CTR9_YEAST
ID CTR9_YEAST Reviewed; 1077 AA.
AC P89105; D6W1S4; O14409; Q07332; Q08292;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=RNA polymerase-associated protein CTR9;
DE AltName: Full=Centromere-binding factor 1-dependent protein 1;
DE AltName: Full=Cln three-requiring protein 9;
GN Name=CTR9; Synonyms=CDP1; OrderedLocusNames=YOL145C;
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=ATCC 204508 / S288c;
RA Arndt K.T., Round E., Hoeppner D.;
RT "CTR9 is required for normal CLN1 and CLN2 G1 cyclin expression.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN CHROMOSOME SEGREGATION.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8978028; DOI=10.1093/genetics/144.4.1387;
RA Foreman P.K., Davis R.W.;
RT "CDP1, a novel Saccharomyces cerevisiae gene required for proper nuclear
RT division and chromosome segregation.";
RL Genetics 144:1387-1397(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553699; DOI=10.1002/yea.320111308;
RA Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J.,
RA Gancedo C., Arino J.;
RT "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast
RT chromosome XV containing seven new open reading frames.";
RL Yeast 11:1281-1288(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 197; 674; 768; 903; 907;
RP 956-959 AND 987.
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 FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10219085; DOI=10.1093/nar/27.10.2126;
RA Koch C., Wollmann P., Dahl M., Lottspeich F.;
RT "A role for Ctr9p and Paf1p in the regulation of G1 cyclin expression in
RT yeast.";
RL Nucleic Acids Res. 27:2126-2134(1999).
RN [7]
RP DNA-BINDING.
RX PubMed=11058104; DOI=10.1093/nar/28.21.4090;
RA Musso M., Bianchi-Scarra G., Van Dyke M.W.;
RT "The yeast CDP1 gene encodes a triple-helical DNA-binding protein.";
RL Nucleic Acids Res. 28:4090-4096(2000).
RN [8]
RP IDENTIFICATION IN THE PAF1 COMPLEX.
RX PubMed=11884586; DOI=10.1128/mcb.22.7.1971-1980.2002;
RA Mueller C.L., Jaehning J.A.;
RT "Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II
RT complex.";
RL Mol. Cell. Biol. 22:1971-1980(2002).
RN [9]
RP INTERACTION WITH POB3 AND SPT16.
RX PubMed=12242279; DOI=10.1128/mcb.22.20.6979-6992.2002;
RA Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A.,
RA Shilatifard A., Buratowski S., Greenblatt J.F.;
RT "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a
RT targeted proteomics approach.";
RL Mol. Cell. Biol. 22:6979-6992(2002).
RN [10]
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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15643076; DOI=10.1128/ec.4.1.209-220.2005;
RA Porter S.E., Penheiter K.L., Jaehning J.A.;
RT "Separation of the Saccharomyces cerevisiae Paf1 complex from RNA
RT polymerase II results in changes in its subnuclear localization.";
RL Eukaryot. Cell 4:209-220(2005).
RN [12]
RP INTERACTION WITH SPT6.
RX PubMed=15531585; DOI=10.1074/jbc.m411108200;
RA Kaplan C.D., Holland M.J., Winston F.;
RT "Interaction between transcription elongation factors and mRNA 3'-end
RT formation at the Saccharomyces cerevisiae GAL10-GAL7 locus.";
RL J. Biol. Chem. 280:913-922(2005).
RN [13]
RP FUNCTION.
RX PubMed=16246725; DOI=10.1016/j.molcel.2005.08.026;
RA Sheldon K.E., Mauger D.M., Arndt K.M.;
RT "A requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3'
RT end formation.";
RL Mol. Cell 20:225-236(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1015 AND SER-1017, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1015 AND SER-1017, AND
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1015 AND SER-1017, 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: The PAF1 complex is a multifunctional complex. Involved in
CC transcription initiation via genetic interactions with TATA-binding
CC proteins. Involved in elongation. It regulates 3'-end formation of
CC snR47 by modulating the recruitment or stable association of NRD1 and
CC NAB3 with RNA polymerase II. Also has a role in transcription-coupled
CC histone modification. Required for activation of RAD6 ubiquitin
CC conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126'
CC histone H2B. Activates the SET1 histone methyltransferase complex for
CC methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of
CC histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. In complex with
CC PAF1, required for normal CLN1 and CLN2 G1 cyclin expression in late
CC G1. Also has a role in chromosome segregation where it appears to be
CC involved in microtubule placement. {ECO:0000269|PubMed:10219085,
CC ECO:0000269|PubMed:15643076, ECO:0000269|PubMed:16246725,
CC ECO:0000269|PubMed:8978028}.
CC -!- SUBUNIT: Component of the PAF1 complex which consists of at least
CC CDC73, CTR9, LEO1, PAF1 and RTF1. Interacts with SPT6. Interacts with
CC FACT subunits POB3 and SPT16. {ECO:0000269|PubMed:10219085,
CC ECO:0000269|PubMed:11884586, ECO:0000269|PubMed:12242279,
CC ECO:0000269|PubMed:15531585}.
