DPOL_THEKO
ID DPOL_THEKO Reviewed; 1671 AA.
AC P77933; Q5JEA7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7 {ECO:0000269|PubMed:9361436};
DE Contains:
DE RecName: Full=Homing endonuclease PI-PkoI {ECO:0000303|PubMed:12654995, ECO:0000303|PubMed:9742242};
DE EC=3.1.-.- {ECO:0000269|PubMed:9742242};
DE AltName: Full=IVS-A;
DE AltName: Full=Pko pol-1 intein;
DE Contains:
DE RecName: Full=Homing endonuclease PI-PkoII {ECO:0000303|PubMed:12654995, ECO:0000303|PubMed:9742242};
DE EC=3.1.-.- {ECO:0000269|PubMed:9742242};
DE AltName: Full=IVS-B;
DE AltName: Full=Pko pol-2 intein;
GN Name=pol; OrderedLocusNames=TK0001;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PROBABLE
RP INTEINS, BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=9361436; DOI=10.1128/aem.63.11.4504-4510.1997;
RA Takagi M., Nishioka M., Kakihara H., Kitabayashi M., Inoue H., Kawakami B.,
RA Oka M., Imanaka T.;
RT "Characterization of DNA polymerase from Pyrococcus sp. strain KOD1 and its
RT application to PCR.";
RL Appl. Environ. Microbiol. 63:4504-4510(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [3]
RP PROTEIN SEQUENCE OF 408-411 AND 852-857, CHARACTERIZATION OF INTEIN
RP ENDONUCLEASE ACTIVITY, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=9742242; DOI=10.1093/nar/26.19.4409;
RA Nishioka M., Fujiwara S., Takagi M., Imanaka T.;
RT "Characterization of two intein homing endonucleases encoded in the DNA
RT polymerase gene of Pyrococcus kodakaraensis strain KOD1.";
RL Nucleic Acids Res. 26:4409-4412(1998).
RN [4]
RP NOMENCLATURE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
RN [5] {ECO:0007744|PDB:1WNS}
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF DNA POLYMERASE, AND DISULFIDE
RP BONDS.
RX PubMed=11178906; DOI=10.1006/jmbi.2000.4403;
RA Hashimoto H., Nishioka M., Fujiwara S., Takagi M., Imanaka T., Inoue T.,
RA Kai Y.;
RT "Crystal structure of DNA polymerase from hyperthermophilic archaeon
RT Pyrococcus kodakaraensis KOD1.";
RL J. Mol. Biol. 306:469-477(2001).
CC -!- FUNCTION: Has high processivity, a high polymerization rate and high
CC fidelity. In addition to polymerase activity, also exhibits 3' to 5'
CC exonuclease activity. {ECO:0000269|PubMed:9361436}.
CC -!- FUNCTION: Intein encoded endonucleases are thought to mediate intein
CC mobility by site-specific recombination initiated by endonuclease
CC cleavage at the 'homing site' in genes that lack the intein (Probable).
CC Upon expression in E.coli PI-PkoI recognizes the minimal sequence 5'-
CC GATTTTAGATCCCTGTACC-3' and cuts after T-10. PI-PkoII recognizes the
CC minimal sequence 5'-CAGCTACTACGGTTAC-3' and cuts after C-10. Given the
CC high intracellular K(+) content (>0.5 M), PI-PkoII is probably more
CC active than PI-PkoI in vivo (PubMed:9742242).
CC {ECO:0000269|PubMed:9742242, ECO:0000305}.
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 Evidence={ECO:0000269|PubMed:9361436};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC DNA polymerase optimum pH is 6.5, very thermostable, has a half-life
CC of 12 hours at 95 and 3 hours at 100 degrees Celsius, for protein
CC cloned without inteins in E.coli. {ECO:0000269|PubMed:9361436};
CC Temperature dependence:
CC DNA polymerase optimum temperature is 75 degrees Celsius, for protein
CC cloned without inteins in E.coli (PubMed:9361436). Both intein
CC endonucleases are thermostable (PubMed:9742242).
