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Database: UniProt
Entry: P06103
LinkDB: P06103
Original site: P06103 
ID   EIF3B_YEAST             Reviewed;         763 AA.
AC   P06103; D6W356;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   07-APR-2021, entry version 209.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Cell cycle regulation and translation initiation protein;
DE   AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit;
DE            Short=eIF3 p90 {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Translation initiation factor eIF3 p90 subunit;
GN   Name=PRT1 {ECO:0000255|HAMAP-Rule:MF_03001}; Synonyms=CDC63;
GN   OrderedLocusNames=YOR361C;
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 [GENOMIC DNA].
RX   PubMed=3029094;
RA   Hanic-Joyce P.J., Singer R.A., Johnston G.C.;
RT   "Molecular characterization of the yeast PRT1 gene in which mutations
RT   affect translation initiation and regulation of cell proliferation.";
RL   J. Biol. Chem. 262:2845-2851(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
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   IDENTIFICATION IN THE EIF-3 CORE COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=9671501; DOI=10.1128/mcb.18.8.4935;
RA   Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R.,
RA   Qin J., Hinnebusch A.G.;
RT   "Identification of a translation initiation factor 3 (eIF3) core complex,
RT   conserved in yeast and mammals, that interacts with eIF5.";
RL   Mol. Cell. Biol. 18:4935-4946(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=11387228; DOI=10.1093/emboj/20.11.2954;
RA   Phan L., Schoenfeld L.W., Valasek L., Nielsen K.H., Hinnebusch A.G.;
RT   "A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates
RT   ribosome binding of mRNA and tRNA(i)Met.";
RL   EMBO J. 20:2954-2965(2001).
RN   [6]
RP   INTERACTION WITH PCI8.
RX   PubMed=11457827; DOI=10.1074/jbc.m102161200;
RA   Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L.,
RA   Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.;
RT   "Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6
RT   interact with the eIF3 core complex by binding to cognate eIF3b subunits.";
RL   J. Biol. Chem. 276:34948-34957(2001).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
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   [9]
RP   INTERACTION WITH HCR1; NIP1; TIF32; TIF34; TIF35; EIF-1; EIF-2 AND EIF-5,
RP   ASSOCIATION WITH THE 40S RIBOSOME, AND MUTAGENESIS OF 124-LYS--GLU-130.
RX   PubMed=16581774; DOI=10.1128/mcb.26.8.2984-2998.2006;
RA   Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.;
RT   "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of
RT   eukaryotic initiation factor 3 in yeast.";
RL   Mol. Cell. Biol. 26:2984-2998(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-669, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   IDENTIFICATION IN THE EIF-3 COMPLEX WITH NIP1; TIF32; TIF34 AND TIF35.
RX   PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA   Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA   Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA   Doudna J.A., Robinson C.V.;
RT   "Mass spectrometry reveals modularity and a complete subunit interaction
RT   map of the eukaryotic translation factor eIF3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND TYR-67, AND
RP   IDENTIFICATION BY 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).
CC   -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:11387228}.
CC   -!- SUBUNIT: The eukaryotic translation initiation factor 3 (eIF-3) core
CC       complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex
CC       of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5
CC       and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC       tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC       ribosome. {ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:9671501}.
CC   -!- INTERACTION:
CC       P06103; Q05911: ADE13; NbExp=2; IntAct=EBI-8973, EBI-14263;
CC       P06103; P32497: NIP1; NbExp=12; IntAct=EBI-8973, EBI-8965;
CC       P06103; P06103: PRT1; NbExp=2; IntAct=EBI-8973, EBI-8973;
CC       P06103; P38249: RPG1; NbExp=13; IntAct=EBI-8973, EBI-8981;
CC       P06103; P40217: TIF34; NbExp=17; IntAct=EBI-8973, EBI-8951;
CC       P06103; Q04067: TIF35; NbExp=14; IntAct=EBI-8973, EBI-8958;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 47500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC       Rule:MF_03001}.
