ID   SPB1_YEAST              Reviewed;         841 AA.
AC   P25582; D6VQW3;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase;
DE            EC=2.1.1.167;
DE   AltName: Full=2'-O-ribose RNA methyltransferase SPB1 {ECO:0000255|HAMAP-Rule:MF_03163};
DE   AltName: Full=AdoMet-dependent rRNA methyltransferase SPB1 {ECO:0000255|HAMAP-Rule:MF_03163};
DE   AltName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000255|HAMAP-Rule:MF_03163};
DE   AltName: Full=Suppressor of PAB1 protein 1;
GN   Name=SPB1 {ECO:0000255|HAMAP-Rule:MF_03163};
GN   OrderedLocusNames=YCL054W; ORFNames=YCL431, YCL54W;
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=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Gromadka R.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-214.
RX   PubMed=1441748; DOI=10.1002/yea.320080813;
RA   Defoor E., Debrabandere R., Keyers B., Voet M., Volckaert G.;
RT   "Nucleotide sequence of D10B, a BamHI fragment on the small-ring chromosome
RT   III of Saccharomyces cerevisiae.";
RL   Yeast 8:681-687(1992).
RN   [5]
RP   FUNCTION.
RX   PubMed=10556316; DOI=10.1093/nar/27.23.4598;
RA   Kressler D., Rojo M., Linder P., de la Cruz J.;
RT   "Spb1p is a putative methyltransferase required for 60S ribosomal subunit
RT   biogenesis in Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 27:4598-4608(1999).
RN   [6]
RP   BINDING TO S-ADENOSYL-L-METHIONINE, INTERACTION WITH NOP1 AND NOP58, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=10648622; DOI=10.1128/mcb.20.4.1370-1381.2000;
RA   Pintard L., Kressler D., Lapeyre B.;
RT   "Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that
RT   is able to bind S-adenosyl-L-methionine in vitro.";
RL   Mol. Cell. Biol. 20:1370-1381(2000).
RN   [7]
RP   IDENTIFICATION IN THE PRE-60S RIBOSOMAL PARTICLE, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=12374754; DOI=10.1093/emboj/cdf547;
RA   Nissan T.A., Bassler J., Petfalski E., Tollervey D., Hurt E.;
RT   "60S pre-ribosome formation viewed from assembly in the nucleolus until
RT   export to the cytoplasm.";
RL   EMBO J. 21:5539-5547(2002).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-52.
RX   PubMed=14636587; DOI=10.1016/s1097-2765(03)00435-0;
RA   Bonnerot C., Pintard L., Lutfalla G.;
RT   "Functional redundancy of Spb1p and a snR52-dependent mechanism for the 2'-
RT   O-ribose methylation of a conserved rRNA position in yeast.";
RL   Mol. Cell 12:1309-1315(2003).
RN   [9]
RP   FUNCTION.
RX   PubMed=15546625; DOI=10.1016/j.molcel.2004.10.022;
RA   Lapeyre B., Purushothaman S.K.;
RT   "Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs
RT   at a late processing stage.";
RL   Mol. Cell 16:663-669(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-529, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-464 AND SER-529, 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: Required for proper assembly of pre-ribosomal particles
CC       during the biogenesis of the 60S ribosomal subunit. Specifically
CC       methylates the guanosine in position 2922 of the 25S rRNA at the stage
CC       of 27S pre-rRNA maturation. Methylates also the uridine in position
CC       2921 in the absence of methylation of this residue guided by snoRNA
CC       snR52 at the stage of 35S pre-rRNA maturation. {ECO:0000255|HAMAP-
CC       Rule:MF_03163, ECO:0000269|PubMed:10556316,
CC       ECO:0000269|PubMed:14636587, ECO:0000269|PubMed:15546625}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2922) in 27S pre-rRNA + S-adenosyl-L-methionine =
CC         2'-O-methylguanosine(2922) in 27S pre-rRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42724, Rhea:RHEA-COMP:10200, Rhea:RHEA-
CC         COMP:10201, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.167;
CC         Evidence={ECO:0000269|PubMed:14636587};
CC   -!- SUBUNIT: Component of the nucleolar and nucleoplasmic pre-60S ribosomal
CC       particle. Interacts with the snoRNA-associated proteins NOP1 and NOP58.
CC       {ECO:0000255|HAMAP-Rule:MF_03163, ECO:0000269|PubMed:10648622,
CC       ECO:0000269|PubMed:12374754}.
