UFD2_YEAST
ID UFD2_YEAST Reviewed; 961 AA.
AC P54860; D6VRG3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=E4 ubiquitin-protein ligase UFD2;
DE EC=2.3.2.27 {ECO:0000269|PubMed:10089879};
DE AltName: Full=RING-type E3 ubiquitin transferase UFD2;
DE AltName: Full=Ubiquitin conjugation factor E4;
DE AltName: Full=Ubiquitin fusion degradation protein 2;
DE Short=UB fusion protein 2;
GN Name=UFD2; OrderedLocusNames=YDL190C; ORFNames=D1255;
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;
RX PubMed=7615550; DOI=10.1074/jbc.270.29.17442;
RA Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.;
RT "A proteolytic pathway that recognizes ubiquitin as a degradation signal.";
RL J. Biol. Chem. 270:17442-17456(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896272;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1065::aid-yea995>3.0.co;2-f;
RA Verhasselt P., Voet M., Mathys J., Volckaert G.;
RT "The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast
RT chromosome IV reveals the location of five known genes and characterizes at
RT least six new open reading frames including putative genes for ribosomal
RT protein L35 and a sugar transport protein.";
RL Yeast 12:1065-1070(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 102 AND 677.
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 FUNCTION, AND INTERACTION WITH CDC48.
RX PubMed=10089879; DOI=10.1016/s0092-8674(00)80574-7;
RA Koegl M., Hoppe T., Schlenker S., Ulrich H.D., Mayer T.U., Jentsch S.;
RT "A novel ubiquitination factor, E4, is involved in multiubiquitin chain
RT assembly.";
RL Cell 96:635-644(1999).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=15240124; DOI=10.1016/j.bbrc.2004.05.216;
RA Saeki Y., Tayama Y., Toh-e A., Yokosawa H.;
RT "Definitive evidence for Ufd2-catalyzed elongation of the ubiquitin chain
RT through Lys48 linkage.";
RL Biochem. Biophys. Res. Commun. 320:840-845(2004).
RN [9]
RP INTERACTION WITH RAD23.
RX PubMed=15121879; DOI=10.1091/mbc.e03-11-0835;
RA Kim I., Mi K., Rao H.;
RT "Multiple interactions of rad23 suggest a mechanism for ubiquitylated
RT substrate delivery important in proteolysis.";
RL Mol. Biol. Cell 15:3357-3365(2004).
RN [10]
RP FUNCTION IN ERAD, AND FUNCTION IN STP23 PROCESSING.
RX PubMed=15652483; DOI=10.1016/j.cell.2004.11.013;
RA Richly H., Rape M., Braun S., Rumpf S., Hoege C., Jentsch S.;
RT "A series of ubiquitin binding factors connects CDC48/p97 to substrate
RT multiubiquitylation and proteasomal targeting.";
RL Cell 120:73-84(2005).
RN [11]
RP INTERACTION WITH CDC48.
RX PubMed=16427015; DOI=10.1016/j.molcel.2005.12.014;
RA Rumpf S., Jentsch S.;
RT "Functional division of substrate processing cofactors of the ubiquitin-
RT selective Cdc48 chaperone.";
RL Mol. Cell 21:261-269(2006).
RN [12]
RP FUNCTION.
RX PubMed=18191224; DOI=10.1016/j.cell.2007.11.023;
RA Nakatsukasa K., Huyer G., Michaelis S., Brodsky J.L.;
RT "Dissecting the ER-associated degradation of a misfolded polytopic membrane
RT protein.";
RL Cell 132:101-112(2008).
RN [13]
RP FUNCTION, AND INTERACTION WITH PEX29.
RX PubMed=20159987; DOI=10.1074/jbc.m110.110551;
RA Liu C., van Dyk D., Xu P., Choe V., Pan H., Peng J., Andrews B., Rao H.;
RT "Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10
RT substrates.";
RL J. Biol. Chem. 285:10265-10272(2010).
RN [14]
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).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS), AND INTERACTION WITH UBC4.
RX PubMed=17890322; DOI=10.1073/pnas.0701369104;
RA Tu D., Li W., Ye Y., Brunger A.T.;
RT "Structure and function of the yeast U-box-containing ubiquitin ligase
RT Ufd2p.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15599-15606(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH DSK2 AND RAD23.
