DPO1_THEAQ
ID DPO1_THEAQ Reviewed; 832 AA.
AC P19821;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA polymerase I, thermostable;
DE EC=2.7.7.7;
DE AltName: Full=Taq polymerase 1;
GN Name=polA; Synonyms=pol1;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2649500; DOI=10.1016/s0021-9258(18)83367-1;
RA Lawyer F.C., Stoffel S., Saiki R.K., Myambo K., Drummond R., Gelfand D.H.;
RT "Isolation, characterization, and expression in Escherichia coli of the DNA
RT polymerase gene from Thermus aquaticus.";
RL J. Biol. Chem. 264:6427-6437(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=7896728; DOI=10.1093/oxfordjournals.jbchem.a124622;
RA Ishino Y., Ueno T., Miyagi M., Uemori T., Imamura M., Tsunasawa S.,
RA Kato I.;
RT "Overproduction of Thermus aquaticus DNA polymerase and its structural
RT analysis by ion-spray mass spectrometry.";
RL J. Biochem. 116:1019-1024(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=7637814; DOI=10.1038/376612a0;
RA Kim Y., Eom S.H., Wang J., Lee D.-S., Suh S.W., Steitz T.A.;
RT "Crystal structure of Thermus aquaticus DNA polymerase.";
RL Nature 376:612-616(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 290-832.
RX PubMed=7568114; DOI=10.1073/pnas.92.20.9264;
RA Korolev S., Nayal M., Barnes W.M., di Cera E., Waksman G.;
RT "Crystal structure of the large fragment of Thermus aquaticus DNA
RT polymerase I at 2.5-A resolution: structural basis for thermostability.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9264-9268(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=8717047; DOI=10.1038/382278a0;
RA Eom S.H., Wang J., Steitz T.A.;
RT "Structure of Taq polymerase with DNA at the polymerase active site.";
RL Nature 382:278-281(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 295-832.
RX PubMed=9857206; DOI=10.1093/emboj/17.24.7514;
RA Li Y., Korolev S., Waksman G.;
RT "Crystal structures of open and closed forms of binary and ternary
RT complexes of the large fragment of Thermus aquaticus DNA polymerase I:
RT structural basis for nucleotide incorporation.";
RL EMBO J. 17:7514-7525(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 290-832.
RX PubMed=9605316; DOI=10.1002/pro.5560070505;
RA Li Y., Kong Y., Korolev S., Waksman G.;
RT "Crystal structures of the Klenow fragment of Thermus aquaticus DNA
RT polymerase I complexed with deoxyribonucleoside triphosphates.";
RL Protein Sci. 7:1116-1123(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 293-831.
RX PubMed=10449720; DOI=10.1073/pnas.96.17.9491;
RA Li Y., Mitaxov V., Waksman G.;
RT "Structure-based design of Taq DNA polymerases with improved properties of
RT dideoxynucleotide incorporation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9491-9496(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- BIOTECHNOLOGY: Used in the PCR method because of its high
CC thermostability. Has a relatively high error rate because it lacks
CC exonuclease proofreading functionality.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J04639; AAA27507.1; -; Genomic_DNA.
DR EMBL; D32013; BAA06775.1; -; Genomic_DNA.
DR PIR; A33530; A33530.
DR PIR; JX0359; JX0359.
DR PDB; 1BGX; X-ray; 2.30 A; T=1-832.
DR PDB; 1JXE; X-ray; 2.85 A; A=293-832.
DR PDB; 1KTQ; X-ray; 2.50 A; A=290-832.
DR PDB; 1QSS; X-ray; 2.30 A; A=293-831.
DR PDB; 1QSY; X-ray; 2.30 A; A=293-831.
DR PDB; 1QTM; X-ray; 2.30 A; A=293-831.
DR PDB; 1TAQ; X-ray; 2.40 A; A=1-832.
DR PDB; 1TAU; X-ray; 3.00 A; A=1-832.
DR PDB; 2KTQ; X-ray; 2.30 A; A=295-832.
DR PDB; 3KTQ; X-ray; 2.30 A; A=293-832.
DR PDB; 3LWL; X-ray; 2.25 A; A=293-832.
DR PDB; 3LWM; X-ray; 2.19 A; A=293-832.
DR PDB; 3M8R; X-ray; 2.00 A; A=293-832.
