DYHC2_PLAF7
ID DYHC2_PLAF7 Reviewed; 5251 AA.
AC Q8IID4; A0A143ZYP5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Dynein heavy chain-like protein 2 {ECO:0000303|PubMed:17653272};
GN ORFNames=PF11_0240, PF3D7_1122900;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
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:0000305}
RP SYNTHESIS OF 3515-3550, AND POSSIBLE CANDIDATE MALARIA EPITOPE.
RX PubMed=17653272; DOI=10.1371/journal.pone.0000645;
RA Villard V., Agak G.W., Frank G., Jafarshad A., Servis C., Nebie I.,
RA Sirima S.B., Felger I., Arevalo-Herrera M., Herrera S., Heitz F.,
RA Baecker V., Druilhe P., Kajava A.V., Corradin G.;
RT "Rapid identification of malaria vaccine candidates based on alpha-helical
RT coiled coil protein motif.";
RL PLoS ONE 2:E645-E645(2007).
CC -!- FUNCTION: Acts as a motor for the intracellular retrograde motility of
CC vesicles and organelles along microtubules. Dynein has ATPase activity;
CC the force-producing power stroke is thought to occur on release of ADP
CC (By similarity). {ECO:0000250|UniProtKB:Q14204}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains. {ECO:0000250|UniProtKB:Q14204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC (which binds cargo and interacts with other dynein components), and the
CC head or motor domain. The motor contains six tandemly-linked AAA
CC domains in the head, which form a ring. A stalk-like structure (formed
CC by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC and terminates in a microtubule-binding site. A seventh domain may also
CC contribute to this ring; it is not clear whether the N-terminus or the
CC C-terminus forms this extra domain. There are four well-conserved and
CC two non-conserved ATPase sites, one per AAA domain. Probably only one
CC of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC regulatory function. {ECO:0000250|UniProtKB:Q14204}.
CC -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC determined by epitope response in sera. {ECO:0000269|PubMed:17653272}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000255}.
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DR EMBL; LN999945; CZT98891.1; -; Genomic_DNA.
DR RefSeq; XP_001347911.1; XM_001347875.1.
DR SMR; Q8IID4; -.
DR STRING; 5833.PF11_0240; -.
DR PRIDE; Q8IID4; -.
DR EnsemblProtists; CZT98891; CZT98891; PF3D7_1122900.
DR GeneID; 810787; -.
DR KEGG; pfa:PF3D7_1122900; -.
DR VEuPathDB; PlasmoDB:PF3D7_1122900; -.
DR HOGENOM; CLU_000038_2_0_1; -.
DR InParanoid; Q8IID4; -.
DR OMA; ERRHVYT; -.
DR PhylomeDB; Q8IID4; -.
DR Proteomes; UP000001450; Chromosome 11.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; ISS:GeneDB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003774; F:cytoskeletal motor activity; ISS:GeneDB.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; ISS:UniProtKB.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; ISS:UniProtKB.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 3.20.180.20; -; 1.
DR Gene3D; 3.40.50.300; -; 5.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR042219; AAA_lid_11_sf.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR041589; DNAH3_AAA_lid_1.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR041228; Dynein_C.
