SDEA_LEGPH
ID SDEA_LEGPH Reviewed; 1499 AA.
AC Q5ZTK4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Ubiquitinating/deubiquitinating enzyme SdeA {ECO:0000305};
DE AltName: Full=Effector protein SdeA {ECO:0000303|PubMed:15773981};
DE Includes:
DE RecName: Full=Deubiquitinase {ECO:0000303|PubMed:26598703};
DE Short=DUB {ECO:0000303|PubMed:26598703};
DE EC=3.4.22.- {ECO:0000269|PubMed:26598703};
DE AltName: Full=Deneddylase {ECO:0000303|PubMed:26598703};
DE AltName: Full=Deubiquitinating enzyme {ECO:0000303|PubMed:26598703};
DE Includes:
DE RecName: Full=Ubiquitin transferase {ECO:0000305|PubMed:27049943};
DE EC=2.3.2.- {ECO:0000305|PubMed:27049943};
DE Includes:
DE RecName: Full=Mono-ADP-ribosyltransferase {ECO:0000305|PubMed:27049943};
DE Short=mART;
DE EC=2.4.2.31 {ECO:0000269|PubMed:27049943, ECO:0000269|PubMed:29795346, ECO:0000269|PubMed:29795347, ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532};
GN Name=sdeA {ECO:0000303|PubMed:15773981};
GN OrderedLocusNames=lpg2157 {ECO:0000312|EMBL:AAU28223.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [2]
RP SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH ICMS, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Philadelphia 1 / Lp02;
RX PubMed=15773981; DOI=10.1111/j.1365-2958.2005.04539.x;
RA Bardill J.P., Miller J.L., Vogel J.P.;
RT "IcmS-dependent translocation of SdeA into macrophages by the Legionella
RT pneumophila type IV secretion system.";
RL Mol. Microbiol. 56:90-103(2005).
RN [3]
RP FUNCTION AS AN UBIQUITINATING ENZYME, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, DOMAIN,
RP SELF-UBIQUITINATION, AND MUTAGENESIS OF CYS-118 AND 860-GLU--GLU-862.
RC STRAIN=Philadelphia 1 / Lp02;
RX PubMed=27049943; DOI=10.1038/nature17657;
RA Qiu J., Sheedlo M.J., Yu K., Tan Y., Nakayasu E.S., Das C., Liu X.,
RA Luo Z.Q.;
RT "Ubiquitination independent of E1 and E2 enzymes by bacterial effectors.";
RL Nature 533:120-124(2016).
RN [4]
RP FUNCTION.
RX PubMed=27912065; DOI=10.1016/j.cell.2016.11.019;
RA Bhogaraju S., Kalayil S., Liu Y., Bonn F., Colby T., Matic I., Dikic I.;
RT "Phosphoribosylation of ubiquitin promotes serine ubiquitination and
RT impairs conventional ubiquitination.";
RL Cell 167:1636-1649(2016).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-193 (DUB DOMAIN) OF WILD-TYPE
RP AND MUTANT ALA-118 ALONE AND IN COMPLEX WITH UBIQUITIN VINYL METHYL ESTER,
RP FUNCTION AS A DEUBIQUITINASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP DOMAIN, MUTAGENESIS OF TYR-33; ASP-61; ASN-114 AND CYS-118, DISRUPTION
RP PHENOTYPE, AND ACTIVE SITE.
RC STRAIN=Philadelphia 1 / Lp02;
RX PubMed=26598703; DOI=10.1073/pnas.1514568112;
RA Sheedlo M.J., Qiu J., Tan Y., Paul L.N., Luo Z.Q., Das C.;
RT "Structural basis of substrate recognition by a bacterial deubiquitinase
RT important for dynamics of phagosome ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:15090-15095(2015).
RN [6]
RP FUNCTION, GLUTAMYLATION AT GLU-860, AND CATALYTIC ACTIVITY.
