UBA1_YEAST
ID UBA1_YEAST Reviewed; 1024 AA.
AC P22515; D6VWZ3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Ubiquitin-activating enzyme E1 1;
DE EC=6.2.1.45 {ECO:0000269|PubMed:18662542, ECO:0000269|PubMed:24816100};
GN Name=UBA1; OrderedLocusNames=YKL210W;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP PATHWAY.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1989885; DOI=10.1002/j.1460-2075.1991.tb07940.x;
RA McGrath J.P., Jentsch S., Varshavsky A.;
RT "UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme.";
RL EMBO J. 10:227-236(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 940-1024.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2569166; DOI=10.1038/340400a0;
RA McGrath J.P., Varshavsky A.;
RT "The yeast STE6 gene encodes a homologue of the mammalian multidrug
RT resistance P-glycoprotein.";
RL Nature 340:400-404(1989).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-914, 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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-595 AND LYS-608, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 10-1024 IN COMPLEX WITH
RP UBIQUITIN, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ILE-912;
RP SER-914; GLU-1004; ASP-1014 AND GLU-1016.
RX PubMed=18662542; DOI=10.1016/j.cell.2008.05.046;
RA Lee I., Schindelin H.;
RT "Structural insights into E1-catalyzed ubiquitin activation and transfer to
RT conjugating enzymes.";
RL Cell 134:268-278(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 9-1024 IN COMPLEX WITH
RP AMP-UBIQUITIN, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ACTIVE SITE, AND
RP SUBUNIT.
RX PubMed=24816100; DOI=10.1107/s1399004714002910;
RA Schafer A., Kuhn M., Schindelin H.;
RT "Structure of the ubiquitin-activating enzyme loaded with two ubiquitin
RT molecules.";
RL Acta Crystallogr. D 70:1311-1320(2014).
CC -!- FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark
CC cellular proteins for degradation through the ubiquitin-proteasome
CC system. Activates ubiquitin by first adenylating its C-terminal glycine
CC residue with ATP, and thereafter linking this residue to the side chain
CC of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free
CC AMP. {ECO:0000269|PubMed:18662542, ECO:0000269|PubMed:1989885,
CC ECO:0000269|PubMed:24816100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000269|PubMed:18662542,
CC ECO:0000269|PubMed:24816100};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:1989885, ECO:0000269|PubMed:24816100}.
CC -!- SUBUNIT: Monomer. Binds simultaneously two ubiquitin chains.
CC {ECO:0000269|PubMed:24816100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC allowing it to accommodate two ubiquitin moieties at a time, with a new
CC ubiquitin forming an adenylate intermediate as the previous one is
CC transferred to the thiol site. {ECO:0000305|PubMed:24816100}.
CC -!- MISCELLANEOUS: Present with 17700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; X55386; CAA39056.1; -; Genomic_DNA.
DR EMBL; Z28210; CAA82055.1; -; Genomic_DNA.
DR EMBL; X15428; CAA33468.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08959.1; -; Genomic_DNA.
DR PIR; S38048; S38048.
DR RefSeq; NP_012712.1; NM_001179775.1.
DR PDB; 3CMM; X-ray; 2.70 A; A/C=10-1024.
DR PDB; 4NNJ; X-ray; 2.40 A; A/C=9-1024.
DR PDB; 5L6H; X-ray; 2.30 A; A/C=1-1024.
DR PDB; 5L6I; X-ray; 2.76 A; A/C=1-1024.
DR PDB; 5L6J; X-ray; 2.68 A; A/C=1-1024.
DR PDB; 5TR4; X-ray; 2.20 A; A/C=9-1024.
DR PDB; 6NYA; X-ray; 2.06 A; A/D=11-1024.
DR PDB; 6ZHS; X-ray; 2.35 A; A=1-1024.
DR PDB; 6ZHT; X-ray; 2.30 A; C=25-1024.
DR PDB; 6ZHU; X-ray; 3.18 A; A/C/E/G=1-1024.
DR PDB; 6ZQH; X-ray; 2.03 A; A/C=1-1024.
DR PDB; 7K5J; X-ray; 3.42 A; A/C/D/G/I/K/S/U=11-1024.
DR PDBsum; 3CMM; -.
DR PDBsum; 4NNJ; -.
DR PDBsum; 5L6H; -.
DR PDBsum; 5L6I; -.
DR PDBsum; 5L6J; -.
DR PDBsum; 5TR4; -.
DR PDBsum; 6NYA; -.
DR PDBsum; 6ZHS; -.
DR PDBsum; 6ZHT; -.
DR PDBsum; 6ZHU; -.
DR PDBsum; 6ZQH; -.
DR PDBsum; 7K5J; -.
DR AlphaFoldDB; P22515; -.
DR SMR; P22515; -.
DR BioGRID; 33955; 154.
DR DIP; DIP-4853N; -.
DR IntAct; P22515; 29.
DR MINT; P22515; -.
DR STRING; 4932.YKL210W; -.
DR iPTMnet; P22515; -.
DR MaxQB; P22515; -.
DR PaxDb; P22515; -.
DR PRIDE; P22515; -.
DR EnsemblFungi; YKL210W_mRNA; YKL210W; YKL210W.
DR GeneID; 853670; -.
DR KEGG; sce:YKL210W; -.
DR SGD; S000001693; UBA1.
DR VEuPathDB; FungiDB:YKL210W; -.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000166138; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; P22515; -.
DR OMA; GANLHAF; -.
DR BioCyc; YEAST:G3O-31969-MON; -.
DR BRENDA; 6.2.1.45; 984.
DR Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P22515; -.
DR PRO; PR:P22515; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P22515; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.2660; -; 1.
