IF2P_YEAST
ID IF2P_YEAST Reviewed; 1002 AA.
AC P39730; D6VPI2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000305|PubMed:12507428};
DE Short=eIF-5B {ECO:0000303|PubMed:12507428};
DE EC=3.6.5.3 {ECO:0000269|PubMed:12507428, ECO:0000269|PubMed:18976658};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000303|PubMed:9624054};
GN Name=FUN12 {ECO:0000303|PubMed:8076820};
GN OrderedLocusNames=YAL035W {ECO:0000312|SGD:S000000033};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [2]
RP SEQUENCE REVISION.
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Vo D.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-1002.
RX PubMed=8076820; DOI=10.1016/0378-1119(94)90294-1;
RA Sutrave P., Shafer B.K., Strathern J.N., Hughes S.H.;
RT "Isolation, identification and characterization of the FUN12 gene of
RT Saccharomyces cerevisiae.";
RL Gene 146:209-213(1994).
RN [5]
RP FUNCTION.
RX PubMed=9624054; DOI=10.1126/science.280.5370.1757;
RA Choi S.K., Lee J.H., Zoll W.L., Merrick W.C., Dever T.E.;
RT "Promotion of met-tRNAiMet binding to ribosomes by yIF2, a bacterial IF2
RT homolog in yeast.";
RL Science 280:1757-1760(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-439 AND HIS-480.
RX PubMed=12507428; DOI=10.1016/s0092-8674(02)01171-6;
RA Shin B.S., Maag D., Roll-Mecak A., Arefin M.S., Burley S.K., Lorsch J.R.,
RA Dever T.E.;
RT "Uncoupling of initiation factor eIF5B/IF2 GTPase and translational
RT activities by mutations that lower ribosome affinity.";
RL Cell 111:1015-1025(2002).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF HIS-480.
RX PubMed=12471154; DOI=10.1073/pnas.262569399;
RA Lee J.H., Pestova T.V., Shin B.S., Cao C., Choi S.K., Dever T.E.;
RT "Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic
RT translation initiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16689-16694(2002).
RN [8]
RP FUNCTION.
RX PubMed=12008673; DOI=10.1017/s1355838202029527;
RA Algire M.A., Maag D., Savio P., Acker M.G., Tarun S.Z. Jr., Sachs A.B.,
RA Asano K., Nielsen K.H., Olsen D.S., Phan L., Hinnebusch A.G., Lorsch J.R.;
RT "Development and characterization of a reconstituted yeast translation
RT initiation system.";
RL RNA 8:382-397(2002).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18976658; DOI=10.1016/j.jmb.2008.10.029;
RA Acker M.G., Shin B.S., Nanda J.S., Saini A.K., Dever T.E., Lorsch J.R.;
RT "Kinetic analysis of late steps of eukaryotic translation initiation.";
RL J. Mol. Biol. 385:491-506(2009).
RN [12]
RP MUTAGENESIS OF GLY-479.
RX PubMed=17913624; DOI=10.1016/s0076-6879(07)29009-3;
RA Shin B.S., Dever T.E.;
RT "Molecular genetic structure-function analysis of translation initiation
RT factor eIF5B.";
RL Methods Enzymol. 429:185-201(2007).
RN [13]
RP FUNCTION.
RX PubMed=19029250; DOI=10.1128/mcb.00896-08;
RA Shin B.S., Kim J.R., Acker M.G., Maher K.N., Lorsch J.R., Dever T.E.;
RT "rRNA suppressor of a eukaryotic translation initiation factor
RT 5B/initiation factor 2 mutant reveals a binding site for translational
RT GTPases on the small ribosomal subunit.";
RL Mol. Cell. Biol. 29:808-821(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP FUNCTION.
RX PubMed=22751017; DOI=10.1038/nsmb.2308;
RA Lebaron S., Schneider C., van Nues R.W., Swiatkowska A., Walsh D.,
RA Boettcher B., Granneman S., Watkins N.J., Tollervey D.;
RT "Proofreading of pre-40S ribosome maturation by a translation initiation
RT factor and 60S subunits.";
RL Nat. Struct. Mol. Biol. 19:744-753(2012).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 401-739.
RX PubMed=24200810; DOI=10.1126/science.1240585;
RA Fernandez I.S., Bai X.C., Hussain T., Kelley A.C., Lorsch J.R.,
RA Ramakrishnan V., Scheres S.H.;
RT "Molecular architecture of a eukaryotic translational initiation complex.";
RL Science 342:1240585-1240585(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 401-1002.
RX PubMed=25478828; DOI=10.1107/s1399004714021476;
RA Zheng A., Yu J., Yamamoto R., Ose T., Tanaka I., Yao M.;
RT "X-ray structures of eIF5B and the eIF5B-eIF1A complex: the conformational
RT flexibility of eIF5B is restricted on the ribosome by interaction with
RT eIF1A.";
RL Acta Crystallogr. D 70:3090-3098(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 399-852 IN COMPLEX WITH GTP, AND
RP FUNCTION.
