DNLJ_ECOLI
ID DNLJ_ECOLI Reviewed; 671 AA.
AC P15042; P78197; P78198;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; Synonyms=dnaL, lig, lop, pdeC; OrderedLocusNames=b2411, JW2403;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-13 AND
RP 666-671.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=3018436; DOI=10.1007/bf00330179;
RA Ishino Y., Shinagawa H., Makino K., Tsunasawa S., Sakiyama F., Nakata A.;
RT "Nucleotide sequence of the lig gene and primary structure of DNA ligase of
RT Escherichia coli.";
RL Mol. Gen. Genet. 204:1-7(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA O'Connor M.J., Ally A., Ally D., Zhang X., Robichaud M., Backman K.;
RL Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
RC STRAIN=PB103;
RX PubMed=9008158; DOI=10.1016/s0092-8674(00)81838-3;
RA Hale C.A., de Boer P.A.J.;
RT "Direct binding of FtsZ to ZipA, an essential component of the septal ring
RT structure that mediates cell division in E. coli.";
RL Cell 88:175-185(1997).
RN [7]
RP CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF GLU-10; TYR-22; HIS-23;
RP ASP-32; TYR-35 AND ASP-36, AND ACTIVE SITE.
RX PubMed=11781321; DOI=10.1074/jbc.m111164200;
RA Sriskanda V., Shuman S.;
RT "Conserved residues in domain Ia are required for the reaction of
RT Escherichia coli DNA ligase with NAD+.";
RL J. Biol. Chem. 277:9695-9700(2002).
RN [8]
RP MUTAGENESIS OF LYS-115; ASP-117; GLY-118; ASP-138; GLU-143; GLY-172;
RP GLU-173; ASN-198; ARG-200; ARG-208; ARG-277; ASP-285; GLY-286; VAL-288;
RP LYS-290 AND LYS-314.
RX PubMed=15671015; DOI=10.1074/jbc.m413685200;
RA Zhu H., Shuman S.;
RT "Structure-guided mutational analysis of the nucleotidyltransferase domain
RT of Escherichia coli NAD+-dependent DNA ligase (LigA).";
RL J. Biol. Chem. 280:12137-12144(2005).
RN [9]
RP MUTAGENESIS OF ARG-333; THR-334; ARG-342; ARG-379; 383-VAL-ILE-384;
RP 446-ARG-ARG-447; GLY-455; ARG-487; GLY-489; GLY-521; GLY-553 AND ARG-614.
RX PubMed=18515356; DOI=10.1074/jbc.m802945200;
RA Wang L.K., Nair P.A., Shuman S.;
RT "Structure-guided mutational analysis of the OB, HhH, and BRCT domains of
RT Escherichia coli DNA ligase.";
RL J. Biol. Chem. 283:23343-23352(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS; AMP AND
RP DNA.
RX PubMed=17466627; DOI=10.1016/j.molcel.2007.02.026;
RA Nandakumar J., Nair P.A., Shuman S.;
RT "Last stop on the road to repair: structure of E. coli DNA ligase bound to
RT nicked DNA-adenylate.";
RL Mol. Cell 26:257-271(2007).
CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC stranded DNA using NAD as a coenzyme and as the energy source for the
CC reaction. It is essential for DNA replication and repair of damaged
CC DNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2;
CC Evidence={ECO:0000269|PubMed:11781321};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11781321};
CC -!- INTERACTION:
CC P15042; P07813: leuS; NbExp=3; IntAct=EBI-553496, EBI-553345;
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily. {ECO:0000305}.
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DR EMBL; M30255; AAA24071.1; -; Genomic_DNA.
DR EMBL; M24278; AAA24070.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75464.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16282.2; -; Genomic_DNA.
DR EMBL; U74650; AAB42062.1; -; Genomic_DNA.
DR PIR; B65015; LQECC6.
DR RefSeq; NP_416906.1; NC_000913.3.
DR RefSeq; WP_000443661.1; NZ_LN832404.1.
DR PDB; 2OWO; X-ray; 2.30 A; A=1-671.
DR PDB; 4GLX; X-ray; 1.90 A; A=1-586.
DR PDB; 5TT5; X-ray; 1.55 A; A=1-671.
DR PDBsum; 2OWO; -.
