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Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_XMRV6               Reviewed;        1733 AA.
A1Z651; Q27IE0;
19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 1.
22-NOV-2017, entry version 85.
RecName: Full=Gag-Pol polyprotein;
Short=Pr180gag-pol;
Contains:
RecName: Full=Matrix protein p15;
Short=MA;
Contains:
RecName: Full=RNA-binding phosphoprotein p12;
AltName: Full=pp12;
Contains:
RecName: Full=Capsid protein p30;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p10;
Short=NC-pol;
Contains:
RecName: Full=Protease p14;
Short=PR;
EC=3.4.23.-;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H p80;
Short=RT;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.4;
Contains:
RecName: Full=Integrase p46;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P03355};
EC=3.1.-.- {ECO:0000250|UniProtKB:P03355};
Name=gag-pol;
Xenotropic MuLV-related virus (isolate VP62) (XMRV).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Gammaretrovirus; unclassified Gammaretrovirus.
NCBI_TaxID=373193;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16609730; DOI=10.1371/journal.ppat.0020025;
Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G.,
Klein E.A., Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D.,
Silverman R.H., DeRisi J.L.;
"Identification of a novel Gammaretrovirus in prostate tumors of
patients homozygous for R462Q RNASEL variant.";
PLoS Pathog. 2:E25-E25(2006).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=17234809; DOI=10.1073/pnas.0610291104;
Dong B., Kim S., Hong S., Das Gupta J., Malathi K., Klein E.A.,
Ganem D., Derisi J.L., Chow S.A., Silverman R.H.;
"An infectious retrovirus susceptible to an IFN antiviral pathway from
human prostate tumors.";
Proc. Natl. Acad. Sci. U.S.A. 104:1655-1660(2007).
-!- FUNCTION: Matrix protein p15 targets Gag and gag-pol polyproteins
to the plasma membrane via a multipartite membrane binding signal,
that includes its myristoylated N-terminus. Also mediates nuclear
localization of the preintegration complex (By similarity).
{ECO:0000250}.
-!- FUNCTION: Capsid protein p30 forms the spherical core of the
virion that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250}.
-!- FUNCTION: Nucleocapsid protein p10 is involved in the packaging
and encapsidation of two copies of the genome. Binds with high
affinity to conserved UCUG elements within the packaging signal,
located near the 5'-end of the genome. This binding is dependent
on genome dimerization (By similarity). {ECO:0000250}.
-!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of
Gag and Gag-Pol polyproteins during or shortly after the release
of the virion from the plasma membrane. Cleavages take place as an
ordered, step-wise cascade to yield mature proteins. This process
is called maturation. Displays maximal activity during the budding
process just prior to particle release from the cell.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H is a
multifunctional enzyme that converts the viral dimeric RNA genome
into dsDNA in the cytoplasm, shortly after virus entry into the
cell. This enzyme displays a DNA polymerase activity that can copy
either DNA or RNA templates, and a ribonuclease H (RNase H)
activity that cleaves the RNA strand of RNA-DNA heteroduplexes in
a partially processive 3' to 5' endonucleasic mode. Conversion of
viral genomic RNA into dsDNA requires many steps. A tRNA binds to
the primer-binding site (PBS) situated at the 5' end of the viral
RNA. RT uses the 3' end of the tRNA primer to perform a short
round of RNA-dependent minus-strand DNA synthesis. The reading
proceeds through the U5 region and ends after the repeated (R)
region which is present at both ends of viral RNA. The portion of
the RNA-DNA heteroduplex is digested by the RNase H, resulting in
a ssDNA product attached to the tRNA primer. This ssDNA/tRNA
hybridizes with the identical R region situated at the 3' end of
viral RNA. This template exchange, known as minus-strand DNA
strong stop transfer, can be either intra- or intermolecular. RT
uses the 3' end of this newly synthesized short ssDNA to perform
the RNA-dependent minus-strand DNA synthesis of the whole
template. RNase H digests the RNA template except for a polypurine
tract (PPT) situated at the 5' end of the genome. It is not clear
if both polymerase and RNase H activities are simultaneous. RNase
H probably can proceed both in a polymerase-dependent (RNA cut
into small fragments by the same RT performing DNA synthesis) and
a polymerase-independent mode (cleavage of remaining RNA fragments
by free RTs). Secondly, RT performs DNA-directed plus-strand DNA
synthesis using the PPT that has not been removed by RNase H as
primers. PPT and tRNA primers are then removed by RNase H. The 3'
and 5' ssDNA PBS regions hybridize to form a circular dsDNA
intermediate. Strand displacement synthesis by RT to the PBS and
PPT ends produces a blunt ended, linear dsDNA copy of the viral
genome that includes long terminal repeats (LTRs) at both ends (By
similarity). {ECO:0000250}.