RX PubMed=20427284; DOI=10.1074/jbc.m110.112532;
RA Haenzelmann P., Stingele J., Hofmann K., Schindelin H., Raasi S.;
RT "The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like
RT domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding
RT domain.";
RL J. Biol. Chem. 285:20390-20398(2010).
CC -!- FUNCTION: E4 ubiquitin chain-elongation enzyme specifically involved in
CC polyubiquitin chain assembly. Binds to CDC48 and elongates mono- and
CC diubiquitinated ERAD substrates presented by the UFD1-NPL4-CDC48/p97
CC (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin
CC moieties. Delivers these polyubiquitinated substrates to RAD23 and
CC DSK2, which target them to the proteasome. Has E3 ubiquitin-protein
CC ligase activity, accepting ubiquitin from its cognate E2 ubiquitin-
CC conjugating enzyme UBC4. Enhances ubiquitination at 'Lys-48', but not
CC at 'Lys-29' of the Ub moiety. Promotes ubiquitin chain elongation at
CC 'Lys-48' on the DOA10 substrate PEX29. Also involved in the proteolytic
CC processing of the ER-bound transcription factor SPT23.
CC {ECO:0000269|PubMed:10089879, ECO:0000269|PubMed:15240124,
CC ECO:0000269|PubMed:15652483, ECO:0000269|PubMed:18191224,
CC ECO:0000269|PubMed:20159987}.
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; Evidence={ECO:0000269|PubMed:10089879};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:10089879}.
CC -!- SUBUNIT: Interacts with CDC48. Interacts with the ubiquitin-like domain
CC of RAD23 and DSK2. Interacts with PEX29. {ECO:0000269|PubMed:10089879,
CC ECO:0000269|PubMed:15121879, ECO:0000269|PubMed:16427015,
CC ECO:0000269|PubMed:17890322, ECO:0000269|PubMed:20159987,
CC ECO:0000269|PubMed:20427284}.
CC -!- INTERACTION:
CC P54860; P25694: CDC48; NbExp=6; IntAct=EBI-20003, EBI-4308;
CC P54860; P32628: RAD23; NbExp=7; IntAct=EBI-20003, EBI-14668;
CC P54860; P34223: SHP1; NbExp=3; IntAct=EBI-20003, EBI-17093;
CC P54860; P33202: UFD4; NbExp=2; IntAct=EBI-20003, EBI-20010;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000269|PubMed:17890322}.
CC -!- MISCELLANEOUS: Present with 2600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000305}.
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; U22154; AAC49024.1; -; Genomic_DNA.
DR EMBL; X83276; CAA58257.1; -; Genomic_DNA.
DR EMBL; Z74238; CAA98767.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11673.2; -; Genomic_DNA.
DR PIR; S58787; S58787.
DR RefSeq; NP_010091.2; NM_001180250.2.
DR PDB; 2QIZ; X-ray; 2.56 A; A=1-961.
DR PDB; 2QJ0; X-ray; 2.65 A; A=1-961.
DR PDB; 3M62; X-ray; 2.40 A; A=1-961.
DR PDB; 3M63; X-ray; 2.40 A; A=1-961.
DR PDBsum; 2QIZ; -.
DR PDBsum; 2QJ0; -.
DR PDBsum; 3M62; -.
DR PDBsum; 3M63; -.
DR AlphaFoldDB; P54860; -.
DR SMR; P54860; -.
DR BioGRID; 31855; 227.
DR ComplexPortal; CPX-1323; CDC48-RAD23-UFD2 complex.
DR DIP; DIP-5925N; -.
DR IntAct; P54860; 16.
DR MINT; P54860; -.
DR STRING; 4932.YDL190C; -.
DR iPTMnet; P54860; -.
DR MaxQB; P54860; -.
DR PaxDb; P54860; -.
DR PRIDE; P54860; -.
DR EnsemblFungi; YDL190C_mRNA; YDL190C; YDL190C.
DR GeneID; 851337; -.
DR KEGG; sce:YDL190C; -.
DR SGD; S000002349; UFD2.
DR VEuPathDB; FungiDB:YDL190C; -.
DR eggNOG; KOG2042; Eukaryota.
DR GeneTree; ENSGT00390000009300; -.
DR HOGENOM; CLU_003224_0_1_1; -.
DR InParanoid; P54860; -.
DR OMA; EHDTSTQ; -.
DR BioCyc; YEAST:G3O-29575-MON; -.
DR BRENDA; 2.3.2.B12; 984.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P54860; -.
