ID IF2G_SACS2 Reviewed; 415 AA.
AC Q980A5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Translation initiation factor 2 subunit gamma {ECO:0000255|HAMAP-Rule:MF_00119};
DE EC=3.6.5.3 {ECO:0000255|HAMAP-Rule:MF_00119, ECO:0000269|PubMed:25690901};
DE AltName: Full=aIF2-gamma {ECO:0000255|HAMAP-Rule:MF_00119};
DE AltName: Full=eIF-2-gamma {ECO:0000255|HAMAP-Rule:MF_00119};
GN Name=eif2g {ECO:0000255|HAMAP-Rule:MF_00119}; OrderedLocusNames=SSO0412;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2] {ECO:0007744|PDB:2AHO}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-415.
RX PubMed=16407071; DOI=10.1016/j.str.2005.09.020;
RA Yatime L., Mechulam Y., Blanquet S., Schmitt E.;
RT "Structural switch of the gamma subunit in an archaeal aIF2 alpha gamma
RT heterodimer.";
RL Structure 14:119-128(2006).
RN [3] {ECO:0007744|PDB:2PLF, ECO:0007744|PDB:2PMD}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
RX PubMed=17825838; DOI=10.1016/j.jmb.2007.07.048;
RA Nikonov O., Stolboushkina E., Nikulin A., Hasenohrl D., Blasi U.,
RA Manstein D.J., Fedorov R., Garber M., Nikonov S.;
RT "New insights into the interactions of the translation initiation factor 2
RT from archaea with guanine nucleotides and initiator tRNA.";
RL J. Mol. Biol. 373:328-336(2007).
RN [4] {ECO:0007744|PDB:2QMU, ECO:0007744|PDB:2QN6}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-415.
RX PubMed=18000047; DOI=10.1073/pnas.0706784104;
RA Yatime L., Mechulam Y., Blanquet S., Schmitt E.;
RT "Structure of an archaeal heterotrimeric initiation factor 2 reveals a
RT nucleotide state between the GTP and the GDP states.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18445-18450(2007).
RN [5] {ECO:0007744|PDB:3CW2}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
RX PubMed=18675278; DOI=10.1016/j.jmb.2008.07.039;
RA Stolboushkina E., Nikonov S., Nikulin A., Blasi U., Manstein D.J.,
RA Fedorov R., Garber M., Nikonov O.;
RT "Crystal structure of the intact archaeal translation initiation factor 2
RT demonstrates very high conformational flexibility in the alpha- and beta-
RT subunits.";
RL J. Mol. Biol. 382:680-691(2008).
RN [6] {ECO:0007744|PDB:3V11}
RP X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 2-415.
RX PubMed=22447243; DOI=10.1038/nsmb.2259;
RA Schmitt E., Panvert M., Lazennec-Schurdevin C., Coureux P.D., Perez J.,
RA Thompson A., Mechulam Y.;
RT "Structure of the ternary initiation complex aIF2-GDPNP-methionylated
RT initiator tRNA.";
RL Nat. Struct. Mol. Biol. 19:450-454(2012).
RN [7] {ECO:0007744|PDB:3QSY}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS).
RX PubMed=23291527; DOI=10.1016/j.jmb.2012.12.023;
RA Stolboushkina E., Nikonov S., Zelinskaya N., Arkhipova V., Nikulin A.,
RA Garber M., Nikonov O.;
RT "Crystal structure of the archaeal translation initiation factor 2 in
RT complex with a GTP analogue and Met-tRNAf(Met.).";
RL J. Mol. Biol. 425:989-998(2013).
RN [8] {ECO:0007744|PDB:4M0L, ECO:0007744|PDB:4M2L, ECO:0007744|PDB:4M4S, ECO:0007744|PDB:4M53}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RX PubMed=24598735; DOI=10.1107/s1399004713032240;
RA Nikonov O., Stolboushkina E., Arkhipova V., Kravchenko O., Nikonov S.,
RA Garber M.;
RT "Conformational transitions in the gamma subunit of the archaeal
RT translation initiation factor 2.";
RL Acta Crystallogr. D 70:658-667(2014).
RN [9] {ECO:0007744|PDB:4RCY, ECO:0007744|PDB:4RCZ, ECO:0007744|PDB:4RD0, ECO:0007744|PDB:4RD1, ECO:0007744|PDB:4RD2, ECO:0007744|PDB:4RD3, ECO:0007744|PDB:4RD4, ECO:0007744|PDB:4RD6}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH GTP, AND MUTAGENESIS
RP OF ASP-19 AND HIS-97.
RX PubMed=25690901; DOI=10.1093/nar/gkv053;
RA Dubiez E., Aleksandrov A., Lazennec-Schurdevin C., Mechulam Y., Schmitt E.;
RT "Identification of a second GTP-bound magnesium ion in archaeal initiation
RT factor 2.";
RL Nucleic Acids Res. 43:2946-2957(2015).
RN [10] {ECO:0007744|PDB:5JB3, ECO:0007744|PDB:5JBH}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.34 ANGSTROMS).