-!- FUNCTION: Integrase catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. This enzyme activity takes place after virion entry
into a cell and reverse transcription of the RNA genome in dsDNA.
The first step in the integration process is 3' processing. This
step requires a complex comprising the viral genome, matrix
protein and integrase. This complex is called the pre-integration
complex (PIC). The integrase protein removes 2 nucleotides from
each 3' end of the viral DNA, leaving recessed CA OH's at the 3'
ends. In the second step that requires cell division, the PIC
enters cell nucleus. In the third step, termed strand transfer,
the integrase protein joins the previously processed 3' ends to
the 5' ends of strands of target cellular DNA at the site of
integration. The last step is viral DNA integration into host
chromosome (By similarity). {ECO:0000250}.
-!- FUNCTION: Gag-Pol polyprotein plays a role in budding and is
processed by the viral protease during virion maturation outside
the cell. During budding, it recruits, in a PPXY-dependent or
independent manner, Nedd4-like ubiquitin ligases that conjugate
ubiquitin molecules to Gag, or to Gag binding host factors.
Interaction with HECT ubiquitin ligases probably link the viral
protein to the host ESCRT pathway and facilitate release (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|PROSITE-ProRule:PRU00408}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for reverse transcriptase polymerase
activity. {ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
{ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Magnesium ions are required for integrase activity. Binds at
least 1, maybe 2 magnesium ions. {ECO:0000250};
-!- SUBUNIT: Capsid protein p30 is a homohexamer, that further
associates as homomultimer. The virus core is composed of a
lattice formed from hexagonal rings, each containing six capsid
monomers. The protease is a homodimer, whose active site consists
of two apposed aspartic acid residues. The reverse transcriptase
is a monomer (By similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-7978477, EBI-7978477;
-!- SUBCELLULAR LOCATION: Gag-Pol polyprotein: Host cell membrane
{ECO:0000305}; Lipid-anchor {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Matrix protein p15: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p30: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p10: Virion
{ECO:0000305}.
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle release. They can occur individually
or in close proximity within structural proteins. They interacts
with sorting cellular proteins of the multivesicular body (MVB)
pathway. Most of these proteins are class E vacuolar protein
sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III
complexes. RNA-binding phosphoprotein p12 contains one L domain: a
PPXY motif which potentially interacts with the WW domain 3 of
NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus
egress. Matrix protein p15 contains one L domain: a PTAP/PSAP
motif, which potentially interacts with the UEV domain of TSG101.
The junction between the matrix protein p15 and RNA-binding
phosphoprotein p12 also contains one L domain: a LYPX(n)L motif
which potentially interacts with PDCD6IP. Both PSAP and LYPX(n)L
domains might play little to no role in budding and possibly drive
residual virus release. contains (By similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages by the viral protease yield
mature proteins. The protease is released by autocatalytic
cleavage. The polyprotein is cleaved during and after budding,
this process is termed maturation (By similarity). {ECO:0000250}.
-!- PTM: Capsid protein p30 is sumoylated; which is required for virus
replication.
-!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
residues. {ECO:0000250}.
-!- MISCELLANEOUS: This protein is translated as a gag-pol fusion
protein by episodic readthrough of the gag protein termination
codon. Readthrough of the terminator codon TAG occurs between the
codons for 536-Asp and 538-Gly (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The nucleocapsid protein p10 released from Pol
polyprotein (NC-pol) is a few amino acids shorter than the
nucleocapsid protein p10 released from Gag polyprotein (NC-gag).
{ECO:0000250}.
-!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme
that lacks a proof-reading function. High mutations rate is a
direct consequence of this characteristic. RT also displays
frequent template swiching leading to high recombination rate.
Recombination mostly occurs between homologous regions of the two
copackaged RNA genomes. If these two RNA molecules derive from
different viral strains, reverse transcription will give rise to
highly recombinated proviral DNAs. {ECO:0000255|PROSITE-
ProRule:PRU00405}.
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EMBL; DQ399707; ABD49687.1; -; Genomic_RNA.
EMBL; EF185282; ABM47428.1; -; Genomic_RNA.
PDB; 3NR6; X-ray; 1.97 A; A/B=533-657.
PDB; 3P1G; X-ray; 1.50 A; A=1155-1328.
PDB; 4E89; X-ray; 2.60 A; A=1164-1320.
