 3.00 A; 1=625-901, 2=138-393, 3=394-624, 4=68-137.
PDB; 2MMH; NMR; -; A=1-67.
PDB; 2MMI; NMR; -; A=1-67.
PDB; 2MMK; NMR; -; A=1-67.
PDB; 2MML; NMR; -; A=1-67.
PDB; 4NYZ; X-ray; 2.15 A; A=1834-2293.
PDB; 4NZ0; X-ray; 2.80 A; A/B/C/D/E/F=1834-2293.
PDB; 4Y2C; X-ray; 2.20 A; A=1834-2293.
PDB; 4Y3C; X-ray; 3.20 A; A/B/C/D/E/F=1834-2293.
PDBsum; 1MEC; -.
PDBsum; 2M7Y; -.
PDBsum; 2MEV; -.
PDBsum; 2MMH; -.
PDBsum; 2MMI; -.
PDBsum; 2MMK; -.
PDBsum; 2MML; -.
PDBsum; 4NYZ; -.
PDBsum; 4NZ0; -.
PDBsum; 4Y2C; -.
PDBsum; 4Y3C; -.
ProteinModelPortal; P12296; -.
SMR; P12296; -.
PRIDE; P12296; -.
OrthoDB; VOG0900006M; -.
EvolutionaryTrace; P12296; -.
Proteomes; UP000008663; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019030; C:icosahedral viral capsid; IEA:InterPro.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; ISS:UniProtKB.
GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
Gene3D; 4.10.90.10; -; 1.
InterPro; IPR015031; Capsid_VP4_Picornavir.
InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR021573; Leader_pept_picornaV.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR037243; Viral_lead_polypep_zc_finger.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 2.
Pfam; PF00910; RNA_helicase; 1.
Pfam; PF08935; VP4_2; 1.
Pfam; PF11475; VP_N-CPKC; 1.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF144251; SSF144251; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Capsid protein; Complete proteome;
Covalent protein-RNA linkage;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Helicase;
Host cytoplasm; Host cytoplasmic vesicle;
Host gene expression shutoff by virus; Host membrane; Host nucleus;
Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host RIG-I by virus;
Inhibition of host RLR pathway by virus; Ion channel; Ion transport;
Lipoprotein; Membrane; Myristate; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease;
Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
Thiol protease; Transferase; Transport; Viral attachment to host cell;
Viral immunoevasion; Viral ion channel; Viral RNA replication; Virion;
Virus entry into host cell.
CHAIN 1 67 Leader protein. {ECO:0000255}.
/FTId=PRO_5000141082.
CHAIN 68 393 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000310965.
CHAIN 68 137 Protein VP4. {ECO:0000255}.
/FTId=PRO_5000141083.
CHAIN 138 393 Protein VP2. {ECO:0000255}.
/FTId=PRO_5000141084.
CHAIN 394 624 Protein VP3. {ECO:0000255}.
/FTId=PRO_5000141085.
CHAIN 625 901 Protein VP1. {ECO:0000255}.
/FTId=PRO_5000141086.
CHAIN 902 1044 Protein 2A. {ECO:0000255}.
/FTId=PRO_5000141087.
CHAIN 1045 1195 Protein 2B. {ECO:0000255}.
/FTId=PRO_5000141088.
CHAIN 1196 1520 Protein 2C. {ECO:0000255}.
/FTId=PRO_5000141089.
CHAIN 1521 1608 Protein 3A. {ECO:0000255}.
/FTId=PRO_5000141090.
CHAIN 1609 1628 Protein 3B. {ECO:0000255}.
/FTId=PRO_5000141091.
CHAIN 1629 1833 Protease 3C. {ECO:0000255}.
/FTId=PRO_5000141092.
CHAIN 1834 2293 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_5000141093.
TOPO_DOM 1 1565 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1566 1584 {ECO:0000255}.
TOPO_DOM 1585 2293 Cytoplasmic. {ECO:0000255}.
