ID   CEF1_YEAST              Reviewed;         590 AA.
AC   Q03654; D6W038; Q6B1D8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Pre-mRNA-splicing factor CEF1;
DE   AltName: Full=PRP nineteen-associated complex protein 85;
DE   AltName: Full=PRP19-associated complex protein 85;
GN   Name=CEF1; Synonyms=NTC85; OrderedLocusNames=YMR213W;
GN   ORFNames=YM8261.07;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   PROTEIN SEQUENCE OF 3-16, FUNCTION, DOMAIN, AND IDENTIFICATION IN THE
RP   PRP19-ASSOCIATED COMPLEX.
RX   PubMed=10092627; DOI=10.1074/jbc.274.14.9455;
RA   Tsai W.-Y., Chow Y.-T., Chen H.-R., Huang K.-T., Hong R.-I., Jan S.-P.,
RA   Kuo N.-Y., Tsao T.Y., Chen C.-H., Cheng S.-C.;
RT   "Cef1p is a component of the Prp19p-associated complex and essential for
RT   pre-mRNA splicing.";
RL   J. Biol. Chem. 274:9455-9462(1999).
RN   [5]
RP   FUNCTION, AND MUTAGENESIS OF TRP-52 AND TRP-84.
RX   PubMed=11784857; DOI=10.1128/mcb.22.3.801-815.2002;
RA   Burns C.G., Ohi R., Mehta S., O'Toole E.T., Winey M., Clark T.A.,
RA   Sugnet C.W., Ares M. Jr., Gould K.L.;
RT   "Removal of a single alpha-tubulin gene intron suppresses cell cycle arrest
RT   phenotypes of splicing factor mutations in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 22:801-815(2002).
RN   [6]
RP   INTERACTION WITH PRP19, AND IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
RX   PubMed=9528791; DOI=10.1128/mcb.18.4.2196;
RA   Chen H.-R., Jan S.-P., Tsao T.Y., Sheu Y.-J., Banroques J., Cheng S.-C.;
RT   "Snt309p, a component of the Prp19p-associated complex that interacts with
RT   Prp19p and associates with the spliceosome simultaneously with or
RT   immediately after dissociation of U4 in the same manner as Prp19p.";
RL   Mol. Cell. Biol. 18:2196-2204(1998).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF TRP-33; TRP-52; TRP-84 AND TYR-102.
RX   PubMed=9632794; DOI=10.1128/mcb.18.7.4097;
RA   Ohi R., Feoktistova A., McCann S., Valentine V., Look A.T., Lipsick J.S.,
RA   Gould K.L.;
RT   "Myb-related Schizosaccharomyces pombe cdc5p is structurally and
RT   functionally conserved in eukaryotes.";
RL   Mol. Cell. Biol. 18:4097-4108(1998).
RN   [8]
RP   FUNCTION.
RX   PubMed=10570151; DOI=10.1073/pnas.96.24.13789;
RA   Burns C.G., Ohi R., Krainer A.R., Gould K.L.;
RT   "Evidence that Myb-related CDC5 proteins are required for pre-mRNA
RT   splicing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13789-13794(1999).
RN   [9]
RP   INTERACTION WITH CLF1; ISY1; NTC20; SYF1 AND SYF2.
RX   PubMed=11102353; DOI=10.1093/genetics/156.4.1503;
RA   Ben-Yehuda S., Dix I., Russell C.S., McGarvey M., Beggs J.D., Kupiec M.;
RT   "Genetic and physical interactions between factors involved in both cell
RT   cycle progression and pre-mRNA splicing in Saccharomyces cerevisiae.";
RL   Genetics 156:1503-1517(2000).
RN   [10]
RP   INTERACTION WITH ISY1; NTC20 AND PRP19.
RX   PubMed=11018040; DOI=10.1074/jbc.m006958200;
RA   Chen C.-H., Tsai W.-Y., Chen H.-R., Wang C.-H., Cheng S.-C.;
RT   "Identification and characterization of two novel components of the Prp19p-
RT   associated complex, Ntc30p and Ntc20p.";
RL   J. Biol. Chem. 276:488-494(2001).
