RPA49_YEAST
ID RPA49_YEAST Reviewed; 415 AA.
AC Q01080; D6W0U5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA49;
DE Short=A49;
DE AltName: Full=DNA-directed RNA polymerase I 49 kDa polypeptide;
GN Name=RPA49; Synonyms=RRN13; OrderedLocusNames=YNL248C; ORFNames=N0880;
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].
RC STRAIN=CMY214;
RX PubMed=1409638; DOI=10.1073/pnas.89.19.9302;
RA Liljelund P., Mariotte S., Buhler J.-M., Sentenac A.;
RT "Characterization and mutagenesis of the gene encoding the A49 subunit of
RT RNA polymerase A in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9302-9305(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11717393; DOI=10.1073/pnas.231181398;
RA Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.;
RT "Differential roles of phosphorylation in the formation of transcriptional
RT active RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, 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 [9]
RP ELECTRON MICROSCOPY OF THE RNA POL I COMPLEX.
RX PubMed=12145213; DOI=10.1093/emboj/cdf392;
RA Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V.,
RA Schultz P.;
RT "Localization of the yeast RNA polymerase I-specific subunits.";
RL EMBO J. 21:4136-4144(2002).
RN [10]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=12407181; DOI=10.1073/pnas.232580799;
RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A.,
RA Riva M., Carles C.;
RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship
RT to Rpb4-Rpb7 pol II subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
RN [11]
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 [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX,
RP FUNCTION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 171-403, FUNCTION, INTERACTION
RP WITH RPA34, DNA-BINDING, MUTAGENESIS OF 325-ASP-GLU-326; LYS-356; SER-358;
RP LYS-359; ARG-365 AND LYS-393, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBUNIT.
RX PubMed=20797630; DOI=10.1016/j.molcel.2010.07.028;
RA Geiger S.R., Lorenzen K., Schreieck A., Hanecker P., Kostrewa D.,
RA Heck A.J., Cramer P.;
RT "RNA polymerase I contains a TFIIF-related DNA-binding subcomplex.";
RL Mol. Cell 39:583-594(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA
CC precursors. Besides, RNA polymerase I has intrinsic RNA cleavage
CC activity. The heterodimer formed by RPA34 and RPA49 stimulates
CC transcript elongation by Pol I. Subunit RPA49 can bind both single-
CC stranded and double-stranded DNA. {ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:20797630, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8,
CC RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of
CC a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5,
CC RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and
CC RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43
CC form the stalk that mediates interactions with transcription initiation
CC factors and newly synthesized RNA. Forms a TFIIF-like heterodimer with
CC RPA34; the heterodimer formed by RPA34 and RPA49 can be dissociated
CC from the Pol I core giving rise to a 12 subunit form A* of Pol I
CC (formerly called pol A) that shows impaired transcript elongation
CC activity and increased sensitivity to alpha-amanitin. The heterodimer
CC formed by RPA34 and RPA49 stabilizes subunit RPA12 and stimulates
CC RPA12-dependent RNA cleavage. {ECO:0000269|PubMed:11717393,
CC ECO:0000269|PubMed:12407181, ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:20797630, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPA49/POLR1E RNA polymerase
CC subunit family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M96600; AAA34380.1; -; Genomic_DNA.
DR EMBL; X96722; CAA65496.1; -; Genomic_DNA.
DR EMBL; Z71524; CAA96155.1; -; Genomic_DNA.
DR EMBL; AY558027; AAS56353.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10311.1; -; Genomic_DNA.
DR PIR; S63221; S63221.
DR RefSeq; NP_014151.1; NM_001183086.1.
DR PDB; 3NFH; X-ray; 2.17 A; A/B=154-399.
DR PDB; 3NFI; X-ray; 1.90 A; A/B/C/D/E=171-403.
DR PDB; 4C2M; X-ray; 2.80 A; 2/M=1-415.
DR PDB; 4C3H; X-ray; 3.27 A; M=1-415.
DR PDB; 4C3I; X-ray; 3.00 A; M=1-415.
DR PDB; 4C3J; X-ray; 3.35 A; M=1-415.
DR PDB; 4YM7; X-ray; 5.50 A; AM/BM/CM/DM/EM/FM=1-415.
DR PDB; 5G5L; EM; 4.80 A; M=1-415.
DR PDB; 5LMX; EM; 4.90 A; M=1-415.
DR PDB; 5M3F; EM; 3.80 A; M=1-415.
DR PDB; 5M3M; EM; 4.00 A; M=1-415.
DR PDB; 5M5W; EM; 3.80 A; M=1-415.
DR PDB; 5M5X; EM; 4.00 A; M=1-415.
DR PDB; 5M5Y; EM; 4.00 A; M=1-415.
DR PDB; 5M64; EM; 4.60 A; M=1-415.
DR PDB; 5N5Y; EM; 7.70 A; M=1-415.
DR PDB; 5N5Z; EM; 7.70 A; M=1-415.
DR PDB; 5N60; EM; 7.70 A; M=1-415.
DR PDB; 5N61; EM; 3.40 A; M=1-415.
DR PDB; 5OA1; EM; 4.40 A; M=1-415.
DR PDB; 5W5Y; EM; 3.80 A; M=1-415.