RX PubMed=31330532; DOI=10.1038/s41586-019-1440-8;
RA Bhogaraju S., Bonn F., Mukherjee R., Adams M., Pfleiderer M.M., Galej W.P.,
RA Matkovic V., Lopez-Mosqueda J., Kalayil S., Shin D., Dikic I.;
RT "Inhibition of bacterial ubiquitin ligases by SidJ-calmodulin catalysed
RT glutamylation.";
RL Nature 572:382-386(2019).
RN [7]
RP FUNCTION, GLUTAMYLATION AT GLU-860, MUTAGENESIS OF GLU-860, AND CATALYTIC
RP ACTIVITY.
RX PubMed=31330531; DOI=10.1038/s41586-019-1439-1;
RA Gan N., Zhen X., Liu Y., Xu X., He C., Qiu J., Liu Y., Fujimoto G.M.,
RA Nakayasu E.S., Zhou B., Zhao L., Puvar K., Das C., Ouyang S., Luo Z.Q.;
RT "Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent
RT glutamylase.";
RL Nature 572:387-391(2019).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 213-907, FUNCTION, MUTAGENESIS OF
RP HIS-277 AND HIS-407, AND CATALYTIC ACTIVITY.
RX PubMed=29795347; DOI=10.1038/s41586-018-0145-8;
RA Kalayil S., Bhogaraju S., Bonn F., Shin D., Liu Y., Gan N., Basquin J.,
RA Grumati P., Luo Z.Q., Dikic I.;
RT "Insights into catalysis and function of phosphoribosyl-linked serine
RT ubiquitination.";
RL Nature 557:734-738(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 206-910, FUNCTION, MUTAGENESIS OF
RP HIS-277; GLU-340 AND HIS-407, AND CATALYTIC ACTIVITY.
RX PubMed=29795346; DOI=10.1038/s41586-018-0147-6;
RA Akturk A., Wasilko D.J., Wu X., Liu Y., Zhang Y., Qiu J., Luo Z.Q.,
RA Reiter K.H., Brzovic P.S., Klevit R.E., Mao Y.;
RT "Mechanism of phosphoribosyl-ubiquitination mediated by a single Legionella
RT effector.";
RL Nature 557:729-733(2018).
CC -!- FUNCTION: Secreted effector that interferes with the host cell
CC ubiquitin pathway and is required for intracellular bacterial
CC replication. Catalyzes the ubiquitination of several mammalian Rab
CC proteins (Rab33b, Rab1, Rab6a and Rab30) during L.pneumophila
CC infection, without engaging the standard cellular enzyme cascade (E1
CC and E2) (PubMed:29795346). Transfers an ADP-ribose moiety from NAD to
CC the 'Arg-42' residue of ubiquitin in a reaction that releases
CC nicotinamide (PubMed:31330532, PubMed:31330531, PubMed:29795347). The
CC modified ubiquitin is subsequently transferred to serine residues of
CC the substrate protein via a phosphoribose linker that results in the
CC release of AMP (PubMed:27912065). Cannot ubiquitinate the endosomal
CC Rab5 or the cytoskeletal small GTPase Rac1 (PubMed:27049943). Also acts
CC as a deubiquitinase (DUB), catalyzing the cleavage of three of the most
CC abundant polyubiquitin chains ('Lys-11', 'Lys-48' and 'Lys-63') with a
CC distinct preference for 'Lys-63' linkages; is thus able to efficiently
CC remove 'Lys-63'-linked polyubiquitin chains from the phagosomal
CC surface. Is also able to remove NEDD8 from neddylated proteins, but is
CC unable to recognize SUMO. The DUB activity of SdeA is important for
CC regulating the dynamics of ubiquitin association with the bacterial
CC phagosome, but is dispensable for its role in intracellular bacterial
CC replication (PubMed:26598703). {ECO:0000269|PubMed:26598703,
CC ECO:0000269|PubMed:27049943, ECO:0000269|PubMed:27912065,
CC ECO:0000269|PubMed:29795346, ECO:0000269|PubMed:29795347,
CC ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142554; EC=2.4.2.31;
CC Evidence={ECO:0000269|PubMed:27049943, ECO:0000269|PubMed:29795346,
CC ECO:0000269|PubMed:29795347, ECO:0000269|PubMed:31330531,
CC ECO:0000269|PubMed:31330532};
CC -!- ACTIVITY REGULATION: Ubiquitination catalyzed by SdeA is insensitive to
CC the cysteine alkylation agent maleimide, suggesting that a cysteine
CC conjugation of ubiquitin does not form during the reaction.