DR PDB; 3M8S; X-ray; 2.20 A; A=293-832.
DR PDB; 3OJS; X-ray; 1.90 A; A=293-832.
DR PDB; 3OJU; X-ray; 2.00 A; A=293-832.
DR PDB; 3PO4; X-ray; 1.80 A; A=293-832.
DR PDB; 3PO5; X-ray; 2.39 A; A=293-832.
DR PDB; 3PY8; X-ray; 1.74 A; A=293-832.
DR PDB; 3RR7; X-ray; 1.95 A; A=293-832.
DR PDB; 3RR8; X-ray; 2.40 A; A=293-832.
DR PDB; 3RRG; X-ray; 2.30 A; A=293-832.
DR PDB; 3RRH; X-ray; 1.80 A; A=293-832.
DR PDB; 3RTV; X-ray; 1.90 A; A=293-832.
DR PDB; 3SV3; X-ray; 2.10 A; A=293-832.
DR PDB; 3SV4; X-ray; 1.99 A; A=293-832.
DR PDB; 3SYZ; X-ray; 1.95 A; A=293-832.
DR PDB; 3SZ2; X-ray; 2.15 A; A=293-832.
DR PDB; 3T3F; X-ray; 1.90 A; A=293-832.
DR PDB; 4BWJ; X-ray; 1.55 A; A=293-832.
DR PDB; 4BWM; X-ray; 1.75 A; A=293-832.
DR PDB; 4C8K; X-ray; 2.17 A; A=293-832.
DR PDB; 4C8L; X-ray; 1.70 A; A=293-832.
DR PDB; 4C8M; X-ray; 1.57 A; A=293-832.
DR PDB; 4C8N; X-ray; 1.88 A; A=293-832.
DR PDB; 4C8O; X-ray; 1.75 A; A=293-832.
DR PDB; 4CCH; X-ray; 2.55 A; A=293-832.
DR PDB; 4DF4; X-ray; 2.20 A; A=293-832.
DR PDB; 4DF8; X-ray; 2.00 A; A=293-832.
DR PDB; 4DFJ; X-ray; 1.90 A; A=293-832.
DR PDB; 4DFK; X-ray; 1.65 A; A=293-832.
DR PDB; 4DFM; X-ray; 1.89 A; A=293-832.
DR PDB; 4DFP; X-ray; 2.00 A; A=293-832.
DR PDB; 4DLE; X-ray; 2.44 A; A=293-832.
DR PDB; 4DLG; X-ray; 1.89 A; A=293-832.
DR PDB; 4ELT; X-ray; 2.20 A; A=293-832.
DR PDB; 4ELU; X-ray; 1.80 A; A=293-832.
DR PDB; 4ELV; X-ray; 1.90 A; A=293-832.
DR PDB; 4KTQ; X-ray; 2.50 A; A=294-832.
DR PDB; 4N56; X-ray; 2.20 A; A=281-832.
DR PDB; 4N5S; X-ray; 1.67 A; A=281-832.
DR PDB; 4XIU; X-ray; 2.50 A; A=294-832.
DR PDB; 5E41; X-ray; 1.80 A; A=293-832.
DR PDB; 5KTQ; X-ray; 2.50 A; A=290-832.
DR PDB; 5NKL; X-ray; 1.70 A; A=293-832.
DR PDB; 5O7T; X-ray; 1.80 A; A=293-832.
DR PDB; 5OXJ; X-ray; 2.00 A; A=293-832.
DR PDB; 5SZT; X-ray; 1.80 A; A=293-832.
DR PDB; 5W6K; X-ray; 2.34 A; A=293-832.
DR PDB; 5W6Q; X-ray; 2.66 A; A/C/G=293-832.
DR PDB; 5YTC; X-ray; 2.28 A; A=294-832.
DR PDB; 5YTD; X-ray; 2.00 A; A=294-832.
DR PDB; 5YTE; X-ray; 2.21 A; A=294-832.
DR PDB; 5YTF; X-ray; 1.98 A; A=294-832.
DR PDB; 5YTG; X-ray; 2.07 A; A=294-832.
DR PDB; 5YTH; X-ray; 2.53 A; A=294-832.
DR PDB; 5Z3N; X-ray; 1.91 A; A=294-832.
