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 29-MAY-2024, entry version 127. 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] RP IDENTIFICATION IN THE HEMOZOIN FORMATION COMPLEX, SUBCELLULAR LOCATION, RP DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23471987; DOI=10.1073/pnas.1218412110; RA Chugh M., Sundararaman V., Kumar S., Reddy V.S., Siddiqui W.A., RA Stuart K.D., Malhotra P.; RT "Protein complex directs hemoglobin-to-hemozoin formation in Plasmodium RT falciparum."; RL Proc. Natl. Acad. Sci. U.S.A. 110:5392-5397(2013). RN [6] {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.6}; CC -!- SUBUNIT: Monomer (By similarity). Component of the hemozoin formation CC complex (HFC) composed of falcipains FP2A and/or FP2B, plasmepsins CC PMII, PMIII/HAP and PMIV, heme detoxifying protein HDP and falcilysin CC FLN (PubMed:23471987). The HFC complex is involved in hemoglobin CC degradation and detoxification of heme in the food vacuole during the CC asexual blood stage (PubMed:23471987). CC {ECO:0000250|UniProtKB:A0A0L7KF24, ECO:0000269|PubMed:23471987}. CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:17074076, CC ECO:0000269|PubMed:23471987}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:A0A0L7KF24}. Plastid, apicoplast CC {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, PubMed:23471987). During the trophozoite and early to CC mid-schizont stages, localizes to the apicoplast (PubMed:17074076). CC {ECO:0000269|PubMed:17074076, ECO:0000269|PubMed:23471987}. 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 ECO:0000269|PubMed:23471987}. 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}. 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; 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 PDB; 7VPE; X-ray; 1.62 A; A=59-1193. DR PDB; 8HO4; X-ray; 1.96 A; A=59-1193. DR PDB; 8HO5; X-ray; 2.00 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 PDBsum; 7VPE; -. DR PDBsum; 8HO4; -. DR PDBsum; 8HO5; -. DR AlphaFoldDB; Q76NL8; -. DR SMR; Q76NL8; -. DR IntAct; Q76NL8; 4. DR STRING; 36329.Q76NL8; -. DR BindingDB; Q76NL8; -. DR ChEMBL; CHEMBL4295876; -. DR MEROPS; M16.011; -. DR SwissPalm; Q76NL8; -. DR PaxDb; 5833-PF13_0322; -. 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; NYLYYIR; -. DR OrthoDB; 5477696at2759; -. DR PhylomeDB; Q76NL8; -. DR Proteomes; UP000001450; Chromosome 13. DR GO; GO:0020011; C:apicoplast; IDA:GeneDB. DR GO; GO:0009507; C:chloroplast; IEA:TreeGrafter. DR GO; GO:0020020; C:food vacuole; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; IEA:TreeGrafter. 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 Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4. 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 PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1. DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1. 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; LuxS/MPP-like metallohydrolase; 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.6, 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.6, 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.6, 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:7VPE" 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 //