UREA_CANEN
ID UREA_CANEN Reviewed; 840 AA.
AC P07374;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Urease;
DE EC=3.5.1.5;
DE AltName: Full=Jack bean urease {ECO:0000303|PubMed:33631299, ECO:0000303|Ref.4};
DE Short=JBU {ECO:0000303|PubMed:33631299};
DE AltName: Full=Urea amidohydrolase;
OS Canavalia ensiformis (Jack bean) (Dolichos ensiformis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Canavalia.
OX NCBI_TaxID=3823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1721034; DOI=10.1016/0378-1119(91)90443-f;
RA Riddles P.W., Whan V., Blakeley R.L., Zerner B.;
RT "Cloning and sequencing of a jack bean urease-encoding cDNA.";
RL Gene 108:265-267(1991).
RN [2]
RP ERRATUM OF PUBMED:1721034.
RX PubMed=1446838; DOI=10.1016/0378-1119(92)90152-f;
RA Riddles P.W., Whan V., Blakeley R.L., Zerner B.;
RL Gene 121:399-400(1992).
RN [3]
RP PROTEIN SEQUENCE.
RX PubMed=3402446; DOI=10.1111/j.1432-1033.1988.tb14177.x;
RA Takishima K., Suga T., Mamiya G.;
RT "The structure of jack bean urease. The complete amino acid sequence,
RT limited proteolysis and reactive cysteine residues.";
RL Eur. J. Biochem. 175:151-165(1988).
RN [4]
RP PROTEIN SEQUENCE.
RA Mamiya G., Takishima K., Masakuni M., Kayumi T., Ogawa K., Sekita T.;
RT "Complete amino acid sequence of jack bean urease.";
RL Proc. Jpn. Acad., B, Phys. Biol. Sci. 61:395-398(1985).
RN [5]
RP PROTEIN SEQUENCE OF 591-637.
RX PubMed=3447159;
RA Takishima K., Mamiya G.;
RT "Location of the essential cysteine residue of jack bean urease.";
RL Protein Seq. Data Anal. 1:103-106(1987).
RN [6]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11696010; DOI=10.1042/0264-6021:3600217;
RA Follmer C., Barcellos G.B., Zingali R.B., Machado O.L., Alves E.W.,
RA Barja-Fidalgo C., Guimaraes J.A., Carlini C.R.;
RT "Canatoxin, a toxic protein from jack beans (Canavalia ensiformis), is a
RT variant form of urease (EC 3.5.1.5): biological effects of urease
RT independent of its ureolytic activity.";
RL Biochem. J. 360:217-224(2001).
RN [7]
RP FUNCTION.
RX PubMed=24583269; DOI=10.1016/j.abb.2014.02.006;
RA Piovesan A.R., Martinelli A.H., Ligabue-Braun R., Schwartz J.L.,
RA Carlini C.R.;
RT "Canavalia ensiformis urease, Jaburetox and derived peptides form ion
RT channels in planar lipid bilayers.";
RL Arch. Biochem. Biophys. 547:6-17(2014).
RN [8]
RP FUNCTION.
RX PubMed=33631299; DOI=10.1016/j.tox.2021.152737;
RA Almeida C.G.M., Costa-Higuchi K., Piovesan A.R., Moro C.F., Venturin G.T.,
RA Greggio S., Costa-Ferro Z.S., Salamoni S.D., Peigneur S., Tytgat J.,
RA de Lima M.E., Silva C.N.D., Vinade L., Rowan E.G., DaCosta J.C.,
RA Dal Belo C.A., Carlini C.R.;
RT "Neurotoxic and convulsant effects induced by jack bean ureases on the
RT mammalian nervous system.";
RL Toxicology 454:152737-152737(2021).
RN [9]
RP REVIEW.
RX PubMed=26690979; DOI=10.1016/j.toxicon.2015.11.020;
RA Carlini C.R., Ligabue-Braun R.;
RT "Ureases as multifunctional toxic proteins: A review.";
RL Toxicon 110:90-109(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH NICKEL IONS, AND
RP CARBOXYLATION AT LYS-490.
RX PubMed=20471401; DOI=10.1016/j.jmb.2010.05.009;
RA Balasubramanian A., Ponnuraj K.;
RT "Crystal structure of the first plant urease from jack bean: 83 years of
RT journey from its first crystal to molecular structure.";
RL J. Mol. Biol. 400:274-283(2010).
CC -!- FUNCTION: Urea hydrolase involved in nitrogen recycling from ureide,
CC purine, and arginine catabolism (PubMed:26690979). Is known to be
CC highly toxic and lethal when given by intravenous route, producing
CC convulsions and other signs of central nervous system intoxication
CC associated with the high levels of ammonia formed in the blood of mice
CC and rabbits (PubMed:26690979). Is neurotoxic in mammals, when directly
CC injected into hippocampus (PubMed:33631299). It may induce seizures by
CC acting at a neuronal network level, thereby disturbing
CC electroencephalographic rhythms and causing metabolic alterations in
CC key areas related to epileptogenesis and to neurogenic pulmonary edema
CC (PubMed:33631299). It increases calcium influx and neuronal firing rate
CC in the hippocampus (PubMed:33631299). Is able to insert itself into
CC lipid bilayers, altering physicochemical properties of artificial
CC membranes, and forming cation-selective ion channels (PubMed:24583269).