RN   [11]
RP   IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA   Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT   "Proteomics analysis reveals stable multiprotein complexes in both fission
RT   and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT   splicing factors, and snRNAs.";
RL   Mol. Cell. Biol. 22:2011-2024(2002).
RN   [12]
RP   INTERACTION WITH PRP19; PRP46 AND SYF1.
RX   PubMed=12088152; DOI=10.1017/s1355838202025050;
RA   Ohi M.D., Gould K.L.;
RT   "Characterization of interactions among the Cef1p-Prp19p-associated
RT   splicing complex.";
RL   RNA 8:798-815(2002).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [14]
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   [15]
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).
CC   -!- FUNCTION: Involved in pre-mRNA splicing and cell cycle control.
CC       Required for the binding of the NTC complex (or PRP19-associated
CC       complex) components to the spliceosome to mediate conformational
CC       rearrangement or to stabilize the structure of the spliceosome after U4
CC       snRNA dissociation, which leads to spliceosome maturation. Its absence
CC       leads to an arrest of the cell cycle, possibly due to the inefficient
CC       splicing of TUB1. {ECO:0000269|PubMed:10092627,
CC       ECO:0000269|PubMed:10570151, ECO:0000269|PubMed:11784857,
CC       ECO:0000269|PubMed:9632794}.
CC   -!- SUBUNIT: Belongs to the NTC complex (or PRP19-associated complex),
CC       composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and
CC       PRP19. The NTC complex associates with the spliceosome after the
CC       release of the U1 and U4 snRNAs and forms the CWC spliceosome
CC       subcomplex (or CEF1-associated complex) reminiscent of a late-stage
CC       spliceosome composed also of the U2, U5 and U6 snRNAs and at least
CC       BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23,
CC       CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11,
CC       PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3,
CC       SNU114, SPP2, RSE1 and YJU2. Interacts with CLF1, ISY1, NTC20, PRP19,
CC       PRP46, SYF1 and SYF2. {ECO:0000269|PubMed:10092627,
CC       ECO:0000269|PubMed:11018040, ECO:0000269|PubMed:11102353,
CC       ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12088152,
CC       ECO:0000269|PubMed:9528791}.
CC   -!- INTERACTION:
CC       Q03654; P25337: BUD31; NbExp=12; IntAct=EBI-476, EBI-547;
CC       Q03654; Q12309: CLF1; NbExp=8; IntAct=EBI-476, EBI-484;
CC       Q03654; Q03772: CWC15; NbExp=3; IntAct=EBI-476, EBI-36780;
CC       Q03654; P38302: NTC20; NbExp=4; IntAct=EBI-476, EBI-20921;
CC       Q03654; P32523: PRP19; NbExp=9; IntAct=EBI-476, EBI-493;
CC       Q03654; Q06411: SPP382; NbExp=3; IntAct=EBI-476, EBI-576;
CC       Q03654; Q04048: SYF1; NbExp=5; IntAct=EBI-476, EBI-540;
CC       Q03654; P53277: SYF2; NbExp=3; IntAct=EBI-476, EBI-23308;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
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DR   EMBL; Z49809; CAA89928.1; -; Genomic_DNA.
DR   EMBL; AY693142; AAT93161.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10112.1; -; Genomic_DNA.
DR   PIR; S55095; S55095.
DR   RefSeq; NP_013940.1; NM_001182720.1.
DR   PDB; 5GM6; EM; 3.50 A; c=1-253, c=482-587.
DR   PDB; 5GMK; EM; 3.40 A; c=1-253, c=482-587.
DR   PDB; 5LJ3; EM; 3.80 A; O=1-590.
DR   PDB; 5LJ5; EM; 3.80 A; O=1-590.
DR   PDB; 5LQW; EM; 5.80 A; W=1-590.
DR   PDB; 5MPS; EM; 3.85 A; O=1-590.
DR   PDB; 5MQ0; EM; 4.17 A; O=1-590.
DR   PDB; 5WSG; EM; 4.00 A; c=9-253, c=482-587.
DR   PDB; 5Y88; EM; 3.70 A; J=1-590.