CC   -!- INTERACTION:
CC       P25582; P43586: LOC1; NbExp=4; IntAct=EBI-17814, EBI-22906;
CC       P25582; Q07896: NOC3; NbExp=3; IntAct=EBI-17814, EBI-36093;
CC       P25582; Q12080: NOP53; NbExp=3; IntAct=EBI-17814, EBI-29395;
CC       P25582; P36160: RPF2; NbExp=6; IntAct=EBI-17814, EBI-15881;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03163, ECO:0000269|PubMed:10648622}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03163}.
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DR   EMBL; X59720; CAA42391.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07432.1; -; Genomic_DNA.
DR   PIR; S74280; S74280.
DR   RefSeq; NP_009877.1; NM_001178698.1.
DR   PDB; 6ELZ; EM; 3.30 A; w=1-841.
DR   PDB; 6EM5; EM; 4.30 A; w=1-841.
DR   PDB; 6YLX; EM; 3.90 A; w=1-841.
DR   PDB; 7NAC; EM; 3.04 A; w=1-841.
DR   PDB; 7NAD; EM; 3.04 A; w=1-841.
DR   PDB; 7NAF; EM; 3.13 A; w=1-389.
DR   PDB; 7OHR; EM; 4.72 A; w=1-841.
DR   PDB; 7OHV; EM; 3.90 A; w=1-841.
DR   PDB; 7R6K; EM; 3.17 A; w=1-841.
DR   PDB; 7R6Q; EM; 2.98 A; w=449-514.
DR   PDB; 7R72; EM; 3.07 A; w=1-841.
DR   PDB; 7R7A; EM; 3.04 A; w=1-841.
DR   PDB; 7R7C; EM; 3.71 A; w=827-838.
DR   PDB; 7R7O; X-ray; 1.58 A; A/B=1-220.
DR   PDB; 7U0H; EM; 2.76 A; w=1-841.
DR   PDBsum; 6ELZ; -.
DR   PDBsum; 6EM5; -.
DR   PDBsum; 6YLX; -.
DR   PDBsum; 7NAC; -.
DR   PDBsum; 7NAD; -.
DR   PDBsum; 7NAF; -.
DR   PDBsum; 7OHR; -.
DR   PDBsum; 7OHV; -.
DR   PDBsum; 7R6K; -.
DR   PDBsum; 7R6Q; -.
DR   PDBsum; 7R72; -.
DR   PDBsum; 7R7A; -.
DR   PDBsum; 7R7C; -.
DR   PDBsum; 7R7O; -.
DR   PDBsum; 7U0H; -.
DR   AlphaFoldDB; P25582; -.
DR   EMDB; EMD-10841; -.
DR   EMDB; EMD-12906; -.
DR   EMDB; EMD-12910; -.
DR   EMDB; EMD-24269; -.
DR   EMDB; EMD-24271; -.
DR   EMDB; EMD-24280; -.
DR   EMDB; EMD-24290; -.
DR   EMDB; EMD-24296; -.
DR   EMDB; EMD-24297; -.
DR   SMR; P25582; -.
DR   BioGRID; 30932; 130.
DR   DIP; DIP-1777N; -.
DR   IntAct; P25582; 22.
DR   MINT; P25582; -.
DR   STRING; 4932.YCL054W; -.
DR   iPTMnet; P25582; -.
DR   MaxQB; P25582; -.
DR   PaxDb; 4932-YCL054W; -.
DR   PeptideAtlas; P25582; -.
DR   EnsemblFungi; YCL054W_mRNA; YCL054W; YCL054W.
DR   GeneID; 850304; -.
DR   KEGG; sce:YCL054W; -.
DR   AGR; SGD:S000000559; -.
DR   SGD; S000000559; SPB1.
DR   VEuPathDB; FungiDB:YCL054W; -.
DR   eggNOG; KOG1098; Eukaryota.
DR   GeneTree; ENSGT00550000075004; -.
DR   HOGENOM; CLU_009422_8_1_1; -.
DR   InParanoid; P25582; -.
DR   OMA; DITTEDC; -.
DR   OrthoDB; 119516at2759; -.
DR   BioCyc; YEAST:YCL054W-MONOMER; -.
DR   BRENDA; 2.1.1.167; 984.
DR   BioGRID-ORCS; 850304; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P25582; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25582; Protein.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR   GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IMP:SGD.
DR   GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IGI:SGD.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR   GO; GO:0031167; P:rRNA methylation; IDA:SGD.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR   InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR028589; SPB1-like.
DR   PANTHER; PTHR10920:SF13; PRE-RRNA 2'-O-RIBOSE RNA METHYLTRANSFERASE FTSJ3; 1.