DR PRO; PR:P54860; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P54860; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:SGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:SGD.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR045132; UBE4.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13931; PTHR13931; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR SMART; SM00504; Ubox; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..961
FT /note="E4 ubiquitin-protein ligase UFD2"
FT /id="PRO_0000194997"
FT DOMAIN 880..954
FT /note="U-box"
FT CONFLICT 102
FT /note="L -> S (in Ref. 2; CAA58257 and 3; CAA98767)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="V -> D (in Ref. 2; CAA58257 and 3; CAA98767)"
FT /evidence="ECO:0000305"
FT HELIX 1..8
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:3M63"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 56..75
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 84..101
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:3M62"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 243..274
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 276..291
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:3M62"
FT TURN 339..343
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 381..395
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 407..421
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 429..460
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 463..484
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:2QJ0"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:2QJ0"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:2QJ0"
FT HELIX 512..517
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 529..541
FT /evidence="ECO:0007829|PDB:3M62"
FT TURN 548..551
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 555..567
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 575..589
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 601..606
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 608..624
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 637..654
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 656..668
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 670..706
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 720..754
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 756..759
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 762..780
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 782..785
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 792..795
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 799..812
FT /evidence="ECO:0007829|PDB:3M62"
FT TURN 813..815
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 817..825
FT /evidence="ECO:0007829|PDB:3M62"
FT TURN 827..829
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 832..842
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 843..846
FT /evidence="ECO:0007829|PDB:2QJ0"
FT HELIX 851..878
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 883..885
FT /evidence="ECO:0007829|PDB:3M62"
FT TURN 888..890
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 895..899
FT /evidence="ECO:0007829|PDB:3M62"
FT TURN 901..903
FT /evidence="ECO:0007829|PDB:3M62"
FT STRAND 906..908
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 909..916
FT /evidence="ECO:0007829|PDB:3M62"
FT TURN 923..925
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 931..933
FT /evidence="ECO:0007829|PDB:3M62"
FT HELIX 938..952
FT /evidence="ECO:0007829|PDB:3M62"
SQ SEQUENCE 961 AA; 109916 MW; 877ACB59AC29634A CRC64;
MTAIEDILQI TTDPSDTRGY SLLKSEEVPQ GSTLGVDFID TLLLYQLTEN EKLDKPFEYL
NDCFRRNQQQ KRITKNKPNA ESLHSTFQEI DRLVIGYGVV ALQIENFCMN GAFINYITGI
VSNVNSYTDF LSQIIQRAIL EGTALDLLNA VFPTLLEYCN KHVSHFDLNE SVIYNNVLTI
FELFVTFKPI AEIFTKIDGF FADYSCKPQD FERKTILGPI LSLSPIEAAV AIRNYGDNLL
RSKQQTAMIH ESLQAEHKVV IDRLFFIVDK LVRGSLNSRT DMISYFAHIA NKNHLRRADH
PPFKELSSNG FMSNITLLLV RFSQPFLDIS YKKIDKIDAN YFNNPSLFID LSGETRLNSD
FKEADAFYDK NRKTADSKPN FISDCFFLTL TYLHYGLGGT LSFEEKMGSE IKALKEEIEK
VKKIAANHDV FARFITAQLS KMEKALKTTE SLRFALQGFF AHRSLQLEVF DFICGASTFL
IRVVDPEHEF PFKQIKLPLI PDQIGVENVD NADFLRAHAP VPFKYYPEFV VEGPVNYSLY
ISKYQTSPIF RNPRLGSFVE FTTMVLRCPE LVSNPHLKGK LVQLLSVGAM PLTDNSPGFM
MDIFEHDELV NKNLLYALLD FYVIVEKTGS SSQFYDKFNS RYSISIILEE LYYKIPSYKN
QLIWQSQNNA DFFVRFVARM LNDLTFLLDE GLSNLAEVHN IQNELDNRAR GAPPTREEED
KELQTRLASA SRQAKSSCGL ADKSMKLFEI YSKDIPAAFV TPEIVYRLAS MLNYNLESLV
GPKCGELKVK DPQSYSFNPK DLLKALTTVY INLSEQSEFI SAVAKDERSF NRNLFVRAVD
ILGRKTGLAS PEFIEKLLNF ANKAEEQRKA DEEEDLEYGD VPDEFLDPLM YTIMKDPVIL
PASKMNIDRS TIKAHLLSDS TDPFNRMPLK LEDVTPNEEL RQKILCFKKQ KKEEAKHKAS
E