DOMAIN 1282 1448 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 2062 2180 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1314 1321 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
ACT_SITE 1674 1674 For protease 3C activity. {ECO:0000255}.
ACT_SITE 1706 1706 For protease 3C activity. {ECO:0000255}.
ACT_SITE 1787 1787 For protease 3C activity. {ECO:0000255}.
SITE 137 138 Cleavage. {ECO:0000255}.
SITE 393 394 Cleavage; by protease 3C. {ECO:0000255}.
SITE 624 625 Cleavage; by protease 3C. {ECO:0000255}.
SITE 901 902 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1044 1045 Cleavage; by ribosomal skip.
{ECO:0000255}.
SITE 1195 1196 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1520 1521 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1608 1609 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1628 1629 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1833 1834 Cleavage; by protease 3C. {ECO:0000255}.
MOD_RES 1611 1611 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 68 68 N-myristoyl glycine; by host.
{ECO:0000250}.
HELIX 1 3 {ECO:0000244|PDB:2MMH}.
STRAND 8 10 {ECO:0000244|PDB:2M7Y}.
TURN 11 13 {ECO:0000244|PDB:2M7Y}.
HELIX 16 18 {ECO:0000244|PDB:2M7Y}.
HELIX 20 24 {ECO:0000244|PDB:2M7Y}.
TURN 26 30 {ECO:0000244|PDB:2MMI}.
STRAND 32 34 {ECO:0000244|PDB:2M7Y}.
STRAND 36 40 {ECO:0000244|PDB:2MMH}.
HELIX 41 45 {ECO:0000244|PDB:2MMH}.
STRAND 46 48 {ECO:0000244|PDB:2M7Y}.
TURN 54 57 {ECO:0000244|PDB:2MMI}.
STRAND 60 62 {ECO:0000244|PDB:2M7Y}.
TURN 63 65 {ECO:0000244|PDB:2M7Y}.
STRAND 78 80 {ECO:0000244|PDB:1MEC}.
HELIX 94 97 {ECO:0000244|PDB:2MEV}.
STRAND 115 117 {ECO:0000244|PDB:2MEV}.
STRAND 124 126 {ECO:0000244|PDB:1MEC}.
STRAND 133 135 {ECO:0000244|PDB:2MEV}.
HELIX 148 150 {ECO:0000244|PDB:1MEC}.
STRAND 152 155 {ECO:0000244|PDB:2MEV}.
STRAND 160 165 {ECO:0000244|PDB:2MEV}.
STRAND 169 171 {ECO:0000244|PDB:2MEV}.
HELIX 172 174 {ECO:0000244|PDB:2MEV}.
HELIX 194 196 {ECO:0000244|PDB:2MEV}.
STRAND 200 208 {ECO:0000244|PDB:2MEV}.
STRAND 216 221 {ECO:0000244|PDB:2MEV}.
HELIX 223 225 {ECO:0000244|PDB:2MEV}.
HELIX 228 230 {ECO:0000244|PDB:2MEV}.
HELIX 231 237 {ECO:0000244|PDB:2MEV}.
STRAND 240 252 {ECO:0000244|PDB:2MEV}.
STRAND 260 269 {ECO:0000244|PDB:2MEV}.
TURN 286 290 {ECO:0000244|PDB:2MEV}.
HELIX 309 314 {ECO:0000244|PDB:2MEV}.
STRAND 315 321 {ECO:0000244|PDB:2MEV}.
TURN 322 324 {ECO:0000244|PDB:2MEV}.
STRAND 326 332 {ECO:0000244|PDB:2MEV}.
STRAND 337 341 {ECO:0000244|PDB:2MEV}.
HELIX 343 345 {ECO:0000244|PDB:2MEV}.
STRAND 349 360 {ECO:0000244|PDB:2MEV}.
STRAND 368 385 {ECO:0000244|PDB:2MEV}.
TURN 402 405 {ECO:0000244|PDB:2MEV}.