DR PDBsum; 4GLX; -.
DR PDBsum; 5TT5; -.
DR AlphaFoldDB; P15042; -.
DR SMR; P15042; -.
DR BioGRID; 4259672; 152.
DR BioGRID; 851225; 9.
DR DIP; DIP-10098N; -.
DR IntAct; P15042; 20.
DR STRING; 511145.b2411; -.
DR jPOST; P15042; -.
DR PaxDb; P15042; -.
DR PRIDE; P15042; -.
DR EnsemblBacteria; AAC75464; AAC75464; b2411.
DR EnsemblBacteria; BAA16282; BAA16282; BAA16282.
DR GeneID; 946885; -.
DR KEGG; ecj:JW2403; -.
DR KEGG; eco:b2411; -.
DR PATRIC; fig|1411691.4.peg.4320; -.
DR EchoBASE; EB0529; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_007764_2_1_6; -.
DR InParanoid; P15042; -.
DR OMA; HDVEHEI; -.
DR PhylomeDB; P15042; -.
DR BioCyc; EcoCyc:EG10534-MON; -.
DR BioCyc; MetaCyc:EG10534-MON; -.
DR BRENDA; 6.5.1.2; 2026.
DR EvolutionaryTrace; P15042; -.
DR PRO; PR:P15042; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IDA:EcoliWiki.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IMP:EcoCyc.
DR GO; GO:0006288; P:base-excision repair, DNA ligation; IDA:EcoCyc.
DR GO; GO:0006266; P:DNA ligation; IDA:EcoCyc.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00114; LIGANc; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR001679; DNAligase.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF03119; DNA_ligase_ZBD; 1.
DR Pfam; PF12826; HHH_2; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00278; HhH1; 4.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR TIGRFAMs; TIGR00575; dnlj; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; Ligase; Magnesium; Metal-binding; NAD; Reference proteome;
KW Zinc.
FT CHAIN 1..671
FT /note="DNA ligase"
FT /id="PRO_0000161745"
FT DOMAIN 593..671
FT /note="BRCT"
FT REGION 330..334
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000305|PubMed:17466627"
FT REGION 453..458
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000305|PubMed:17466627"
FT REGION 519..524
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000305|PubMed:17466627"
FT REGION 551..556
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000305|PubMed:17466627"
FT ACT_SITE 115
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000269|PubMed:11781321"
FT BINDING 32..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 81..82
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000305|PubMed:17466627"
FT BINDING 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000305|PubMed:17466627"
FT BINDING 136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000305|PubMed:17466627"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000305|PubMed:17466627"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000269|PubMed:17466627"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000269|PubMed:17466627"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000269|PubMed:17466627"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588,
FT ECO:0000269|PubMed:17466627"
FT SITE 487
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000305|PubMed:17466627"
FT SITE 492
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000305|PubMed:17466627"
FT MUTAGEN 10
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 22
FT /note="Y->A,S: Reduces nick joining activity by 99.9%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 22
FT /note="Y->F: Reduces nick joining activity by 91%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 23
FT /note="H->A,Y: Reduces nick joining activity by 90%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 32
FT /note="D->A,E: Reduces nick joining activity by 99%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 32
FT /note="D->N: Reduces nick joining activity by 91%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 35
FT /note="Y->A: Reduces nick joining activity by 98%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 35
FT /note="Y->F: Reduces nick joining activity by 77%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 35
FT /note="Y->S: Reduces nick joining activity by 99.9%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 36
FT /note="D->A: Reduces nick joining activity by 99.8%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 36
FT /note="D->E: Reduces nick joining activity by 96%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 36
FT /note="D->N: Reduces nick joining activity by 88%."