DR InterPro; IPR043160; Dynein_C_barrel.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676; PTHR10676; 1.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF12777; MT; 1.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Kelch repeat;
KW Merozoite; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..5251
FT /note="Dynein heavy chain-like protein 2"
FT /id="PRO_0000370750"
FT REPEAT 37..87
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 95..143
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 266..317
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 318..367
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 372..421
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT REPEAT 1639..1685
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT REPEAT 2447..2494
FT /note="Kelch 7"
FT /evidence="ECO:0000255"
FT REGION 140..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2152..2171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3138..3163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3652..3686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4042..4250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4280..4299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4773..4824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4910..4948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1155..1225
FT /evidence="ECO:0000255"
FT COILED 1544..1610
FT /evidence="ECO:0000255"
FT COILED 2136..2188
FT /evidence="ECO:0000255"
FT COMPBIAS 140..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3138..3152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3652..3676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4042..4060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4061..4091
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4092..4250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4773..4800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1895..1902
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 2224..2231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 2546..2553
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 2890..2897
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 5251 AA; 617381 MW; 14C220359A132AD1 CRC64;
MTKFSEGHYD ILNLIEVKSN IQEKNILGYS IDYTVGGLFL FGGFKIDIEE NNGIICNDAY
LIHIKNDKAE YETLSIKIKP SIRCYHNSCT LLENYVIIFG GLNSEVPFVA LNDLWVFNSL
NKTFVEIKLK CKEKNKEKNL QNGINGTNEK GYISQTDDEN CSDNKYGENQ DYGSNDSDSK
DGEDIDKDDS ILDNSYVKNL RKYLKSNKSD ELHSSDIPCP RYFSSLDLYI IRKNNIEEEK
GFKKDEIKII KNNIIVSNSL NYEYFSLILF GGYGGYDRSS YNDLYEFNIL NNEWILRGCK
GNVPSTRYGH ISFIHGNNLF ILGGTNAEIS FNDMYSCDLK NNEWSEVDFS YSFNISKVFC
RSVLVESIDR NIIFIFGGYN IISDEKGNRK IEYNNIELNM LKLYDTFKLE ELKYNIIQNN