CC -!- INTERACTION:
CC P89105; P38439: LEO1; NbExp=5; IntAct=EBI-5283, EBI-10108;
CC P89105; P38351: PAF1; NbExp=5; IntAct=EBI-5283, EBI-12855;
CC P89105; P04050: RPO21; NbExp=4; IntAct=EBI-5283, EBI-15760;
CC P89105; P53064: RTF1; NbExp=8; IntAct=EBI-5283, EBI-16303;
CC P89105; Q00772: SLT2; NbExp=2; IntAct=EBI-5283, EBI-17372;
CC P89105; P27692: SPT5; NbExp=2; IntAct=EBI-5283, EBI-17937;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:10219085, ECO:0000269|PubMed:15643076}.
CC -!- MISCELLANEOUS: Present with 12900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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; U69264; AAB38704.1; -; Genomic_DNA.
DR EMBL; U31217; AAB81882.1; -; Genomic_DNA.
DR EMBL; Z48239; CAA88282.1; -; Genomic_DNA.
DR EMBL; Z74887; CAA99166.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10640.2; -; Genomic_DNA.
DR PIR; S66842; S66842.
DR RefSeq; NP_014496.2; NM_001183399.2.
DR PDB; 5ZYP; X-ray; 2.53 A; A=1-313.
DR PDB; 7DKH; X-ray; 2.90 A; A/E/I=1-972.
DR PDBsum; 5ZYP; -.
DR PDBsum; 7DKH; -.
DR AlphaFoldDB; P89105; -.
DR SMR; P89105; -.
DR BioGRID; 34272; 218.
DR ComplexPortal; CPX-1726; PAF1 complex.
DR DIP; DIP-2814N; -.
DR IntAct; P89105; 36.
DR MINT; P89105; -.
DR STRING; 4932.YOL145C; -.
DR CarbonylDB; P89105; -.
DR iPTMnet; P89105; -.
DR MaxQB; P89105; -.
DR PaxDb; P89105; -.
DR PRIDE; P89105; -.
DR EnsemblFungi; YOL145C_mRNA; YOL145C; YOL145C.
DR GeneID; 854020; -.
DR KEGG; sce:YOL145C; -.
DR SGD; S000005505; CTR9.
DR VEuPathDB; FungiDB:YOL145C; -.
DR eggNOG; KOG2002; Eukaryota.
DR GeneTree; ENSGT00390000005097; -.
DR HOGENOM; CLU_003008_0_1_1; -.
DR InParanoid; P89105; -.
DR OMA; MSNCIEI; -.
DR BioCyc; YEAST:G3O-33535-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:P89105; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P89105; protein.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IPI:SGD.
DR GO; GO:0000791; C:euchromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IDA:SGD.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IPI:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IPI:SGD.
DR GO; GO:0045142; F:triplex DNA binding; IDA:SGD.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:SGD.
DR GO; GO:0016571; P:histone methylation; IC:ComplexPortal.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:1901525; P:negative regulation of mitophagy; IMP:SGD.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; IMP:SGD.
DR GO; GO:2001165; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues; IMP:SGD.
DR GO; GO:2001209; P:positive regulation of transcription elongation from RNA polymerase I promoter; IDA:SGD.
DR GO; GO:2001173; P:regulation of histone H2B conserved C-terminal lysine ubiquitination; IDA:SGD.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IMP:SGD.
DR GO; GO:0060260; P:regulation of transcription initiation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0090262; P:regulation of transcription-coupled nucleotide-excision repair; IGI:SGD.
DR GO; GO:0031126; P:sno(s)RNA 3'-end processing; IMP:SGD.
DR GO; GO:0001015; P:snoRNA transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IGI:SGD.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR031101; Ctr9.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14027; PTHR14027; 1.