CC {ECO:0000269|PubMed:27049943}.
CC -!- SUBUNIT: Interacts with IcmS. {ECO:0000269|PubMed:15773981}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15773981}. Host cell
CC {ECO:0000269|PubMed:15773981}. Note=Translocated across the phagosomal
CC membrane into host macrophages via the Dot/Icm type IV secretion system
CC (T4SS) in an IcmS-dependent manner. Appears to localize to the
CC cytoplasmic face of the Legionella-containing vacuole (LCV) in the
CC early stages of infection. {ECO:0000269|PubMed:15773981}.
CC -!- INDUCTION: Expression is induced during the transition from exponential
CC to stationary phase. {ECO:0000269|PubMed:15773981}.
CC -!- DOMAIN: Contains an N-terminal deubiquitinase domain (DUB)
CC (PubMed:26598703). The DUB domain does not interfere with the ubiquitin
CC conjugation activity catalyzed by the central domain of SdeA, which
CC causes toxicity (PubMed:27049943). {ECO:0000269|PubMed:26598703,
CC ECO:0000269|PubMed:27049943}.
CC -!- PTM: Is able to ubiquitinate itself, but this modification is not
CC required to ubiquitinate Rab33b. {ECO:0000269|PubMed:27049943}.
CC -!- PTM: Glutamylated at Glu-860 by SidJ; glutamylation inhibits SdeA
CC activity to catalyze the production of ADP-ribosylated ubiquitin.
CC {ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking all four members of the SidE family
CC (SdeA, SdeB, SdeC and SidE) show no intracellular growth defect in
CC mouse bone marrow macrophages (BMM), but display attenuated growth
CC inside the protozoan hosts A.castellanii and D.discoideum
CC (PubMed:15773981, PubMed:27049943). This mutant no longer recruits the
CC endoplasmic reticulum (ER) marker GFP-HDEL to its vacuoles, even at 10
CC hours post infection, and is unable to induce Rab33b ubiquitination
CC during infection (PubMed:27049943). The rate of ubiquitin-positive
CC Legionella-containing vacuoles increases from 40% (wild-type) to
CC approximately 90% in infections using the SidE family deletion mutant
CC strain (PubMed:26598703). All these defects can be completely
CC complemented by expressing sdeA on a plasmid (PubMed:15773981,
CC PubMed:27049943, PubMed:26598703). {ECO:0000269|PubMed:15773981,
CC ECO:0000269|PubMed:26598703, ECO:0000269|PubMed:27049943}.
CC -!- SIMILARITY: Belongs to the SidE family. {ECO:0000305|PubMed:15773981}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU28223.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE017354; AAU28223.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015444208.1; NC_002942.5.
DR RefSeq; YP_096170.1; NC_002942.5.
DR PDB; 5CRA; X-ray; 2.64 A; A/B=1-193.
DR PDB; 5CRB; X-ray; 2.00 A; A/B=1-193.
DR PDB; 5CRC; X-ray; 2.85 A; A/B=1-193.
DR PDB; 5YSI; X-ray; 1.55 A; A=756-905.
DR PDB; 5YSJ; X-ray; 2.06 A; A/B/C/D=756-905.
DR PDB; 5YSK; X-ray; 2.40 A; A/B/C/D=756-905.
DR PDB; 6B7Q; X-ray; 2.20 A; A=206-910.
DR PDB; 6G0C; X-ray; 2.80 A; A=213-907.
