ID   RLI1_YEAST              Reviewed;         608 AA.
AC   Q03195; D6VS78;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Translation initiation factor RLI1;
DE   AltName: Full=ATP-binding cassette sub-family E member RLI1;
DE   AltName: Full=RNase L inhibitor;
GN   Name=RLI1; OrderedLocusNames=YDR091C;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION, IDENTIFICATION IN THE MFC COMPLEX, MUTAGENESIS OF GLY-224;
RP   GLY-225; GLY-470; GLY-471 AND GLU-493, AND SUBCELLULAR LOCATION.
RX   PubMed=15277527; DOI=10.1074/jbc.m404502200;
RA   Dong J., Lai R., Nielsen K., Fekete C.A., Qiu H., Hinnebusch A.G.;
RT   "The essential ATP-binding cassette protein RLI1 functions in translation
RT   by promoting preinitiation complex assembly.";
RL   J. Biol. Chem. 279:42157-42168(2004).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH PRE-RIBOSOMAL PARTICLES,
RP   AND IDENTIFICATION IN THE MFC COMPLEX.
RX   PubMed=15660135; DOI=10.1038/sj.emboj.7600540;
RA   Yarunin A., Panse V.G., Petfalski E., Dez C., Tollervey D., Hurt E.C.;
RT   "Functional link between ribosome formation and biogenesis of iron-sulfur
RT   proteins.";
RL   EMBO J. 24:580-588(2005).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP   ASSOCIATION WITH PRE-RIBOSOMAL PARTICLES, AND IDENTIFICATION IN THE MFC
RP   COMPLEX.
RX   PubMed=15660134; DOI=10.1038/sj.emboj.7600541;
RA   Kispal G., Sipos K., Lange H., Fekete Z., Bedekovics T., Janaky T.,
RA   Bassler J., Aguilar Netz D.J., Balk J., Rotte C., Lill R.;
RT   "Biogenesis of cytosolic ribosomes requires the essential iron-sulphur
RT   protein Rli1p and mitochondria.";
RL   EMBO J. 24:589-598(2005).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, 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   [11]
RP   INTERACTION WITH YAE1, AND MUTAGENESIS OF CYS-25.
RX   PubMed=23318452; DOI=10.1038/onc.2012.604;
RA   Zhai C., Li Y., Mascarenhas C., Lin Q., Li K., Vyrides I., Grant C.M.,
RA   Panaretou B.;
RT   "The function of ORAOV1/LTO1, a gene that is overexpressed frequently in
RT   cancer: essential roles in the function and biogenesis of the ribosome.";
RL   Oncogene 33:484-494(2014).
RN   [12]
RP   INTERACTION WITH YAE1, AND MUTAGENESIS OF CYS-25 AND CYS-61.
RX   PubMed=26182403; DOI=10.7554/elife.08231;
RA   Paul V.D., Muehlenhoff U., Stuempfig M., Seebacher J., Kugler K.G.,
RA   Renicke C., Taxis C., Gavin A.C., Pierik A.J., Lill R.;
RT   "The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC
RT   protein Rli1 for iron-sulfur cluster insertion.";
RL   Elife 4:E08231-E08231(2015).
CC   -!- FUNCTION: Component of the multifactor complex (MFC) involved in
CC       translation initiation. Required for the binding of MFC to the 40S
CC       ribosome. Required for the processing and nuclear export of the 60S and
CC       40S ribosomal subunits. {ECO:0000269|PubMed:15277527,
CC       ECO:0000269|PubMed:15660134, ECO:0000269|PubMed:15660135}.
CC   -!- SUBUNIT: Component of the multifactor complex (MFC) composed of at
CC       least RLI1, the eIF2 subunit SUI2, TIF5/eIF5, and the eIF3 subunits
CC       PRT1, HCR1, NIP1, RPG1, TIF34 and TIF35. The complex associates with
CC       pre-initiation complexes. Interacts with the complex YAE1:LTO1; the
CC       complex bridges the interaction between the CIA complex and RLI1
CC       (PubMed:23318452). {ECO:0000269|PubMed:15277527,
CC       ECO:0000269|PubMed:15660134, ECO:0000269|PubMed:15660135,
CC       ECO:0000269|PubMed:23318452}.
