FCLN_PLAF7
ID FCLN_PLAF7 Reviewed; 1193 AA.
AC Q76NL8; Q9U7N7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Falcilysin {ECO:0000303|PubMed:10542284};
DE EC=3.4.24.- {ECO:0000269|PubMed:17074076};
GN Name=FLN {ECO:0000303|PubMed:17074076};
GN ORFNames=PF3D7_1360800 {ECO:0000312|EMBL:CAD52728.1};
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|EMBL:AAF06062.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|EMBL:AAF06062.1};
RX PubMed=10542284; DOI=10.1074/jbc.274.45.32411;
RA Eggleson K.K., Duffin K.L., Goldberg D.E.;
RT "Identification and characterization of falcilysin, a metallopeptidase
RT involved in hemoglobin catabolism within the malaria parasite Plasmodium
RT falciparum.";
RL J. Biol. Chem. 274:32411-32417(1999).
RN [2] {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 [3] {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 [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17074076; DOI=10.1111/j.1365-2958.2006.05443.x;
RA Ponpuak M., Klemba M., Park M., Gluzman I.Y., Lamppa G.K., Goldberg D.E.;
RT "A role for falcilysin in transit peptide degradation in the Plasmodium
RT falciparum apicoplast.";
RL Mol. Microbiol. 63:314-334(2007).
RN [5] {ECO:0007744|PDB:3S5H, ECO:0007744|PDB:3S5I, ECO:0007744|PDB:3S5K, ECO:0007744|PDB:3S5M}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ZINC.
RA Morgunova E., Ponpuak M., Istvan E., Popov A., Goldberg D., Eneqvist T.;
RT "Crystal structures of falcilysin, a M16 metalloprotease from the malaria
RT parasite Plasmodium falciparum.";
RL Submitted (MAY-2011) to the PDB data bank.
CC -!- FUNCTION: In the food vacuole, acts downstream of proteases plasmepsins
CC PMI and PMII and falcipains during the catabolism of host hemoglobin by
CC cleaving peptide fragments of alpha and beta hemoglobin subunits
CC generated by PMI and PMII and falcipains (PubMed:17074076). In the
CC apicoplast, degrades apicoplast transit peptides after their cleavage
CC (PubMed:17074076). Prefers bulky hydrophobic amino acids in the P1'
CC position at both acidic and neutral pH (By similarity). At P2', prefers
CC hydrophobic residues at acidic pH; at neutral pH, these same residues
CC are abundant but prefers Arg (By similarity). At P3', prefers
CC hydrophobic residues, especially Met, at both pH conditions. At P4' and
CC P5', prefers acidic residues at acidic pH, however, at neutral pH, the
CC enzyme is less selective at these positions (By similarity). The
CC optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH,
CC MKRHS-|-FRMRG (By similarity). {ECO:0000250|UniProtKB:A0A0L7KF24,
CC ECO:0000269|PubMed:17074076}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:A0A0L7KF24};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|Ref.5};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A0A0L7KF24}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17074076};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:A0A0L7KF24}.
CC Plastid, apicoplast {ECO:0000269|PubMed:17074076}. Vesicle
CC {ECO:0000250|UniProtKB:A0A0L7KF24}. Note=Localizes to the food (or
CC digestive) vacuole, an acidic vacuole where host hemoglobin is digested
CC (PubMed:17074076). During the trophozoite and early to mid-schizont
CC stages, localizes to the apicoplast (PubMed:17074076).
CC {ECO:0000269|PubMed:17074076}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage;
CC expression begins at the late ring, early trophozoite stage, increases
CC in the mid-trophozoite stage, and persists throughout the schizont
CC stage (at protein level). {ECO:0000269|PubMed:17074076}.
CC -!- PTM: Does not require processing for targeting to the food vacuole or
CC maturation. {ECO:0000250|UniProtKB:A0A0L7KF24}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; AF123458; AAF06062.1; -; Genomic_DNA.
DR EMBL; AL844509; CAD52728.1; -; Genomic_DNA.
DR RefSeq; XP_001350319.1; XM_001350283.1.
DR PDB; 3S5H; X-ray; 1.60 A; A=1-1193.
