SPT5_YEAST
ID SPT5_YEAST Reviewed; 1063 AA.
AC P27692; D6VZG4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=Chromatin elongation factor SPT5;
GN Name=SPT5; OrderedLocusNames=YML010W; ORFNames=YM9571.08;
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=ATCC 204508 / S288c;
RX PubMed=1840633; DOI=10.1128/mcb.11.6.3009-3019.1991;
RA Swanson M.S., Malone E.A., Winston F.;
RT "SPT5, an essential gene important for normal transcription in
RT Saccharomyces cerevisiae, encodes an acidic nuclear protein with a carboxy-
RT terminal repeat.";
RL Mol. Cell. Biol. 11:3009-3019(1991).
RN [2]
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 [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 FUNCTION IN TRANSCRIPTION ELONGATION, AND IDENTIFICATION IN THE SPT4-SPT5
RP COMPLEX.
RX PubMed=9450930; DOI=10.1101/gad.12.3.357;
RA Hartzog G.A., Wada T., Handa H., Winston F.;
RT "Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA
RT polymerase II in Saccharomyces cerevisiae.";
RL Genes Dev. 12:357-369(1998).
RN [5]
RP CHARACTERIZATION.
RX PubMed=14668364; DOI=10.1093/genetics/165.3.1059;
RA Howard S.C., Hester A., Herman P.K.;
RT "The Ras/PKA signaling pathway may control RNA polymerase II elongation via
RT the Spt4p/Spt5p complex in Saccharomyces cerevisiae.";
RL Genetics 165:1059-1070(2003).
RN [6]
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 [7]
RP FUNCTION IN TRANSCRIPTION ELONGATION AND MRNA PROCESSING.
RX PubMed=12556496; DOI=10.1128/mcb.23.4.1368-1378.2003;
RA Lindstrom D.L., Squazzo S.L., Muster N., Burckin T.A., Wachter K.C.,
RA Emigh C.A., McCleery J.A., Yates J.R. III, Hartzog G.A.;
RT "Dual roles for Spt5 in pre-mRNA processing and transcription elongation
RT revealed by identification of Spt5-associated proteins.";
RL Mol. Cell. Biol. 23:1368-1378(2003).
RN [8]
RP FUNCTION IN TRANSCRIPTION ELONGATION.
RX PubMed=12554661; DOI=10.1093/emboj/cdg047;
RA Rondon A.G., Garcia-Rubio M., Gonzalez-Barrera S., Aguilera A.;
RT "Molecular evidence for a positive role of Spt4 in transcription
RT elongation.";
RL EMBO J. 22:612-620(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [10]
RP FUNCTION IN PROCESSIVITY.
RX PubMed=15780939; DOI=10.1016/j.molcel.2005.02.017;
RA Mason P.B., Struhl K.;
RT "Distinction and relationship between elongation rate and processivity of
RT RNA polymerase II in vivo.";
RL Mol. Cell 17:831-840(2005).
RN [11]
RP FUNCTION IN ALTERNATIVE SPLICING.
RX PubMed=16172632; DOI=10.1371/journal.pcbi.0010039;
RA Xiao Y., Yang Y.H., Burckin T.A., Shiue L., Hartzog G.A., Segal M.R.;
RT "Analysis of a splice array experiment elucidates roles of chromatin
RT elongation factor Spt4-5 in splicing.";
RL PLoS Comput. Biol. 1:276-288(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133 AND SER-136, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
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 [14]
RP SUBCELLULAR LOCATION.
RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA Andrews B.J.;
RT "Two-color cell array screen reveals interdependent roles for histone
RT chaperones and a chromatin boundary regulator in histone gene repression.";
RL Mol. Cell 35:340-351(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-188 AND SER-219, 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).
RN [16]
RP INTERACTION WITH SHE2.
RX PubMed=20713510; DOI=10.1101/gad.1937510;
RA Shen Z., St-Denis A., Chartrand P.;
RT "Cotranscriptional recruitment of She2p by RNA pol II elongation factor
RT Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud.";
RL Genes Dev. 24:1914-1926(2010).
CC -!- FUNCTION: The SPT4-SPT5 complex mediates both activation and inhibition
CC of transcription elongation, and plays a role in pre-mRNA processing.
CC This complex seems to be important for the stability of the RNA
CC polymerase II elongation machinery on the chromatin template but not
CC for the inherent ability of this machinery to translocate down the
CC gene. {ECO:0000269|PubMed:12554661, ECO:0000269|PubMed:12556496,
CC ECO:0000269|PubMed:15780939, ECO:0000269|PubMed:16172632,
CC ECO:0000269|PubMed:9450930}.
CC -!- SUBUNIT: Component of the SPT4-SPT5 complex. Interacts with RNA
CC polymerase II. Interacts with SHE2. {ECO:0000269|PubMed:20713510,
CC ECO:0000269|PubMed:9450930}.
