PREP1_ARATH
ID PREP1_ARATH Reviewed; 1080 AA.
AC Q9LJL3; Q8RUN6;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Presequence protease 1, chloroplastic/mitochondrial;
DE Short=AtPreP1;
DE Short=PreP 1;
DE EC=3.4.24.-;
DE AltName: Full=Zinc metalloprotease 1;
DE Short=AtZnMP1;
DE Flags: Precursor;
GN Name=PREP1; Synonyms=ZNMP1; OrderedLocusNames=At3g19170;
GN ORFNames=MVI11.6, MVI11.7, MVI11_8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=12138166; DOI=10.1074/jbc.m205500200;
RA Staahl A., Moberg P., Ytterberg J., Panfilov O.,
RA Brockenhuus Von Lowenhielm H., Nilsson F., Glaser E.;
RT "Isolation and identification of a novel mitochondrial metalloprotease
RT (PreP) that degrades targeting presequences in plants.";
RL J. Biol. Chem. 277:41931-41939(2002).
RN [5]
RP CHARACTERIZATION, MUTAGENESIS OF HIS-162; GLU-165; HIS-166; GLU-240 AND
RP GLU-245, AND SUBCELLULAR LOCATION.
RX PubMed=14617063; DOI=10.1046/j.1365-313x.2003.01904.x;
RA Moberg P., Staahl A., Bhushan S., Wright S.J., Eriksson A., Bruce B.D.,
RA Glaser E.;
RT "Characterization of a novel zinc metalloprotease involved in degrading
RT targeting peptides in mitochondria and chloroplasts.";
RL Plant J. 36:616-628(2003).
RN [6]
RP CHARACTERIZATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15827031; DOI=10.1093/pcp/pci107;
RA Bhushan S., Staahl A., Nilsson S., Lefebvre B., Seki M., Roth C.,
RA McWilliam D., Wright S.J., Liberles D.A., Shinozaki K., Bruce B.D.,
RA Boutry M., Glaser E.;
RT "Catalysis, subcellular localization, expression and evolution of the
RT targeting peptides degrading protease, AtPreP2.";
RL Plant Cell Physiol. 46:985-996(2005).
RN [7]
RP CLEAVAGE SPECIFICITY.
RX PubMed=15893767; DOI=10.1016/j.jmb.2005.04.023;
RA Staahl A., Nilsson S., Lundberg P., Bhushan S., Biverstaahl H., Moberg P.,
RA Morisset M., Vener A., Maeler L., Langel U., Glaser E.;
RT "Two novel targeting peptide degrading proteases, PrePs, in mitochondria
RT and chloroplasts, so similar and still different.";
RL J. Mol. Biol. 349:847-860(2005).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-86, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-85, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 86-1080, AND MUTAGENESIS OF
RP GLU-179; ASN-194; LYS-256; GLU-262; LYS-264; ALA-416; GLU-430; ASN-700;
RP SER-767; GLN-895; ARG-933; GLY-937 AND TYR-939.
RX PubMed=16601675; DOI=10.1038/sj.emboj.7601080;
RA Johnson K.A., Bhushan S., Staahl A., Hallberg B.M., Frohn A., Glaser E.,
RA Eneqvist T.;
RT "The closed structure of presequence protease PreP forms a unique 10,000
RT Angstroms3 chamber for proteolysis.";
RL EMBO J. 25:1977-1986(2006).
CC -!- FUNCTION: ATP-independent protease that degrades both mitochondrial and
CC chloroplastic transit peptides after their cleavage. Also degrades
CC other unstructured peptides. Specific for peptides in the range of 10
CC to 65 residues. Shows a preference for cleavage after small polar
CC residues and before basic residues, with a bias for positively charged
CC amino acid residues. {ECO:0000269|PubMed:12138166}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 Magnesium ions per subunit.;
CC -!- ACTIVITY REGULATION: Inactive in the absence of MgCl(2) and CaCl(2) and
CC full activation at 10 mM concentrations of either ion. Completely
CC inhibited by the metal chelator orthophenanthroline, but not affected
CC by phenylmethylsulfonyl fluoride (PMSF) or N-ethylmaleimide (NEM).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active from pH 4 to 10.;
CC Temperature dependence:
CC Optimum temperature is 28 degrees Celsius. Active from 4 to 40
CC degrees Celsius.;
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q9LJL3; P17614: ATPB; Xeno; NbExp=6; IntAct=EBI-7143359, EBI-7143406;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Mitochondrion
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LJL3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed only in siliques and flowers.