EENIIKNNNM EEINNMNSNN VKNEIISTKH DIYEDSNISN NITFCSITYD FMDSNLIITD
NKKKIYIMNI SNIIGPKYAI FNIWPKQCDI NGNKKLLFRG KGFTNEGKIL VKYKSDDINL
YSEGIYINEN NIYTIVPNAK NKIKNNICQV QLSINDKCYT TNSCFLEYYY NIDPKNTLIF
GSGLLEPVCL QKDNIFFLIA KNSLNEHKKI GGDKFQISII YEQKSEQYDI KYFVYDLNNG
FYIVKYFSFL NDKQMKVKMQ NVGKNNNIEQ RNNNNDNNDN NNNDNNNNNN NDNNNNNNNN
NNNNNNNNDN LNEQLNCNVV QRKNQNDLET LEGPQNISNK NSMNNEDIKS NTNNHMEILD
LNGTLKITVK LKDENIQNSP FFLKVDNNLK DKIIYVKQFI NDRLENLLRK GECLFDLIKN
KNMNTNNLIQ LNINIDHFLN TFPKAIHDIN IIEQYILYGL IDIDKIKNVI TNLHEEDNLV
NASQEEEIYI DKEIHELINN EKFKNDQTDE MGEYTATTTN NVKHTNNTNN NDTHITDTLT
HINENNDTRN NFLKVKDNHK IVDFINENKL KFLDYIDPNI MKKLRNYINL LNTEELNLKN
KKDNKKIDDS NKKDLLGIKK KRSEDKFHLD NNLEKDEKKI EVIKNLLIFY HKLKTVCLSK
KEKELKDEFI KEEKESIKKL KLNYNKFVNI KKNLEVSNVY LHNNGYDSSL KELETTKKYL
IEIKDEVTKI KQISDNIIKI DNVEELNKDI ENLNNEIHEI EKMWLFIKKK EEILNEFFFC
PFKDLDVEDF DIQIKKLQND FKKIKVDRKH NICKEETLKL KEIIKFISVL CEIKKPFIKD
RHIKEMENNI NEEKEKNKEE DKINIIIDDS TLTIYFYKLN IMKYHDTIEE VIIKAYNEKI
IEETINKFED YWDKIYFKKK EYKNNILLTY IDDICIDTIE EHQVTLQNCF SSKYFLFFSD
ELNLWQKKIS NIYEVIQLLK DIEKLWIYLQ NMYIYSEEVK KELPLYSKFF LTINDEYLEM
LKQIIDNNIK VVDFSNEGGI IEKLEELKVK LCKSEKPLNE YLDSKRKSFP RFFFISSTDL
IDILSNGNNF KLVNTHVQKI FLSIRKFVTK NEQLTDNEIQ NEVKLNNQET ITEEKNKNAN
ENSNEIETNK YNKKEELTNN RDGDGDDDDN IKNDKDEKDE KEETIIKLIS SYGEEICNFH
EGLVLKGKVE CYLNDIIDHI KYTLKYYITN LFRLKDLFNN EKEKWIDENY LAQVFILCNT
IFFVNDVENI LIKKDINIYE ELNKYYKNHI LQLENVIKKV QKKLTIKNRI KIMCIITLDT
FYRDVLEVIL KNKSSISINM FDWQSQIRMY PFFKNQKIYE QNENQTEESN LKLDNKNLDN
EHQEGKQEYN NKNNDNDNNN NNNNNNILNN ELSKYTCLTH FKDLYIKIKI MDCSFNYSYD
YIGNYQRLVI TPLTSRIYIT ATQALSLYMG CAPAGPAGTG KTETTKDLSS FFGKNCYVFN
CSDQLDYKSM GNIFKGIGST GCWCCFDEFN RLIPEVLSVC SIQFKSILDC KRNNNNVCII
GSDEIIVKKN CAVFITMNPD YLGRSKLPES LKILFRPITV IIPDFNKICE NMLMAEGYVN
AKYLSIKFTT FFELAKSLLK DKHCDWGLRS IKSVLTKAGD LKRNYPDVDE NKLLYSAIHD
INIAKISSSN CPIFSGLLND IFFSNQNDIT DINDINDINE NKKEKDNIEE LKSDNVKEEK
KTKKKHLEDN NNNKKKELFN LNNIEKELMD ICKKNHLFGL NYFVKKIIQL NDIMNIRHCV
FIMGEAGCGK TTLFNMLMEY QKKQNLKTVS IRINPKSINI DDLYGNVHIK TREWKDGVFS
KYMRNYSKKD DCDKAYIIFD GNLDSHWIEN MNSVMDDNKV LTLSSNERIL LKNHMNLVFE
FSDLMFATPA TISRAGLVYF SVDPNDLWKN YFLSWIDKHD NFNSNIKKLF EKLMYKYVEP
TFSYLSTLQT SIKISPMSHI QSLSALLDIL LIDNNYESVE HYFIYSVIWC FGGFLGEKDN
VNYKKSFDKY WKNTFKSIKV NRKISVFDFY VENNKFKEWD EAEITNELKQ NYVLQDDIFI
ETIESYSYKY ICKLFLKSDM PILFIGKTGV GKTQLCKKIL NEEKEEFKSF YMIFNYYTTS
KNVQTLMQSC LEKKSGKQFS PPYQQKLIYF IDDINMPKCD DYNTQSAIEL LCQYIDTNSW
FDLEKLNLIK ILNTKLISCM NYNRGNFTIN PRLIRHFFIL NINFPENNTV NSIFSVLLKN
HFNNFKQDVS DLIPSILKST ISLFYNIEKT FKRTATYFYY EFNLRDIHSI VKGLLTTTPV
TFQDCDKLLF LWLHECERVY SDKLNKKDKN KYKKIITDII KKMYNKYEIN KFVMKYDSTL
