SUB1_PLAF7
ID SUB1_PLAF7 Reviewed; 688 AA.
AC Q8I0V0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Subtilisin-like protease 1 {ECO:0000303|PubMed:18083098};
DE EC=3.4.21.62 {ECO:0000269|PubMed:18083098, ECO:0000269|PubMed:19214190, ECO:0000269|PubMed:21220481, ECO:0000269|PubMed:31942933};
DE AltName: Full=PfSUB1 {ECO:0000303|PubMed:18083098};
DE Flags: Precursor;
GN Name=SUB1 {ECO:0000303|PubMed:18083098};
GN ORFNames=PF3D7_0507500 {ECO:0000312|EMBL:CAD51440.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-606.
RX PubMed=18083098; DOI=10.1016/j.cell.2007.10.049;
RA Yeoh S., O'Donnell R.A., Koussis K., Dluzewski A.R., Ansell K.H.,
RA Osborne S.A., Hackett F., Withers-Martinez C., Mitchell G.H.,
RA Bannister L.H., Bryans J.S., Kettleborough C.A., Blackman M.J.;
RT "Subcellular discharge of a serine protease mediates release of invasive
RT malaria parasites from host erythrocytes.";
RL Cell 131:1072-1083(2007).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=19214190; DOI=10.1038/emboj.2009.22;
RA Koussis K., Withers-Martinez C., Yeoh S., Child M., Hackett F.,
RA Knuepfer E., Juliano L., Woehlbier U., Bujard H., Blackman M.J.;
RT "A multifunctional serine protease primes the malaria parasite for red
RT blood cell invasion.";
RL EMBO J. 28:725-735(2009).
RN [5] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21220481; DOI=10.1128/iai.00902-10;
RA Silmon de Monerri N.C., Flynn H.R., Campos M.G., Hackett F., Koussis K.,
RA Withers-Martinez C., Skehel J.M., Blackman M.J.;
RT "Global identification of multiple substrates for Plasmodium falciparum
RT SUB1, an essential malarial processing protease.";
RL Infect. Immun. 79:1086-1097(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29459732; DOI=10.1038/s41564-018-0111-0;
RA Thomas J.A., Tan M.S.Y., Bisson C., Borg A., Umrekar T.R., Hackett F.,
RA Hale V.L., Vizcay-Barrena G., Fleck R.A., Snijders A.P., Saibil H.R.,
RA Blackman M.J.;
RT "A protease cascade regulates release of the human malaria parasite
RT Plasmodium falciparum from host red blood cells.";
RL Nat. Microbiol. 3:447-455(2018).
RN [7] {ECO:0000305}
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=31942933; DOI=10.1042/bcj20190918;
RA Tarr S.J., Withers-Martinez C., Flynn H.R., Snijders A.P., Masino L.,
RA Koussis K., Conway D.J., Blackman M.J.;
RT "A malaria parasite subtilisin propeptide-like protein is a potent
RT inhibitor of the egress protease SUB1.";
RL Biochem. J. 477:525-540(2020).
RN [8]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=32109369; DOI=10.1016/j.chom.2020.02.005;
RA Favuzza P., de Lera Ruiz M., Thompson J.K., Triglia T., Ngo A.,
RA Steel R.W.J., Vavrek M., Christensen J., Healer J., Boyce C., Guo Z.,
RA Hu M., Khan T., Murgolo N., Zhao L., Penington J.S., Reaksudsan K.,
RA Jarman K., Dietrich M.H., Richardson L., Guo K.Y., Lopaticki S., Tham W.H.,
RA Rottmann M., Papenfuss T., Robbins J.A., Boddey J.A., Sleebs B.E.,
RA Sabroux H.J., McCauley J.A., Olsen D.B., Cowman A.F.;
RT "Dual Plasmepsin-Targeting Antimalarial Agents Disrupt Multiple Stages of
RT the Malaria Parasite Life Cycle.";
RL Cell Host Microbe 27:642-658.e12(2020).
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 (PubMed:18083098, PubMed:19214190, PubMed:21220481,
CC PubMed:29459732). Mediates the proteolytic maturation of serine
CC proteases SERA4, SERA5 and SERA6 just prior to merozoite egress
CC (PubMed:18083098, PubMed:19214190, PubMed:29459732). Prior to merozoite
CC egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which
CC form the MSP1/6/7 complex, and thereby may prime the parasite cell
CC surface for invasion of fresh erythrocytes (PubMed:19214190,
CC PubMed:29459732). Prior to merozoite egress, cleaves MSRP2 converting
CC it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form
CC (PubMed:21220481). {ECO:0000269|PubMed:18083098,
CC ECO:0000269|PubMed:19214190, ECO:0000269|PubMed:21220481,
CC ECO:0000269|PubMed:29459732}.
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:18083098, ECO:0000269|PubMed:19214190,
CC ECO:0000269|PubMed:21220481, ECO:0000269|PubMed:31942933};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:O61142};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:O61142};
CC -!- ACTIVITY REGULATION: p54 and probably p47 forms are inhibited by the
CC non-covalent interaction with the cleaved propeptide (PubMed:19214190).
CC Inhibited by subtilisin propeptide-like protein SUB1-ProM
CC (PubMed:31942933). Inhibited by small molecule MRT12113
CC (PubMed:18083098). {ECO:0000269|PubMed:18083098,
CC ECO:0000269|PubMed:19214190, ECO:0000269|PubMed:31942933}.
CC -!- SUBUNIT: Heterodimer between p54 form and propeptide p31; the
CC interaction inhibits p54 catalytic activity.
CC {ECO:0000250|UniProtKB:O61142}.