RX PubMed=24686316; DOI=10.1002/embj.201387344;
RA Kuhle B., Ficner R.;
RT "eIF5B employs a novel domain release mechanism to catalyze ribosomal
RT subunit joining.";
RL EMBO J. 33:1177-1191(2014).
CC -!- FUNCTION: Plays a role in translation initiation (PubMed:9624054).
CC Translational GTPase that catalyzes the joining of the 40S and 60S
CC subunits to form the 80S initiation complex with the initiator
CC methionine-tRNA in the P-site base paired to the start codon
CC (PubMed:12507428, PubMed:12471154, PubMed:12008673). GTP binding and
CC hydrolysis induces conformational changes in the enzyme that renders it
CC active for productive interactions with the ribosome (PubMed:25478828).
CC The release of the enzyme after formation of the initiation complex is
CC a prerequisite to form elongation-competent ribosomes (PubMed:12507428,
CC PubMed:18976658, PubMed:19029250). Stimulates 20S pre-rRNA cleavage to
CC mature 18S rRNA by PIN-domain endonuclease NOB1 (PubMed:22751017).
CC {ECO:0000269|PubMed:12008673, ECO:0000269|PubMed:12471154,
CC ECO:0000269|PubMed:12507428, ECO:0000269|PubMed:18976658,
CC ECO:0000269|PubMed:19029250, ECO:0000269|PubMed:22751017,
CC ECO:0000269|PubMed:25478828, ECO:0000269|PubMed:9624054}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000269|PubMed:12507428, ECO:0000269|PubMed:18976658};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC Note=Binds 1 monovalent cation per monomer in the active site, which
CC can be sodium or potassium. This structural cofactor stabilizes the
CC GTP-bound 'on' state, and may also act as a transition state stabilizer
CC of the hydrolysis reaction. {ECO:0000250|UniProtKB:G0S8G9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9624054}.
CC -!- MISCELLANEOUS: Present with 13400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57228.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U12980; AAC04996.1; -; Genomic_DNA.
DR EMBL; L29389; AAA57228.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006935; DAA06952.1; -; Genomic_DNA.
DR PIR; S70292; S70292.
DR RefSeq; NP_009365.1; NM_001178180.1.
DR PDB; 3WBI; X-ray; 2.35 A; A=401-1002.
DR PDB; 3WBJ; X-ray; 2.50 A; A=401-855.
DR PDB; 3WBK; X-ray; 3.30 A; A/B=401-1002.
DR PDB; 4N3S; X-ray; 1.83 A; A/B=399-852.
DR PDB; 4NCF; X-ray; 3.02 A; A/B=399-852.
DR PDB; 4V8Y; EM; 4.30 A; CP=401-739.
DR PDB; 4V8Z; EM; 6.60 A; CV=401-739.
DR PDB; 6WOO; EM; 2.90 A; 1=401-1000.
DR PDBsum; 3WBI; -.
DR PDBsum; 3WBJ; -.
DR PDBsum; 3WBK; -.
DR PDBsum; 4N3S; -.
DR PDBsum; 4NCF; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 6WOO; -.
DR AlphaFoldDB; P39730; -.
DR SMR; P39730; -.
DR BioGRID; 31730; 129.
DR DIP; DIP-3790N; -.
DR IntAct; P39730; 58.
DR MINT; P39730; -.
DR STRING; 4932.YAL035W; -.
DR CarbonylDB; P39730; -.
DR iPTMnet; P39730; -.
DR MaxQB; P39730; -.
DR PaxDb; P39730; -.
DR PRIDE; P39730; -.
DR EnsemblFungi; YAL035W_mRNA; YAL035W; YAL035W.
DR GeneID; 851196; -.
DR KEGG; sce:YAL035W; -.
DR SGD; S000000033; FUN12.
DR VEuPathDB; FungiDB:YAL035W; -.
DR eggNOG; KOG1144; Eukaryota.
DR GeneTree; ENSGT00940000163243; -.
DR HOGENOM; CLU_002656_1_0_1; -.
DR InParanoid; P39730; -.
DR OMA; RDVMMAG; -.
DR BioCyc; YEAST:G3O-28845-MON; -.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:P39730; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39730; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0031369; F:translation initiation factor binding; IDA:SGD.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IDA:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:SGD.
DR GO; GO:0006446; P:regulation of translational initiation; IMP:SGD.
DR GO; GO:0042255; P:ribosome assembly; IMP:SGD.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Initiation factor;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW Protein biosynthesis; Reference proteome; Sodium.
FT CHAIN 1..1002
FT /note="Eukaryotic translation initiation factor 5B"
FT /id="PRO_0000137296"
FT DOMAIN 403..621
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..419
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 437..441
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 476..479
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 530..533
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 598..600
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 25..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..340
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..371
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415..420
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24686316"
FT BINDING 415
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT BINDING 415
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT BINDING 431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT BINDING 437..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT BINDING 437
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT BINDING 437
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:G0S8G9"
FT BINDING 530..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24686316"
FT BINDING 599..600
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24686316"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 439
FT /note="T->A: Impairs the GTPase activity, but not the
FT ribosome joining function."