DR   PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR   Pfam; PF11861; DUF3381; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF07780; Spb1_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribosome biogenesis; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..841
FT                   /note="27S pre-rRNA (guanosine(2922)-2'-O)-
FT                   methyltransferase"
FT                   /id="PRO_0000155604"
FT   REGION          480..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          360..389
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   COMPBIAS        480..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..533
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..639
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..654
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         60
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   BINDING         119
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         529
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MUTAGEN         52
FT                   /note="D->A: Abolishes methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:14636587"
FT   HELIX           6..8
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   HELIX           59..67
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          73..80
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          88..92
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   HELIX           98..108
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   HELIX           128..149
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          150..161
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   HELIX           166..176
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          177..183
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          194..202
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   HELIX           215..218
FT                   /evidence="ECO:0007829|PDB:7R7O"
FT   HELIX           230..233
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   HELIX           259..264
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   HELIX           268..272
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   STRAND          276..279
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   HELIX           285..291
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   STRAND          292..296
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   HELIX           301..304
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   HELIX           312..328
FT                   /evidence="ECO:0007829|PDB:7NAF"
FT   HELIX           349..387
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           410..415
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           420..424
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           457..478
FT                   /evidence="ECO:0007829|PDB:7R6Q"
FT   TURN            482..484
FT                   /evidence="ECO:0007829|PDB:7R6Q"
FT   HELIX           487..489
FT                   /evidence="ECO:0007829|PDB:7R6Q"
FT   STRAND          499..501
FT                   /evidence="ECO:0007829|PDB:7R6Q"
FT   HELIX           503..509
FT                   /evidence="ECO:0007829|PDB:7R6Q"
FT   HELIX           510..512
FT                   /evidence="ECO:0007829|PDB:7R6Q"
FT   HELIX           553..559
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   STRAND          564..566
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           639..651
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   HELIX           660..670
FT                   /evidence="ECO:0007829|PDB:7R6K"
FT   HELIX           676..682
FT                   /evidence="ECO:0007829|PDB:7R6K"
FT   STRAND          693..695
FT                   /evidence="ECO:0007829|PDB:7R6K"
FT   HELIX           697..700
FT                   /evidence="ECO:0007829|PDB:7NAD"
FT   TURN            704..706
FT                   /evidence="ECO:0007829|PDB:7R6K"
FT   HELIX           715..724
FT                   /evidence="ECO:0007829|PDB:7R6K"
FT   HELIX           733..758
FT                   /evidence="ECO:0007829|PDB:7R6K"
SQ   SEQUENCE   841 AA;  96485 MW;  D7A080299B0C7E24 CRC64;
     MGKTQKKNSK GRLDRYYYLA KEKGYRARSS FKIIQINEKY GHFLEKSKVV IDLCAAPGSW
     CQVASKLCPV NSLIIGVDIV PMKPMPNVIT FQSDITTEDC RSKLRGYMKT WKADTVLHDG
     APNVGLGWVQ DAFTQSQLTL QALKLAVENL VVNGTFVTKI FRSKDYNKLI WVFQQLFEKV
     EATKPPASRN VSAEIFVVCK GFKAPKRLDP RLLDPKEVFE ELPDGQQNME SKIYNPEKKV
     RKRQGYEEGD NLLYHETSIL DFVRTEDPIS MLGEMNKFTI DENDHEWKIL KKLKQTTDEF
     RSCIEDLKVL GKKDFKMILR WRKIAREILG IEVKDDAKTE IEVVPLTEEE QIEKDLQGLQ
     EKQRLNVKRE RRRKNEMKQK ELQRMQMNMI TPTDIGIEAA SLGKESLFNL KTAEKTGILN
     DLAKGKKRMI FTDDELAKDN DIYIDENIMI KDKDSAADAD DLESELNAMY SDYKTRRSER
     DAKFRAKQAR GGDNEEEWTG FNEGSLEKKE EEGKDYIEDN DDEGVEGDSD DDEAITNLIS
     KLKGQEGDHK LSSKARMIFN DPIFNNVEPD LPVNTVNDGI MSSESVGDIS KLNKKRKHEE
     MHQKQDEADS SDESSSDDSD FEIVANDNAS EEFDSDYDSE EEKNQTKKEK HSRDIDIATV
     EAMTLAHQLA LGQKNKHDLV DEGFNRYTFR DTENLPDWFL EDEKEHSKIN KPITKEAAMA
     IKEKIKAMNA RPIKKVAEAK ARKRMRAVAR LEKIKKKAGL INDDSDKTEK DKAEEISRLM
     RKVTKKPKTK PKVTLVVASG RNKGLAGRPK GVKGKYKMVD GVMKNEQRAL RRIAKKHHKK
     K
//