DR PDB; 6WTG; X-ray; 2.63 A; A=1-193.
DR PDB; 7MIR; EM; 2.50 A; C=231-1190.
DR PDB; 7PPO; EM; 2.91 A; A=231-1190.
DR PDB; 7PQE; EM; 3.70 A; A=231-1190.
DR PDBsum; 5CRA; -.
DR PDBsum; 5CRB; -.
DR PDBsum; 5CRC; -.
DR PDBsum; 5YSI; -.
DR PDBsum; 5YSJ; -.
DR PDBsum; 5YSK; -.
DR PDBsum; 6B7Q; -.
DR PDBsum; 6G0C; -.
DR PDBsum; 6WTG; -.
DR PDBsum; 7MIR; -.
DR PDBsum; 7PPO; -.
DR PDBsum; 7PQE; -.
DR AlphaFoldDB; Q5ZTK4; -.
DR SASBDB; Q5ZTK4; -.
DR SMR; Q5ZTK4; -.
DR STRING; 272624.lpg2157; -.
DR PaxDb; Q5ZTK4; -.
DR PRIDE; Q5ZTK4; -.
DR EnsemblBacteria; AAU28223; AAU28223; lpg2157.
DR GeneID; 66491287; -.
DR KEGG; lpn:lpg2157; -.
DR PATRIC; fig|272624.6.peg.2264; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_002024_0_0_6; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IDA:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019784; F:deNEDDylase activity; IDA:UniProtKB.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR InterPro; IPR043934; SidE_DUB.
DR InterPro; IPR043935; SidE_mART.
DR InterPro; IPR021014; SidE_PDE.
DR Pfam; PF19049; SidE_DUB; 1.
DR Pfam; PF19048; SidE_mART; 1.
DR Pfam; PF12252; SidE_PDE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Glycosyltransferase; Hydrolase; Isopeptide bond;
KW Multifunctional enzyme; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Protease; Reference proteome; Secreted; Thiol protease; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Virulence.
FT CHAIN 1..1499
FT /note="Ubiquitinating/deubiquitinating enzyme SdeA"
FT /id="PRO_0000436968"
FT REGION 1..193
FT /note="Deubiquitinase"
FT /evidence="ECO:0000269|PubMed:26598703"
FT REGION ?519..?
FT /note="Ubiquitin transferase"
FT /evidence="ECO:0000305|PubMed:27049943"
FT REGION ?760..?1000
FT /note="Mono-ADP-ribosyltransferase"
FT /evidence="ECO:0000305|PubMed:27049943"
FT COILED 1059..1181
FT /evidence="ECO:0000255"
FT ACT_SITE 64
FT /note="For deubiquitinase activity"
FT /evidence="ECO:0000305|PubMed:26598703"
FT ACT_SITE 80
FT /note="For deubiquitinase activity"
FT /evidence="ECO:0000305|PubMed:26598703"
FT ACT_SITE 118
FT /note="Nucleophile; for deubiquitinase activity"
FT /evidence="ECO:0000305|PubMed:26598703"
FT BINDING 766..772
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21454,
FT ECO:0000305|PubMed:27049943"
FT BINDING 862
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21454,
FT ECO:0000305|PubMed:27049943"
FT MOD_RES 860
FT /note="5-glutamyl glutamate"
FT /evidence="ECO:0000269|PubMed:31330531,
FT ECO:0000269|PubMed:31330532"
FT MUTAGEN 33
FT /note="Y->A: Loss of deubiquitinase and deneddylase
FT activity."
FT /evidence="ECO:0000269|PubMed:26598703"
FT MUTAGEN 61
FT /note="D->A: Loss of deubiquitinase and deneddylase
FT activity."
FT /evidence="ECO:0000269|PubMed:26598703"
FT MUTAGEN 114
FT /note="N->A: Loss of deubiquitinase and deneddylase
FT activity."