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DR   EMBL; J02674; AAA34917.1; -; Genomic_DNA.
DR   EMBL; Z75269; CAA99690.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11122.1; -; Genomic_DNA.
DR   PIR; A29562; A29562.
DR   RefSeq; NP_015006.3; NM_001183781.3.
DR   PDB; 3JAP; EM; 4.90 A; r=704-734.
DR   PDB; 3JAQ; EM; 6.00 A; r=704-737.
DR   PDB; 3NS5; X-ray; 2.60 A; A/B=76-161.
DR   PDB; 3NS6; X-ray; 1.25 A; A/B=76-170.
DR   PDB; 3ZWL; X-ray; 2.20 A; E/F=693-739.
DR   PDB; 4U1E; X-ray; 2.00 A; B=694-737.
DR   PDB; 4U1F; X-ray; 2.20 A; A/B=172-665.
DR   PDB; 6FYX; EM; 3.05 A; p=1-763.
DR   PDB; 6FYY; EM; 3.05 A; p=1-763.
DR   PDB; 6GSM; EM; 5.15 A; p=77-737.
DR   PDB; 6GSN; EM; 5.75 A; p=72-737.
DR   PDB; 6ZCE; EM; 5.30 A; p=1-763.
DR   PDB; 6ZU9; EM; 6.20 A; p=1-763.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 3JAQ; -.
DR   PDBsum; 3NS5; -.
DR   PDBsum; 3NS6; -.
DR   PDBsum; 3ZWL; -.
DR   PDBsum; 4U1E; -.
DR   PDBsum; 4U1F; -.
DR   PDBsum; 6FYX; -.
DR   PDBsum; 6FYY; -.
DR   PDBsum; 6GSM; -.
DR   PDBsum; 6GSN; -.
DR   PDBsum; 6ZCE; -.
DR   PDBsum; 6ZU9; -.
DR   SMR; P06103; -.
DR   BioGRID; 34746; 186.
DR   ComplexPortal; CPX-1831; Eukaryotic translation initiation factor 3 core complex.
DR   DIP; DIP-2519N; -.
DR   IntAct; P06103; 46.
DR   MINT; P06103; -.
DR   STRING; 4932.YOR361C; -.
DR   iPTMnet; P06103; -.
DR   MaxQB; P06103; -.
DR   PaxDb; P06103; -.
DR   PRIDE; P06103; -.
DR   EnsemblFungi; YOR361C_mRNA; YOR361C; YOR361C.
DR   GeneID; 854543; -.
DR   KEGG; sce:YOR361C; -.
DR   SGD; S000005888; PRT1.
DR   VEuPathDB; FungiDB:YOR361C; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   GeneTree; ENSGT00550000074913; -.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   InParanoid; P06103; -.
DR   OMA; LIDFSPN; -.
DR   BioCyc; YEAST:G3O-33831-MONOMER; -.
DR   Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR   EvolutionaryTrace; P06103; -.
DR   PRO; PR:P06103; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P06103; protein.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:SGD.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:SGD.
DR   GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IDA:SGD.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IDA:SGD.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011400; EIF3B.
DR   InterPro; IPR034363; eIF3B_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR14068; PTHR14068; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome; Repeat; RNA-binding; WD repeat.
FT   CHAIN           1..763
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000123535"
FT   DOMAIN          77..162
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   REPEAT          228..266
FT                   /note="WD 1"
FT   REPEAT          277..325
FT                   /note="WD 2"
FT   REPEAT          373..416
FT                   /note="WD 3"
FT   REPEAT          484..524
FT                   /note="WD 4"
FT   REPEAT          544..589
FT                   /note="WD 5"
FT   REPEAT          605..650
FT                   /note="WD 6"
FT   REGION          1..136
FT                   /note="Sufficient for interaction with HCR1 and TIF32"
FT                   /evidence="ECO:0000269|PubMed:16581774"
FT   REGION          28..261
FT                   /note="Sufficient for interaction with PIC8"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         67
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         669
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         124..130
FT                   /note="KGFLFVE->AAAAAAA: Impairs interaction with HCR1 and
FT                   TIF32, impairs interaction of the eIF-3 complex with eIF-1,
FT                   eIF-2 and the 40S ribosome, and impairs initiation of
FT                   translation."