PDB; 4HKQ; X-ray; 3.04 A; A=658-1328.
PDBsum; 3NR6; -.
PDBsum; 3P1G; -.
PDBsum; 4E89; -.
PDBsum; 4HKQ; -.
ProteinModelPortal; A1Z651; -.
SMR; A1Z651; -.
IntAct; A1Z651; 1.
MINT; MINT-8386873; -.
MEROPS; A02.008; -.
OrthoDB; VOG090000AJ; -.
Proteomes; UP000002240; Genome.
Proteomes; UP000180675; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
GO; GO:0019068; P:virion assembly; IEA:InterPro.
CDD; cd06095; RP_RTVL_H_like; 1.
Gene3D; 1.10.150.180; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 4.10.60.10; -; 1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR000840; G_retro_matrix.
InterPro; IPR036946; G_retro_matrix_sf.
InterPro; IPR002079; Gag_p12.
InterPro; IPR003036; Gag_P30.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR034145; RP_RTVL-H-like.
InterPro; IPR000477; RT_dom.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF01140; Gag_MA; 1.
Pfam; PF01141; Gag_p12; 1.
Pfam; PF02093; Gag_p30; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 2.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Capsid protein; Coiled coil;
Complete proteome; DNA integration; DNA recombination; DNA-binding;
DNA-directed DNA polymerase; Endonuclease; Host cell membrane;
Host membrane; Hydrolase; Lipoprotein; Magnesium; Membrane;
Metal-binding; Multifunctional enzyme; Myristate; Nuclease;
Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
RNA suppression of termination; RNA-binding;
RNA-directed DNA polymerase; Transferase; Ubl conjugation;
Viral genome integration; Viral matrix protein; Viral nucleoprotein;
Virion; Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 1733 Gag-Pol polyprotein. {ECO:0000250}.
/FTId=PRO_0000390868.
CHAIN 2 129 Matrix protein p15. {ECO:0000250}.
/FTId=PRO_0000390869.
CHAIN 130 213 RNA-binding phosphoprotein p12.
{ECO:0000250}.
/FTId=PRO_0000390870.
CHAIN 214 476 Capsid protein p30. {ECO:0000250}.
/FTId=PRO_0000390871.
CHAIN 477 532 Nucleocapsid protein p10. {ECO:0000250}.
/FTId=PRO_0000390872.
CHAIN 533 657 Protease p14. {ECO:0000250}.
/FTId=PRO_0000390873.
CHAIN 658 1328 Reverse transcriptase/ribonuclease H p80.
{ECO:0000250}.
/FTId=PRO_0000390874.
CHAIN 1329 1733 Integrase p46. {ECO:0000250}.
/FTId=PRO_0000390875.
DOMAIN 559 629 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 739 930 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1172 1318 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1442 1600 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 500 517 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
COILED 436 476 {ECO:0000255}.
MOTIF 109 112 PTAP/PSAP motif.
MOTIF 128 132 LYPX(n)L motif.
MOTIF 161 164 PPXY motif.
COMPBIAS 71 191 Pro-rich.
COMPBIAS 71 168 Pro-rich.
ACT_SITE 564 564 Protease; shared with dimeric partner.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
METAL 807 807 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 881 881 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 882 882 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1181 1181 Magnesium; for RNase H activity.
{ECO:0000255|PROSITE-ProRule:PRU00408}.
METAL 1219 1219 Magnesium; for RNase H activity.
{ECO:0000255|PROSITE-ProRule:PRU00408}.
METAL 1240 1240 Magnesium; for RNase H activity.
{ECO:0000255|PROSITE-ProRule:PRU00408}.
METAL 1310 1310 Magnesium; for RNase H activity.
{ECO:0000255|PROSITE-ProRule:PRU00408}.
METAL 1453 1453 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1512 1512 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
SITE 129 130 Cleavage; by viral protease p14.
{ECO:0000250}.
SITE 213 214 Cleavage; by viral protease p14.
{ECO:0000250}.
SITE 476 477 Cleavage; by viral protease p14.
{ECO:0000250}.
SITE 532 533 Cleavage; by viral protease p14.
{ECO:0000250}.
SITE 657 658 Cleavage; by viral protease p14.
{ECO:0000250}.
SITE 1328 1329 Cleavage; by viral protease p14.
{ECO:0000250}.
MOD_RES 190 190 Phosphoserine; by host. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
VARIANT 659 659 L -> V.
VARIANT 666 666 R -> W.
VARIANT 669 671 ETS -> DTR.
VARIANT 687 687 P -> L.
VARIANT 1079 1079 D -> N.
