GCYB_PLAF7
ID GCYB_PLAF7 Reviewed; 3179 AA.
AC Q8IDA0; Q9GVB8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Guanylate cyclase beta {ECO:0000305};
DE Short=PfGCbeta {ECO:0000303|PubMed:10747978};
DE EC=4.6.1.2 {ECO:0000269|PubMed:10747978, ECO:0000269|PubMed:11703675, ECO:0000305|PubMed:18452584};
DE AltName: Full=Guanylyl cyclase beta {ECO:0000303|PubMed:10747978};
GN Name=GCbeta {ECO:0000303|PubMed:10747978};
GN ORFNames=PF3D7_1360500 {ECO:0000312|EMBL:CAD52725.2};
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:CAC05389.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=10747978; DOI=10.1074/jbc.m001021200;
RA Carucci D.J., Witney A.A., Muhia D.K., Warhurst D.C., Schaap P., Meima M.,
RA Li J.L., Taylor M.C., Kelly J.M., Baker D.A.;
RT "Guanylyl cyclase activity associated with putative bifunctional integral
RT membrane proteins in Plasmodium falciparum.";
RL J. Biol. Chem. 275:22147-22156(2000).
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, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=11703675; DOI=10.1046/j.1365-2958.2001.02665.x;
RA Muhia D.K., Swales C.A., Deng W., Kelly J.M., Baker D.A.;
RT "The gametocyte-activating factor xanthurenic acid stimulates an increase
RT in membrane-associated guanylyl cyclase activity in the human malaria
RT parasite Plasmodium falciparum.";
RL Mol. Microbiol. 42:553-560(2001).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=18452584; DOI=10.1111/j.1365-2958.2008.06267.x;
RA Taylor C.J., McRobert L., Baker D.A.;
RT "Disruption of a Plasmodium falciparum cyclic nucleotide phosphodiesterase
RT gene causes aberrant gametogenesis.";
RL Mol. Microbiol. 69:110-118(2008).
CC -!- FUNCTION: Catalyzes the synthesis of the second messenger cGMP from GTP
CC (PubMed:10747978, PubMed:11703675, PubMed:18452584). Regulates cGMP
CC production in gametocytes; however, is dispensable for the initiation
CC of gametogenesis (PubMed:18452584). Does not have adenylate cyclase
CC activity (PubMed:10747978). {ECO:0000269|PubMed:10747978,
CC ECO:0000269|PubMed:11703675, ECO:0000269|PubMed:18452584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:10747978, ECO:0000269|PubMed:11703675,
CC ECO:0000305|PubMed:18452584};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:11703675};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:10747978, ECO:0000305|PubMed:11703675};
CC Note=Binds 2 magnesium ions per subunit (By similarity). Is also active
CC with manganese (in vitro) (Probable). {ECO:0000250|UniProtKB:P30803,
CC ECO:0000305|PubMed:10747978, ECO:0000305|PubMed:11703675};
CC -!- ACTIVITY REGULATION: Basal guanylate activity of the recombinant
CC guanylate cyclase domains 1 and 2 is not modulated by an increase in
CC Ca(2+) levels or by the gametogenesis inducer xanthurenic acid.
CC {ECO:0000269|PubMed:11703675}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: During the blood stage, specifically expressed in
CC gametocytes. {ECO:0000269|PubMed:10747978}.
CC -!- DOMAIN: The N-terminus contains a P-type ATPase-like domain which is
CC required for guanylate cyclase activity. {ECO:0000269|PubMed:18452584}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the cation transport
CC ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the adenylyl cyclase
CC class-4/guanylyl cyclase family. {ECO:0000305}.
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DR EMBL; AJ249165; CAC05389.1; -; Genomic_DNA.
DR EMBL; AL844509; CAD52725.2; -; Genomic_DNA.
DR RefSeq; XP_001350316.2; XM_001350280.2.
DR STRING; 5833.MAL13P1.301; -.
DR PRIDE; Q8IDA0; -.
DR EnsemblProtists; CAD52725; CAD52725; PF3D7_1360500.
DR GeneID; 813865; -.
DR KEGG; pfa:PF3D7_1360500; -.
DR VEuPathDB; PlasmoDB:PF3D7_1360500; -.
DR VEuPathDB; PlasmoDB:Pf7G8_130065100; -.
DR VEuPathDB; PlasmoDB:PfCD01_130066200; -.
DR VEuPathDB; PlasmoDB:PfDd2_130066400; -.
DR VEuPathDB; PlasmoDB:PfGA01_130066700; -.
DR VEuPathDB; PlasmoDB:PfGB4_130066500; -.
DR VEuPathDB; PlasmoDB:PfGN01_130067300; -.
DR VEuPathDB; PlasmoDB:PfHB3_130067000; -.
DR VEuPathDB; PlasmoDB:PfIT_130065900; -.
DR VEuPathDB; PlasmoDB:PfKE01_130066200; -.
DR VEuPathDB; PlasmoDB:PfKH01_130064600; -.
DR VEuPathDB; PlasmoDB:PfKH02_130063500; -.