CC -!- INTERACTION:
CC P27692; Q06697: CDC73; NbExp=6; IntAct=EBI-17937, EBI-29913;
CC P27692; P89105: CTR9; NbExp=2; IntAct=EBI-17937, EBI-5283;
CC P27692; P40164: PSY2; NbExp=7; IntAct=EBI-17937, EBI-29107;
CC P27692; P04050: RPO21; NbExp=3; IntAct=EBI-17937, EBI-15760;
CC P27692; P53064: RTF1; NbExp=5; IntAct=EBI-17937, EBI-16303;
CC P27692; P32914: SPT4; NbExp=11; IntAct=EBI-17937, EBI-17928;
CC P27692; P23615: SPT6; NbExp=2; IntAct=EBI-17937, EBI-17947;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14576278}.
CC Mitochondrion {ECO:0000269|PubMed:14576278}. Chromosome
CC {ECO:0000269|PubMed:19683497}. Note=Associates with the coding region
CC of HTA1. {ECO:0000269|PubMed:19683497}.
CC -!- DOMAIN: The C-terminal repeats are critical for activity.
CC -!- MISCELLANEOUS: It is phosphorylated in a PKA-dependent manner in vitro.
CC -!- MISCELLANEOUS: Present with 2340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be involved in the transcription
CC initiation step. {ECO:0000305}.
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DR EMBL; M62882; AAA35085.1; -; Genomic_DNA.
DR EMBL; Z49810; CAA89942.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09888.1; -; Genomic_DNA.
DR PIR; A40253; A40253.
DR RefSeq; NP_013703.1; NM_001182366.1.
DR PDB; 2EXU; X-ray; 2.23 A; A=285-375.
DR PDB; 4YTK; X-ray; 1.09 A; A=382-511.
DR PDB; 4YTL; X-ray; 1.60 A; A/B=534-632.
DR PDB; 7NKX; EM; 2.90 A; Z=1-1063.
DR PDB; 7NKY; EM; 3.20 A; Z=1-1063.
DR PDBsum; 2EXU; -.
DR PDBsum; 4YTK; -.
DR PDBsum; 4YTL; -.
DR PDBsum; 7NKX; -.
DR PDBsum; 7NKY; -.
DR AlphaFoldDB; P27692; -.
DR SMR; P27692; -.
DR BioGRID; 35159; 211.
DR ComplexPortal; CPX-1661; SPT4-SPT5 transcription elongation factor complex.
DR DIP; DIP-6621N; -.
DR IntAct; P27692; 94.
DR MINT; P27692; -.
DR STRING; 4932.YML010W; -.
DR iPTMnet; P27692; -.
DR MaxQB; P27692; -.
DR PaxDb; P27692; -.
DR PRIDE; P27692; -.
DR EnsemblFungi; YML010W_mRNA; YML010W; YML010W.
DR GeneID; 854999; -.
DR KEGG; sce:YML010W; -.
DR SGD; S000004470; SPT5.
DR VEuPathDB; FungiDB:YML010W; -.
DR eggNOG; KOG1999; Eukaryota.
DR GeneTree; ENSGT00440000037640; -.
DR HOGENOM; CLU_003537_1_0_1; -.
DR InParanoid; P27692; -.
DR OMA; VGYMNTP; -.
DR BioCyc; YEAST:G3O-32614-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR EvolutionaryTrace; P27692; -.
DR PRO; PR:P27692; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P27692; protein.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032044; C:DSIF complex; IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0001042; F:RNA polymerase I core binding; IDA:SGD.
DR GO; GO:0001179; F:RNA polymerase I general transcription initiation factor binding; IDA:SGD.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IDA:SGD.
DR GO; GO:0070990; F:snRNP binding; IDA:SGD.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:SGD.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:SGD.
DR GO; GO:0030621; F:U4 snRNA binding; IDA:SGD.
DR GO; GO:0030623; F:U5 snRNA binding; IDA:SGD.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:SGD.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
DR GO; GO:2001208; P:negative regulation of transcription elongation by RNA polymerase I; IGI:SGD.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:SGD.
DR GO; GO:2001209; P:positive regulation of transcription elongation from RNA polymerase I promoter; IMP:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:2000232; P:regulation of rRNA processing; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0090262; P:regulation of transcription-coupled nucleotide-excision repair; IGI:SGD.
DR GO; GO:0000245; P:spliceosomal complex assembly; IDA:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06082; KOW_Spt5_2; 1.
DR CDD; cd06083; KOW_Spt5_3; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd06085; KOW_Spt5_5; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 3.30.70.940; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041975; KOW_Spt5_2.
DR InterPro; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 4.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Mitochondrion; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription.
