UBR1_YEAST
ID UBR1_YEAST Reviewed; 1950 AA.
AC P19812; D6VUW7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=E3 ubiquitin-protein ligase UBR1;
DE EC=2.3.2.27;
DE AltName: Full=N-end-recognizing protein;
DE AltName: Full=N-recognin-1;
DE AltName: Full=RING-type E3 ubiquitin transferase UBR1;
GN Name=UBR1; Synonyms=PTR1; OrderedLocusNames=YGR184C; ORFNames=G7168;
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=S288c / GRF88;
RX PubMed=2209542; DOI=10.1002/j.1460-2075.1990.tb07516.x;
RA Bartel B., Wuenning I., Varshavsky A.;
RT "The recognition component of the N-end rule pathway.";
RL EMBO J. 9:3179-3189(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9133739;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<357::aid-yea77>3.0.co;2-j;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M.,
RA Nombela C.;
RT "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:357-363(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP INTERACTION WITH UBC2, AND MUTAGENESIS OF LYS-1168; ARG-1169; LYS-1173;
RP CYS-1220; CYS-1223; CYS-1295; HIS-1297 AND CYS-1320.
RX PubMed=10581257; DOI=10.1093/emboj/18.23.6832;
RA Xie Y., Varshavsky A.;
RT "The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3
RT is required for the synthesis of multiubiquitin chain.";
RL EMBO J. 18:6832-6844(1999).
RN [6]
RP INTERACTION WITH RPN2; RPT1 AND RPT6.
RX PubMed=10688918; DOI=10.1073/pnas.060025497;
RA Xie Y., Varshavsky A.;
RT "Physical association of ubiquitin ligases and the 26S proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2497-2502(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-300, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-300 AND SER-1938,
RP AND 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with UBC2. Interacts with RPN2, RPT1 and RPT6 from
CC the 26S proteasome. {ECO:0000269|PubMed:10581257,
CC ECO:0000269|PubMed:10688918}.
CC -!- INTERACTION:
CC P19812; P21965: MCK1; NbExp=3; IntAct=EBI-19909, EBI-10517;
CC P19812; P26188: MGT1; NbExp=2; IntAct=EBI-19909, EBI-10873;
CC P19812; P06104: RAD6; NbExp=4; IntAct=EBI-19909, EBI-19722;
CC P19812; P32565: RPN2; NbExp=2; IntAct=EBI-19909, EBI-15919;
CC P19812; P33299: RPT1; NbExp=2; IntAct=EBI-19909, EBI-13910;
CC P19812; Q01939: RPT6; NbExp=4; IntAct=EBI-19909, EBI-13914;
CC P19812; P23291: YCK1; NbExp=2; IntAct=EBI-19909, EBI-4718;
CC -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His
CC ligand in place of the fourth Cys of the classical motif.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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DR EMBL; X53747; CAA37779.1; -; Genomic_DNA.
DR EMBL; X99074; CAA67528.1; -; Genomic_DNA.
DR EMBL; Z72969; CAA97210.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08278.1; -; Genomic_DNA.
DR PIR; S12332; S12332.
DR RefSeq; NP_011700.1; NM_001181313.1.
DR PDB; 3NIH; X-ray; 2.10 A; A=115-194.
DR PDB; 3NII; X-ray; 2.10 A; A=115-194.
DR PDB; 3NIJ; X-ray; 2.10 A; A=115-194.
DR PDB; 3NIK; X-ray; 1.85 A; A/B/D/F=115-194.
DR PDB; 3NIL; X-ray; 1.75 A; A/B/D/F=115-194.
DR PDB; 3NIM; X-ray; 2.00 A; A/B/D/F=115-194.
DR PDB; 3NIN; X-ray; 2.10 A; A/B=115-194.
DR PDB; 3NIS; X-ray; 1.68 A; A/B/D/F=115-194.
DR PDB; 3NIT; X-ray; 2.60 A; A=107-194.
DR PDB; 6KGI; X-ray; 1.04 A; B=113-194.
DR PDB; 7MEX; EM; 3.35 A; A=1-1950.
DR PDB; 7MEY; EM; 3.67 A; A=1-1950.
DR PDBsum; 3NIH; -.
DR PDBsum; 3NII; -.
DR PDBsum; 3NIJ; -.
DR PDBsum; 3NIK; -.
DR PDBsum; 3NIL; -.
DR PDBsum; 3NIM; -.
DR PDBsum; 3NIN; -.
DR PDBsum; 3NIS; -.
DR PDBsum; 3NIT; -.
DR PDBsum; 6KGI; -.
DR PDBsum; 7MEX; -.
DR PDBsum; 7MEY; -.
DR AlphaFoldDB; P19812; -.
DR SMR; P19812; -.
DR BioGRID; 33436; 247.
DR ComplexPortal; CPX-2918; UBR1-RAD6 ubiquitin ligase complex.
DR DIP; DIP-2517N; -.
DR IntAct; P19812; 18.
DR MINT; P19812; -.
DR STRING; 4932.YGR184C; -.
DR iPTMnet; P19812; -.
DR MaxQB; P19812; -.