DR Pfam; PF13176; TPR_7; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1077
FT /note="RNA polymerase-associated protein CTR9"
FT /id="PRO_0000106280"
FT REPEAT 56..89
FT /note="TPR 1"
FT REPEAT 138..174
FT /note="TPR 2"
FT REPEAT 183..216
FT /note="TPR 3"
FT REPEAT 218..251
FT /note="TPR 4"
FT REPEAT 298..332
FT /note="TPR 5"
FT REPEAT 338..371
FT /note="TPR 6"
FT REPEAT 373..405
FT /note="TPR 7"
FT REPEAT 421..455
FT /note="TPR 8"
FT REPEAT 462..495
FT /note="TPR 9"
FT REPEAT 501..534
FT /note="TPR 10"
FT REPEAT 540..572
FT /note="TPR 11"
FT REPEAT 664..697
FT /note="TPR 12"
FT REPEAT 699..731
FT /note="TPR 13"
FT REPEAT 732..764
FT /note="TPR 14"
FT REPEAT 768..801
FT /note="TPR 15"
FT REPEAT 830..863
FT /note="TPR 16"
FT REGION 959..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1006
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 197
FT /note="K -> E (in Ref. 3; CAA88282 and 4; CAA99166)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="I -> V (in Ref. 2; AAB81882)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="E -> G (in Ref. 3; CAA88282 and 4; CAA99166)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="R -> T (in Ref. 3; CAA88282 and 4; CAA99166)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="E -> K (in Ref. 3; CAA88282 and 4; CAA99166)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="S -> R (in Ref. 3; CAA88282 and 4; CAA99166)"
FT /evidence="ECO:0000305"
FT CONFLICT 926..927
FT /note="GW -> ER (in Ref. 1; AAB38704 and 2; AAB81882)"
FT /evidence="ECO:0000305"
FT CONFLICT 956..959
FT /note="LIQE -> IFQV (in Ref. 3; CAA88282 and 4; CAA99166)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="K -> Q (in Ref. 3; CAA88282 and 4; CAA99166)"
FT /evidence="ECO:0000305"
FT CONFLICT 1045..1077
FT /note="DSDEEEAQMSGSEQNKNDDNDENNDNDDNDGLF -> R (in Ref. 3;
FT CAA88282)"
FT /evidence="ECO:0000305"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:5ZYP"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:5ZYP"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:5ZYP"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:5ZYP"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 113..133
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 154..174
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:5ZYP"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:5ZYP"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 334..350
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 354..367
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:7DKH"
FT TURN 400..404
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 406..425
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 431..454
FT /evidence="ECO:0007829|PDB:7DKH"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 462..474
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 478..494
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 501..514
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 517..529
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 537..549
FT /evidence="ECO:0007829|PDB:7DKH"
FT TURN 550..553
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 555..568
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 573..585
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 591..602
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 609..622
FT /evidence="ECO:0007829|PDB:7DKH"
FT STRAND 623..626
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 628..641
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 647..665
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 675..693
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 698..710
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 714..725
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 731..743
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 747..759
FT /evidence="ECO:0007829|PDB:7DKH"
FT TURN 764..766
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 767..783
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 788..808
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 812..834
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 838..840
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 843..864
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 876..884
FT /evidence="ECO:0007829|PDB:7DKH"
FT HELIX 887..919
FT /evidence="ECO:0007829|PDB:7DKH"
SQ SEQUENCE 1077 AA; 124709 MW; F794ECBAD26D4820 CRC64;
MTNAMKVEGY PSMEWPTSLD IPLKASEELV GIDLETDLPD DPTDLKTLLV EENSEKEHWL
TIALAYCNHG KTNEGIKLIE MALDVFQNSE RASLHTFLTW AHLNLAKGQS LSVETKEHEL
TQAELNLKDA IGFDPTWIGN MLATVELYYQ RGHYDKALET SDLFVKSIHA EDHRSGRQSK
PNCLFLLLRA KLLYQKKNYM ASLKIFQELL VINPVLQPDP RIGIGLCFWQ LKDSKMAIKS
WQRALQLNPK NTSASILVLL GEFRESFTNS TNDKTFKEAF TKALSDLNNI FSENQHNPVL
LTLLQTYYYF KGDYQTVLDI YHHRILKMSP MIAKIVLSES SFWCGRAHYA LGDYRKSFIM
FQESLKKNED NLLAKLGLGQ TQIKNNLLEE SIITFENLYK TNESLQELNY ILGMLYAGKA
FDAKTAKNTS AKEQSNLNEK ALKYLERYLK LTLATKNQLV ISRAYLVISQ LYELQNQYKT
SLDYLSKALE EMEFIKKEIP LEVLNNLACY HFINGDFIKA DDLFKQAKAK VSDKDESVNI
TLEYNIARTN EKNDCEKSES IYSQVTSLHP AYIAARIRNL YLKFAQSKIE DSDMSTEMNK
LLDLNKSDLE IRSFYGWYLK NSKERKNNEK STTHNKETLV KYNSHDAYAL ISLANLYVTI
ARDGKKSRNP KEQEKSKHSY LKAIQLYQKV LQVDPFNIFA AQGLAIIFAE SKRLGPALEI
LRKVRDSLDN EDVQLNLAHC YLEMREYGKA IENYELVLKK FDNEKTRPHI LNLLGRAWYA
RAIKERSVNF YQKALENAKT ALDLFVKESS KSKFIHSVKF NIALLHFQIA ETLRRSNPKF
RTVQQIKDSL EGLKEGLELF RELNDLKEFN MIPKEELEQR IQLGETTMKS ALERSLNEQE
EFEKEQSAKI DEARKILEEN ELKEQGWMKQ EEEARRLKLE KQAEEYRKLQ DEAQKLIQER
EAMAISEHNV KDDSDLSDKD NEYDEEKPRQ KRKRSTKTKN SGESKRRKAA KKTLSDSDED
DDDVVKKPSH NKGKKSQLSN EFIEDSDEEE AQMSGSEQNK NDDNDENNDN DDNDGLF