FT /evidence="ECO:0000269|PubMed:26598703"
FT MUTAGEN 118
FT /note="C->A: Loss of deubiquitinase and deneddylase
FT activity. No effect on ubiquitination activity. Is still
FT able to restore the intracellular growth defect in
FT D.discoideum exhibited by cells lacking all four members of
FT the SidE family."
FT /evidence="ECO:0000269|PubMed:26598703,
FT ECO:0000269|PubMed:27049943"
FT MUTAGEN 277
FT /note="H->A: Defective in substrate ubiquitination."
FT /evidence="ECO:0000269|PubMed:29795346,
FT ECO:0000269|PubMed:29795347"
FT MUTAGEN 340
FT /note="E->A: Defective in substrate ubiquitination."
FT /evidence="ECO:0000269|PubMed:29795346"
FT MUTAGEN 407
FT /note="H->A: Defective in substrate ubiquitination."
FT /evidence="ECO:0000269|PubMed:29795346,
FT ECO:0000269|PubMed:29795347"
FT MUTAGEN 860..862
FT /note="ESE->ASA: Loss of Rab protein ubiquitination
FT activity. This mutant has completely lost its toxicity to
FT yeast and is also defective in inhibiting the secretion of
FT the secreted form of the embryonic alkaline phosphatase
FT (SEAP) by mammalian cells. Is not able to restore the
FT intracellular growth defect in D.discoideum as well as the
FT ER marker recruitment defect exhibited by cells lacking all
FT four members of the SidE family."
FT /evidence="ECO:0000269|PubMed:27049943"
FT MUTAGEN 860
FT /note="E->A: Loss of glutamylation."
FT /evidence="ECO:0000269|PubMed:31330531"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:6WTG"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6WTG"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6WTG"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:6WTG"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:6WTG"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:6WTG"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:6WTG"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:6WTG"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6WTG"
FT HELIX 118..133
FT /evidence="ECO:0007829|PDB:6WTG"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6WTG"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:6WTG"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:6WTG"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:6B7Q"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:6G0C"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 279..301
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:6B7Q"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 344..363
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 418..433
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 435..451
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:7MIR"
FT TURN 470..473
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:6G0C"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:6G0C"
FT HELIX 516..521
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 523..526
FT /evidence="ECO:0007829|PDB:6B7Q"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 545..552
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 555..560
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 564..585
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 600..614
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 633..642
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 645..650
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 654..666