CC {ECO:0000269|PubMed:9361436, ECO:0000269|PubMed:9742242};
CC -!- PTM: Undergoes a protein self splicing that involves a post-
CC translational excision of the intervening region (intein) followed by
CC peptide ligation. {ECO:0000305|PubMed:9361436,
CC ECO:0000305|PubMed:9742242}.
CC -!- BIOTECHNOLOGY: Pyrococcus kodakaraensis enzyme is a very fast,
CC thermostable DNA polymerase (130 nucleotides/s) used in high-
CC performance PCR. {ECO:0000269|PubMed:9361436}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; D29671; BAA06142.2; -; Genomic_DNA.
DR EMBL; AP006878; BAD84190.1; -; Genomic_DNA.
DR PIR; S71551; S71551.
DR RefSeq; WP_011248956.1; NC_006624.1.
DR PDB; 1WN7; X-ray; 2.75 A; A=1-810.
DR PDB; 1WNS; X-ray; 3.00 A; A=1-1671.
DR PDB; 2CW7; X-ray; 2.70 A; A=852-1388.
DR PDB; 2CW8; X-ray; 2.50 A; A=852-1388.
DR PDB; 4K8Z; X-ray; 2.29 A; A=1-1671.
DR PDB; 5OMF; X-ray; 2.09 A; A=1-1671.
DR PDB; 6Q4T; X-ray; 2.00 A; A=1-1671.
DR PDB; 7OM3; X-ray; 1.92 A; A=1-1671.
DR PDB; 7OMB; X-ray; 2.01 A; A=1-1671.
DR PDB; 7OMG; X-ray; 2.10 A; A=1-1671.
DR PDBsum; 1WN7; -.
DR PDBsum; 1WNS; -.
DR PDBsum; 2CW7; -.
DR PDBsum; 2CW8; -.
DR PDBsum; 4K8Z; -.
DR PDBsum; 5OMF; -.
DR PDBsum; 6Q4T; -.
DR PDBsum; 7OM3; -.
DR PDBsum; 7OMB; -.
DR PDBsum; 7OMG; -.
DR AlphaFoldDB; P77933; -.
DR SMR; P77933; -.
DR STRING; 69014.TK0001; -.
DR MEROPS; N10.007; -.
DR REBASE; 3792; PI-PkoI.
DR REBASE; 3793; PI-PkoII.
DR EnsemblBacteria; BAD84190; BAD84190; TK0001.
DR GeneID; 3233723; -.
DR KEGG; tko:TK0001; -.
DR PATRIC; fig|69014.16.peg.1; -.
DR eggNOG; arCOG00328; Archaea.
DR eggNOG; arCOG03145; Archaea.
DR HOGENOM; CLU_000203_6_4_2; -.
DR InParanoid; P77933; -.
DR OMA; YAHNSYY; -.
DR OrthoDB; 35869at2157; -.
DR BRENDA; 2.7.7.7; 5246.
DR EvolutionaryTrace; P77933; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.10.28.10; -; 2.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 3.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR041005; PI-TkoII_IV.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00136; DNA_pol_B; 2.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR Pfam; PF14528; LAGLIDADG_3; 3.
DR Pfam; PF18714; PI-TkoII_IV; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 2.
DR SMART; SM00306; HintN; 2.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF51294; SSF51294; 2.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55608; SSF55608; 2.
DR SUPFAM; SSF56672; SSF56672; 3.