FT /evidence="ECO:0000269|PubMed:11781321"
FT MUTAGEN 115
FT /note="K->Q,R: Reduces nick joining activity by 99.9%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 117
FT /note="D->E: Reduces nick joining activity by 97%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 117
FT /note="D->N: Reduces nick joining activity by 99.9%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 118
FT /note="G->A: Reduces nick joining activity by 99.9%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 138
FT /note="D->A: Reduces nick joining activity by 63%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 143
FT /note="E->A: Reduces nick joining activity by 48%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 172
FT /note="G->A: Reduces nick joining activity by 64%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 173
FT /note="E->A,D,Q: Reduces nick joining activity by 99.9%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 198
FT /note="N->A: Reduces nick joining activity by 74%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 200
FT /note="R->A,K,Q: Reduces nick joining activity by 99.9%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 208
FT /note="R->A,K,Q: Reduces nick joining activity by 99%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 277
FT /note="R->A: Reduces nick joining activity by 99%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 285
FT /note="D->E: Reduces nick joining activity by 96%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 285
FT /note="D->N: Reduces nick joining activity by 99%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 286
FT /note="G->A: Reduces nick joining activity by 86%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 288
FT /note="V->A: Reduces nick joining activity by 25%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 290
FT /note="K->A: Reduces nick joining activity by 87%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 314
FT /note="K->Q: Reduces nick joining activity by 99%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 314
FT /note="K->R: Reduces nick joining activity by 95%."
FT /evidence="ECO:0000269|PubMed:15671015"
FT MUTAGEN 333
FT /note="R->A,Q: Reduces nick joining activity by over 95%.
FT Abolishes nick joining activity; when associated with A-
FT 334."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 334
FT /note="T->A: Abolishes nick joining activity; when
FT associated with A-333."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 342
FT /note="R->A: Reduces nick joining activity by 80%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 379
FT /note="R->A,Q: Reduces nick joining activity by over 95%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 383..384
FT /note="VI->AA: Reduces nick joining activity by 95%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 446..447
FT /note="RR->AA: Reduces nick joining activity by 95%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 455
FT /note="G->A: Reduces nick joining activity by 50%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 455
FT /note="G->D,V: Reduces nick joining activity by 95%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 487
FT /note="R->A: Reduces nick joining activity by over 90%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 489
FT /note="G->D,V: Reduces nick joining activity by 95%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 521
FT /note="G->A: Reduces nick joining activity by 95%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 521
FT /note="G->D,V: Loss of nick joining activity."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 553
FT /note="G->D,V: Reduces nick joining activity by 95%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT MUTAGEN 614
FT /note="R->A: Reduces nick joining activity by 85%."
FT /evidence="ECO:0000269|PubMed:18515356"
FT CONFLICT 69
FT /note="A -> R (in Ref. 1; AAA24071)"
FT /evidence="ECO:0000305"
FT HELIX 4..23
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4GLX"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2OWO"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2OWO"
FT STRAND 110..126
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 221..233
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 318..331
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 335..348
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:5TT5"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:5TT5"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:5TT5"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 436..443
FT /evidence="ECO:0007829|PDB:5TT5"
FT TURN 446..449
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 471..475
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 479..483
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 490..503
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 522..532
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 535..540
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 543..547
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 554..565
FT /evidence="ECO:0007829|PDB:5TT5"
FT HELIX 567..578
FT /evidence="ECO:0007829|PDB:5TT5"
SQ SEQUENCE 671 AA; 73606 MW; DD2BDC64D8E65256 CRC64;
MESIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRELETKHP ELITPDSPTQ
RVGAAPLAAF SQIRHEVPML SLDNVFDEES FLAFNKRVQD RLKNNEKVTW CCELKLDGLA
VSILYENGVL VSAATRGDGT TGEDITSNVR TIRAIPLKLH GENIPARLEV RGEVFLPQAG
FEKINEDARR TGGKVFANPR NAAAGSLRQL DPRITAKRPL TFFCYGVGVL EGGELPDTHL
GRLLQFKKWG LPVSDRVTLC ESAEEVLAFY HKVEEDRPTL GFDIDGVVIK VNSLAQQEQL
GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVHVAG VLVSNATLHN
ADEIERLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEDTR EVVFPTHCPV CGSDVERVEG
EAVARCTGGL ICGAQRKESL KHFVSRRAMD VDGMGDKIID QLVEKEYVHT PADLFKLTAG
KLTGLERMGP KSAQNVVNAL EKAKETTFAR FLYALGIREV GEATAAGLAA YFGTLEALEA
ASIEELQKVP DVGIVVASHV HNFFAEESNR NVISELLAEG VHWPAPIVIN AEEIDSPFAG
KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA KAQELGIEVI
DEAEMLRLLG S
