NOT1_YEAST
ID NOT1_YEAST Reviewed; 2108 AA.
AC P25655; D6VR93;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=General negative regulator of transcription subunit 1;
DE AltName: Full=Cell division cycle protein 39;
GN Name=CDC39; Synonyms=NOT1, ROS1; OrderedLocusNames=YCR093W;
GN ORFNames=YCR1151, YCR93W;
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], AND CHARACTERIZATION.
RC STRAIN=KY803;
RX PubMed=8428577; DOI=10.1002/j.1460-2075.1993.tb05643.x;
RA Collart M.A., Struhl K.;
RT "CDC39, an essential nuclear protein that negatively regulates
RT transcription and differentially affects the constitutive and inducible
RT HIS3 promoters.";
RL EMBO J. 12:177-186(1993).
RN [2]
RP ERRATUM OF PUBMED:8428577.
RA Collart M.A., Struhl K.;
RL EMBO J. 12:2990-2990(1993).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 1298.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP CHARACTERIZATION.
RX PubMed=7926748; DOI=10.1101/gad.8.5.525;
RA Collart M.A., Struhl K.;
RT "NOT1(CDC39), NOT2(CDC36), NOT3, and NOT4 encode a global-negative
RT regulator of transcription that differentially affects TATA-element
RT utilization.";
RL Genes Dev. 8:525-537(1994).
RN [7]
RP IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX, AND FUNCTION OF THE CCR4-NOT
RP CORE COMPLEX IN TRANSCRIPTIONAL REGULATION.
RX PubMed=9463387; DOI=10.1093/emboj/17.4.1096;
RA Liu H.Y., Badarinarayana V., Audino D.C., Rappsilber J., Mann M.,
RA Denis C.L.;
RT "The NOT proteins are part of the CCR4 transcriptional complex and affect
RT gene expression both positively and negatively.";
RL EMBO J. 17:1096-1106(1998).
RN [8]
RP INTERACTION WITH CCR4; POP2; NOT2; NOT4 AND NOT5.
RX PubMed=10490603; DOI=10.1128/mcb.19.10.6642;
RA Bai Y., Salvadore C., Chiang Y.C., Collart M.A., Liu H.Y., Denis C.L.;
RT "The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and
RT functionally separated from NOT2, NOT4, and NOT5.";
RL Mol. Cell. Biol. 19:6642-6651(1999).
RN [9]
RP IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX, AND INTERACTION WITH CAF40 AND
RP CAF130.
RX PubMed=11733989; DOI=10.1006/jmbi.2001.5162;
RA Chen J., Rappsilber J., Chiang Y.C., Russell P., Mann M., Denis C.L.;
RT "Purification and characterization of the 1.0 MDa CCR4-NOT complex
RT identifies two novel components of the complex.";
RL J. Mol. Biol. 314:683-694(2001).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=11889048; DOI=10.1093/emboj/21.6.1427;
RA Tucker M., Staples R.R., Valencia-Sanchez M.A., Muhlrad D., Parker R.;
RT "Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase
RT complex in Saccharomyces cerevisiae.";
RL EMBO J. 21:1427-1436(2002).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2102, 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).
CC -!- FUNCTION: Acts as component of the CCR4-NOT core complex, which in the
CC nucleus seems to be a general transcription factor, and in the
CC cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT
CC protein subcomplex negatively regulates the basal and activated
CC transcription of many genes. Preferentially affects TC-type TATA
CC element-dependent transcription. Could directly or indirectly inhibit
CC component(s) of the general transcription machinery.
CC {ECO:0000269|PubMed:9463387}.
CC -!- SUBUNIT: Forms a NOT protein complex that comprises NOT1, NOT2, NOT3,
CC NOT4 and NOT5. Subunit of the 1.0 MDa CCR4-NOT core complex that
CC contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In
CC the complex interacts with CCR4, POP2, NOT2, NOT4 and NOT5. The core
CC complex probably is part of a less characterized 1.9 MDa CCR4-NOT
CC complex. {ECO:0000269|PubMed:10490603, ECO:0000269|PubMed:11733989,
CC ECO:0000269|PubMed:9463387}.