DR TIGRFAMs; TIGR01443; intein_Cterm; 2.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 2.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR PROSITE; PS50817; INTEIN_N_TER; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Direct protein sequencing;
KW Disulfide bond; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Endonuclease; Exonuclease; Hydrolase; Intron homing; Nuclease;
KW Nucleotidyltransferase; Protein splicing; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..407
FT /note="DNA polymerase, 1st part"
FT /id="PRO_0000007325"
FT CHAIN 408..766
FT /note="Homing endonuclease PI-PkoI"
FT /evidence="ECO:0000269|PubMed:9742242"
FT /id="PRO_0000007326"
FT CHAIN 767..851
FT /note="DNA polymerase, 2nd part"
FT /id="PRO_0000007327"
FT CHAIN 852..1388
FT /note="Homing endonuclease PI-PkoII"
FT /evidence="ECO:0000269|PubMed:9742242"
FT /id="PRO_0000007328"
FT CHAIN 1389..1671
FT /note="DNA polymerase, 3rd part"
FT /id="PRO_0000007329"
FT DOMAIN 524..665
FT /note="DOD-type homing endonuclease 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 1132..1265
FT /note="DOD-type homing endonuclease 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT REGION 135..326
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000305"
FT DISULFID 788..802
FT /evidence="ECO:0000269|PubMed:11178906,
FT ECO:0007744|PDB:1WNS"
FT DISULFID 1403..1406
FT /evidence="ECO:0000269|PubMed:11178906,
FT ECO:0007744|PDB:1WNS"
FT CONFLICT 911
FT /note="K -> N (in Ref. 1; BAA06142)"
FT /evidence="ECO:0000305"
FT CONFLICT 1120..1121
FT /note="SP -> RK (in Ref. 1; BAA06142)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:7OM3"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 305..337
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 395..406
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 768..775
FT /evidence="ECO:0007829|PDB:7OM3"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:7OM3"
FT TURN 795..797
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 808..829
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 833..850
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 858..863
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 866..871
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 872..881
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 893..897
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 900..906
FT /evidence="ECO:0007829|PDB:2CW8"
FT TURN 908..910
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 913..935
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 940..944
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 948..953
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 956..961
FT /evidence="ECO:0007829|PDB:2CW8"
FT TURN 962..964
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 970..975
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 985..987
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 988..993
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 997..999
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1004..1011
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1015..1026
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1036..1046
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1048..1051
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1053..1059
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1061..1077
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1079..1081
FT /evidence="ECO:0007829|PDB:2CW7"
FT TURN 1082..1084
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1085..1088
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1091..1094
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1095..1098
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1103..1106
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1110..1112
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1118..1124
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1127..1139
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1140..1145
FT /evidence="ECO:0007829|PDB:2CW8"
FT TURN 1147..1150
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1153..1159
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1163..1177
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1184..1189
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1192..1202
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1206..1208
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1213..1215
