RLI1_YEAST
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 03-AUG-2022, entry version 188.
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 SMR; Q03195; -.
DR BioGRID; 32148; 208.
DR DIP; DIP-4492N; -.
DR IntAct; Q03195; 45.
DR MINT; Q03195; -.
DR STRING; 4932.YDR091C; -.
DR iPTMnet; Q03195; -.
DR MaxQB; Q03195; -.
DR PaxDb; Q03195; -.
DR PRIDE; Q03195; -.
DR TopDownProteomics; Q03195; -.
DR EnsemblFungi; YDR091C_mRNA; YDR091C; YDR091C.
DR GeneID; 851665; -.
DR KEGG; sce:YDR091C; -.
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; VCVQQAD; -.
DR BioCyc; YEAST:G3O-29696-MON; -.
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: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; -; 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; PTHR19248; 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; SSF52540; SSF52540; 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