DR VEuPathDB; PlasmoDB:PfML01_110043200; -.
DR VEuPathDB; PlasmoDB:PfSD01_130067300; -.
DR VEuPathDB; PlasmoDB:PfSN01_130063600; -.
DR VEuPathDB; PlasmoDB:PfTG01_130066300; -.
DR HOGENOM; CLU_225548_0_0_1; -.
DR InParanoid; Q8IDA0; -.
DR OMA; NNNKYHH; -.
DR PhylomeDB; Q8IDA0; -.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW cGMP biosynthesis; Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..3179
FT /note="Guanylate cyclase beta"
FT /id="PRO_0000452806"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..88
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..328
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..988
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1010..1020
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1042..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1091..1102
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1103..1123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1124..1127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1149..1168
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1169..1189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1190..1304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1305..1325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1326..1331
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1332..1352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1353..1360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1361..1381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1382..1401
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1402..1422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1423..1464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1465..1485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1486..1507
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1508..1528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1529..2739
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2740..2760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2761..2770
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2771..2791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2792..2809
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2810..2830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2831..2842
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2843..2863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2864..2870
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2871..2891
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2892..2895
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2896..2916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2917..3179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 1548..1700
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 2968..3102
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 2123..2153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2355..2379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2576..2656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2362..2376
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2587..2612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2615..2643
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2973
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 2973
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 2974
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 3017
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 3017
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 1383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 2045
FT /note="F -> C (in Ref. 1; CAC05389)"
FT /evidence="ECO:0000305"
FT CONFLICT 2059..2064
FT /note="KKIEKK -> NKI (in Ref. 1; CAC05389)"
FT /evidence="ECO:0000305"
FT CONFLICT 2072
FT /note="N -> Y (in Ref. 1; CAC05389)"
FT /evidence="ECO:0000305"
FT CONFLICT 2140