FT CHAIN 1..1063
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000208477"
FT DOMAIN 382..415
FT /note="KOW 1"
FT DOMAIN 533..560
FT /note="KOW 2"
FT DOMAIN 584..615
FT /note="KOW 3"
FT DOMAIN 799..832
FT /note="KOW 4"
FT REPEAT 931..936
FT /note="1"
FT REPEAT 937..942
FT /note="2"
FT REPEAT 948..953
FT /note="3"
FT REPEAT 958..963
FT /note="4"
FT REPEAT 969..974
FT /note="5"
FT REPEAT 975..980
FT /note="6"
FT REPEAT 981..986
FT /note="7"
FT REPEAT 987..992
FT /note="8"
FT REPEAT 1000..1005
FT /note="9"
FT REPEAT 1009..1014
FT /note="10"
FT REPEAT 1015..1020
FT /note="11"
FT REPEAT 1032..1037
FT /note="12"
FT REPEAT 1043..1048
FT /note="13"
FT REPEAT 1052..1057
FT /note="14"
FT REPEAT 1058..1063
FT /note="15"
FT REGION 1..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1063
FT /note="15 X 6 AA tandem repeats of S-[TA]-W-G-G-[AQ]"
FT REGION 942..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 133
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 297..314
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:7NKY"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:7NKX"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:4YTK"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:4YTK"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:4YTK"
FT STRAND 409..416
FT /evidence="ECO:0007829|PDB:4YTK"
FT TURN 422..425
FT /evidence="ECO:0007829|PDB:4YTK"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:4YTK"
FT HELIX 453..460
FT /evidence="ECO:0007829|PDB:4YTK"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:4YTK"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:4YTK"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:4YTK"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:4YTK"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:4YTK"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:4YTK"
FT HELIX 502..507
FT /evidence="ECO:0007829|PDB:4YTK"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:4YTL"
FT TURN 546..549
FT /evidence="ECO:0007829|PDB:4YTL"
FT STRAND 551..566
FT /evidence="ECO:0007829|PDB:4YTL"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:4YTL"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:4YTL"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:4YTL"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:4YTL"
FT TURN 596..599
FT /evidence="ECO:0007829|PDB:4YTL"
FT STRAND 601..608
FT /evidence="ECO:0007829|PDB:4YTL"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:4YTL"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:4YTL"
FT STRAND 620..626
FT /evidence="ECO:0007829|PDB:4YTL"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:4YTL"
FT TURN 799..802
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 804..807
FT /evidence="ECO:0007829|PDB:7NKX"
FT TURN 811..814
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 816..822
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 827..835
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 842..844
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 845..848
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 850..853
FT /evidence="ECO:0007829|PDB:7NKX"
SQ SEQUENCE 1063 AA; 115650 MW; E4324DB6B1E4721A CRC64;
MSDNSDTNVS MQDHDQQFAD PVVVPQSTDT KDENTSDKDT VDSGNVTTTE STERAESTSN
IPPLDGEEKE AKSEPQQPED NAETAATEQV SSSNGPATDD AQATLNTDSS EANEIVKKEE
GSDERKRPRE EDTKNSDGDT KDEGDNKDED DDEDDDDDDD DEDDDDEAPT KRRRQERNRF
LDIEAEVSDD EDEDEDEEDS ELVREGFITH GDDEDDEASA PGARRDDRLH RQLDQDLNKT
SEEDAQRLAK ELRERYGRSS SKQYRAAAQD GYVPQRFLLP SVDTATIWGV RCRPGKEKEL
IRKLLKKKFN LDRAMGKKKL KILSIFQRDN YTGRIYIEAP KQSVIEKFCN GVPDIYISQK
LLIPVQELPL LLKPNKSDDV ALEEGSYVRI KRGIYKGDLA MVDQISENNL EVMLKIVPRL
DYGKFDEIDP TTQQRKSRRP TFAHRAPPQL FNPTMALRLD QANLYKRDDR HFTYKNEDYI
DGYLYKSFRI QHVETKNIQP TVEELARFGS KEGAVDLTSV SQSIKKAQAA KVTFQPGDRI
EVLNGEQRGS KGIVTRTTKD IATIKLNGFT TPLEFPISTL RKIFEPGDHV TVINGEHQGD
AGLVLMVEQG QVTFMSTQTS REVTITANNL SKSIDTTATS SEYALHDIVE LSAKNVACII
QAGHDIFKVI DETGKVSTIT KGSILSKINT ARARVSSVDA NGNEIKIGDT IVEKVGSRRE
GQVLYIQTQQ IFVVSKKIVE NAGVFVVNPS NVEAVASKDN MLSNKMDLSK MNPEIISKMG
PPSSKTFQQP IQSRGGREVA LGKTVRIRSA GYKGQLGIVK DVNGDKATVE LHSKNKHITI
DKHKLTYYNR EGGEGITYDE LVNRRGRVPQ ARMGPSYVSA PRNMATGGIA AGAAATSSGL
SGGMTPGWSS FDGGKTPAVN AHGGSGGGGV SSWGGASTWG GQGNGGASAW GGAGGGASAW
GGQGTGATST WGGASAWGNK SSWGGASTWA SGGESNGAMS TWGGTGDRSA YGGASTWGGN
NNNKSTRDGG ASAWGNQDDG NRSAWNNQGN KSNYGGNSTW GGH