DR PDB; 6FBC; X-ray; 1.54 A; A=293-832.
DR PDB; 6FBD; X-ray; 2.10 A; A=293-832.
DR PDB; 6FBE; X-ray; 1.59 A; A=293-832.
DR PDB; 6FBF; X-ray; 2.00 A; A=293-832.
DR PDB; 6FBG; X-ray; 1.70 A; A=293-832.
DR PDB; 6FBH; X-ray; 1.80 A; A=293-832.
DR PDB; 6FBI; X-ray; 1.90 A; A=293-832.
DR PDB; 6Q4U; X-ray; 2.00 A; A=293-832.
DR PDB; 6Q4V; X-ray; 2.01 A; A=293-832.
DR PDBsum; 1BGX; -.
DR PDBsum; 1JXE; -.
DR PDBsum; 1KTQ; -.
DR PDBsum; 1QSS; -.
DR PDBsum; 1QSY; -.
DR PDBsum; 1QTM; -.
DR PDBsum; 1TAQ; -.
DR PDBsum; 1TAU; -.
DR PDBsum; 2KTQ; -.
DR PDBsum; 3KTQ; -.
DR PDBsum; 3LWL; -.
DR PDBsum; 3LWM; -.
DR PDBsum; 3M8R; -.
DR PDBsum; 3M8S; -.
DR PDBsum; 3OJS; -.
DR PDBsum; 3OJU; -.
DR PDBsum; 3PO4; -.
DR PDBsum; 3PO5; -.
DR PDBsum; 3PY8; -.
DR PDBsum; 3RR7; -.
DR PDBsum; 3RR8; -.
DR PDBsum; 3RRG; -.
DR PDBsum; 3RRH; -.
DR PDBsum; 3RTV; -.
DR PDBsum; 3SV3; -.
DR PDBsum; 3SV4; -.
DR PDBsum; 3SYZ; -.
DR PDBsum; 3SZ2; -.
DR PDBsum; 3T3F; -.
DR PDBsum; 4BWJ; -.
DR PDBsum; 4BWM; -.
DR PDBsum; 4C8K; -.
DR PDBsum; 4C8L; -.
DR PDBsum; 4C8M; -.
DR PDBsum; 4C8N; -.
DR PDBsum; 4C8O; -.
DR PDBsum; 4CCH; -.
DR PDBsum; 4DF4; -.
DR PDBsum; 4DF8; -.
DR PDBsum; 4DFJ; -.
DR PDBsum; 4DFK; -.
DR PDBsum; 4DFM; -.
DR PDBsum; 4DFP; -.
DR PDBsum; 4DLE; -.
DR PDBsum; 4DLG; -.
DR PDBsum; 4ELT; -.
DR PDBsum; 4ELU; -.
DR PDBsum; 4ELV; -.
DR PDBsum; 4KTQ; -.
DR PDBsum; 4N56; -.
DR PDBsum; 4N5S; -.
DR PDBsum; 4XIU; -.
DR PDBsum; 5E41; -.
DR PDBsum; 5KTQ; -.
DR PDBsum; 5NKL; -.
DR PDBsum; 5O7T; -.
DR PDBsum; 5OXJ; -.
DR PDBsum; 5SZT; -.
DR PDBsum; 5W6K; -.
DR PDBsum; 5W6Q; -.
DR PDBsum; 5YTC; -.
DR PDBsum; 5YTD; -.
DR PDBsum; 5YTE; -.
DR PDBsum; 5YTF; -.
DR PDBsum; 5YTG; -.
DR PDBsum; 5YTH; -.
DR PDBsum; 5Z3N; -.
DR PDBsum; 6FBC; -.
DR PDBsum; 6FBD; -.
DR PDBsum; 6FBE; -.
DR PDBsum; 6FBF; -.
DR PDBsum; 6FBG; -.
DR PDBsum; 6FBH; -.
DR PDBsum; 6FBI; -.
DR PDBsum; 6Q4U; -.
DR PDBsum; 6Q4V; -.
DR AlphaFoldDB; P19821; -.
DR SMR; P19821; -.
DR BindingDB; P19821; -.
DR ChEMBL; CHEMBL3564; -.
DR DrugBank; DB03258; 2'-Deoxycytidine 5'-triphosphate.
DR DrugBank; DB03152; B-2-Octylglucoside.