DR   PDB; 5YLZ; EM; 3.60 A; J=1-590.
DR   PDB; 6BK8; EM; 3.30 A; S=1-590.
DR   PDB; 6EXN; EM; 3.70 A; O=1-590.
DR   PDB; 6J6G; EM; 3.20 A; c=1-590.
DR   PDB; 6J6H; EM; 3.60 A; c=1-590.
DR   PDB; 6J6N; EM; 3.86 A; c=1-590.
DR   PDB; 6J6Q; EM; 3.70 A; c=1-590.
DR   PDB; 7DCO; EM; 2.50 A; L=1-590.
DR   PDBsum; 5GM6; -.
DR   PDBsum; 5GMK; -.
DR   PDBsum; 5LJ3; -.
DR   PDBsum; 5LJ5; -.
DR   PDBsum; 5LQW; -.
DR   PDBsum; 5MPS; -.
DR   PDBsum; 5MQ0; -.
DR   PDBsum; 5WSG; -.
DR   PDBsum; 5Y88; -.
DR   PDBsum; 5YLZ; -.
DR   PDBsum; 6BK8; -.
DR   PDBsum; 6EXN; -.
DR   PDBsum; 6J6G; -.
DR   PDBsum; 6J6H; -.
DR   PDBsum; 6J6N; -.
DR   PDBsum; 6J6Q; -.
DR   PDBsum; 7DCO; -.
DR   AlphaFoldDB; Q03654; -.
DR   EMDB; EMD-0686; -.
DR   EMDB; EMD-0687; -.
DR   EMDB; EMD-0691; -.
DR   EMDB; EMD-0692; -.
DR   EMDB; EMD-30637; -.
DR   EMDB; EMD-3539; -.
DR   EMDB; EMD-3541; -.
DR   EMDB; EMD-3979; -.
DR   EMDB; EMD-4055; -.
DR   EMDB; EMD-4057; -.
DR   EMDB; EMD-6817; -.
DR   EMDB; EMD-6839; -.
DR   EMDB; EMD-7109; -.
DR   EMDB; EMD-9525; -.
DR   SMR; Q03654; -.
DR   BioGRID; 35391; 314.
DR   ComplexPortal; CPX-1651; PRP19-associated complex.
DR   ComplexPortal; CPX-1885; NineTeen complex.
DR   DIP; DIP-1113N; -.
DR   IntAct; Q03654; 51.
DR   MINT; Q03654; -.
DR   STRING; 4932.YMR213W; -.
DR   iPTMnet; Q03654; -.
DR   MaxQB; Q03654; -.
DR   PaxDb; 4932-YMR213W; -.
DR   PeptideAtlas; Q03654; -.
DR   EnsemblFungi; YMR213W_mRNA; YMR213W; YMR213W.
DR   GeneID; 855253; -.
DR   KEGG; sce:YMR213W; -.
DR   AGR; SGD:S000004826; -.
DR   SGD; S000004826; CEF1.
DR   VEuPathDB; FungiDB:YMR213W; -.
DR   eggNOG; KOG0050; Eukaryota.
DR   GeneTree; ENSGT00550000074922; -.
DR   HOGENOM; CLU_009082_2_1_1; -.
DR   InParanoid; Q03654; -.
DR   OMA; KYGTHQW; -.
DR   OrthoDB; 131128at2759; -.
DR   BioCyc; YEAST:G3O-32896-MONOMER; -.
DR   BioGRID-ORCS; 855253; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q03654; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03654; Protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000974; C:Prp19 complex; IDA:SGD.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IMP:SGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd11659; SANT_CDC5_II; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   InterPro; IPR047242; CDC5L/Cef1.
DR   InterPro; IPR021786; Cdc5p/Cef1_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR047240; SANT_CDC5L_II.
DR   PANTHER; PTHR45885; CELL DIVISION CYCLE 5-LIKE PROTEIN; 1.
DR   PANTHER; PTHR45885:SF1; CELL DIVISION CYCLE 5-LIKE PROTEIN; 1.
DR   Pfam; PF11831; Myb_Cef; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 2.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS51294; HTH_MYB; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW   Spliceosome.