CC -!- INTERACTION:
CC P25655; P53280: CAF130; NbExp=6; IntAct=EBI-12139, EBI-23322;
CC P25655; P53829: CAF40; NbExp=9; IntAct=EBI-12139, EBI-28306;
CC P25655; P31384: CCR4; NbExp=8; IntAct=EBI-12139, EBI-4396;
CC P25655; P06100: CDC36; NbExp=7; IntAct=EBI-12139, EBI-12153;
CC P25655; P34909: MOT2; NbExp=8; IntAct=EBI-12139, EBI-12174;
CC P25655; P06102: NOT3; NbExp=3; IntAct=EBI-12139, EBI-12165;
CC P25655; Q12514: NOT5; NbExp=6; IntAct=EBI-12139, EBI-12184;
CC P25655; P39008: POP2; NbExp=10; IntAct=EBI-12139, EBI-13629;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11889048}. Nucleus
CC {ECO:0000269|PubMed:11889048}.
CC -!- MISCELLANEOUS: Present with 4300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CNOT1 family. {ECO:0000305}.
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DR EMBL; X70151; CAA49721.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42248.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07562.1; -; Genomic_DNA.
DR PIR; S28417; S28417.
DR RefSeq; NP_010017.2; NM_001178799.1.
DR PDB; 4B89; X-ray; 1.50 A; A=755-1000.
DR PDB; 4B8A; X-ray; 2.40 A; A=755-1000.
DR PDB; 4B8B; X-ray; 2.80 A; A/B=151-753.
DR PDB; 4B8C; X-ray; 3.41 A; B/G/H/I=755-1000.
DR PDB; 4BY6; X-ray; 2.80 A; A/D=1541-2093.
DR PDB; 4CV5; X-ray; 3.81 A; A/C=1071-1282.
DR PDB; 5AJD; X-ray; 3.62 A; A/C/E/G/I/K=1541-2093.
DR PDBsum; 4B89; -.
DR PDBsum; 4B8A; -.
DR PDBsum; 4B8B; -.
DR PDBsum; 4B8C; -.
DR PDBsum; 4BY6; -.
DR PDBsum; 4CV5; -.
DR PDBsum; 5AJD; -.
DR AlphaFoldDB; P25655; -.
DR SMR; P25655; -.
DR BioGRID; 31065; 364.
DR ComplexPortal; CPX-1800; CCR4-NOT mRNA deadenylase complex.
DR DIP; DIP-1202N; -.
DR IntAct; P25655; 44.
DR MINT; P25655; -.
DR STRING; 4932.YCR093W; -.
DR iPTMnet; P25655; -.
DR MaxQB; P25655; -.
DR PaxDb; P25655; -.
DR PRIDE; P25655; -.
DR EnsemblFungi; YCR093W_mRNA; YCR093W; YCR093W.
DR GeneID; 850455; -.
DR KEGG; sce:YCR093W; -.
DR SGD; S000000689; CDC39.
DR VEuPathDB; FungiDB:YCR093W; -.
DR eggNOG; KOG1831; Eukaryota.
DR GeneTree; ENSGT00390000014869; -.
DR HOGENOM; CLU_000286_3_1_1; -.
DR InParanoid; P25655; -.
DR OMA; AIRRYHK; -.
DR BioCyc; YEAST:G3O-29387-MON; -.
DR PRO; PR:P25655; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25655; protein.
DR GO; GO:0030015; C:CCR4-NOT core complex; IPI:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0010607; P:negative regulation of cytoplasmic mRNA processing body assembly; IDA:SGD.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:SGD.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IPI:SGD.
DR GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR Gene3D; 1.25.40.840; -; 1.
DR InterPro; IPR007196; CCR4-Not_Not1_C.
DR InterPro; IPR032191; CNOT1_CAF1_bind.
DR InterPro; IPR024557; CNOT1_dom_4.
DR InterPro; IPR032194; CNOT1_HEAT.
DR InterPro; IPR032195; CNOT1_HEAT_N.
DR InterPro; IPR032193; CNOT1_TTP_bind.
DR InterPro; IPR038535; CNOT1_TTP_bind_sf.
DR InterPro; IPR040398; Not1.
DR PANTHER; PTHR13162; PTHR13162; 1.
DR Pfam; PF16415; CNOT1_CAF1_bind; 1.
DR Pfam; PF16418; CNOT1_HEAT; 1.