CC   -!- INTERACTION:
CC       Q03195; Q05775: HCR1; NbExp=4; IntAct=EBI-35146, EBI-8944;
CC       Q03195; P12385: SUP45; NbExp=5; IntAct=EBI-35146, EBI-6533;
CC       Q03195; Q6Q7I0: SUP35; Xeno; NbExp=2; IntAct=EBI-35146, EBI-7724365;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15277527, ECO:0000269|PubMed:15660134,
CC       ECO:0000269|PubMed:15660135}. Nucleus {ECO:0000269|PubMed:15277527,
CC       ECO:0000269|PubMed:15660134, ECO:0000269|PubMed:15660135}.
CC       Note=Shuttles between the nucleus and the cytoplasm.
CC       {ECO:0000269|PubMed:15660134, ECO:0000269|PubMed:15660135}.
CC   -!- MISCELLANEOUS: Present with 6280 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE family.
CC       {ECO:0000305}.
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DR   EMBL; Z50111; CAA90450.1; -; Genomic_DNA.
DR   EMBL; AY723776; AAU09693.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11938.1; -; Genomic_DNA.
DR   PIR; S58091; S58091.
DR   RefSeq; NP_010376.3; NM_001180399.3.
DR   PDB; 3J16; EM; -; B=1-608.
DR   PDB; 4CRM; EM; 8.75 A; P=1-608.
DR   PDB; 5LL6; EM; 3.90 A; h=1-608.
DR   PDB; 6ZCE; EM; 5.30 A; k=1-608.
DR   PDB; 6ZU9; EM; 6.20 A; k=1-608.
DR   PDB; 7A1G; EM; 3.00 A; x=4-604.
DR   PDBsum; 3J16; -.
DR   PDBsum; 4CRM; -.
DR   PDBsum; 5LL6; -.
DR   PDBsum; 6ZCE; -.
DR   PDBsum; 6ZU9; -.
DR   PDBsum; 7A1G; -.
DR   AlphaFoldDB; Q03195; -.
DR   EMDB; EMD-11160; -.
DR   EMDB; EMD-11439; -.
DR   EMDB; EMD-11608; -.
DR   EMDB; EMD-2598; -.
DR   SMR; Q03195; -.
DR   BioGRID; 32148; 221.
DR   DIP; DIP-4492N; -.
DR   IntAct; Q03195; 47.
DR   MINT; Q03195; -.
DR   STRING; 4932.YDR091C; -.
DR   GlyGen; Q03195; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q03195; -.
DR   MaxQB; Q03195; -.
DR   PaxDb; 4932-YDR091C; -.
DR   PeptideAtlas; Q03195; -.
DR   TopDownProteomics; Q03195; -.
DR   EnsemblFungi; YDR091C_mRNA; YDR091C; YDR091C.
DR   GeneID; 851665; -.
DR   KEGG; sce:YDR091C; -.
DR   AGR; SGD:S000002498; -.
DR   SGD; S000002498; RLI1.
DR   VEuPathDB; FungiDB:YDR091C; -.
DR   eggNOG; KOG0063; Eukaryota.
DR   GeneTree; ENSGT00390000015089; -.
DR   HOGENOM; CLU_017344_4_1_1; -.
DR   InParanoid; Q03195; -.
DR   OMA; MVCIQNG; -.
DR   OrthoDB; 1110105at2759; -.
DR   BioCyc; YEAST:G3O-29696-MONOMER; -.
DR   BioGRID-ORCS; 851665; 1 hit in 10 CRISPR screens.
DR   PRO; PR:Q03195; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03195; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IDA:SGD.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:UniProtKB.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:SGD.
DR   GO; GO:0032790; P:ribosome disassembly; IDA:SGD.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006413; P:translational initiation; IMP:SGD.
DR   GO; GO:0006415; P:translational termination; IGI:SGD.
DR   CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013283; RLI1.
DR   InterPro; IPR034348; RLI_dom_1.
DR   InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR   PANTHER; PTHR19248:SF16; ATP-BINDING CASSETTE SUB-FAMILY E MEMBER 1; 1.