HELIX 540 542 {ECO:0000244|PDB:3NR6}.
STRAND 547 554 {ECO:0000244|PDB:3NR6}.
STRAND 557 563 {ECO:0000244|PDB:3NR6}.
STRAND 578 586 {ECO:0000244|PDB:3NR6}.
STRAND 593 598 {ECO:0000244|PDB:3NR6}.
STRAND 601 605 {ECO:0000244|PDB:3NR6}.
STRAND 608 612 {ECO:0000244|PDB:3NR6}.
STRAND 620 622 {ECO:0000244|PDB:3NR6}.
HELIX 627 633 {ECO:0000244|PDB:3NR6}.
STRAND 636 639 {ECO:0000244|PDB:3NR6}.
STRAND 644 647 {ECO:0000244|PDB:3NR6}.
HELIX 687 689 {ECO:0000244|PDB:4HKQ}.
HELIX 691 694 {ECO:0000244|PDB:4HKQ}.
HELIX 725 730 {ECO:0000244|PDB:4HKQ}.
HELIX 732 739 {ECO:0000244|PDB:4HKQ}.
TURN 740 742 {ECO:0000244|PDB:4HKQ}.
STRAND 743 746 {ECO:0000244|PDB:4HKQ}.
HELIX 775 778 {ECO:0000244|PDB:4HKQ}.
TURN 789 791 {ECO:0000244|PDB:4HKQ}.
HELIX 792 795 {ECO:0000244|PDB:4HKQ}.
STRAND 802 808 {ECO:0000244|PDB:4HKQ}.
HELIX 812 814 {ECO:0000244|PDB:4HKQ}.
STRAND 815 817 {ECO:0000244|PDB:4HKQ}.
TURN 819 821 {ECO:0000244|PDB:4HKQ}.
HELIX 822 824 {ECO:0000244|PDB:4HKQ}.
STRAND 825 827 {ECO:0000244|PDB:4HKQ}.
STRAND 840 844 {ECO:0000244|PDB:4HKQ}.
HELIX 852 870 {ECO:0000244|PDB:4HKQ}.
STRAND 874 879 {ECO:0000244|PDB:4HKQ}.
STRAND 882 889 {ECO:0000244|PDB:4HKQ}.
HELIX 890 907 {ECO:0000244|PDB:4HKQ}.
STRAND 913 915 {ECO:0000244|PDB:4HKQ}.
STRAND 917 925 {ECO:0000244|PDB:4HKQ}.
STRAND 928 931 {ECO:0000244|PDB:4HKQ}.
STRAND 934 937 {ECO:0000244|PDB:4HKQ}.
HELIX 939 946 {ECO:0000244|PDB:4HKQ}.
HELIX 954 964 {ECO:0000244|PDB:4HKQ}.
HELIX 965 970 {ECO:0000244|PDB:4HKQ}.
HELIX 974 977 {ECO:0000244|PDB:4HKQ}.
TURN 978 981 {ECO:0000244|PDB:4HKQ}.
HELIX 982 984 {ECO:0000244|PDB:4HKQ}.
HELIX 995 1009 {ECO:0000244|PDB:4HKQ}.
STRAND 1023 1030 {ECO:0000244|PDB:4HKQ}.
STRAND 1033 1042 {ECO:0000244|PDB:4HKQ}.
STRAND 1045 1055 {ECO:0000244|PDB:4HKQ}.
HELIX 1058 1062 {ECO:0000244|PDB:4HKQ}.
HELIX 1065 1084 {ECO:0000244|PDB:4HKQ}.
STRAND 1089 1095 {ECO:0000244|PDB:4HKQ}.
HELIX 1098 1102 {ECO:0000244|PDB:4HKQ}.
HELIX 1114 1121 {ECO:0000244|PDB:4HKQ}.
TURN 1124 1126 {ECO:0000244|PDB:4HKQ}.
STRAND 1127 1132 {ECO:0000244|PDB:4HKQ}.
TURN 1137 1140 {ECO:0000244|PDB:4HKQ}.
STRAND 1167 1169 {ECO:0000244|PDB:3P1G}.
STRAND 1175 1187 {ECO:0000244|PDB:3P1G}.
STRAND 1190 1198 {ECO:0000244|PDB:3P1G}.
STRAND 1203 1209 {ECO:0000244|PDB:3P1G}.
HELIX 1215 1229 {ECO:0000244|PDB:3P1G}.
TURN 1230 1232 {ECO:0000244|PDB:3P1G}.
STRAND 1233 1239 {ECO:0000244|PDB:3P1G}.
