ATC3_YEAST
ID ATC3_YEAST Reviewed; 1355 AA.
AC P39524; D6VPJ2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Probable phospholipid-transporting ATPase DRS2;
DE EC=7.6.2.1;
GN Name=DRS2; OrderedLocusNames=YAL026C; ORFNames=FUN38;
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.
RX PubMed=8247005; DOI=10.1128/mcb.13.12.7901-7912.1993;
RA Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr.;
RT "DRS1 to DRS7, novel genes required for ribosome assembly and function in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:7901-7912(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 45-46; 450; 674; 891-892;
RP 953-954 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 [4]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12372257; DOI=10.1016/s0960-9822(02)01148-x;
RA Gall W.E., Geething N.C., Hua Z., Ingram M.F., Liu K., Chen S.I.,
RA Graham T.R.;
RT "Drs2p-dependent formation of exocytic clathrin-coated vesicles in vivo.";
RL Curr. Biol. 12:1623-1627(2002).
RN [5]
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 [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 INTERACTION WITH CDC50.
RX PubMed=15090616; DOI=10.1091/mbc.e03-11-0829;
RA Saito K., Fujimura-Kamada K., Furuta N., Kato U., Umeda M., Tanaka K.;
RT "Cdc50p, a protein required for polarized growth, associates with the Drs2p
RT P-type ATPase implicated in phospholipid translocation in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 15:3418-3432(2004).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP 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: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of phospholipids (Potential). Seems to
CC be involved in ribosome assembly. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBUNIT: Interacts with CDC50. {ECO:0000269|PubMed:15090616}.
CC -!- INTERACTION:
CC P39524; P25656: CDC50; NbExp=10; IntAct=EBI-3106, EBI-22014;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:12372257, ECO:0000269|PubMed:14562095}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12372257,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; L01795; AAA16891.1; -; Unassigned_RNA.
DR EMBL; U12980; AAC05006.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06962.2; -; Genomic_DNA.
DR PIR; S51995; S51995.
DR RefSeq; NP_009376.2; NM_001178171.2.
DR PDB; 6PSX; EM; 3.30 A; A=1-1355.
DR PDB; 6PSY; EM; 2.80 A; A=1-1355.
DR PDB; 6ROH; EM; 2.80 A; A=1-1355.
DR PDB; 6ROI; EM; 3.70 A; A=1-1355.
DR PDB; 6ROJ; EM; 2.90 A; A=1-1355.
DR PDB; 7OH4; EM; 3.00 A; A=1-1355.
DR PDB; 7OH5; EM; 2.90 A; A=1-1355.
DR PDB; 7OH6; EM; 3.00 A; A=1-1355.
DR PDB; 7OH7; EM; 3.80 A; A=1-1355.
DR PDBsum; 6PSX; -.
DR PDBsum; 6PSY; -.
DR PDBsum; 6ROH; -.
DR PDBsum; 6ROI; -.
DR PDBsum; 6ROJ; -.
DR PDBsum; 7OH4; -.
DR PDBsum; 7OH5; -.
DR PDBsum; 7OH6; -.
DR PDBsum; 7OH7; -.
DR AlphaFoldDB; P39524; -.
DR SMR; P39524; -.
DR BioGRID; 31740; 601.
DR ComplexPortal; CPX-1018; DRS2-CDC50 P4-ATPase complex.
DR DIP; DIP-2216N; -.
DR IntAct; P39524; 11.
DR MINT; P39524; -.
DR STRING; 4932.YAL026C; -.
DR TCDB; 3.A.3.8.2; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P39524; -.
DR MaxQB; P39524; -.
DR PaxDb; P39524; -.
DR PRIDE; P39524; -.
DR EnsemblFungi; YAL026C_mRNA; YAL026C; YAL026C.
DR GeneID; 851207; -.
DR KEGG; sce:YAL026C; -.
DR SGD; S000000024; DRS2.
DR VEuPathDB; FungiDB:YAL026C; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000168736; -.
DR HOGENOM; CLU_000846_3_0_1; -.
DR InParanoid; P39524; -.
DR OMA; QFWYSFQ; -.
DR BioCyc; YEAST:G3O-28837-MON; -.
DR BRENDA; 7.6.2.1; 984.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR PRO; PR:P39524; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39524; protein.
DR GO; GO:1990530; C:Cdc50p-Drs2p complex; IPI:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IGI:SGD.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IMP:SGD.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; IMP:SGD.