DR   PANTHER; PTHR19248; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF04068; RLI; 1.
DR   PRINTS; PR01868; ABCEFAMILY.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Initiation factor;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW   Transport.
FT   CHAIN           1..608
FT                   /note="Translation initiation factor RLI1"
FT                   /id="PRO_0000268703"
FT   DOMAIN          7..39
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          46..75
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          70..320
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          345..568
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         385..392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         25
FT                   /note="C->S: Not viable in aerobic conditions. Lethal; when
FT                   associated with S-61."
FT                   /evidence="ECO:0000269|PubMed:23318452,
FT                   ECO:0000269|PubMed:26182403"
FT   MUTAGEN         61
FT                   /note="C->S: Lethal; when associated with S-25."
FT                   /evidence="ECO:0000269|PubMed:26182403"
FT   MUTAGEN         224
FT                   /note="G->D: Lethal; when associated with D-225."
FT                   /evidence="ECO:0000269|PubMed:15277527"
FT   MUTAGEN         225
FT                   /note="G->D: Lethal; when associated with D-224."
FT                   /evidence="ECO:0000269|PubMed:15277527"
FT   MUTAGEN         470
FT                   /note="G->D: Lethal; when associated with D-471."
FT                   /evidence="ECO:0000269|PubMed:15277527"
FT   MUTAGEN         471
FT                   /note="G->D: Lethal; when associated with D-470."
FT                   /evidence="ECO:0000269|PubMed:15277527"
FT   MUTAGEN         493
FT                   /note="E->Q: Lethal. Inhibits translation in vitro."
FT                   /evidence="ECO:0000269|PubMed:15277527"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            18..20
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           24..28
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           60..63
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           116..124
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           140..146
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           151..160
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            173..178
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           187..193
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            199..201
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           205..208
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           224..237
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          241..247
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            248..251
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           254..266
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          273..277
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           281..287
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          289..297
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            298..300
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          301..304
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           310..319
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            323..326
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          377..379
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          381..383
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           391..398
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           430..436
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          444..447
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           448..452
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           457..460
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          462..465
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           470..482
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          486..490
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           500..516
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           529..533
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          536..539
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          554..556
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           557..566
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            567..569
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          572..574
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   TURN            576..578
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   STRAND          581..583
FT                   /evidence="ECO:0007829|PDB:7A1G"
FT   HELIX           589..597
FT                   /evidence="ECO:0007829|PDB:7A1G"
SQ   SEQUENCE   608 AA;  68340 MW;  1E76EC3D0457963D CRC64;
     MSDKNSRIAI VSADKCKPKK CRQECKRSCP VVKTGKLCIE VTPTSKIAFI SEILCIGCGI
     CVKKCPFDAI QIINLPTNLE AHVTHRYSAN SFKLHRLPTP RPGQVLGLVG TNGIGKSTAL
     KILAGKQKPN LGRFDDPPEW QEIIKYFRGS ELQNYFTKML EDDIKAIIKP QYVDNIPRAI
     KGPVQKVGEL LKLRMEKSPE DVKRYIKILQ LENVLKRDIE KLSGGELQRF AIGMSCVQEA
     DVYMFDEPSS YLDVKQRLNA AQIIRSLLAP TKYVICVEHD LSVLDYLSDF VCIIYGVPSV
     YGVVTLPASV REGINIFLDG HIPAENLRFR TEALQFRIAD ATEDLQNDSA SRAFSYPSLK
     KTQGDFVLNV EEGEFSDSEI LVMMGENGTG KTTLIKLLAG ALKPDEGQDI PKLNVSMKPQ
     KIAPKFPGTV RQLFFKKIRG QFLNPQFQTD VVKPLRIDDI IDQEVQHLSG GELQRVAIVL
     ALGIPADIYL IDEPSAYLDS EQRIICSKVI RRFILHNKKT AFIVEHDFIM ATYLADKVIV
     FEGIPSKNAH ARAPESLLTG CNRFLKNLNV TFRRDPNSFR PRINKLDSQM DKEQKSSGNY
     FFLDNTGI
//