DR Gene3D; 2.40.30.180; -; 1.
DR Gene3D; 3.10.290.60; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; SSF69572; 2.
DR TIGRFAMs; TIGR01408; Ube1; 1.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Ligase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1024
FT /note="Ubiquitin-activating enzyme E1 1"
FT /id="PRO_0000194977"
FT REPEAT 27..164
FT /note="1-1"
FT REPEAT 425..579
FT /note="1-2"
FT REGION 27..579
FT /note="2 approximate repeats"
FT ACT_SITE 600
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132,
FT ECO:0000269|PubMed:24816100"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24816100"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24816100"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24816100"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24816100"
FT BINDING 544..545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24816100"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 595
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 608
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 912
FT /note="I->P: Strongly reduces formation of the thioester
FT intermediate with ubiquitin; when associated with P-914."
FT /evidence="ECO:0000269|PubMed:18662542"
FT MUTAGEN 914
FT /note="S->P: Strongly reduces formation of the thioester
FT intermediate with ubiquitin; when associated with P-912."
FT /evidence="ECO:0000269|PubMed:18662542"
FT MUTAGEN 1004
FT /note="E->K: Strongly reduces formation of the thioester
FT intermediate with ubiquitin."
FT /evidence="ECO:0000269|PubMed:18662542"
FT MUTAGEN 1014
FT /note="D->K: Strongly reduces formation of the thioester
FT intermediate with ubiquitin; when associated with K-1016."
FT /evidence="ECO:0000269|PubMed:18662542"
FT MUTAGEN 1016
FT /note="E->K: Strongly reduces formation of the thioester
FT intermediate with ubiquitin; when associated with K-1014."
FT /evidence="ECO:0000269|PubMed:18662542"
FT CONFLICT 526
FT /note="E -> K (in Ref. 1; CAA39056)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="S -> N (in Ref. 1; CAA39056)"
FT /evidence="ECO:0000305"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:6ZHT"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:7K5J"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:6NYA"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:7K5J"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 288..305
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 316..332
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 334..337
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 360..379
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 418..424
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 426..433
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 444..456
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 494..505
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 546..559
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 572..578
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 599..603
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 609..624
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 626..636
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 640..646
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 651..663
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 669..684
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 686..694
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 725..742
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 755..763
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 781..784
FT /evidence="ECO:0007829|PDB:5L6H"
FT HELIX 796..804
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:7K5J"
FT HELIX 826..828
FT /evidence="ECO:0007829|PDB:6ZHS"
FT HELIX 830..844
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 852..859
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 867..885
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 891..893
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 896..900
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 901..904
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 905..910
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 916..919
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 922..925
FT /evidence="ECO:0007829|PDB:6ZQH"
FT TURN 926..928
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 930..936
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 939..949
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 953..959
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 962..966
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 971..977
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 982..990
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 1000..1008
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 1010..1015
FT /evidence="ECO:0007829|PDB:6ZHT"
FT STRAND 1019..1023
FT /evidence="ECO:0007829|PDB:6ZQH"
SQ SEQUENCE 1024 AA; 114266 MW; 8910804DF9156661 CRC64;
MSSNNSGLSA AGEIDESLYS RQLYVLGKEA MLKMQTSNVL ILGLKGLGVE IAKNVVLAGV
KSMTVFDPEP VQLADLSTQF FLTEKDIGQK RGDVTRAKLA ELNAYVPVNV LDSLDDVTQL
SQFQVVVATD TVSLEDKVKI NEFCHSSGIR FISSETRGLF GNTFVDLGDE FTVLDPTGEE
PRTGMVSDIE PDGTVTMLDD NRHGLEDGNF VRFSEVEGLD KLNDGTLFKV EVLGPFAFRI
GSVKEYGEYK KGGIFTEVKV PRKISFKSLK QQLSNPEFVF SDFAKFDRAA QLHLGFQALH
QFAVRHNGEL PRTMNDEDAN ELIKLVTDLS VQQPEVLGEG VDVNEDLIKE LSYQARGDIP
GVVAFFGGLV AQEVLKACSG KFTPLKQFMY FDSLESLPDP KNFPRNEKTT QPVNSRYDNQ
IAVFGLDFQK KIANSKVFLV GSGAIGCEML KNWALLGLGS GSDGYIVVTD NDSIEKSNLN
RQFLFRPKDV GKNKSEVAAE AVCAMNPDLK GKINAKIDKV GPETEEIFND SFWESLDFVT
NALDNVDART YVDRRCVFYR KPLLESGTLG TKGNTQVIIP RLTESYSSSR DPPEKSIPLC
TLRSFPNKID HTIAWAKSLF QGYFTDSAEN VNMYLTQPNF VEQTLKQSGD VKGVLESISD
SLSSKPHNFE DCIKWARLEF EKKFNHDIKQ LLFNFPKDAK TSNGEPFWSG AKRAPTPLEF
DIYNNDHFHF VVAGASLRAY NYGIKSDDSN SKPNVDEYKS VIDHMIIPEF TPNANLKIQV
NDDDPDPNAN AANGSDEIDQ LVSSLPDPST LAGFKLEPVD FEKDDDTNHH IEFITACSNC
RAQNYFIETA DRQKTKFIAG RIIPAIATTT SLVTGLVNLE LYKLIDNKTD IEQYKNGFVN
LALPFFGFSE PIASPKGEYN NKKYDKIWDR FDIKGDIKLS DLIEHFEKDE GLEITMLSYG
VSLLYASFFP PKKLKERLNL PITQLVKLVT KKDIPAHVST MILEICADDK EGEDVEVPFI
TIHL