DR PDB; 5W64; EM; 4.20 A; M=1-415.
DR PDB; 5W65; EM; 4.30 A; M=1-415.
DR PDB; 5W66; EM; 3.90 A; M=1-415.
DR PDB; 6H67; EM; 3.60 A; M=1-415.
DR PDB; 6H68; EM; 4.60 A; M=1-415.
DR PDB; 6HKO; EM; 3.42 A; M=1-415.
DR PDB; 6RQH; EM; 3.70 A; M=1-415.
DR PDB; 6RQL; EM; 2.90 A; M=1-415.
DR PDB; 6RQT; EM; 4.00 A; M=1-415.
DR PDB; 6RRD; EM; 3.10 A; M=1-415.
DR PDB; 6RUI; EM; 2.70 A; M=1-415.
DR PDB; 6RUO; EM; 3.50 A; M=1-415.
DR PDB; 6RWE; EM; 3.00 A; M=1-415.
DR PDB; 6TPS; EM; 3.54 A; M=1-415.
DR PDBsum; 3NFH; -.
DR PDBsum; 3NFI; -.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR AlphaFoldDB; Q01080; -.
DR SMR; Q01080; -.
DR BioGRID; 35591; 517.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR DIP; DIP-6577N; -.
DR IntAct; Q01080; 16.
DR MINT; Q01080; -.
DR STRING; 4932.YNL248C; -.
DR iPTMnet; Q01080; -.
DR MaxQB; Q01080; -.
DR PaxDb; Q01080; -.
DR PRIDE; Q01080; -.
DR EnsemblFungi; YNL248C_mRNA; YNL248C; YNL248C.
DR GeneID; 855473; -.
DR KEGG; sce:YNL248C; -.
DR SGD; S000005192; RPA49.
DR VEuPathDB; FungiDB:YNL248C; -.
DR eggNOG; KOG4183; Eukaryota.
DR GeneTree; ENSGT00390000018004; -.
DR HOGENOM; CLU_034953_2_0_1; -.
DR InParanoid; Q01080; -.
DR OMA; DVYPFDE; -.
DR BioCyc; YEAST:G3O-33245-MON; -.
DR Reactome; R-SCE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR EvolutionaryTrace; Q01080; -.
DR PRO; PR:Q01080; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; Q01080; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:SGD.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR DisProt; DP02519; -.
DR InterPro; IPR009668; RNA_pol-assoc_fac_A49-like.
DR PANTHER; PTHR14440; PTHR14440; 1.
DR Pfam; PF06870; RNA_pol_I_A49; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Transcription; Transferase.
FT CHAIN 1..415
FT /note="DNA-directed RNA polymerase I subunit RPA49"
FT /id="PRO_0000073955"
FT REGION 322..415
FT /note="Interaction with DNA"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 325..326
FT /note="ED->AA: No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:20797630"
FT MUTAGEN 356
FT /note="K->A: Loss of DNA binding; when associated with A-
FT 358."
FT /evidence="ECO:0000269|PubMed:20797630"
FT MUTAGEN 358
FT /note="S->A: Loss of DNA binding; when associated with A-
FT 356."
FT /evidence="ECO:0000269|PubMed:20797630"
FT MUTAGEN 359
FT /note="K->A: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:20797630"
FT MUTAGEN 365
FT /note="R->A: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:20797630"
FT MUTAGEN 393
FT /note="K->A: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:20797630"
FT CONFLICT 66
FT /note="T -> P (in Ref. 1; AAA34380)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> C (in Ref. 1; AAA34380)"
FT /evidence="ECO:0000305"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6RUO"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6RUO"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:4C2M"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6RWE"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:6RWE"
FT TURN 133..137
FT /evidence="ECO:0007829|PDB:6RWE"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:6RWE"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:6RWE"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6RWE"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:6RWE"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 256..273
FT /evidence="ECO:0007829|PDB:3NFI"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:3NFI"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:3NFI"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 322..339
FT /evidence="ECO:0007829|PDB:3NFI"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3NFI"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 357..366
FT /evidence="ECO:0007829|PDB:3NFI"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 376..382
FT /evidence="ECO:0007829|PDB:3NFI"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:3NFI"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:3NFI"
SQ SEQUENCE 415 AA; 46651 MW; 3D9BF05440D26021 CRC64;
MSVKRSVSEI EIESVQDQPS VAVGSFFKGF RAPSDTTFDL YKKKKSEKDE FVLHGENERL
EYEGYTDSSS QASNQYVVGL FNPEKKSIQL YKAPVLVSKV VSKSSKNLRG PKIKSKSDTR
PSALRNALGE AFGTKKAKKA IADLERNRID SDKLTDSAID IVDSVRTASK DLPTRAQLDE
ITSNDRPTPL ANIDATDVEQ IYPIESIIPK KELQFIRVSS ILKEADKEKK LELFPYQNNS
KYVAKKLDSL TQPSQMTKLQ LLYYLSLLLG VYENRRVNNK TKLLERLNSP PEILVDGILS
RFTVIKPGQF GRSKDRSYFI DPQNEDKILC YILAIIMHLD NFIVEITPLA HELNLKPSKV
VSLFRVLGAI VKGATVAQAE AFGIPKSTAA SYKIATMKVP FKLPEMTRRG RGPRR