DR ABCD; P19821; 1 sequenced antibody.
DR BRENDA; 2.7.7.7; 6334.
DR EvolutionaryTrace; P19821; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR GO; GO:0001882; F:nucleoside binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR CDD; cd09898; H3TH_53EXO; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015361; Taq_pol_thermo_exonuc.
DR PANTHER; PTHR10133; PTHR10133; 2.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF09281; Taq-exonuc; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00593; pola; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..832
FT /note="DNA polymerase I, thermostable"
FT /id="PRO_0000101256"
FT DOMAIN 175..261
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000255"
FT REGION 410..832
FT /note="Polymerase"
FT /evidence="ECO:0000250"
FT CONFLICT 155
FT /note="V -> A (in Ref. 2; BAA06775)"
FT /evidence="ECO:0000305"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1TAQ"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1TAQ"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1TAQ"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1BGX"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1TAQ"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1TAQ"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:1TAQ"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1TAQ"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1BGX"
FT TURN 179..184
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1BGX"
FT TURN 203..207
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1TAQ"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1BGX"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1TAQ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:1BGX"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:1TAQ"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4DLE"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:6FBC"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 373..380
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 402..419
FT /evidence="ECO:0007829|PDB:6FBC"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 424..432
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 453..478
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 487..495
FT /evidence="ECO:0007829|PDB:6FBC"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:1BGX"
FT HELIX 516..520
FT /evidence="ECO:0007829|PDB:6FBC"
FT TURN 521..525
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 527..544
FT /evidence="ECO:0007829|PDB:6FBC"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:6FBC"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 575..579
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:4C8M"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:4C8L"
FT HELIX 589..595
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 604..611
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 614..623
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 626..633
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 638..647
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 656..670
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 675..682
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 686..699
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 702..717
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:5KTQ"
FT STRAND 727..729
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 731..734
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 738..775
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 778..782
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 784..792
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 796..808
FT /evidence="ECO:0007829|PDB:6FBC"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:1BGX"
FT STRAND 819..826
FT /evidence="ECO:0007829|PDB:6FBC"
FT HELIX 827..830
FT /evidence="ECO:0007829|PDB:6FBC"
SQ SEQUENCE 832 AA; 93910 MW; F1731055B5246F03 CRC64;
MRGMLPLFEP KGRVLLVDGH HLAYRTFHAL KGLTTSRGEP VQAVYGFAKS LLKALKEDGD
AVIVVFDAKA PSFRHEAYGG YKAGRAPTPE DFPRQLALIK ELVDLLGLAR LEVPGYEADD
VLASLAKKAE KEGYEVRILT ADKDLYQLLS DRIHVLHPEG YLITPAWLWE KYGLRPDQWA
DYRALTGDES DNLPGVKGIG EKTARKLLEE WGSLEALLKN LDRLKPAIRE KILAHMDDLK
LSWDLAKVRT DLPLEVDFAK RREPDRERLR AFLERLEFGS LLHEFGLLES PKALEEAPWP
PPEGAFVGFV LSRKEPMWAD LLALAAARGG RVHRAPEPYK ALRDLKEARG LLAKDLSVLA
LREGLGLPPG DDPMLLAYLL DPSNTTPEGV ARRYGGEWTE EAGERAALSE RLFANLWGRL
EGEERLLWLY REVERPLSAV LAHMEATGVR LDVAYLRALS LEVAEEIARL EAEVFRLAGH
PFNLNSRDQL ERVLFDELGL PAIGKTEKTG KRSTSAAVLE ALREAHPIVE KILQYRELTK
LKSTYIDPLP DLIHPRTGRL HTRFNQTATA TGRLSSSDPN LQNIPVRTPL GQRIRRAFIA
EEGWLLVALD YSQIELRVLA HLSGDENLIR VFQEGRDIHT ETASWMFGVP REAVDPLMRR
AAKTINFGVL YGMSAHRLSQ ELAIPYEEAQ AFIERYFQSF PKVRAWIEKT LEEGRRRGYV
ETLFGRRRYV PDLEARVKSV REAAERMAFN MPVQGTAADL MKLAMVKLFP RLEEMGARML
LQVHDELVLE APKERAEAVA RLAKEVMEGV YPLAVPLEVE VGIGEDWLSA KE
