SUB1_PLAFA
ID SUB1_PLAFA Reviewed; 690 AA.
AC O61142; Q7KAN4; Q868D6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Subtilisin-like protease 1 {ECO:0000303|PubMed:9722575};
DE EC=3.4.21.62 {ECO:0000269|PubMed:10617661, ECO:0000269|PubMed:12764150, ECO:0000269|PubMed:24785947};
DE AltName: Full=PfSUB-1 {ECO:0000303|PubMed:9722575};
DE Flags: Precursor;
GN Name=SUB1 {ECO:0000250|UniProtKB:Q8I0V0};
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833 {ECO:0000312|EMBL:CAA05627.1};
RN [1] {ECO:0000312|EMBL:CAA05261.1, ECO:0000312|EMBL:CAA05627.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=T9/96 {ECO:0000312|EMBL:CAA05261.1};
RX PubMed=9722575; DOI=10.1074/jbc.273.36.23398;
RA Blackman M.J., Fujioka H., Stafford W.H., Sajid M., Clough B., Fleck S.L.,
RA Aikawa M., Grainger M., Hackett F.;
RT "A subtilisin-like protein in secretory organelles of Plasmodium falciparum
RT merozoites.";
RL J. Biol. Chem. 273:23398-23409(1998).
RN [2] {ECO:0000312|EMBL:CAC80338.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10611405; DOI=10.1093/protein/12.12.1113;
RA Withers-Martinez C., Carpenter E.P., Hackett F., Sajid M., Grainger M.,
RA Blackman M.J.;
RT "PCR-based gene synthesis as an efficient approach for expression of the
RT A+T-rich malaria genome.";
RL Protein Eng. 12:1113-1120(1999).
RN [3] {ECO:0000305}
RP CATALYTIC ACTIVITY, SUBUNIT, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE,
RP GLYCOSYLATION, AND MUTAGENESIS OF SER-608.
RX PubMed=10617661; DOI=10.1074/jbc.275.1.631;
RA Sajid M., Withers-Martinez C., Blackman M.J.;
RT "Maturation and specificity of Plasmodium falciparum subtilisin-like
RT protease-1, a malaria merozoite subtilisin-like serine protease.";
RL J. Biol. Chem. 275:631-641(2000).
RN [4] {ECO:0000305}
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=12764150; DOI=10.1074/jbc.m303827200;
RA Jean L., Hackett F., Martin S.R., Blackman M.J.;
RT "Functional characterization of the propeptide of Plasmodium falciparum
RT subtilisin-like protease-1.";
RL J. Biol. Chem. 278:28572-28579(2003).
RN [5] {ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 330-673 AND 127-219 IN COMPLEX
RP WITH CALCIUM, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, DISULFIDE BONDS, AND
RP MUTAGENESIS OF CYS-523; CYS-536 AND CYS-583.
RX PubMed=24785947; DOI=10.1038/ncomms4726;
RA Withers-Martinez C., Strath M., Hackett F., Haire L.F., Howell S.A.,
RA Walker P.A., Christodoulou E., Evangelos C., Dodson G.G., Blackman M.J.;
RT "The malaria parasite egress protease SUB1 is a calcium-dependent redox
RT switch subtilisin.";
RL Nat. Commun. 5:3726-3726(2014).
CC -!- FUNCTION: Serine protease which plays an essential role in merozoite
CC invasion of and egress from host erythrocytes by processing and
CC activating various merozoite surface and parasitophorous vacuole
CC proteins. Mediates the proteolytic maturation of serine proteases
CC SERA4, SERA5 and SERA6 just prior to merozoite egress. Prior to
CC merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and
CC MSP7, which form the MSP1/6/7 complex, and thereby may prime the
CC parasite cell surface for invasion of fresh erythrocytes. Prior to
CC merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and
CC RAP1 converting it to RAP1 p67 form. {ECO:0000250|UniProtKB:Q8I0V0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC Evidence={ECO:0000269|PubMed:10617661, ECO:0000269|PubMed:12764150,
CC ECO:0000269|PubMed:24785947};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:24785947};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:24785947};
CC -!- ACTIVITY REGULATION: p54 and probably p47 forms are inhibited by the
CC non-covalent interaction with the cleaved propeptide (PubMed:12764150).
CC Inhibited by subtilisin propeptide-like protein SUB1-ProM (By
CC similarity). {ECO:0000250|UniProtKB:Q8I0V0,
CC ECO:0000269|PubMed:12764150}.