DR Pfam; PF16419; CNOT1_HEAT_N; 1.
DR Pfam; PF16417; CNOT1_TTP_bind; 1.
DR Pfam; PF12842; DUF3819; 1.
DR Pfam; PF04054; Not1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..2108
FT /note="General negative regulator of transcription subunit
FT 1"
FT /id="PRO_0000096955"
FT REGION 1323..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 795..813
FT /evidence="ECO:0000255"
FT COILED 1021..1046
FT /evidence="ECO:0000255"
FT MOD_RES 2102
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956"
FT CONFLICT 526
FT /note="T -> A (in Ref. 1; CAA49721)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="A -> R (in Ref. 1; CAA49721)"
FT /evidence="ECO:0000305"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 301..312
FT /evidence="ECO:0007829|PDB:4B8B"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4B8B"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 347..358
FT /evidence="ECO:0007829|PDB:4B8B"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 367..382
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 384..393
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 405..421
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 437..450
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 457..464
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 468..474
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 484..490
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 495..502
FT /evidence="ECO:0007829|PDB:4B8B"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 508..520
FT /evidence="ECO:0007829|PDB:4B8B"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 536..547
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 553..569
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:4B8B"
FT TURN 574..577
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 581..585
FT /evidence="ECO:0007829|PDB:4B8B"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 595..609
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 615..626
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 631..647
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 648..653
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 656..671
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 677..691
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 698..709
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 710..716
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 718..727
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 729..733
FT /evidence="ECO:0007829|PDB:4B8B"
FT HELIX 735..743
FT /evidence="ECO:0007829|PDB:4B8B"
FT STRAND 765..767
FT /evidence="ECO:0007829|PDB:4B8C"
FT HELIX 783..795
FT /evidence="ECO:0007829|PDB:4B89"
FT TURN 798..800
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 801..811
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 814..816
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 817..827
FT /evidence="ECO:0007829|PDB:4B89"
FT TURN 828..831
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 833..835
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 836..846
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 849..867
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 872..874
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 877..890
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 892..894
FT /evidence="ECO:0007829|PDB:4B89"
FT TURN 900..902
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 905..914
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 918..929
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 930..932
FT /evidence="ECO:0007829|PDB:4B89"
FT STRAND 936..939
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 943..958
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 963..975
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 980..982
FT /evidence="ECO:0007829|PDB:4B89"
FT HELIX 1568..1583
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1591..1601
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 1602..1604
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1609..1628
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1638..1652
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1661..1681
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1690..1711
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1717..1740