LFSNFHKGSH DKTYDICKNM EELTLFLNEE LNEYNNSYNV NIVLFSDAIK HICKLIRIVD
NLKAHALLLG IGGCGKTTIS KFSSYISSKT FFEMDFSAHC TDNDIKKYLQ NIFHKCAMKN
EDIVLFLKES KIHDTFFIYV NEYMCSNNII DLYTKEERDY IIHNIRNIAK ADGIEQSDNN
IFDYYIKKVN DNLHFILCFS PTSNNFRDKS NNFQCILNNT MIDIYDNWEA DSLMCVGKNY
VSNIYMNINT GDILLDQEYI NLKNKNIEKD ITLGNKQIEK NYIPTISTND GDDHYKDMDK
TNMKNGDITT TINNIPIDNN NNNNNNRDNI DGNNFFKNRE GNDENMKRKV YSNNFTNQND
LNTNITNNNN NNSNNNNNNI YDKNDSILKE EEYVNLKDII TEYLKECYED LLDISSFYYS
HERSHIYITP KLYLESIKTY HIMLLKNITN INNKMNMLKN GITKMNETSS NVENIKNCLK
DKKKISEEKM EAAEKYAIDI GNEKMVVKKE SDLADIEEQN CLEIQKKVLK QQEECENDIR
LGIPLIEQAE EALNTLNKKN IQELKTLNKP PPGVEDITAA VMQLLATIDT TISIDKFGKI
KDRSWKSAQK MMINPEKFIS LLKDYKNKID ENLVPDCNFK YVENLINLPH FNKNAIQKKS
KAAAGLAEWV LNITSFYKII QNILPKRILL DNTKKGLEEA NEKLQIVREK VQSLKAKLSE
LISQYDHAIY ERDLVILEEK KLKTKLELSI RLIDALSSEE ISWSKQYESL KKKKKTILTD
ILLSSTFVTF CGGFTKKYRN KIMTNCVDTL KRKNEIQNNI FNNMLKKINN NDQNFINNNN
NNNSSNNNST NFGYNEDPQK KDNHNNFDIS NKLNIKNEKK DNELGNDNLK KEEMIYDIFL
VNNFNLDLLI NEEVLSKLSK QGLTLNSVCI ENNIILENSD KFPIIIDPQM ESLKWLINSH
KEKSEKLIIT DINDKILLKK IEECISFGYS IIVENADEYI DNTLYNVISK NIIKRKNNYY
ININDKELMF HPSFYIILHT QLSNPHYQPE IQSACSLINF TVTPDDLEEH LLSITLENEF
NHLSKKKKKL SLLKYDYMCQ LSFLQSSILQ KLTDAKGDIL EDVSLIENLE KTKLLSENIA
KKTEIVKNTE VHINTIINLY RPLSKRGVMY FFILQKLKNL HSFYFYSLEI FLKIFIKCLN
DSSPNRSPSK VNQEQEYYLK SEDNDFNDDY LGSTKEEEKM EDEEKMEEEK VDEEKMEEEK
VDEEKMEDEK VEEKMEEEKV VEENTEDEKA IEINTEDEKA VEKNTEDEKA VEKNTEDEKA
IEKNTEDEKA VEKNTEDEKA VEKNTEDEKA IEKNTEDEKA VEKNTEDEKA VEQNTEDEKV
VEENTEDEKA VEKNTEDEKA VEKNTEDEKV VEEKIEDEKG EEQKAEEENV GIEEVEKVQI
DDYKVSEKKG ENKNCTYEEN GKIDKDKEDD LEEEEDFEND DFTNEETKID KNEVEKRVNM
LTDLLNIKMW MYMDKGLLER DKLIVKCLIM LHLEKLNDKI SEEEEEIFIN PKYKLSNNNI
TSIRNKKENE SMEKKLMNKS FINEELYEDC KNLENLKDFE NITESFESES MSWKQWFLSE
KVENEELPRK YNNIKDFSKL LLIRVLRKDR FLIALKNYIT KNIKMTNDEK NNTYALENIL
DEYIDNKTPV LFLLTTGYDP SKEIEDYINK MKNNAIKKND SNKKESNKNN IAYVNISMGQ
GQENIALKYL KEISKCGGYI FLQNIHLMTK WLKEFEEILD KIFLDAHVNF RLFLSAAIPN
EKDTKLLPEK LLKKCFRINN EKSYSLKDNI KCCLDKFENG QYDDKLKTVI LGLSYYHSLL
LGRFLYGKIG FSQSYSFNDN DLEISFNIIK RYLKTYESFP LADVLFLIGE IIYGGHITDI
WDRRINKTYV KNILKEIYRN IISINEKNKN INMDFHHPND SNNNYNDDDN NNSHKNNKNN
NNNNNKDDDD ESNNSNDNEE ENEEKLILKN TKHNILFDVF KFPDCSKYNI NQLKKYIDEK
LNKEQTYLLG LHINAEIEYM KNECSRILQT LQELSNKEIA STESYKKNTK IIKKEKPGDN
KDNKYTHDQK KETIHKEEDD EDEKHSGSNK STKIIYDIIN HLLNELPDKI DTNDLKIEDS
QTNTFMVIAL KEAEKFNKLI ECINDTLIEI KLVLDGILNM NDKIQNTIKS LMLHNIPHIW
INYSYPSKKK LMPWFENFKL RIIFIKEWIS KIRNNIFLPN SVWLSALFNP ISFLTAIKQK
FAQENKVPID KLKLKWQVTN ITKLEDLNNK NNALYIHGLY LQGASWFINS KNDTFTFDKD
NINDNVSYGN IIESVPKHIY YSMPLIYVYC ISNEQDELLK ENMEYRSLDT PLYVTSDRGN
TFVCSIDLNL EMEDIEDKWI LAGVALFLSD D