HELIX 437 439 {ECO:0000244|PDB:2MEV}.
TURN 440 442 {ECO:0000244|PDB:2MEV}.
STRAND 455 460 {ECO:0000244|PDB:2MEV}.
STRAND 466 468 {ECO:0000244|PDB:1MEC}.
STRAND 470 476 {ECO:0000244|PDB:2MEV}.
HELIX 480 482 {ECO:0000244|PDB:2MEV}.
HELIX 486 491 {ECO:0000244|PDB:2MEV}.
STRAND 494 499 {ECO:0000244|PDB:2MEV}.
STRAND 501 507 {ECO:0000244|PDB:2MEV}.
STRAND 514 522 {ECO:0000244|PDB:2MEV}.
STRAND 524 526 {ECO:0000244|PDB:2MEV}.
HELIX 532 535 {ECO:0000244|PDB:2MEV}.
STRAND 538 544 {ECO:0000244|PDB:2MEV}.
STRAND 546 548 {ECO:0000244|PDB:2MEV}.
STRAND 550 555 {ECO:0000244|PDB:2MEV}.
STRAND 560 567 {ECO:0000244|PDB:2MEV}.
TURN 573 575 {ECO:0000244|PDB:1MEC}.
STRAND 579 589 {ECO:0000244|PDB:2MEV}.
STRAND 598 606 {ECO:0000244|PDB:2MEV}.
STRAND 611 615 {ECO:0000244|PDB:2MEV}.
HELIX 629 631 {ECO:0000244|PDB:2MEV}.
TURN 639 642 {ECO:0000244|PDB:2MEV}.
STRAND 654 656 {ECO:0000244|PDB:1MEC}.
HELIX 657 661 {ECO:0000244|PDB:2MEV}.
STRAND 665 670 {ECO:0000244|PDB:2MEV}.
HELIX 676 678 {ECO:0000244|PDB:2MEV}.
STRAND 685 688 {ECO:0000244|PDB:2MEV}.
STRAND 690 694 {ECO:0000244|PDB:2MEV}.
HELIX 703 705 {ECO:0000244|PDB:2MEV}.
STRAND 727 729 {ECO:0000244|PDB:2MEV}.
STRAND 731 733 {ECO:0000244|PDB:2MEV}.
HELIX 736 740 {ECO:0000244|PDB:2MEV}.
STRAND 745 758 {ECO:0000244|PDB:2MEV}.
STRAND 765 770 {ECO:0000244|PDB:2MEV}.
STRAND 788 790 {ECO:0000244|PDB:2MEV}.
STRAND 792 794 {ECO:0000244|PDB:2MEV}.
STRAND 796 799 {ECO:0000244|PDB:2MEV}.
STRAND 808 812 {ECO:0000244|PDB:2MEV}.
STRAND 817 824 {ECO:0000244|PDB:2MEV}.
STRAND 848 854 {ECO:0000244|PDB:2MEV}.
STRAND 860 873 {ECO:0000244|PDB:2MEV}.
STRAND 894 896 {ECO:0000244|PDB:1MEC}.
STRAND 1836 1838 {ECO:0000244|PDB:4NYZ}.
HELIX 1859 1862 {ECO:0000244|PDB:4NYZ}.
STRAND 1865 1868 {ECO:0000244|PDB:4NYZ}.
HELIX 1882 1885 {ECO:0000244|PDB:4NYZ}.
HELIX 1886 1890 {ECO:0000244|PDB:4NYZ}.
HELIX 1899 1916 {ECO:0000244|PDB:4NYZ}.
HELIX 1925 1930 {ECO:0000244|PDB:4NYZ}.
STRAND 1933 1935 {ECO:0000244|PDB:4NYZ}.
STRAND 1940 1942 {ECO:0000244|PDB:4NYZ}.
TURN 1946 1952 {ECO:0000244|PDB:4NYZ}.
HELIX 1955 1958 {ECO:0000244|PDB:4NYZ}.