CC In vitro, has the ability to induce platelet aggregation, platelet
CC granules secretion and release of ATP (PubMed:11696010). In contrast to
CC canatoxin, another urease from C.ensiformis, is not lethal to mice when
CC intraperitoneally injected (PubMed:11696010).
CC {ECO:0000269|PubMed:11696010, ECO:0000269|PubMed:24583269,
CC ECO:0000269|PubMed:33631299, ECO:0000305|PubMed:26690979}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000305|PubMed:11696010};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: P-hydroxymercuribenzoate irreversibly abolishes
CC ureolytic activity, but does not inhibit the ability to activate
CC platelets (PubMed:11696010). Also inhibited by acetohydroxamic acid
CC (AHA), a chelator of Ni2+ and Zn2+ ions (PubMed:11696010).
CC {ECO:0000269|PubMed:11696010}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for urea (at 37 degrees Celsius and pH 6.5)
CC {ECO:0000269|PubMed:11696010};
CC KM=2.9 mM for urea (at 37 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:11696010};
CC KM=7.1 mM for urea (at 37 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:11696010};
CC Vmax=6000 umol/min/mg enzyme (at 37 degrees Celsius and pH 6.5)
CC {ECO:0000269|PubMed:11696010};
CC Vmax=13700 umol/min/mg enzyme (at 37 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:11696010};
CC Vmax=26700 umol/min/mg enzyme (at 37 degrees Celsius and pH 8.5)
CC {ECO:0000269|PubMed:11696010};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1.
CC -!- SUBUNIT: Homohexamer (Probable). Other oligomeric forms may exist
CC depending on pH and presence of salts (Probable).
CC {ECO:0000305|PubMed:11696010, ECO:0000305|PubMed:33631299}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000269|PubMed:20471401}.
CC -!- MISCELLANEOUS: Was isolated in 1926 by James B. Sumner. It was the
CC first enzyme ever obtained in a crystalline form, demonstrating that
CC enzymes could be proteins. {ECO:0000305|PubMed:33631299}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent
CC hydrolases superfamily. Urease alpha subunit family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="http://www.worthington-biochem.com/URC/";
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; M65260; AAA83831.1; -; mRNA.
DR PIR; JC1396; URJB.
DR PDB; 3LA4; X-ray; 2.05 A; A=1-840.
DR PDB; 4GOA; X-ray; 2.20 A; A=1-840.
DR PDB; 4GY7; X-ray; 1.49 A; A=1-840.
DR PDB; 4H9M; X-ray; 1.52 A; A=1-840.
DR PDB; 7KNS; EM; 2.77 A; A/B/C/D/E/F=1-840.
DR PDBsum; 3LA4; -.
DR PDBsum; 4GOA; -.
DR PDBsum; 4GY7; -.
DR PDBsum; 4H9M; -.
DR PDBsum; 7KNS; -.
DR AlphaFoldDB; P07374; -.
DR SMR; P07374; -.
DR BindingDB; P07374; -.
DR ChEMBL; CHEMBL4161; -.
DR DrugCentral; P07374; -.
DR MEROPS; M38.982; -.
DR BRENDA; 3.5.1.5; 1091.
DR SABIO-RK; P07374; -.
DR UniPathway; UPA00258; UER00370.
DR EvolutionaryTrace; P07374; -.
DR GO; GO:0035550; C:urease complex; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00375; Urease_alpha; 1.
DR CDD; cd00407; Urease_beta; 1.
DR CDD; cd00390; Urease_gamma; 1.
DR Gene3D; 2.10.150.10; -; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR Gene3D; 3.30.280.10; -; 1.
DR HAMAP; MF_01953; Urease_alpha; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR008221; Urease.
DR InterPro; IPR011612; Urease_alpha_N_dom.
DR InterPro; IPR017950; Urease_AS.
DR InterPro; IPR005848; Urease_asu.
DR InterPro; IPR017951; Urease_asu_c.
DR InterPro; IPR002019; Urease_beta.
DR InterPro; IPR036461; Urease_betasu_sf.
DR InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR InterPro; IPR036463; Urease_gamma_sf.
DR InterPro; IPR040881; Urease_linker.
DR InterPro; IPR029754; Urease_Ni-bd.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR Pfam; PF00699; Urease_beta; 1.
DR Pfam; PF00547; Urease_gamma; 1.
DR Pfam; PF18473; Urease_linker; 1.
DR PIRSF; PIRSF001222; Urease; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51278; SSF51278; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR SUPFAM; SSF54111; SSF54111; 1.
DR TIGRFAMs; TIGR01792; urease_alph; 1.
DR TIGRFAMs; TIGR00192; urease_beta; 1.
DR TIGRFAMs; TIGR00193; urease_gam; 1.
DR PROSITE; PS01120; UREASE_1; 1.
DR PROSITE; PS00145; UREASE_2; 1.