CC -!- SUBUNIT: Heterodimer between p54 form and propeptide p31; the
CC interaction inhibits p54 catalytic activity.
CC {ECO:0000269|PubMed:10617661, ECO:0000269|PubMed:12764150,
CC ECO:0000269|PubMed:24785947}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9722575}.
CC Parasitophorous vacuole lumen {ECO:0000250|UniProtKB:Q8I0V0}. Note=At
CC the schizont stage, in merozoites, localizes to dense secretory
CC granules called exonemes (PubMed:9722575). Just prior to egress
CC secreted into the parasitophorous vacuole (By similarity).
CC {ECO:0000250|UniProtKB:Q8I0V0, ECO:0000269|PubMed:9722575}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC specifically in schizonts and merozoites (at protein level).
CC {ECO:0000269|PubMed:10617661, ECO:0000269|PubMed:9722575}.
CC -!- PTM: The propeptide (p31) is cleaved, probably by autocatalysis, during
CC the transport to or in the Golgi apparatus, and remains non-covalently
CC associated with the p54 form as an inhibitor (PubMed:9722575,
CC PubMed:10617661, PubMed:12764150). p54 is further cleaved into the p45
CC form (PubMed:9722575, PubMed:10617661). This cleavage is likely
CC occurring in the exoneme prior to egress and is mediated by
CC PMX/plasmepsin X (By similarity). {ECO:0000250|UniProtKB:W7K9M0,
CC ECO:0000269|PubMed:10617661, ECO:0000269|PubMed:12764150,
CC ECO:0000269|PubMed:9722575}.
CC -!- PTM: The disulfide bond between Cys-523 and Cys-536 acts as a redox-
CC sensitive disulfide switch (PubMed:24785947). The oxidized form is
CC required for catalytic activity (PubMed:24785947).
CC {ECO:0000269|PubMed:24785947}.
CC -!- PTM: The relevance of N-glycosylation is not clear. In an insect
CC expression system, SUB1 glycosylation appears to affect its processing
CC into the active mature form suggesting that SUB1 may not be N-
CC glycosylated in parasites. {ECO:0000269|PubMed:10617661}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000255|RuleBase:RU003355}.
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DR EMBL; AJ002594; CAA05627.1; -; mRNA.
DR EMBL; AJ002233; CAA05261.1; -; Genomic_DNA.
DR EMBL; AJ242589; CAC80338.1; -; Genomic_DNA.
DR PDB; 4LVN; X-ray; 2.25 A; A=330-673, P=127-219.
DR PDB; 4LVO; X-ray; 2.26 A; A=330-673, P=127-219.
DR PDBsum; 4LVN; -.
DR PDBsum; 4LVO; -.
DR AlphaFoldDB; O61142; -.
DR SMR; O61142; -.
DR BindingDB; O61142; -.
DR ChEMBL; CHEMBL2052035; -.
DR MEROPS; S08.012; -.
DR VEuPathDB; PlasmoDB:PF3D7_0507500; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000126800; -.
DR VEuPathDB; PlasmoDB:Pf7G8_050012800; -.
DR VEuPathDB; PlasmoDB:PfCD01_050014000; -.
DR VEuPathDB; PlasmoDB:PfDd2_050012500; -.
DR VEuPathDB; PlasmoDB:PfGA01_050012000; -.
DR VEuPathDB; PlasmoDB:PfGB4_050012800; -.
DR VEuPathDB; PlasmoDB:PfGN01_050012500; -.
DR VEuPathDB; PlasmoDB:PfHB3_050012500; -.
DR VEuPathDB; PlasmoDB:PfIT_050012700; -.
DR VEuPathDB; PlasmoDB:PfKE01_050012000; -.
DR VEuPathDB; PlasmoDB:PfKH01_050012900; -.
DR VEuPathDB; PlasmoDB:PfKH02_050013100; -.
DR VEuPathDB; PlasmoDB:PfML01_050012400; -.
DR VEuPathDB; PlasmoDB:PfNF135_050013100; -.
DR VEuPathDB; PlasmoDB:PfNF166_050012700; -.
DR VEuPathDB; PlasmoDB:PfNF54_050011800; -.
DR VEuPathDB; PlasmoDB:PfSD01_050012500; -.
DR VEuPathDB; PlasmoDB:PfSN01_050012800; -.