FT   CHAIN           1..590
FT                   /note="Pre-mRNA-splicing factor CEF1"
FT                   /id="PRO_0000197107"
FT   DOMAIN          1..60
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          63..110
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        33..56
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        84..106
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          244..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..490
FT                   /note="Interaction with PRP19 and self-interaction"
FT   COMPBIAS        244..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         33
FT                   /note="W->G: No effect. Slower growth and
FT                   thermosensitivity; when associated with G-84. Complete loss
FT                   of function; when associated with G-52 and G-84. Complete
FT                   loss of function; when associated with G-52; G-84 and
FT                   G-102."
FT                   /evidence="ECO:0000269|PubMed:9632794"
FT   MUTAGEN         52
FT                   /note="W->G: No effect. Slower growth and
FT                   thermosensitivity; when associated with G-84. Complete loss
FT                   of function; when associated with G-33 and G-84. Complete
FT                   loss of function; when associated with G-33; G-84 and
FT                   G-102."
FT                   /evidence="ECO:0000269|PubMed:11784857,
FT                   ECO:0000269|PubMed:9632794"
FT   MUTAGEN         84
FT                   /note="W->G: No effect. Slower growth and
FT                   thermosensitivity; when associated with G-33 or G-52.
FT                   Complete loss of function; when associated with G-33 and
FT                   G-52 or G-52 and Y-102. Complete loss of function; when
FT                   associated with G-33; G-52 and G-102."
FT                   /evidence="ECO:0000269|PubMed:11784857,
FT                   ECO:0000269|PubMed:9632794"
FT   MUTAGEN         102
FT                   /note="Y->G: No effect. Slower growth and
FT                   thermosensitivity; when associated with G-52 or G-84.
FT                   Complete loss of function; when associated with G-33; G-52
FT                   and G-84."
FT                   /evidence="ECO:0000269|PubMed:9632794"
FT   CONFLICT        11
FT                   /note="G -> E (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="K -> E (in Ref. 3; AAT93161)"
FT                   /evidence="ECO:0000305"
FT   HELIX           15..28
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           45..54
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:5GMK"
FT   HELIX           84..91
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           95..106
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:6BK8"
FT   HELIX           146..159
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           165..193
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           232..251
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   STRAND          335..337
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           338..355
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           359..363
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           374..379
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           388..400
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   TURN            423..425
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           426..437
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           445..468
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           483..581
FT                   /evidence="ECO:0007829|PDB:6J6G"
FT   HELIX           583..586
FT                   /evidence="ECO:0007829|PDB:6J6G"
SQ   SEQUENCE   590 AA;  67731 MW;  A4C417A8B330EA9C CRC64;
     MPPVPIYVKG GVWTNVEDQI LKAAVQKYGT HQWSKVASLL QKKTARQSEL RWNEYLNPKL
     NFTEFSKEED AQLLDLAREL PNQWRTIADM MARPAQVCVE RYNRLLESED SGGAALSTGV
     TDLKAGDINP NAETQMARPD NGDLEDEEKE MLAEARARLL NTQGKKATRK IRERMLEESK
     RIAELQKRRE LKQAGINVAI KKPKKKYGTD IDYNEDIVYE QAPMPGIYDT STEDRQIKKK
     FEQFERKVNR KGLDGNKDKP SKKNKDKKRK HDENEHVEKA ALGESTTLTD EYKKPKLILS
     APGTKQGKVT YKKKLESKRQ KLIEAQATGT VLTPKELLPH DSGQEDNERS NIKSGKQLKS
     RIRKFLVQMF ASLPSPKNDF EIVLSEDEKE EDAEIAEYEK EFENERAMNE EDNFIEPPSQ
     NDAPRVSLVA VPLAYSTLPI PEFKNNPQSA IDNKYNLLVA NAINKEPHMV PEDTVDFLKE
     VESRMQHITQ GRTSMKIQFK TAMPPTEVLL ESIQSKVESI EQLQRKLQHV QPLEQQNNEM
     CSTLCHHSLP ALIEGQRKYY ADYYAYRQEI RSLEGRRKRL QAMLNSSSSI
//