TURN 1961 1964 {ECO:0000244|PDB:4NYZ}.
HELIX 1968 1978 {ECO:0000244|PDB:4NYZ}.
STRAND 1987 1991 {ECO:0000244|PDB:4NYZ}.
STRAND 1994 1997 {ECO:0000244|PDB:4NYZ}.
HELIX 1998 2002 {ECO:0000244|PDB:4NYZ}.
STRAND 2008 2011 {ECO:0000244|PDB:4NYZ}.
HELIX 2014 2031 {ECO:0000244|PDB:4NYZ}.
TURN 2037 2040 {ECO:0000244|PDB:4NYZ}.
HELIX 2047 2058 {ECO:0000244|PDB:4NYZ}.
STRAND 2061 2068 {ECO:0000244|PDB:4NYZ}.
TURN 2072 2075 {ECO:0000244|PDB:4NZ0}.
HELIX 2078 2087 {ECO:0000244|PDB:4NYZ}.
HELIX 2091 2093 {ECO:0000244|PDB:4NYZ}.
HELIX 2099 2107 {ECO:0000244|PDB:4NYZ}.
STRAND 2108 2113 {ECO:0000244|PDB:4NYZ}.
STRAND 2116 2122 {ECO:0000244|PDB:4NYZ}.
STRAND 2126 2128 {ECO:0000244|PDB:4NYZ}.
HELIX 2131 2150 {ECO:0000244|PDB:4NYZ}.
HELIX 2156 2158 {ECO:0000244|PDB:4NYZ}.
STRAND 2160 2164 {ECO:0000244|PDB:4NYZ}.
STRAND 2167 2174 {ECO:0000244|PDB:4NYZ}.
HELIX 2178 2186 {ECO:0000244|PDB:4NYZ}.
TURN 2187 2189 {ECO:0000244|PDB:4NYZ}.
STRAND 2195 2197 {ECO:0000244|PDB:4NYZ}.
TURN 2207 2209 {ECO:0000244|PDB:4NYZ}.
STRAND 2215 2220 {ECO:0000244|PDB:4NYZ}.
STRAND 2223 2228 {ECO:0000244|PDB:4NYZ}.
HELIX 2230 2238 {ECO:0000244|PDB:4NYZ}.
HELIX 2245 2256 {ECO:0000244|PDB:4NYZ}.
HELIX 2257 2259 {ECO:0000244|PDB:4NYZ}.
HELIX 2261 2273 {ECO:0000244|PDB:4NYZ}.
HELIX 2281 2290 {ECO:0000244|PDB:4NYZ}.
SEQUENCE 2293 AA; 255528 MW; 0394484E477B94E7 CRC64;
MATTMEQEIC AHSMTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE DDVFDPDLDM
EVVFETQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI DLSANATGSD PPKTYGQFSN
LLSGAVNAFS NMLPLLADQN TEEMENLSDR VSQDTAGNTV TNTQSTVGRL VGYGTVHDGE
HPASCADTAS EKILAVERYY TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGATLRRH
YLVKTGWRVQ VQCNASQFHA GSLLVFMAPE YPTLDVFAMD NRWSKDNLPN GTRTQTNRKG
PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT LVIAVVAPLT
YSTGASTSLD ITASIQPVRP VFNGLRHEVL SRQSPIPVTI REHAGTWYST LPDSTVPIYG
KTPVAPANYM VGEYKDFLEI AQIPTFIGNK VPNAVPYIEA SNTAVKTQPL AVYQVTLSCS
CLANTFLAAL SRNFAQYRGS LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY
AIWDLGLNSS YSFTVPFISP THFRMVGTDQ ANITNVDGWV TVWQLTPLTY PPGCPTSAKI
LTMVSAGKDF SLKMPISPAP WSPQGVENAE KGVTENTDAT ADFVAQPVYL PENQTKVAFF
YDRSSPIGAF AVKSGSLESG FAPFSNKACP NSVILTPGPQ FDPAYDQLRP QRLTEIWGNG
NEETSEVFPL KTKQDYSFCL FSPFVYYKCD LEVTLSPHTS GAHGLLVRWC PTGTPTKPTT
QVLHEVSSLS EGRTPQVYSA GPGTSNQISF VVPYNSPLSV LPAVWYNGHK RFDNTGDLGI
APNSDFGTLF FAGTKPDIKF TVYLRYKNMR VFCPRPTVFF PWPTSGDKID MTPRAGVLML
ESPNPLDVSK TYPTLHILLQ FNHRGLEARI FRHGQLWAET HAEVVLRSKT KQISFLSNGS
YPSMDATTPL NPWKSTYQAV LRAEPHRVTM DVYHKRIRPF RLPLVQKEWR TCEENVFGLY
HVFETHYAGY FSDLLIHDVE TNPGPFTFKP RQRPVFQTQG AAVSSMAQTL LPNDLASKAM
GSAFTALLDA NEDAQKAMKI IKTLSSLSDA WENVKGTLNN PEFWKQLLSR CVQLIAGMTI
AVMHPDPLTL LCLGVLTAAE ITSQTSLCEE IAAKFKTIFT TPPPRFPVIS LFQQQSPLKQ
VNDVFSLAKN LDWAVKTVEK VVDWFGTWVA QEEREQTLDQ LLQRFPEHAK RISDLRNGMA
AYVECKESFD FFEKLYNQAV KEKRTGIAAV CEKFRQKHDH ATARCEPVVI VLRGDAGQGK
SLSSQIIAQA VSKTIFGRQS VYSLPPDSDF FDGYENQFAA IMDDLGQNPD GSDFTTFCQM
VSTTNLLPNM ASLERKGTPF TSQLVVATTN LPEFRPVTIA HYPAVERRIT FDYSVSAGPV
CSKTEAGCKV LDVERAFRPT GDAPLPCFQN NCLFLEKAGL QFRDNRSKEI LSLVDVIERA
VTRIERKKKV LTAVQTLVAQ GPVDEVSFYS VVQQLKARQE ATDEQLEELQ EAFARVQERS
SVFSDWMKIS AMLCAATLAL TQVVKMAKAV KQMVRPDLVR VQLDEQEQGP YNETTRIKPK
TLQLLDVQGP NPTMDFEKFV AKFVTAPIGF VYPTGVSTQT CLLVKGRTLA VNRHMAESDW
TSIVVRGVSH TRSSVKIIAI AKAGKETDVS FIRLSSGPLF RDNTSKFVKA SDVLPHSSSP
LIGIMNVDIP MMYTGTFLKA GVSVPVETGQ TFNHCIHYKA NTRKGWCGSA ILADLGGSKK
ILGFHSAGSM GVAAASIISQ EMIDAVVQAF EPQGALERLP DGPRIHVPRK TALRPTVARQ
VFQPAFAPAV LSKFDPRTDA DVDEVAFSKH TSNQETLPPV FRMVAREYAN RVFALLGRDN
GRLSVKQALD GLEGMDPMDK NTSPGLPYTT LGMRRTDVVD WETATLIPFA AERLEKMNNK
DFSDIVYQTF LKDELRPIEK VQAAKTRIVD VPPFEHCILG RQLLGKFASK FQTQPGLELG
SAIGCDPDVH WTAFGVAMQG FERVYDVDYS NFDSTHSVAV FRLLAEEFFS EENGFDPLVK
DYLESLAISK HAYEEKRYLI TGGLPSGCAA TSMLNTIMNN IIIRAGLYLT YKNFEFDDVK
VLSYGDDLLV ATNYQLNFDR VRTSLAKTGY KITPANKTST FPLESTLEDV VFLKRKFKKE
GPLYRPVMNR EALEAMLSYY RPGTLSEKLT SITMLAVHSG KQEYDRLFAP FREVGVIVPT
FESVEYRWRS LFW


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