FT                   /evidence="ECO:0000269|PubMed:16581774"
FT   STRAND          78..83
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   HELIX           89..91
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   HELIX           92..104
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   STRAND          109..113
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   TURN            118..121
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   STRAND          125..133
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   HELIX           134..144
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   STRAND          148..152
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   STRAND          156..160
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   HELIX           161..168
FT                   /evidence="ECO:0007744|PDB:3NS6"
FT   HELIX           186..189
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   HELIX           191..194
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          201..205
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          207..214
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          224..234
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          236..238
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          245..248
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          250..257
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   TURN            258..261
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          262..268
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          272..277
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          283..290
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   HELIX           305..307
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          312..316
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   TURN            317..319
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          322..326
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          338..341
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          345..352
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          355..360
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   HELIX           361..363
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   HELIX           371..373
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          380..383
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          395..397
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          400..407
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          411..413
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          416..422
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          427..432
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          435..443
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          447..457
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          464..472
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          480..484
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          486..494
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          501..506
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          519..527
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          538..547
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          551..554
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          558..565
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          571..573
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          575..580
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          593..596
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          600..603
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          611..615
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          622..626
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   TURN            628..630
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          636..641
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          646..651
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   STRAND          657..660
FT                   /evidence="ECO:0007744|PDB:4U1F"
FT   HELIX           694..728
FT                   /evidence="ECO:0007744|PDB:4U1E"
SQ   SEQUENCE   763 AA;  88130 MW;  F5E4E783408EE948 CRC64;
     MKNFLPRTLK NIYELYFNNI SVHSIVSRNT QLKRSKIIQM TTETFEDIKL EDIPVDDIDF
     SDLEEQYKVT EEFNFDQYIV VNGAPVIPSA KVPVLKKALT SLFSKAGKVV NMEFPIDEAT
     GKTKGFLFVE CGSMNDAKKI IKSFHGKRLD LKHRLFLYTM KDVERYNSDD FDTEFREPDM
     PTFVPSSSLK SWLMDDKVRD QFVLQDDVKT SVFWNSMFNE EDSLVESREN WSTNYVRFSP
     KGTYLFSYHQ QGVTAWGGPN FDRLRRFYHP DVRNSSVSPN EKYLVTFSTE PIIVEEDNEF
     SPFTKKNEGH QLCIWDIASG LLMATFPVIK SPYLKWPLVR WSYNDKYCAR MVGDSLIVHD
     ATKNFMPLEA KALKPSGIRD FSFAPEGVKL QPFRNGDEPS VLLAYWTPET NNSACTATIA
     EVPRGRVLKT VNLVQVSNVT LHWQNQAEFL CFNVERHTKS GKTQFSNLQI CRLTERDIPV
     EKVELKDSVF EFGWEPHGNR FVTISVHEVA DMNYAIPANT IRFYAPETKE KTDVIKRWSL
     VKEIPKTFAN TVSWSPAGRF VVVGALVGPN MRRSDLQFYD MDYPGEKNIN DNNDVSASLK
     DVAHPTYSAA TNITWDPSGR YVTAWSSSLK HKVEHGYKIF NIAGNLVKED IIAGFKNFAW
     RPRPASILSN AERKKVRKNL REWSAQFEEQ DAMEADTAMR DLILHQRELL KQWTEYREKI
     GQEMEKSMNF KIFDVQPEDA SDDFTTIEEI VEEVLEETKE KVE
//
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