DR PDB; 3S5I; X-ray; 1.74 A; A=1-1193.
DR PDB; 3S5K; X-ray; 3.20 A; A=1-1193.
DR PDB; 3S5M; X-ray; 1.55 A; A=1-1193.
DR PDB; 7DI7; X-ray; 1.82 A; A=59-1193.
DR PDB; 7DIA; X-ray; 1.55 A; A=59-1193.
DR PDB; 7DIJ; X-ray; 1.90 A; A=59-1193.
DR PDBsum; 3S5H; -.
DR PDBsum; 3S5I; -.
DR PDBsum; 3S5K; -.
DR PDBsum; 3S5M; -.
DR PDBsum; 7DI7; -.
DR PDBsum; 7DIA; -.
DR PDBsum; 7DIJ; -.
DR AlphaFoldDB; Q76NL8; -.
DR SMR; Q76NL8; -.
DR IntAct; Q76NL8; 4.
DR STRING; 5833.PF13_0322; -.
DR BindingDB; Q76NL8; -.
DR ChEMBL; CHEMBL4295876; -.
DR MEROPS; M16.011; -.
DR SwissPalm; Q76NL8; -.
DR PRIDE; Q76NL8; -.
DR EnsemblProtists; CAD52728; CAD52728; PF3D7_1360800.
DR GeneID; 814283; -.
DR KEGG; pfa:PF3D7_1360800; -.
DR VEuPathDB; PlasmoDB:PF3D7_1360800; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000463200; -.
DR VEuPathDB; PlasmoDB:Pf7G8_130065300; -.
DR VEuPathDB; PlasmoDB:PfCD01_130066400; -.
DR VEuPathDB; PlasmoDB:PfDd2_130066600; -.
DR VEuPathDB; PlasmoDB:PfGA01_130066900; -.
DR VEuPathDB; PlasmoDB:PfGB4_130066700; -.
DR VEuPathDB; PlasmoDB:PfGN01_130067500; -.
DR VEuPathDB; PlasmoDB:PfHB3_130067200; -.
DR VEuPathDB; PlasmoDB:PfIT_130066100; -.
DR VEuPathDB; PlasmoDB:PfKE01_130066400; -.
DR VEuPathDB; PlasmoDB:PfKH01_130064800; -.
DR VEuPathDB; PlasmoDB:PfKH02_130063700; -.
DR VEuPathDB; PlasmoDB:PfML01_130064900; -.
DR VEuPathDB; PlasmoDB:PfNF135_130065000; -.
DR VEuPathDB; PlasmoDB:PfNF166_130065700; -.
DR VEuPathDB; PlasmoDB:PfNF54_130065400; -.
DR VEuPathDB; PlasmoDB:PfSD01_130067500; -.
DR VEuPathDB; PlasmoDB:PfSN01_130063800; -.
DR VEuPathDB; PlasmoDB:PfTG01_130066500; -.
DR HOGENOM; CLU_009165_1_0_1; -.
DR InParanoid; Q76NL8; -.
DR OMA; MTYPDKT; -.
DR PhylomeDB; Q76NL8; -.
DR BioCyc; MetaCyc:MON-15381; -.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0020011; C:apicoplast; IDA:GeneDB.
DR GO; GO:0020020; C:food vacuole; IDA:GeneDB.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042540; P:hemoglobin catabolic process; IDA:GeneDB.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
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; 2.
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; Apicoplast; Coiled coil; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Plastid; Protease; Reference proteome; Vacuole; Zinc.