DR PaxDb; P19812; -.
DR PRIDE; P19812; -.
DR EnsemblFungi; YGR184C_mRNA; YGR184C; YGR184C.
DR GeneID; 853096; -.
DR KEGG; sce:YGR184C; -.
DR SGD; S000003416; UBR1.
DR VEuPathDB; FungiDB:YGR184C; -.
DR eggNOG; KOG1140; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_238060_0_0_1; -.
DR InParanoid; P19812; -.
DR OMA; WANTISM; -.
DR BioCyc; YEAST:G3O-30874-MON; -.
DR BRENDA; 2.3.2.26; 984.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P19812; -.
DR PRO; PR:P19812; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P19812; protein.
DR GO; GO:0005737; C:cytoplasm; IMP:SGD.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IPI:SGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:1990303; C:UBR1-RAD6 ubiquitin ligase complex; IPI:SGD.
DR GO; GO:1904855; F:proteasome regulatory particle binding; IPI:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0090089; P:regulation of dipeptide transport; IMP:SGD.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IMP:SGD.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1950
FT /note="E3 ubiquitin-protein ligase UBR1"
FT /id="PRO_0000056135"
FT ZN_FING 121..194
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1220..1324
FT /note="RING-type; atypical"
FT REGION 1117..1219
FT /note="Interaction with UBC2"
FT /evidence="ECO:0000269|PubMed:10581257"
FT REGION 1826..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1935..1950
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1938
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 1168
FT /note="K->S: Impairs interaction with UBC2, but does not
FT affect degradation of N-end rule substrates."
FT /evidence="ECO:0000269|PubMed:10581257"
FT MUTAGEN 1169
FT /note="R->L: Impairs interaction with UBC2, but does not
FT affect degradation of N-end rule substrates."
FT /evidence="ECO:0000269|PubMed:10581257"
FT MUTAGEN 1173
FT /note="K->A: Impairs interaction with UBC2, but does not
FT affect degradation of N-end rule substrates."
FT /evidence="ECO:0000269|PubMed:10581257"
FT MUTAGEN 1220
FT /note="C->S: No effect on interaction with UBC2, but
FT inhibits degradation of N-end rule substrates."
FT /evidence="ECO:0000269|PubMed:10581257"
FT MUTAGEN 1223
FT /note="C->S: No effect on interaction with UBC2, but
FT inhibits degradation of N-end rule substrates."
FT /evidence="ECO:0000269|PubMed:10581257"
FT MUTAGEN 1295
FT /note="C->S: No effect on interaction with UBC2, but
FT inhibits degradation of N-end rule substrates."
FT /evidence="ECO:0000269|PubMed:10581257"
FT MUTAGEN 1297
FT /note="H->A: No effect on interaction with UBC2, but
FT inhibits degradation of N-end rule substrates."
FT /evidence="ECO:0000269|PubMed:10581257"
FT MUTAGEN 1320
FT /note="C->S: No effect on interaction with UBC2, but
FT inhibits degradation of N-end rule substrates."
FT /evidence="ECO:0000269|PubMed:10581257"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 34..56
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6KGI"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6KGI"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6KGI"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:6KGI"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:6KGI"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6KGI"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3NIS"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6KGI"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6KGI"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6KGI"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 217..239
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 338..342
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 351..360
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 383..402
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 408..423
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 427..431
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 436..442
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 502..508
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 515..531
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 536..545
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 547..555
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 566..572
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 577..584
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 588..600
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 624..641
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 652..663
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 664..667
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 686..709
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 716..731
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 761..772
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 775..780
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 789..806
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 807..812
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 815..824
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 832..845
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 851..861
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 865..868
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 874..876
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 883..899
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 910..926
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 933..939
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 942..944
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 948..958
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 959..962
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 966..968
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 972..975
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 978..982
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 988..990
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 996..1006
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1007..1010
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1011..1015
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1029..1035
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1036..1039
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1041..1057