FT /evidence="ECO:0007829|PDB:6B7Q"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 674..677
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 684..695
FT /evidence="ECO:0007829|PDB:6B7Q"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 701..714
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 716..726
FT /evidence="ECO:0007829|PDB:6B7Q"
FT HELIX 735..755
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 762..768
FT /evidence="ECO:0007829|PDB:5YSI"
FT HELIX 772..788
FT /evidence="ECO:0007829|PDB:5YSI"
FT HELIX 790..796
FT /evidence="ECO:0007829|PDB:5YSI"
FT HELIX 799..808
FT /evidence="ECO:0007829|PDB:5YSI"
FT HELIX 809..815
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 817..823
FT /evidence="ECO:0007829|PDB:5YSI"
FT HELIX 825..831
FT /evidence="ECO:0007829|PDB:5YSI"
FT STRAND 835..841
FT /evidence="ECO:0007829|PDB:5YSI"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:7PPO"
FT STRAND 847..852
FT /evidence="ECO:0007829|PDB:5YSI"
FT HELIX 855..857
FT /evidence="ECO:0007829|PDB:5YSJ"
FT STRAND 862..866
FT /evidence="ECO:0007829|PDB:5YSI"
FT STRAND 871..883
FT /evidence="ECO:0007829|PDB:5YSI"
FT STRAND 885..887
FT /evidence="ECO:0007829|PDB:6B7Q"
FT STRAND 889..899
FT /evidence="ECO:0007829|PDB:5YSI"
FT TURN 901..903
FT /evidence="ECO:0007829|PDB:6B7Q"
FT TURN 909..912
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 913..931
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 1067..1074
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 1079..1085
FT /evidence="ECO:0007829|PDB:7MIR"
FT HELIX 1100..1117
FT /evidence="ECO:0007829|PDB:7MIR"
SQ SEQUENCE 1499 AA; 169043 MW; 06BD224FFD0EDF4D CRC64;
MPKYVEGVEL TQEGMHAIFA RMGYGDITSG SIYNGVPTID TGALNRQGFM PVLTGVGPHR
DSGHWIMLIK GPGNQYYLFD PLGKTSGEGY QNILAAQLPM GSTLSVIPNG SGLNMGLCGY
WVASAGLRAH QALNQHNPPT LLNVGQTITN EMRNELDHDG YRKITGWLRA VADEFPEGDP
QLDGKALREN TEKDLKIEIP TLVLPGKDTS PKEMSVKPTA PQDKSVPVWN GFSLYTDDTV
KAAAQYAYDN YLGKPYTGSV ESAPANFGGR MVYRQHHGLS HTLRTMAYAE LIVEEARKAK
LRGETLGKFK DGRTIADVTP QELKKIMIAQ AFFVAGRDDE ASDAKNYQKY HEQSRDAFLK
YVKDNESTLI PDVFKDQEDV NFYARVIEDK SHDWESTPAH VLINQGHMVD LVRVKQPPES
FLQRYFSSMQ RWIGSQATEA VFGIQRQFFH ATYEVVAGFD SDNKEPHLVV SGLGRYVIGE
DGQPIREAPK KGQKEGDLKV FPQTYKLKEN ERLMRVDEFL KLPEIQNTFP GSGKHLQGGM
PGMNEMDYWN RLNSLNRARC ENDVDFCLKQ LQTAHDKAKI EPIKQAFQSS KGKERRQPNV
DEIAAARIIQ QILANPDCIH DDHVLINGQK LEQQFFRDLL AKCEMAVVGS LLNDTDIGNI
DTLMRHEKDT EFHSTNPEAV PVKIGEYWIN DQRINNSSGN ITQKKHDLIF LMQNDAWYFS
RVNAIAQNRD KGSTFKEVLI TTLMTPLTSK ALVDTSQAKP PTRLFRGLNL SEEFTKGLID
QANAMIANTT ERLFTDHSPE AFKQIKLNDL SKMSGRTNAS TTTEIKLVKE TWDSNVIFEM
LDPDGLLHSK QVGRHGEGTE SEFSVYLPED VALVPVKVTL DGKTQKGENR YVFTFVAVKS
PDFTPRHESG YAVEPFLRMQ AAKLAEVKSS IEKAQRAPDL ETIFNLQNEV EAVQYSHLST
GYKNFLKNTV GPVLENSLSG LMESDTDTLS KALAAFPSDT QWSAFNFEEA RQAKRQMDAI
KQMVGNKVVL DALTQCQDAL EKQNIAGALD ALKKIPSEKE MGTIRRELRE QIQSARQELE
SLQRAVVTPV VTDEKKVRER YDALIENTSK KITELETGKL PNLDAVKKGI SNLSNLKQEV
TVLRNEKIRM HVGTDKVDFS DVEKLEQQIQ VIDTKLADAY LLEVTKQISA LDNTKPKNQT
ELKTKIAAFL DRTTDIEMLR NERIKKHGSS KDPLDLSDLD KLSGSLQRIN QSLVSDLITT
IRVSINQMEA KTFHEQEKEI QQNFELLAKL EKTLDKSKTS EKLREDIPKL NDLLVAKQKA
YPQMVQMQLK SEVFVTQLRE VCQANHDDLD KTRNARLREL DRLDREAGIT RMVGNLIWGL
TNKVGLTTDE RLDIRTKQQS LARFKNELFN DKIDTDQLIS NLARKRPSEL QEGLGISTDN
AMELHLLLTE LAGKTTSPDE LEERMKAIDD ISTKIGREPE HLKFVMVEED ESNKKTIGF