DR VEuPathDB; PlasmoDB:PfTG01_050012500; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07473; Peptidases_S8_Subtilisin_like; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR017314; Pept_S8A_PfSUB_1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034204; PfSUB1-like_cat_dom.
DR InterPro; IPR041089; SUB1_ProdP9.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF18213; SUB1_ProdP9; 1.
DR PIRSF; PIRSF037900; Subtilisin_rel_PfSUB_1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW Metal-binding; Protease; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000305|PubMed:10617661"
FT PROPEP 26..219
FT /note="Inhibition peptide"
FT /evidence="ECO:0000269|PubMed:12764150,
FT ECO:0000305|PubMed:10617661"
FT /id="PRO_0000450201"
FT CHAIN 220..690
FT /note="Subtilisin-like protease 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004159015"
FT DOMAIN 345..663
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 99..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 430
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 608
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT BINDING 448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT SITE 219..220
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:10617661"
FT SITE 245..246
FT /note="Cleavage; by PMX"
FT /evidence="ECO:0000250|UniProtKB:Q8I0V0"
FT SITE 251..252
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:10617661"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 371..481
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT DISULFID 460..477
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT DISULFID 523..536
FT /evidence="ECO:0000269|PubMed:24785947,
FT ECO:0007744|PDB:4LVN, ECO:0007744|PDB:4LVO"
FT MUTAGEN 523
FT /note="C->A: Severely reduces catalytic activity without
FT affecting processing into mature form."
FT /evidence="ECO:0000269|PubMed:24785947"
FT MUTAGEN 536
FT /note="C->A: Severely reduces catalytic activity without
FT affecting processing into mature form."
FT /evidence="ECO:0000269|PubMed:24785947"
FT MUTAGEN 583
FT /note="C->A: No effect on catalytic activity and processing
FT into mature form."
FT /evidence="ECO:0000269|PubMed:24785947"
FT MUTAGEN 608
FT /note="S->A: Abolishes the autocatalytic processing of the
FT p54 form."
FT /evidence="ECO:0000269|PubMed:10617661"
FT CONFLICT 1
FT /note="Missing (in Ref. 1; CAA05261)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="H -> HHHHHH (in Ref. 2; CAC80338)"
FT /evidence="ECO:0000305"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:4LVO"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:4LVN"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:4LVN"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:4LVN"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 471..483
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 515..519
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 533..536
FT /evidence="ECO:0007829|PDB:4LVN"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 546..550
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 555..563
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:4LVN"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:4LVN"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 600..604
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 607..624
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 630..639
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:4LVN"
FT TURN 648..650
FT /evidence="ECO:0007829|PDB:4LVN"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:4LVN"
FT HELIX 659..668
FT /evidence="ECO:0007829|PDB:4LVN"
SQ SEQUENCE 690 AA; 77875 MW; 4E8CDCDE99F5AD71 CRC64;
MMLNKKVVAL CTLTLHLFCI FLCLGKEVRS EENGKIQDDA KKIVSELRFL EKVEDVIEKS
NIGGNEVDAD ENSFNPDTEV PIEEIEEIKM RELKDVKEEK NKNDNHNNNN NNNNISSSSS
SSSNTFGEEK EEVSKKKKKL RLIVSENHAT TPSFFQESLL EPDVLSFLES KGNLSNLKNI
NSMIIELKED TTDDELISYI KILEEKGALI ESDKLVSADN IDISGIKDAI RRGEENIDVN
DYKSMLEVEN DAEDYDKMFG MFNESHAATS KRKRHSTNER GYDTFSSPSY KTYSKSDYLY
DDDNNNNNYY YSHSSNGHNS SSRNSSSSRS RPGKYHFNDE FRNLQWGLDL SRLDETQELI
NEHQVMSTRI CVIDSGIDYN HPDLKDNIEL NLKELHGRKG FDDDNNGIVD DIYGANFVNN
SGNPMDDNYH GTHVSGIISA IGNNNIGVVG VDVNSKLIIC KALDEHKLGR LGDMFKCLDY
CISRNAHMIN GSFSFDEYSG IFNSSVEYLQ RKGILFFVSA SNCSHPKSST PDIRKCDLSI
NAKYPPILST VYDNVISVAN LKKNDNNNHY SLSINSFYSN KYCQLAAPGT NIYSTAPHNS
YRKLNGTSMA APHVAAIASL IFSINPDLSY KKVIQILKDS IVYLPSLKNM VAWAGYADIN
KAVNLAIKSK KTYINSNISN KWKKKSRYLH