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1063..1081
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1089..1092
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1095..1103
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1112..1128
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1130..1140
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1142..1152
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1164..1193
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1194..1196
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1221..1223
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1235..1240
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1252..1255
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1274..1283
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1290..1294
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1301..1310
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1317..1319
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1321..1323
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1345..1350
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1355..1358
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1359..1361
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1367..1383
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1385..1387
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1389..1393
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1394..1396
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1399..1401
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1402..1420
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1421..1423
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1427..1434
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1436..1455
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1478..1488
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1490..1492
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1494..1513
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1519..1521
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1522..1533
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1541..1550
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1562..1593
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1596..1599
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1609..1613
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1620..1629
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1630..1634
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1635..1640
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1649..1651
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1673..1676
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1677..1680
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1687..1689
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1694..1696
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1700..1703
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1704..1706
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1709..1711
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1716..1719
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1721..1724
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1725..1727
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1729..1736
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1737..1740
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1741..1746
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1747..1750
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1751..1756
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1758..1761
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1768..1771
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1772..1774
FT /evidence="ECO:0007829|PDB:7MEX"
FT STRAND 1777..1779
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1781..1792
FT /evidence="ECO:0007829|PDB:7MEX"
FT TURN 1793..1795
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1796..1804
FT /evidence="ECO:0007829|PDB:7MEX"
FT HELIX 1806..1811
FT /evidence="ECO:0007829|PDB:7MEX"
SQ SEQUENCE 1950 AA; 224838 MW; 33E4CD3A031AF523 CRC64;
MSVADDDLGS LQGHIRRTLR SIHNLPYFRY TRGPTERADM SRALKEFIYR YLYFVISNSG
ENLPTLFNAH PKQKLSNPEL TVFPDSLEDA VDIDKITSQQ TIPFYKIDES RIGDVHKHTG
RNCGRKFKIG EPLYRCHECG CDDTCVLCIH CFNPKDHVNH HVCTDICTEF TSGICDCGDE
EAWNSPLHCK AEEQENDISE DPATNADIKE EDVWNDSVNI ALVELVLAEV FDYFIDVFNQ
NIEPLPTIQK DITIKLREMT QQGKMYERAQ FLNDLKYEND YMFDGTTTAK TSPSNSPEAS
PSLAKIDPEN YTVIIYNDEY HNYSQATTAL RQGVPDNVHI DLLTSRIDGE GRAMLKCSQD
LSSVLGGFFA VQTNGLSATL TSWSEYLHQE TCKYIILWIT HCLNIPNSSF QTTFRNMMGK
TLCSEYLNAT ECRDMTPVVE KYFSNKFDKN DPYRYIDLSI LADGNQIPLG HHKILPESST
HSLSPLINDV ETPTSRTYSN TRLQHILYFD NRYWKRLRKD IQNVIIPTLA SSNLYKPIFC
QQVVEIFNHI TRSVAYMDRE PQLTAIRECV VQLFTCPTNA KNIFENQSFL DIVWSIIDIF
KEFCKVEGGV LIWQRVQKSN LTKSYSISFK QGLYTVETLL SKVHDPNIPL RPKEIISLLT
LCKLFNGAWK IKRKEGEHVL HEDQNFISYL EYTTSIYSII QTAEKVSEKS KDSIDSKLFL
NAIRIISSFL GNRSLTYKLI YDSHEVIKFS VSHERVAFMN PLQTMLSFLI EKVSLKDAYE
ALEDCSDFLK ISDFSLRSVV LCSQIDVGFW VRNGMSVLHQ ASYYKNNPEL GSYSRDIHLN
QLAILWERDD IPRIIYNILD RWELLDWFTG EVDYQHTVYE DKISFIIQQF IAFIYQILTE
RQYFKTFSSL KDRRMDQIKN SIIYNLYMKP LSYSKLLRSV PDYLTEDTTE FDEALEEVSV
FVEPKGLADN GVFKLKASLY AKVDPLKLLN LENEFESSAT IIKSHLAKDK DEIAKVVLIP
QVSIKQLDKD ALNLGAFTRN TVFAKVVYKL LQVCLDMEDS TFLNELLHLV HGIFRDDELI
NGKDSIPEAY LSKPICNLLL SIANAKSDVF SESIVRKADY LLEKMIMKKP NELFESLIAS
FGNQYVNDYK DKKLRQGVNL QETEKERKRR LAKKHQARLL AKFNNQQTKF MKEHESEFDE
QDNDVDMVGE KVYESEDFTC ALCQDSSSTD FFVIPAYHDH SPIFRPGNIF NPNEFMPMWD
GFYNDDEKQA YIDDDVLEAL KENGSCGSRK VFVSCNHHIH HNCFKRYVQK KRFSSNAFIC
PLCQTFSNCT LPLCQTSKAN TGLSLDMFLE SELSLDTLSR LFKPFTEENY RTINSIFSLM
ISQCQGFDKA VRKRANFSHK DVSLILSVHW ANTISMLEIA SRLEKPYSIS FFRSREQKYK
TLKNILVCIM LFTFVIGKPS MEFEPYPQQP DTVWNQNQLF QYIVRSALFS PVSLRQTVTE
ALTTFSRQFL RDFLQGLSDA EQVTKLYAKA SKIGDVLKVS EQMLFALRTI SDVRMEGLDS
ESIIYDLAYT FLLKSLLPTI RRCLVFIKVL HELVKDSENE TLVINGHEVE EELEFEDTAE
FVNKALKMIT EKESLVDLLT TQESIVSHPY LENIPYEYCG IIKLIDLSKY LNTYVTQSKE
IKLREERSQH MKNADNRLDF KICLTCGVKV HLRADRHEMT KHLNKNCFKP FGAFLMPNSS
EVCLHLTQPP SNIFISAPYL NSHGEVGRNA MRRGDLTTLN LKRYEHLNRL WINNEIPGYI
SRVMGDEFRV TILSNGFLFA FNREPRPRRI PPTDEDDEDM EEGEDGFFTE GNDEMDVDDE
TGQAANLFGV GAEGIAGGGV RDFFQFFENF RNTLQPQGNG DDDAPQNPPP ILQFLGPQFD
GATIIRNTNP RNLDEDDSDD NDDSDEREIW