CC {ECO:0000269|PubMed:15827031}.
CC -!- MISCELLANEOUS: The 2 enzymes halves enclose a large proteolytic chamber
CC spacious enough to hold peptide substrates, but sufficiently small to
CC exclude larger, folded proteins. Since the active site includes
CC residues from both the N- and C-terminal part of the protein,
CC proteolysis can occur only when the chamber is closed. Covalently
CC locking the 2 halves of the protease with disulfide bonds induces a
CC loss of activity.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02957.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP000419; BAB02957.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE76201.1; -; Genomic_DNA.
DR EMBL; AY090240; AAL90904.1; -; mRNA.
DR EMBL; AY091051; AAM13872.1; -; mRNA.
DR EMBL; BT006362; AAP21170.1; -; mRNA.
DR EMBL; BT002372; AAN86205.1; -; mRNA.
DR RefSeq; NP_188548.2; NM_112804.5. [Q9LJL3-1]
DR PDB; 2FGE; X-ray; 2.10 A; A/B=86-1080.
DR PDBsum; 2FGE; -.
DR AlphaFoldDB; Q9LJL3; -.
DR SMR; Q9LJL3; -.
DR BioGRID; 6784; 15.
DR IntAct; Q9LJL3; 4.
DR MINT; Q9LJL3; -.
DR STRING; 3702.AT3G19170.1; -.
DR MEROPS; M16.012; -.
DR iPTMnet; Q9LJL3; -.
DR MetOSite; Q9LJL3; -.
DR PaxDb; Q9LJL3; -.
DR PRIDE; Q9LJL3; -.
DR ProteomicsDB; 236596; -. [Q9LJL3-1]
DR EnsemblPlants; AT3G19170.1; AT3G19170.1; AT3G19170. [Q9LJL3-1]
DR GeneID; 821451; -.
DR Gramene; AT3G19170.1; AT3G19170.1; AT3G19170. [Q9LJL3-1]
DR KEGG; ath:AT3G19170; -.
DR Araport; AT3G19170; -.
DR TAIR; locus:2094138; AT3G19170.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_009165_1_0_1; -.
DR InParanoid; Q9LJL3; -.
DR PhylomeDB; Q9LJL3; -.
DR EvolutionaryTrace; Q9LJL3; -.
DR PRO; PR:Q9LJL3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJL3; baseline and differential.
DR Genevisible; Q9LJL3; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:TAIR.
DR GO; GO:0016485; P:protein processing; IDA:TAIR.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chloroplast; Coiled coil;
KW Hydrolase; Magnesium; Metal-binding; Metalloprotease; Mitochondrion;
KW Plastid; Protease; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..85
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 86..1080
FT /note="Presequence protease 1, chloroplastic/mitochondrial"
FT /id="PRO_0000249938"
FT COILED 571..612
FT /evidence="ECO:0000255"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:16601675"
FT ACT_SITE 240
FT /evidence="ECO:0000305"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16601675"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16601675"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16601675"
FT MOD_RES 86
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 162
FT /note="H->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14617063"
FT MUTAGEN 165
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14617063"
FT MUTAGEN 166
FT /note="H->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14617063"
FT MUTAGEN 179
FT /note="E->Q: Decreased activity toward some substrates."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 194
FT /note="N->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 240
FT /note="E->Q: Decreased activity toward some substrates."
FT /evidence="ECO:0000269|PubMed:14617063"
FT MUTAGEN 245
FT /note="E->Q: No loss of activity."
FT /evidence="ECO:0000269|PubMed:14617063"
FT MUTAGEN 256
FT /note="K->C: Inactive under oxidizing conditions and fully
FT active under reducing conditions; when associated with C-
FT 937."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 262
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 264
FT /note="K->C: Inactive under oxidizing conditions and fully
FT active under reducing conditions; when associated with C-
FT 895."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 416
FT /note="A->C: Little or no effect; when associated with C-
FT 700."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 430
FT /note="E->C: Inactive under oxidizing conditions and fully
FT active under reducing conditions; when associated with C-
FT 767."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 700
FT /note="N->C: Little or no effect; when associated with C-
FT 416."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 767
FT /note="S->C: Inactive under oxidizing conditions and fully
FT active under reducing conditions; when associated with C-
FT 430."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 895
FT /note="Q->C: Inactive under oxidizing conditions and fully
FT active under reducing conditions; when associated with C-
FT 264."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 933
FT /note="R->A,K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 937
FT /note="G->C: Inactive under oxidizing conditions and fully
FT active under reducing conditions; when associated with C-
FT 256."