RX PubMed=27819266; DOI=10.1038/ncomms13366;
RA Coureux P.D., Lazennec-Schurdevin C., Monestier A., Larquet E.,
RA Cladiere L., Klaholz B.P., Schmitt E., Mechulam Y.;
RT "Cryo-EM study of start codon selection during archaeal translation
RT initiation.";
RL Nat. Commun. 7:13366-13366(2016).
RN [11] {ECO:0007744|PDB:6H6K, ECO:0007744|PDB:6I5M}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RX PubMed=30988256; DOI=10.1107/s2059798319002304;
RA Nikonov O., Kravchenko O., Nevskaya N., Stolboushkina E., Garber M.,
RA Nikonov S.;
RT "The third structural switch in the archaeal translation initiation factor
RT 2 (aIF2) molecule and its possible role in the initiation of GTP hydrolysis
RT and the removal of aIF2 from the ribosome.";
RL Acta Crystallogr. D 75:392-399(2019).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
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:0000255|HAMAP-Rule:MF_00119,
CC ECO:0000269|PubMed:25690901};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00119,
CC ECO:0000269|PubMed:25690901};
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
CC -!- INTERACTION:
CC Q980A5; Q97Z79: eif2a; NbExp=2; IntAct=EBI-9010337, EBI-9010365;
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00119}.
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DR EMBL; AE006641; AAK40740.1; -; Genomic_DNA.
DR PIR; E90185; E90185.
DR RefSeq; WP_009988771.1; NC_002754.1.
DR PDB; 2AHO; X-ray; 3.00 A; A=2-415.
DR PDB; 2PLF; X-ray; 2.90 A; A=2-415.
DR PDB; 2PMD; X-ray; 2.65 A; A/B=1-415.
DR PDB; 2QMU; X-ray; 3.20 A; A=2-415.
DR PDB; 2QN6; X-ray; 2.15 A; A=2-415.
DR PDB; 3CW2; X-ray; 2.80 A; A/B/E/F=1-415.
DR PDB; 3I1F; X-ray; 2.50 A; A/B=1-415.
DR PDB; 3PEN; X-ray; 2.30 A; A=2-415.
DR PDB; 3QSY; X-ray; 3.20 A; A=1-415.
DR PDB; 3SJZ; X-ray; 2.80 A; A=2-415.
DR PDB; 3V11; X-ray; 5.00 A; A=2-415.
DR PDB; 4M0L; X-ray; 2.60 A; A/B/C/D/E/F=1-415.
DR PDB; 4M2L; X-ray; 2.15 A; A=1-415.
DR PDB; 4M4S; X-ray; 2.25 A; A=1-415.
DR PDB; 4M53; X-ray; 2.00 A; A=1-415.
DR PDB; 4NBS; X-ray; 2.30 A; A=1-415.
DR PDB; 4QFM; X-ray; 2.30 A; A=1-415.
DR PDB; 4QHY; X-ray; 3.29 A; A=1-415.
DR PDB; 4RCY; X-ray; 1.65 A; A=1-415.
DR PDB; 4RCZ; X-ray; 1.43 A; A=1-415.
DR PDB; 4RD0; X-ray; 1.71 A; A=1-415.
DR PDB; 4RD1; X-ray; 1.50 A; A=1-415.
DR PDB; 4RD2; X-ray; 1.58 A; A=1-415.
DR PDB; 4RD3; X-ray; 1.69 A; A=1-415.
DR PDB; 4RD4; X-ray; 1.30 A; A=1-415.
DR PDB; 4RD6; X-ray; 1.94 A; A=1-415.
DR PDB; 4RJL; X-ray; 1.64 A; A=1-415.
DR PDB; 5DSZ; X-ray; 2.50 A; A/B=1-415.
DR PDB; 5JB3; EM; 5.34 A; 7=1-415.
DR PDB; 5JBH; EM; 5.34 A; 7=1-415.
DR PDB; 6H6K; X-ray; 2.00 A; A/B/C/D/E=1-415.
DR PDB; 6I5M; X-ray; 2.40 A; A=1-415.
DR PDB; 6R8S; X-ray; 2.18 A; A=1-415.
DR PDB; 6R8T; X-ray; 2.10 A; A=1-415.
DR PDB; 6SW9; EM; 4.20 A; 7=2-415.
DR PDB; 6SWC; EM; 3.30 A; 7=1-415.
DR PDBsum; 2AHO; -.
DR PDBsum; 2PLF; -.
DR PDBsum; 2PMD; -.
DR PDBsum; 2QMU; -.
DR PDBsum; 2QN6; -.
DR PDBsum; 3CW2; -.
DR PDBsum; 3I1F; -.
DR PDBsum; 3PEN; -.
DR PDBsum; 3QSY; -.
DR PDBsum; 3SJZ; -.
DR PDBsum; 3V11; -.
DR PDBsum; 4M0L; -.
DR PDBsum; 4M2L; -.
DR PDBsum; 4M4S; -.
DR PDBsum; 4M53; -.
DR PDBsum; 4NBS; -.