HELIX 1242 1249 {ECO:0000244|PDB:3P1G}.
HELIX 1252 1255 {ECO:0000244|PDB:4E89}.
STRAND 1257 1261 {ECO:0000244|PDB:4E89}.
HELIX 1271 1280 {ECO:0000244|PDB:3P1G}.
STRAND 1283 1291 {ECO:0000244|PDB:3P1G}.
HELIX 1293 1295 {ECO:0000244|PDB:4E89}.
STRAND 1296 1300 {ECO:0000244|PDB:4E89}.
HELIX 1301 1321 {ECO:0000244|PDB:3P1G}.
SEQUENCE 1733 AA; 193862 MW; 5A4D87D1E1D7069D CRC64;
MGQTVTTPLS LTLQHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW PQDGTFNLGV
ISQVKSRVFC PGPHGHPDQV PYIVTWEALA YDPPPWVKPF VSPKPPPLPT APVLPPGPSA
QPPSRSALYP ALTPSIKSKP PKPQVLPDSG GPLIDLLTED PPPYGAQPSS SARENNEEEA
ATTSEVSPPS PMVSRLRGRR DPPAADSTTS QAFPLRMGGD GQLQYWPFSS SDLYNWKNNN
PSFSEDPGKL TALIESVLIT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGNDGRPT
QLPNEVNAAF PLERPDWDYT TTEGRNHLVL YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN
ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA PDIGRKLERL EDLKSKTLGD
LVREAEKIFN KRETPEEREE RIRREIEEKE ERRRAEDEQR ERERDRRRHR EMSKLLATVV
IGQRQDRQGG ERRRPQLDKD QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGDXGGQ
GQEPPPEPRI TLKVGGQPVT FLVDTGAQHS VLTQNPGPLS DKSAWVQGAT GGKRYRWTTD
RKVHLATGKV THSFLHVPDC PYPLLGRDLL TKLKAQIHFE GSGAQVVGPM GQPLQVLTLN
IEDEYRLHET SKEPDVPLGS TWLSDFPQAW AETGGMGLAV RQAPLIIPLK ATSTPVSIKQ
YPMSQEARLG IKPHIQRLLD QGILVPCQSP WNTPLLPVKK PGTNDYRPVQ DLREVNKRVE
DIHPTVPNPY NLLSGLPPSH QWYTVLDLKD AFFCLRLHPT SQPLFAFEWR DPEMGISGQL
TWTRLPQGFK NSPTLFDEAL HRDLADFRIQ HPDLILLQYV DDLLLAATSE QDCQRGTRAL
LQTLGNLGYR ASAKKAQICQ KQVKYLGYLL KEGQRWLTEA RKETVMGQPT PKTPRQLREF
LGTAGFCRLW IPGFAEMAAP LYPLTKTGTL FNWGPDQQKA YQEIKQALLT APALGLPDLT
KPFELFVDEK QGYAKGVLTQ KLGPWRRPVA YLSKKLDPVA AGWPPCLRMV AAIAVLTKDA
GKLTMGQPLV ILAPHAVEAL VKQPPDRWLS NARMTHYQAM LLDTDRVQFG PVVALNPATL
LPLPEKEAPH DCLEILAETH GTRPDLTDQP IPDADYTWYT DGSSFLQEGQ RRAGAAVTTE
TEVIWARALP AGTSAQRAEL IALTQALKMA EGKKLNVYTD SRYAFATAHV HGEIYRRRGL
LTSEGREIKN KNEILALLKA LFLPKRLSII HCPGHQKGNS AEARGNRMAD QAAREAAMKA
VLETSTLLIE DSTPYTPPHF HYTETDLKRL RELGATYNQT KGYWVLQGKP VMPDQSVFEL
LDSLHRLTHL SPQKMKALLD REESPYYMLN RDRTIQYVTE TCTACAQVNA SKAKIGAGVR
VRGHRPGTHW EVDFTEVKPG LYGYKYLLVF VDTFSGWVEA FPTKRETAKV VSKKLLEDIF
PRFGMPQVLG SDNGPAFASQ VSQSVADLLG IDWKLHCAYR PQSSGQVERM NRTIKETLTK
LTLASGTRDW VLLLPLALYR ARNTPGPHGL TPYEILYGAP PPLVNFHDPE MSKLTNSPSL
QAHLQALQAV QQEVWKPLAA AYQDQLDQPV IPHPFRVGDA VWVRRHQTKN LEPRWKGPYT
VLLTTPTALK VDGISAWIHA AHVKAATTPP AGTAWKVQRS QNPLKIRLTR GAP


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