FT /note="K -> V (in Ref. 1; CAC05389)"
FT /evidence="ECO:0000305"
FT CONFLICT 2192
FT /note="F -> V (in Ref. 1; CAC05389)"
FT /evidence="ECO:0000305"
FT CONFLICT 2211
FT /note="K -> E (in Ref. 1; CAC05389)"
FT /evidence="ECO:0000305"
FT CONFLICT 3128..3179
FT /note="Missing (in Ref. 1; CAC05389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3179 AA; 376990 MW; D89AD593C4FBE547 CRC64;
MKTQTLSLMN INGKRKFLGT NNKIYRKVII NPTSEDDIQK FCRNYFRIYN FSLYNFIRRL
ISFDAILVYS LFLTVYIFSE INHGETKKYL FIDTAISLFF NIILLIVIES LFELKKLKDV
KNANSQYYLR IVPKMSYFEK VMTKDIKVGN IIRIFQGDEF PADVVILYVK NNANAIVDSF
KIDGLFRKSI KYAVDKYKID KDYLKMLSEI NGVIRCELPN KNIFCFQGNF KLDKHPRSLL
LNYENFALQS SVLKGAEYID AVVVYTGADT KKNLNIPQKI EENKTFCIKM NNIVYYLIFM
YFVFVVLSIV IKTIFFHKKN SFQNSRDSFL SMLEDFVGLY ILVLPIMMYS EKSLIYIIQS
LRIENDLRMR NTDSEKPKVF NKNKNDSLGN VDLLATSRNG VLVKRKELLV SCVINNVMYG
KKDIICSRTN FKLPTLNILD SERKNVSNLL NLDERIFKDP ENIFFPTRDF YSFLKLFENK
ISSIYNPYSS SLSNLLKEKY KNYVNEEILN KNVKLTSFVK SQLTIGYNQI CEDDELSYNC
YEIKEDSQKE NIQSVKIEDF ILGLCGCNRI IIYNEKSLDI SMNEYKSDNF METYSKFETE
NEEYHENDHD EYHNMEHSDD ENINSIEYED ICLYNIIRNT GFSIYCYKNT LFLYNLMKEC
KVYFLTCYHD FLRSNKFSMC ILKCGYSINN EKEGGILYVR GYDFNILPYI SKEKNNIKKI
KNVIKIYTLN YLKVIILCKK QISNEDIAKY IILKSISKKL SFKFYDLIKL FFLYDLEVIG
IIGLKNQLRE GVKETFNDVI NFDIKSWIFA NECSKDTYLT ALQCNLIVSS SNLFLINYYN
LKNTHEEGAN ILFHNFISSL YKLKSNSYAV VINDESIKNI MTNVESMKIF LCIAMRATVV
LFCKLQNETK GKIIRTLYAL TSPKLTVLGI GTTLNDAYLL KYSSISVFLS LNEHVNILYN
ISDYVLQEFK FISELLILGR LNRFSLCKVF LWIIYLKITV VSFYFFHNFD NYFSGSSASS
ILYTQTTFAL LHYFLIIAFS AYEIDLPYKF VRRLPYIYQL SRRKYFLNNN IILLTIIEAI
LISLTSYYIL RLNVFHLITH REFTFHIFIL NVFITTEKIL LLSKTWHIYF FIMAVLIIGI
LLIYVNIFTL VDCIKNGKCE FSLFQMENIY FWTSLFPILY INFIFDKLMK YIKNRIYPDI
SDYLRKYFLR RICCHNNDKF LSQRKIKGIN KFVNFEKNDI LLKYIPTPKI YKIKDDPTYY
NKSKRSKFLY DTFRKVIDIN VKYRNQQLNL EYKTYEKGNK LKLRIIVILL FLIYIIIFSS
QTIIDINTKS NIHYITMFYI IYFVLACVLL IYIRIRNKAT STFFFFLSRF LLICGFCIEL
YDNISNDILN VLITYSFTVS YIFFMSFKIL EALLVCISIL LLTFGVYYEK NKNMIDICTH
FCSNPYLSIN NLDHMNISCL CKKQIVIFLI SLLSFTLICL SMKYYEIFYL KKKFLFRYKQ
KVNLAKQIEI LHTMLPNFLV EYLLISDPKN DGIMVGKNIS GEDRGIISVI FCDIDDFQNM
VSTLQPHVLV ETLDNLYLYF DKCIKYFNCI KIETVFESYL AASGLSEKKN NALDKIMYDT
KCAIKLAIAQ LSAKYYISYK VLDTREHFSD NSTSYDKYIN KNISLKIGIH TGKAISGVIG
SVKPQYALFG DTVNTASRMK STSLPDHIHV SYDTYKYLKE DNTFIWKERK VFIKGKGKMK
TYLLVDILDD VKRKGESLNY YSSSNLLLSQ LGSEAVSIYE EREDIKEGSM DIIKESSRDI
IKEDSRDIIK EISTNISKSS SRNISKSSSR SISDIKEGQI IDKEDLIFKI NRMKNKIDSR
YSKRIDKESR DKISDKTNHV LDEVVKHSDI HLLNYEINNK RCKKMKGDTN NENKLIGDIF
NMYDKKIKYI YKKNYKSKSM ENISFIKHYR NTKYKKSDYL LLDNKGESKK FKRNTSYVLE
SPLHLIGDIV DNNIKRKKKK KEIKTIVSDD MFTSPVNIKE YNYNEQERKK EIVGNLSYDK
TKKIFPFIKF TKEGRIKKKK IEKKEKKEKK ENNNNFLYND DYSSYSSPKY GDNENNFVIK
YIRERKDFQK KFDHPNFNFS KFLHNYNPMK NKNKNKKNNK NVRRNEYPNY TSSSKDGVSY
NFLSDSLFSS DNEYSSDNEY SSDSEKYYKK RFKKNKKIIK FDDLFTKIYI KKKRLLQMNN
YDVKGKGKKL KNKGMERNKT KYKNVNEITK MKYFVNNENR DHEVNKEDIS KSMQKYFLHI
SKHKKEQIED KKKTHKYFHK NVECVYPYAG NNINHNFSRN EKRKYSINLY DHLDEQEKIK
GKKKYFNKDK ELIGSINKQT ERKPKKKNKK NIENKKDKKK IRMITNKTKE KHSNSIISVE
EQNMNHNNSL KKKEVNFTGK NEEYLNRANT NCSLGIKEME EDVYEFHSNN IYYNNQTSYS
DDINNTTKLK GMGNNTNDIS KNKGKNKLGK KISFFSMNNK YHESEIMNEE DNKNMLNLTQ
SQIINKDKYN YFTHCPSLKK KKSVFTKINN LFKNYFKSID VHEKFGFSKK FKFHSKDSDD
IKGNNNKISK NRYNNNNNNN NSNYSNIDSG KYSHNNKKNH HHNNNKYHHH NNNKYHHHNN
NKYHHQNNNY EKHHHSNNSR VMLSKGEKTE KNENVDYAYQ FDNYDKKLLK KLTSNLQLNK
KNVKNFNMFY YKFNDEELEE EYTRNYYREI INIDLTKKLI IIFIFTEIFL SLCNIIELSF
YEKKLRYNDS IVIIWLIRSI YLFIITYIWI ILKTKLKEYK NNSSKMMWTI FILNIFLCSW
GIILIDLSCI HYSMLLGNKN ERALFFMKDA SELIICIQLI FIKNMLFKHK FFFFVFFYIF
LIYSFSKLFS IHTCQTHICC SIILFISINI LYFWYSEYLD RIQFLVKRKR NRMEKISQDF
LTKILPRQVL EEYQNDNLQL TYKHEKIAFL FADIVGFTKW SKTVSPKEVL KLLQKLISKI
DKDTIKLGLY KLFTIGDAYV ATSQPNSSIT DESEALEGIL NILKLAKLIL HNINTIKIQF
NKHDFNMRIG LHYGSCVGGI IGSVRIRYDM WGLDVLIANK IESNGIPGEI ICSEQFRHFF
IQNEPQAKLN FWYYKSISIN DQDIKLYVIE DKNYEEDYDP KVIDYTTLLK LRQKKGLRS