DR PDBsum; 4QFM; -.
DR PDBsum; 4QHY; -.
DR PDBsum; 4RCY; -.
DR PDBsum; 4RCZ; -.
DR PDBsum; 4RD0; -.
DR PDBsum; 4RD1; -.
DR PDBsum; 4RD2; -.
DR PDBsum; 4RD3; -.
DR PDBsum; 4RD4; -.
DR PDBsum; 4RD6; -.
DR PDBsum; 4RJL; -.
DR PDBsum; 5DSZ; -.
DR PDBsum; 5JB3; -.
DR PDBsum; 5JBH; -.
DR PDBsum; 6H6K; -.
DR PDBsum; 6I5M; -.
DR PDBsum; 6R8S; -.
DR PDBsum; 6R8T; -.
DR PDBsum; 6SW9; -.
DR PDBsum; 6SWC; -.
DR AlphaFoldDB; Q980A5; -.
DR EMDB; EMD-10320; -.
DR EMDB; EMD-10322; -.
DR EMDB; EMD-8148; -.
DR EMDB; EMD-8149; -.
DR SMR; Q980A5; -.
DR DIP; DIP-29031N; -.
DR IntAct; Q980A5; 1.
DR STRING; 273057.SSO0412; -.
DR PaxDb; 273057-SSO0412; -.
DR EnsemblBacteria; AAK40740; AAK40740; SSO0412.
DR GeneID; 72912224; -.
DR KEGG; sso:SSO0412; -.
DR PATRIC; fig|273057.12.peg.407; -.
DR eggNOG; arCOG01563; Archaea.
DR HOGENOM; CLU_027154_0_1_2; -.
DR InParanoid; Q980A5; -.
DR PhylomeDB; Q980A5; -.
DR BRENDA; 3.6.5.3; 6163.
DR EvolutionaryTrace; Q980A5; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00119; eIF_2_gamma; 1.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR022424; TIF2_gsu.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR NCBIfam; TIGR03680; eif2g_arch; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Hydrolase; Initiation factor; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..415
FT /note="Translation initiation factor 2 subunit gamma"
FT /id="PRO_0000137463"
FT DOMAIN 7..206
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 16..23
FT /note="G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 44..48
FT /note="G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 93..96
FT /note="G3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 149..152
FT /note="G4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT REGION 184..186
FT /note="G5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119"
FT BINDING 19..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RCY,
FT ECO:0007744|PDB:4RD1"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RD1"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16407071, ECO:0000269|PubMed:25690901,
FT ECO:0007744|PDB:2AHO"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RD1"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:16407071, ECO:0000269|PubMed:25690901,
FT ECO:0007744|PDB:2AHO"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8U082, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8U082, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8U082, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8U082, ECO:0000255|HAMAP-
FT Rule:MF_00119"
FT BINDING 149..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RCY,
FT ECO:0007744|PDB:4RD1"
FT BINDING 184..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00119,
FT ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RCY,
FT ECO:0007744|PDB:4RD1"
FT MUTAGEN 19
FT /note="D->A: Reduces GTP hydrolysis 8.5-fold. Completely
FT aboloshes GTPase activity; when associated with A-97."
FT /evidence="ECO:0000269|PubMed:25690901"
FT MUTAGEN 97
FT /note="H->A: Reduces GTP hydrolysis 17.5-fold. Completely
FT aboloshes GTPase activity; when associated with A-19."
FT /evidence="ECO:0000269|PubMed:25690901"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2QMU"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:4RD4"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:3I1F"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4M4S"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3CW2"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 156..170
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5DSZ"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4RD4"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6H6K"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 252..263
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4RD4"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4RD4"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 325..335
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:4RD6"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 364..373
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 375..387
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:4RJL"
FT STRAND 393..401
FT /evidence="ECO:0007829|PDB:4RD4"
FT STRAND 404..414
FT /evidence="ECO:0007829|PDB:4RD4"
SQ SEQUENCE 415 AA; 45792 MW; 74A1F3C850D2D3D2 CRC64;
MAWPKVQPEV NIGVVGHVDH GKTTLVQAIT GIWTSKHSEE LKRGMTIKLG YAETNIGVCE
SCKKPEAYVT EPSCKSCGSD DEPKFLRRIS FIDAPGHEVL MATMLSGAAL MDGAILVVAA
NEPFPQPQTR EHFVALGIIG VKNLIIVQNK VDVVSKEEAL SQYRQIKQFT KGTWAENVPI
IPVSALHKIN IDSLIEGIEE YIKTPYRDLS QKPVMLVIRS FDVNKPGTQF NELKGGVIGG
SIIQGLFKVD QEIKVLPGLR VEKQGKVSYE PIFTKISSIR FGDEEFKEAK PGGLVAIGTY
LDPSLTKADN LLGSIITLAD AEVPVLWNIR IKYNLLERVV GAKEMLKVDP IRAKETLMLS
VGSSTTLGIV TSVKKDEIEV ELRRPVAVWS NNIRTVISRQ IAGRWRMIGW GLVEI
//