FT /evidence="ECO:0007829|PDB:4BY6"
FT TURN 1743..1745
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1747..1749
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1750..1757
FT /evidence="ECO:0007829|PDB:4BY6"
FT TURN 1760..1762
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1763..1766
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1770..1772
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1775..1791
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1801..1819
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1821..1826
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1828..1834
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1840..1847
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1866..1868
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1870..1873
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1882..1889
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1890..1898
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1902..1916
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 1917..1921
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 1923..1930
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1932..1952
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1964..1974
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1978..1990
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 1994..1996
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 1997..2011
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 2019..2034
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 2035..2038
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 2042..2052
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 2059..2061
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 2063..2066
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 2069..2077
FT /evidence="ECO:0007829|PDB:4BY6"
SQ SEQUENCE 2108 AA; 240279 MW; 5B2AE15BCF95E009 CRC64;
MLSATYRDLN TASNLETSKE KQAAQIVIAQ ISLLFTTLNN DNFESVEREI RHILDRSSVD
IYIKVWERLL TLSSRDILQA GKFLLQENLL HRLLLEFAKD LPKKSTDLIE LLKERTFNNQ
EFQKQTGITL SLFIDLFDKS ANKDIIESLD RSSQINDFKT IKMNHTNYLR NFFLQTTPET
LESNLRDLLH SLEGESLNDL LALLLSEILS PGSQNLQNDP TRSWLTPPMV LDATNRGNVI
ARSISSLQAN QINWNRVFNL MSTKYFLSAP LMPTTASLSC LFAALHDGPV IDEFFSCDWK
VIFKLDLAIQ LHKWSVQNGC FDLLNAEGTR KVSETIPNTK QSLLYLLSIA SLNLELFLQR
EELSDGPMLA YFQECFFEDF NYAPEYLILA LVKEMKRFVL LIENRTVIDE ILITLLIQVH
NKSPSSFKDV ISTITDDSKI VDAAKIIINS DDAPIANFLK SLLDTGRLDT VINKLPFNEA
FKILPCARQI GWEGFDTFLK TKVSPSNVDV VLESLEVQTK MTDTNTPFRS LKTFDLFAFH
SLIEVLNKCP LDVLQLQRFE SLEFSLLIAF PRLINFGFGH DEAILANGDI AGINNDIEKE
MQNYLQKMYS GELAIKDVIE LLRRLRDSDL PRDQEVFTCI THAVIAESTF FQDYPLDALA
TTSVLFGSMI LFQLLRGFVL DVAFRIIMRF AKEPPESKMF KFAVQAIYAF RIRLAEYPQY
CKDLLRDVPA LKSQAQVYQS IVEAATLANA PKERSRPVQE MIPLKFFAVD EVSCQINQEG
APKDVVEKVL FVLNNVTLAN LNNKVDELKK SLTPNYFSWF STYLVTQRAK TEPNYHDLYS
KVIVAMGSGL LHQFMVNVTL RQLFVLLSTK DEQAIDKKHL KNLASWLGCI TLALNKPIKH
KNIAFREMLI EAYKENRLEI VVPFVTKILQ RASESKIFKP PNPWTVGILK LLIELNEKAN
WKLSLTFEVE VLLKSFNLTT KSLKPSNFIN TPEVIETLSG ALGSITLEQQ QTEQQRQIIL
MQQHQQQMLI YQQRQQQQQQ RQQQQQHHIS ANTIADQQAA FGGEGSISHD NPFNNLLGST
IFVTHPDLKR VFQMALAKSV REILLEVVEK SSGIAVVTTT KIILKDFATE VDESKLKTAA
IIMVRHLAQS LARATSIEPL KEGIRSTMQS LAPNLMSLSS SPAEELDTAI NENIGIALVL
IEKASMDKST QDLADQLMQA IAIRRYHKER RADQPFITQN TNPYSLSLPE PLGLKNTGVT
PQQFRVYEEF GKNIPNLDVI PFAGLPAHAP PMTQNVGLTQ PQQQQAQMPT QILTSEQIRA
QQQQQQLQKS RLNQPSQSAQ PPGVNVPNPQ GGIAAVQSDL EQNQRVLVHL MDILVSQIKE
NATKNNLAEL GDQNQIKTII FQILTFIAKS AQKDQLALKV SQAVVNSLFA TSESPLCREV
LSLLLEKLCS LSLVARKDVV WWLVYALDSR KFNVPVIRSL LEVNLIDATE LDNVLVTAMK
NKMENSTEFA MKLIQNTVLS DDPILMRMDF IKTLEHLASS EDENVKKFIK EFEDTKIMPV
RKGTKTTRTE KLYLVFTEWV KLLQRVENND VITTVFIKQL VEKGVISDTD NLLTFVKSSL
ELSVSSFKES DPTDEVFIAI DALGSLIIKL LILQGFKDDT RRDYINAIFS VIVLVFAKDH
SQEGTTFNER PYFRLFSNIL YEWATIRTHN FVRISDSSTR QELIEFDSVF YNTFSGYLHA
LQPFAFPGFS FAWVTLLSHR MLLPIMLRLP NKIGWEKLML LIIDLFKFLD QYTSKHAVSD
AVSVVYKGTL RVILGISNDM PSFLIENHYE LMNNLPPTYF QLKNVILSAI PKNMTVPNPY
DVDLNMEDIP ACKELPEVFF DPVIDLHSLK KPVDNYLRIP SNSLLRTILS AIYKDTYDIK
KGVGYDFLSV DSKLIRAIVL HVGIEAGIEY KRTSSNAVFN TKSSYYTLLF NLIQNGSIEM
KYQIILSIVE QLRYPNIHTY WFSFVLMNMF KSDEWNDQKL EVQEIILRNF LKRIIVNKPH
TWGVSVFFTQ LINNNDINLL DLPFVQSVPE IKLILQQLVK YSKKYTTSEQ DDQSATINRR
QTPLQSNA