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1220..1234
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1240..1248
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1250..1262
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1268..1272
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1277..1281
FT /evidence="ECO:0007829|PDB:2CW8"
FT TURN 1292..1295
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1298..1300
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1304..1311
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1321..1329
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1335..1338
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1339..1341
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1342..1346
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1347..1371
FT /evidence="ECO:0007829|PDB:2CW8"
FT TURN 1372..1374
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1376..1379
FT /evidence="ECO:0007829|PDB:2CW8"
FT STRAND 1384..1387
FT /evidence="ECO:0007829|PDB:2CW8"
FT HELIX 1390..1394
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1404..1429
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 1432..1444
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1450..1467
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 1474..1487
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 1490..1495
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 1500..1505
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1506..1508
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 1510..1512
FT /evidence="ECO:0007829|PDB:4K8Z"
FT HELIX 1514..1528
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1533..1548
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1554..1557
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 1559..1562
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1567..1569
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1575..1585
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 1595..1602
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1607..1610
FT /evidence="ECO:0007829|PDB:7OM3"
FT STRAND 1611..1613
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1614..1616
FT /evidence="ECO:0007829|PDB:7OM3"
FT TURN 1619..1621
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1626..1631
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1634..1642
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1643..1645
FT /evidence="ECO:0007829|PDB:7OM3"
FT HELIX 1649..1651
FT /evidence="ECO:0007829|PDB:7OM3"
SQ SEQUENCE 1671 AA; 193405 MW; D9C0029BE7EE2203 CRC64;
MILDTDYITE DGKPVIRIFK KENGEFKIEY DRTFEPYFYA LLKDDSAIEE VKKITAERHG
TVVTVKRVEK VQKKFLGRPV EVWKLYFTHP QDVPAIRDKI REHPAVIDIY EYDIPFAKRY
LIDKGLVPME GDEELKMLAF DIETLYHEGE EFAEGPILMI SYADEEGARV ITWKNVDLPY
VDVVSTEREM IKRFLRVVKE KDPDVLITYN GDNFDFAYLK KRCEKLGINF ALGRDGSEPK
IQRMGDRFAV EVKGRIHFDL YPVIRRTINL PTYTLEAVYE AVFGQPKEKV YAEEITTAWE
TGENLERVAR YSMEDAKVTY ELGKEFLPME AQLSRLIGQS LWDVSRSSTG NLVEWFLLRK
AYERNELAPN KPDEKELARR RQSYEGGYVK EPERGLWENI VYLDFRCHPA DTKVVVKGKG
IINISEVQEG DYVLGIDGWQ RVRKVWEYDY KGELVNINGL KCTPNHKLPV VTKNERQTRI
RDSLAKSFLT KKVKGKIITT PLFYEIGRAT SENIPEEEVL KGELAGILLA EGTLLRKDVE
YFDSSRKKRR ISHQYRVEIT IGKDEEEFRD RITYIFERLF GITPSISEKK GTNAVTLKVA
KKNVYLKVKE IMDNIESLHA PSVLRGFFEG DGSVNRVRRS IVATQGTKNE WKIKLVSKLL
SQLGIPHQTY TYQYQENGKD RSRYILEITG KDGLILFQTL IGFISERKNA LLNKAISQRE
MNNLENNGFY RLSEFNVSTE YYEGKVYDLT LEGTPYYFAN GILTHNSLYP SIIITHNVSP
DTLNREGCKE YDVAPQVGHR FCKDFPGFIP SLLGDLLEER QKIKKKMKAT IDPIERKLLD
YRQRAIKILA NSILPEEWLP VLEEGEVHFV RIGELIDRMM EENAGKVKRE GETEVLEVSG
LEVPSFNRRT KKAELKRVKA LIRHDYSGKV YTIRLKSGRR IKITSGHSLF SVRNGELVEV
TGDELKPGDL VAVPRRLELP ERNHVLNLVE LLLGTPEEET LDIVMTIPVK GKKNFFKGML
RTLRWIFGEE KRPRTARRYL RHLEDLGYVR LKKIGYEVLD WDSLKNYRRL YEALVENVRY
NGNKREYLVE FNSIRDAVGI MPLKELKEWK IGTLNGFRMS PLIEVDESLA KLLGYYVSEG
YARKQRNPKN GWSYSVKLYN EDPEVLDDME RLASRFFGKV RRGRNYVEIP KKIGYLLFEN
MCGVLAENKR IPEFVFTSPK GVRLAFLEGY FIGDGDVHPN KRLRLSTKSE LLANQLVLLL
NSVGVSAVKL GHDSGVYRVY INEELPFVKL DKKKNAYYSH VIPKEVLSEV FGKVFQKNVS
PQTFRKMVED GRLDPEKAQR LSWLIEGDVV LDRVESVDVE DYDGYVYDLS VEDNENFLVG
FGLVYAHNSY YGYYGYARAR WYCKECAESV TAWGREYITM TIKEIEEKYG FKVIYSDTDG
FFATIPGADA ETVKKKAMEF LKYINAKLPG ALELEYEGFY KRGFFVTKKK YAVIDEEGKI
TTRGLEIVRR DWSEIAKETQ ARVLEALLKD GDVEKAVRIV KEVTEKLSKY EVPPEKLVIH
EQITRDLKDY KATGPHVAVA KRLAARGVKI RPGTVISYIV LKGSGRIGDR AIPFDEFDPT
KHKYDAEYYI ENQVLPAVER ILRAFGYRKE DLRYQKTRQV GLSAWLKPKG T