CC -!- INTERACTION:
CC Q8I0V0; O96164: PF3D7_0207700; NbExp=2; IntAct=EBI-1568896, EBI-824760;
CC Q8I0V0; Q9TY95: SERA5; NbExp=3; IntAct=EBI-1568896, EBI-826913;
CC Q8I0V0; Q9TY96: SERA6; NbExp=2; IntAct=EBI-1568896, EBI-827996;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18083098}.
CC Parasitophorous vacuole lumen {ECO:0000269|PubMed:18083098}. Note=At
CC the schizont stage, in merozoites, localizes to dense secretory
CC granules called exonemes (PubMed:18083098). Just prior to egress
CC secreted into the parasitophorous vacuole (PubMed:18083098).
CC {ECO:0000269|PubMed:18083098}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC specifically in schizonts (at protein level).
CC {ECO:0000269|PubMed:18083098}.
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. p54 is further cleaved
CC into the p45 form (By similarity). This cleavage is likely occurring in
CC the exoneme prior to egress and is mediated by PMX/plasmepsin X
CC (PubMed:32109369). {ECO:0000250|UniProtKB:O61142,
CC ECO:0000269|PubMed:32109369}.
CC -!- PTM: The disulfide bond between Cys-521 and Cys-534 acts as a redox-
CC sensitive disulfide switch. The oxidized form is required for catalytic
CC activity. {ECO:0000250|UniProtKB:O61142}.
CC -!- PTM: The relevance of the 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:0000250|UniProtKB:O61142}.
CC -!- DISRUPTION PHENOTYPE: Blood stage parasites are not viable
CC (PubMed:18083098, PubMed:29459732). Initial schizont development is
CC normal but merozoite egress is abolished due to a failure to rupture
CC the parasitophorous vacuole membrane (PubMed:29459732).
CC {ECO:0000269|PubMed:18083098, ECO:0000269|PubMed:29459732}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000255|RuleBase:RU003355}.
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DR EMBL; AL844504; CAD51440.1; -; Genomic_DNA.
DR RefSeq; XP_001351633.1; XM_001351597.1.
DR AlphaFoldDB; Q8I0V0; -.
DR SMR; Q8I0V0; -.
DR IntAct; Q8I0V0; 3.
DR STRING; 5833.PFE0370c; -.
DR GuidetoPHARMACOLOGY; 3184; -.
DR MEROPS; S08.012; -.
DR PRIDE; Q8I0V0; -.
DR EnsemblProtists; CAD51440; CAD51440; PF3D7_0507500.
DR GeneID; 812875; -.
DR KEGG; pfa:PF3D7_0507500; -.
DR VEuPathDB; PlasmoDB:PF3D7_0507500; -.
DR HOGENOM; CLU_455979_0_0_1; -.
DR InParanoid; Q8I0V0; -.
DR OMA; FKCIDYC; -.
DR PhylomeDB; Q8I0V0; -.
DR Proteomes; UP000001450; Chromosome 5.
DR GO; GO:0044311; C:exoneme; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020026; C:merozoite dense granule; IDA:GeneDB.
DR GO; GO:0020004; C:symbiont-containing vacuolar space; IDA:UniProtKB.
DR GO; GO:0020003; C:symbiont-containing vacuole; IDA:GeneDB.
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:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; TAS:GeneDB.
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 Calcium; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT PROPEP 26..217
FT /note="Inhibition peptide"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT /id="PRO_0000450200"
FT CHAIN 218..688
FT /note="Subtilisin-like protease 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004308256"
FT DOMAIN 343..661
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 99..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 428
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 606
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 396
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 402
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT SITE 217..218
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT SITE 243..244
FT /note="Cleavage; by PMX"
FT /evidence="ECO:0000269|PubMed:32109369"
FT SITE 249..250
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 369..479
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT DISULFID 458..475
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT DISULFID 521..534
FT /evidence="ECO:0000250|UniProtKB:O61142"
FT MUTAGEN 606
FT /note="S->A: Loss of catalytic activity. Blood stage
FT parasites are not viable."
FT /evidence="ECO:0000269|PubMed:18083098"
SQ SEQUENCE 688 AA; 77647 MW; FACFEFB495AEF4F7 CRC64;
MMLNKKVVAL CTLTLHLFCI FLCLGKEVRS EENGKIQDDA KKIVSELRFL EKVEDVIEKS
NIGGNEVDAD ENSFNPDTEV PIEEIEEIKM RELKDVKEEK NKNDNHNNNN NNISSSSSSS
SNTFGEEKEE VSKKKKKLRL IVSENHATTP SFFQESLLEP DVLSFLESKG NLSNLKNINS
MIIELKEDTT DDELISYIKI LEEKGALIES DKLVSADNID ISGIKDAIRR GEENIDVNDY
KSMLEVENDA EDYDKMFGMF NESHAATSKR KRHSTNERGY DTFSSPSYKT YSKSDYLYDD
DNNNNNYYYS HSSNGHNSSS RNSSSSRSRP GKYHFNDEFR NLQWGLDLSR LDETQELINE
HQVMSTRICV IDSGIDYNHP DLKDNIELNL KELHGRKGFD DDNNGIVDDI YGANFVNNSG
NPMDDNYHGT HVSGIISAIG NNNIGVVGVD VNSKLIICKA LDEHKLGRLG DMFKCLDYCI
SRNAHMINGS FSFDEYSGIF NSSVEYLQRK GILFFVSASN CSHPKSSTPD IRKCDLSINA
KYPPILSTVY DNVISVANLK KNDNNNHYSL SINSFYSNKY CQLAAPGTNI YSTAPHNSYR
KLNGTSMAAP HVAAIASLIF SINPDLSYKK VIQILKDSIV YLPSLKNMVA WAGYADINKA
VNLAIKSKKT YINSNISNKW KKKSRYLH