FT CHAIN 1..1193
FT /note="Falcilysin"
FT /id="PRO_0000454646"
FT REGION 376..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 583..619
FT /evidence="ECO:0000255"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:3S5K,
FT ECO:0007744|PDB:3S5M"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:3S5K,
FT ECO:0007744|PDB:3S5M"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:3S5K,
FT ECO:0007744|PDB:3S5M"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:7DIA"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:3S5K"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 166..177
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 218..222
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:3S5I"
FT HELIX 410..424
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 457..465
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 478..496
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 500..517
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:3S5K"
FT HELIX 523..536
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 541..545
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 547..560
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 564..572
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 579..589
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 590..608
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 611..629
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 634..637
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 670..678
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 681..695
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 722..725
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 727..733
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 739..747
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 753..756
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 759..765
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 766..768
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 771..774
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 776..786
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 788..797
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 802..804
FT /evidence="ECO:0007829|PDB:3S5K"
FT STRAND 812..822
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 823..825
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 826..838
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 845..865
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 867..874
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 875..879
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 881..890
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 892..907
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 909..923
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 929..935
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 937..940
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 941..944
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 945..947
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 948..960
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 961..964
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 970..972
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 980..986
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 996..1001
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 1005..1014
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1025..1035
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1037..1042
FT /evidence="ECO:0007829|PDB:3S5M"
FT TURN 1043..1046
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 1049..1055
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 1059..1069
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1072..1079
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1081..1091
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1094..1108
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1115..1126
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1131..1142
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1146..1158
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1160..1163
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 1166..1171
FT /evidence="ECO:0007829|PDB:3S5M"
FT HELIX 1173..1182
FT /evidence="ECO:0007829|PDB:3S5M"
FT STRAND 1188..1191
FT /evidence="ECO:0007829|PDB:3S5M"
SQ SEQUENCE 1193 AA; 138863 MW; DBA1FC548ED5056A CRC64;
MNLTKLMKVI GYINIITNCV QSFTNRADKK RYNVFAKSFI NTINTNLYTF KAVMSKTPEW
IHEKSPKHNS YDIIEKRYNE EFKMTYTVYQ HKKAKTQVIS LGTNDPLDVE QAFAFYVKTL
THSGKGIPHI LEHSVLSGSK NYNYKNSIGL LEKGTLHTHL NAYTFNDRTV YMAGSMNNKD
FFNIMGVYMD SVFQPNVLEN KYIFETEGWT YEVEKLKEDE KGKAEIPQMK DYKVSFNGIV
YNEMKGALSS PLEDLYHEEM KYMFPDNVHS NNSGGDPKEI TNLTYEEFKE FYYKNYNPKK
VKVFFFSKNN PTELLNFVDQ YLGQLDYSKY RDDAVESVEY QTYKKGPFYI KKKYGDHSEE
KENLVSVAWL LNPKVDKTNN HNNNHSNNQS SENNGYSNGS HSSDLSLENP TDYFVLLIIN
NLLIHTPESV LYKALTDCGL GNNVIDRGLN DSLVQYIFSI GLKGIKRNNE KIKNFDKVHY
EVEDVIMNAL KKVVKEGFNK SAVEASINNI EFILKEANLK TSKSIDFVFE MTSKLNYNRD
PLLIFEFEKY LNIVKNKIKN EPMYLEKFVE KHFINNAHRS VILLEGDENY AQEQENLEKQ
ELKKRIENFN EQEKEQVIKN FEELSKYKNA EESPEHLNKF PIISISDLNK KTLEVPVNVY
FTNINENNNI METYNKLKTN EHMLKDNMDV FLKKYVLKND KHNTNNNNNN NNNMDYSFTE
TKYEGNVPIL VYEMPTTGIV YLQFVFSLDH LTVDELAYLN LFKTLILENK TNKRSSEDFV
ILREKNIGSM SANVALYSKD DHLNVTDKYN AQALFNLEMH VLSHKCNDAL NIALEAVKES
DFSNKKKVID ILKRKINGMK TTFSEKGYAI LMKYVKAHLN SKHYAHNIIY GYENYLKLQE
QLELAENDFK TLENILVRIR NKIFNKKNLM VSVTSDYGAL KHLFVNSNES LKNLVSYFEE
NDKYINDMQN KVNDPTVMGW NEEIKSKKLF DEEKVKKEFF VLPTFVNSVS MSGILFKPGE
YLDPSFTVIV AALKNSYLWD TVRGLNGAYG VFADIEYDGS VVFLSARDPN LEKTLATFRE
SAKGLRKMAD TMTENDLLRY IINTIGTIDK PRRGIELSKL SFLRLISNES EQDRVEFRKR
IMNTKKEDFY KFADLLESKV NEFEKNIVII TTKEKANEYI ANVDGEFKKV LIE