FT /evidence="ECO:0000269|PubMed:12507428"
FT MUTAGEN 479
FT /note="G->A: Reduces GTP binding and impairs subunit
FT joining and ribosome-dependent GTP hydrolysis."
FT /evidence="ECO:0000269|PubMed:17913624"
FT MUTAGEN 480
FT /note="H->E: Impairs the GTPase activity, but not the
FT ribosome joining function."
FT /evidence="ECO:0000269|PubMed:12471154,
FT ECO:0000269|PubMed:12507428"
FT CONFLICT 266
FT /note="L -> V (in Ref. 4; AAA57228)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="A -> S (in Ref. 4; AAA57228)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="A -> D (in Ref. 4; AAA57228)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="G -> R (in Ref. 4; AAA57228)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="E -> Q (in Ref. 4; AAA57228)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="L -> H (in Ref. 4; AAA57228)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="R -> T (in Ref. 4; AAA57228)"
FT /evidence="ECO:0000305"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:3WBI"
FT HELIX 421..425
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 449..456
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 495..502
FT /evidence="ECO:0007829|PDB:4N3S"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 546..551
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 555..573
FT /evidence="ECO:0007829|PDB:4N3S"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:4N3S"
FT TURN 588..590
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:4N3S"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 605..619
FT /evidence="ECO:0007829|PDB:4N3S"
FT TURN 621..624
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 631..640
FT /evidence="ECO:0007829|PDB:4N3S"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 644..657
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 669..681
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 685..688
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 692..709
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 720..723
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 730..746
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 755..761
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 762..774
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 789..796
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 798..801
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 807..812
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 817..826
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 829..835
FT /evidence="ECO:0007829|PDB:4N3S"
FT HELIX 836..851
FT /evidence="ECO:0007829|PDB:4N3S"
FT STRAND 866..879
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 881..892
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 896..903
FT /evidence="ECO:0007829|PDB:3WBI"
FT TURN 904..907
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 908..922
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 925..931
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 939..944
FT /evidence="ECO:0007829|PDB:3WBI"
FT TURN 954..956
FT /evidence="ECO:0007829|PDB:3WBI"
FT STRAND 963..965
FT /evidence="ECO:0007829|PDB:3WBI"
FT HELIX 969..974
FT /evidence="ECO:0007829|PDB:3WBI"
FT HELIX 978..981
FT /evidence="ECO:0007829|PDB:3WBI"
FT HELIX 986..999
FT /evidence="ECO:0007829|PDB:3WBI"
SQ SEQUENCE 1002 AA; 112268 MW; 1A496195DAE1C283 CRC64;
MAKKSKKNQQ NYWDEEFEED AAQNEEISAT PTPNPESSAG ADDTSREASA SAEGAEAIEG
DFMSTLKQSK KKQEKKVIEE KKDGKPILKS KKEKEKEKKE KEKQKKKEQA ARKKAQQQAQ
KEKNKELNKQ NVEKAAAEKA AAEKSQKSKG ESDKPSASAK KPAKKVPAGL AALRRQLELK
KQLEEQEKLE REEEERLEKE EEERLANEEK MKEEAKAAKK EKEKAKREKR KAEGKLLTRK
QKEEKKLLER RRAALLSSGN VKVAGLAKKD GEENKPKKVV YSKKKKRTTQ ENASEAIKSD
SKKDSEVVPD DELKESEDVL IDDWENLALG DDDEEGTNEE TQESTASHEN EDQNQGEEEE
EGEEEEEEEE ERAHVHEVAK STPAATPAAT PTPSSASPNK KDLRSPICCI LGHVDTGKTK
LLDKIRQTNV QGGEAGGITQ QIGATYFPID AIKAKTKVMA EYEKQTFDVP GLLVIDTPGH
ESFSNLRSRG SSLCNIAILV IDIMHGLEQQ TIESIKLLRD RKAPFVVALN KIDRLYDWKA
IPNNSFRDSF AKQSRAVQEE FQSRYSKIQL ELAEQGLNSE LYFQNKNMSK YVSIVPTSAV
TGEGVPDLLW LLLELTQKRM SKQLMYLSHV EATILEVKVV EGFGTTIDVI LSNGYLREGD
RIVLCGMNGP IVTNIRALLT PQPLRELRLK SEYVHHKEVK AALGVKIAAN DLEKAVSGSR
LLVVGPEDDE DELMDDVMDD LTGLLDSVDT TGKGVVVQAS TLGSLEALLD FLKDMKIPVM
SIGLGPVYKR DVMKASTMLE KAPEYAVMLC FDVKVDKEAE QYAEQEGIKI FNADVIYHLF
DSFTAYQEKL LEERRKDFLD YAIFPCVLQT LQIINKRGPM IIGVDVLEGT LRVGTPICAV
KTDPTTKERQ TLILGKVISL EINHQPVQEV KKGQTAAGVA VRLEDPSGQQ PIWGRHVDEN
DTLYSLVSRR SIDTLKDKAF RDQVARSDWL LLKKLKVVFG IE