FT /evidence="ECO:0000269|PubMed:16601675"
FT MUTAGEN 939
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16601675"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 211..226
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 320..328
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 330..341
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 398..412
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 445..453
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 458..475
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 479..495
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 503..515
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 528..541
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 543..554
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 561..569
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 572..589
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 593..610
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 640..653
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 657..667
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 673..675
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 679..688
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 696..706
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 707..719
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 722..736
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 740..753
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 759..779
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 781..791
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 795..804
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 806..821
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 823..837
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 844..849
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 851..866
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 888..891
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 895..904
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 905..908
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 915..925
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 927..931
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 932..936
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 939..946
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 947..950
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 951..960
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 963..970
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 972..977
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 983..997
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 1003..1015
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 1020..1031
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 1035..1051
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 1053..1058
FT /evidence="ECO:0007829|PDB:2FGE"
FT HELIX 1060..1069
FT /evidence="ECO:0007829|PDB:2FGE"
FT TURN 1070..1072
FT /evidence="ECO:0007829|PDB:2FGE"
FT STRAND 1074..1077
FT /evidence="ECO:0007829|PDB:2FGE"
SQ SEQUENCE 1080 AA; 121015 MW; 9FD259970195B9FC CRC64;
MLRTVSCLAS RSSSSLFFRF FRQFPRSYMS LTSSTAALRV PSRNLRRISS PSVAGRRLLL
RRGLRIPSAA VRSVNGQFSR LSVRAVATQP APLYPDVGQD EAEKLGFEKV SEEFISECKS
KAILFKHKKT GCEVMSVSNE DENKVFGVVF RTPPKDSTGI PHILEHSVLC GSRKYPVKEP
FVELLKGSLH TFLNAFTYPD RTCYPVASTN TKDFYNLVDV YLDAVFFPKC VDDAHTFQQE
GWHYELNDPS EDISYKGVVF NEMKGVYSQP DNILGRIAQQ ALSPENTYGV DSGGDPKDIP
NLTFEEFKEF HRQYYHPSNA RIWFYGDDDP VHRLRVLSEY LDMFEASPSP NSSKIKFQKL
FSEPVRLVEK YPAGRDGDLK KKHMLCVNWL LSEKPLDLQT QLALGFLDHL MLGTPASPLR
KILLESGLGE ALVSSGLSDE LLQPQFGIGL KGVSEENVQK VEELIMDTLK KLAEEGFDND
AVEASMNTIE FSLRENNTGS FPRGLSLMLQ SISKWIYDMD PFEPLKYTEP LKALKTRIAE
EGSKAVFSPL IEKLILNNSH RVTIEMQPDP EKATQEEVEE KNILEKVKAA MTEEDLAELA
RATEELKLKQ ETPDPPEALR CVPSLNLGDI PKEPTYVPTE VGDINGVKVL RHDLFTNDII
YTEVVFDIGS LKHELLPLVP LFCQSLLEMG TKDLTFVQLN QLIGRKTGGI SVYPLTSSVR
GKDEPCSKII VRGKSMAGRA DDLFNLMNCL LQEVQFTDQQ RFKQFVSQSR ARMENRLRGS
GHGIAAARMD AMLNIAGWMS EQMGGLSYLE FLHTLEKKVD EDWEGISSSL EEIRRSLLAR
NGCIVNMTAD GKSLTNVEKS VAKFLDLLPE NPSGGLVTWD GRLPLRNEAI VIPTQVNYVG
KAGNIYSTGY ELDGSAYVIS KHISNTWLWD RVRVSGGAYG GFCDFDSHSG VFSYLSYRDP
NLLKTLDIYD GTGDFLRGLD VDQETLTKAI IGTIGDVDSY QLPDAKGYSS LLRHLLGVTD
EERQRKREEI LTTSLKDFKD FAQAIDVVRD KGVAVAVASA EDIDAANNER SNFFEVKKAL