DR GO; GO:0032456; P:endocytic recycling; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IGI:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IGI:SGD.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Golgi apparatus; Magnesium; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1355
FT /note="Probable phospholipid-transporting ATPase DRS2"
FT /id="PRO_0000046233"
FT TOPO_DOM 1..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..246
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..490
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..1012
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1013..1033
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1034..1043
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1044..1064
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1065..1094
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1095..1115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1116..1131
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1132..1152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1153..1161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1162..1182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1183..1202
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1203..1223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1224..1355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 560
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 45..46
FT /note="AN -> GY (in Ref. 1; AAA16891 and 2; AAC05006)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="A -> R (in Ref. 1; AAA16891 and 2; AAC05006)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="P -> G (in Ref. 1; AAA16891 and 2; AAC05006)"
FT /evidence="ECO:0000305"
FT CONFLICT 891..892
FT /note="NT -> KS (in Ref. 1; AAA16891 and 2; AAC05006)"
FT /evidence="ECO:0000305"
FT CONFLICT 953..954
FT /note="GD -> AS (in Ref. 1; AAA16891 and 2; AAC05006)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="V -> L (in Ref. 1; AAA16891 and 2; AAC05006)"
FT /evidence="ECO:0000305"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:6ROH"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:6ROH"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:7OH5"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 249..280
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:7OH4"
FT STRAND 318..327
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 352..356
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 439..472
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:6ROH"
FT TURN 478..481
FT /evidence="ECO:0007829|PDB:6ROH"
FT HELIX 487..501
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 511..525
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:6ROJ"
FT TURN 534..537
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 562..565
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 571..579
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:6ROH"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:6ROH"
FT HELIX 601..611
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 612..615
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:6ROJ"
FT HELIX 620..632
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 637..640
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 653..663
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:7OH5"
FT STRAND 668..672
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 676..681
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 689..692
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 700..702
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 704..710
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 716..722
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 733..736
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 739..750
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 755..763
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 766..780
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:6ROH"
FT HELIX 786..796
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 800..810
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 817..825
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 826..828
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 830..834
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 839..848
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 868..880
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 881..883
FT /evidence="ECO:0007829|PDB:6ROH"
FT TURN 887..889
FT /evidence="ECO:0007829|PDB:6ROH"
FT HELIX 890..892
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 894..897
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 900..903
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 908..910
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 911..918
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 921..926
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 931..943
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 949..955
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 956..958
FT /evidence="ECO:0007829|PDB:6ROH"
FT HELIX 959..963
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 965..971
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 973..975
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 978..981
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 983..988
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 992..998
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 999..1001
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1002..1022
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1025..1028
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1030..1033
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1043..1049
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 1050..1053
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1056..1062
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1072..1075
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1077..1080
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1081..1084
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 1087..1089
FT /evidence="ECO:0007829|PDB:7OH5"
FT HELIX 1091..1115
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 1116..1119
FT /evidence="ECO:0007829|PDB:6ROJ"
FT STRAND 1124..1126
FT /evidence="ECO:0007829|PDB:6PSX"
FT HELIX 1131..1152
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 1155..1157
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1161..1164
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1166..1182
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 1183..1187
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1190..1192
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1195..1199
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1203..1229
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 1233..1235
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1236..1239
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1255..1261
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 1263..1266
FT /evidence="ECO:0007829|PDB:6PSY"
FT HELIX 1281..1283
FT /evidence="ECO:0007829|PDB:6PSY"
FT TURN 1286..1291
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 1294..1296
FT /evidence="ECO:0007829|PDB:6PSY"
FT STRAND 1300..1303
FT /evidence="ECO:0007829|PDB:6PSY"
SQ SEQUENCE 1355 AA; 153765 MW; 5745B92901F8E1AE CRC64;
MNDDRETPPK RKPGEDDTLF DIDFLDDTTS HSGSRSKVTN SHANANYIPP SHVLPEETID
LDADDDNIEN DVHENLFMSN NHDDQTSWNA NRFDSDAYQP QSLRAVKPPG LFARFGNGLK
NAFTFKRKKG PESFEMNHYN AVTNNELDDN YLDSRNKFNI KILFNRYILR KNVGDAEGNG
EPRVIHINDS LANSSFGYSD NHISTTKYNF ATFLPKFLFQ EFSKYANLFF LCTSAIQQVP
HVSPTNRYTT IGTLLVVLIV SAMKECIEDI KRANSDKELN NSTAEIFSEA HDDFVEKRWI
DIRVGDIIRV KSEEPIPADT IILSSSEPEG LCYIETANLD GETNLKIKQS RVETAKFIDV
KTLKNMNGKV VSEQPNSSLY TYEGTMTLND RQIPLSPDQM ILRGATLRNT AWIFGLVIFT
GHETKLLRNA TATPIKRTAV EKIINRQIIA LFTVLIVLIL ISSIGNVIMS TADAKHLSYL
YLEGTNKAGL FFKDFLTFWI LFSNLVPISL FVTVELIKYY QAFMIGSDLD LYYEKTDTPT
VVRTSSLVEE LGQIEYIFSD KTGTLTRNIM EFKSCSIAGH CYIDKIPEDK TATVEDGIEV
GYRKFDDLKK KLNDPSDEDS PIINDFLTLL ATCHTVIPEF QSDGSIKYQA ASPDEGALVQ
GGADLGYKFI IRKPNSVTVL LEETGEEKEY QLLNICEFNS TRKRMSAIFR FPDGSIKLFC
KGADTVILER LDDEANQYVE ATMRHLEDYA SEGLRTLCLA MRDISEGEYE EWNSIYNEAA
TTLDNRAEKL DEAANLIEKN LILIGATAIE DKLQDGVPET IHTLQEAGIK IWVLTGDRQE
TAINIGMSCR LLSEDMNLLI INEETRDDTE RNLLEKINAL NEHQLSTHDM NTLALVIDGK
SLGFALEPEL EDYLLTVAKL CKAVICCRVS PLQKALVVKM VKRKSSSLLL AIGDGANDVS
MIQAAHVGVG ISGMEGMQAA RSADIAVGQF KFLKKLLLVH GSWSYQRISV AILYSFYKNT
ALYMTQFWYV FANAFSGQSI MESWTMSFYN LFFTVWPPFV IGVFDQFVSS RLLERYPQLY
KLGQKGQFFS VYIFWGWIIN GFFHSAIVFI GTILIYRYGF ALNMHGELAD HWSWGVTVYT
TSVIIVLGKA ALVTNQWTKF TLIAIPGSLL FWLIFFPIYA SIFPHANISR EYYGVVKHTY
GSGVFWLTLI VLPIFALVRD FLWKYYKRMY EPETYHVIQE MQKYNISDSR PHVQQFQNAI
RKVRQVQRMK KQRGFAFSQA EEGGQEKIVR MYDTTQKRGK YGELQDASAN PFNDNNGLGS
NDFESAEPFI ENPFADGNQN SNRFSSSRDD ISFDI