DR PROSITE; PS51368; UREASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Metal-binding;
KW Neurotoxin; Nickel; Toxin.
FT CHAIN 1..840
FT /note="Urease"
FT /evidence="ECO:0000269|PubMed:3402446, ECO:0000269|Ref.4"
FT /id="PRO_0000067524"
FT DOMAIN 402..840
FT /note="Urease"
FT ACT_SITE 593
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20471401,
FT ECO:0007744|PDB:3LA4, ECO:0007744|PDB:4GOA,
FT ECO:0007744|PDB:4GY7, ECO:0007744|PDB:4H9M"
FT BINDING 409
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20471401,
FT ECO:0007744|PDB:3LA4, ECO:0007744|PDB:4GOA,
FT ECO:0007744|PDB:4GY7, ECO:0007744|PDB:4H9M"
FT BINDING 490
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:20471401,
FT ECO:0007744|PDB:3LA4, ECO:0007744|PDB:4GOA,
FT ECO:0007744|PDB:4GY7, ECO:0007744|PDB:4H9M"
FT BINDING 490
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:20471401,
FT ECO:0007744|PDB:3LA4, ECO:0007744|PDB:4GOA,
FT ECO:0007744|PDB:4GY7, ECO:0007744|PDB:4H9M"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20471401,
FT ECO:0007744|PDB:3LA4, ECO:0007744|PDB:4GOA,
FT ECO:0007744|PDB:4GY7, ECO:0007744|PDB:4H9M"
FT BINDING 545
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:20471401,
FT ECO:0007744|PDB:3LA4, ECO:0007744|PDB:4GOA,
FT ECO:0007744|PDB:4GY7, ECO:0007744|PDB:4H9M"
FT BINDING 633
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20471401,
FT ECO:0007744|PDB:3LA4, ECO:0007744|PDB:4GOA,
FT ECO:0007744|PDB:4GY7, ECO:0007744|PDB:4H9M"
FT MOD_RES 490
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:20471401"
FT CONFLICT 247
FT /note="K -> R (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="S -> P (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="P -> S (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="D -> Y (in Ref. 1; AAA83831)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="K -> P (in Ref. 1; AAA83831)"
FT /evidence="ECO:0000305"
FT HELIX 5..25
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:7KNS"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 338..348
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 351..360
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 447..456
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 460..469
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 476..484
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 499..512
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 515..519
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 544..547
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:7KNS"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 557..562
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 581..592
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 600..609
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 612..623
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 640..642
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 643..658
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 670..678
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 679..681
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 682..688
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 694..697
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 705..708
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 713..715
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 718..722
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 725..731
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:7KNS"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 756..759
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 762..765
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 767..771
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 774..778
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 782..786
FT /evidence="ECO:0007829|PDB:4GY7"
FT HELIX 795..797
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 811..813
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:4GY7"
FT STRAND 832..834
FT /evidence="ECO:0007829|PDB:4GY7"
FT TURN 835..837
FT /evidence="ECO:0007829|PDB:4GY7"
SQ SEQUENCE 840 AA; 90748 MW; 1407E4ECCF00727F CRC64;
MKLSPREVEK LGLHNAGYLA QKRLARGVRL NYTEAVALIA SQIMEYARDG EKTVAQLMCL
GQHLLGRRQV LPAVPHLLNA VQVEATFPDG TKLVTVHDPI SRENGELQEA LFGSLLPVPS
LDKFAETKED NRIPGEILCE DECLTLNIGR KAVILKVTSK GDRPIQVGSH YHFIEVNPYL
TFDRRKAYGM RLNIAAGTAV RFEPGDCKSV TLVSIEGNKV IRGGNAIADG PVNETNLEAA
MHAVRSKGFG HEEEKDASEG FTKEDPNCPF NTFIHRKEYA NKYGPTTGDK IRLGDTNLLA
EIEKDYALYG DECVFGGGKV IRDGMGQSCG HPPAISLDTV ITNAVIIDYT GIIKADIGIK
DGLIASIGKA GNPDIMNGVF SNMIIGANTE VIAGEGLIVT AGAIDCHVHY ICPQLVYEAI
SSGITTLVGG GTGPAAGTRA TTCTPSPTQM RLMLQSTDDL PLNFGFTGKG SSSKPDELHE
IIKAGAMGLK LHEDWGSTPA AIDNCLTIAE HHDIQINIHT DTLNEAGFVE HSIAAFKGRT
IHTYHSEGAG GGHAPDIIKV CGIKNVLPSS TNPTRPLTSN TIDEHLDMLM VCHHLDREIP
EDLAFAHSRI RKKTIAAEDV LNDIGAISII SSDSQAMGRV GEVISRTWQT ADKMKAQTGP
LKCDSSDNDN FRIRRYIAKY TINPAIANGF SQYVGSVEVG KLADLVMWKP SFFGTKPEMV
IKGGMVAWAD IGDPNASIPT PEPVKMRPMY GTLGKAGGAL SIAFVSKAAL DQRVNVLYGL
NKRVEAVSNV RKLTKLDMKL NDALPEITVD PESYTVKADG KLLCVSEATT VPLSRNYFLF
