DYHC_EMENI
ID DYHC_EMENI Reviewed; 4345 AA.
AC P45444; C8VQK6; Q5BH62;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Dynein heavy chain, cytoplasmic;
DE AltName: Full=Dynein heavy chain, cytosolic;
DE Short=DYHC;
GN Name=nudA; ORFNames=AN0118;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8134356; DOI=10.1073/pnas.91.6.2100;
RA Xiang X., Beckwith S.M., Morris R.N.;
RT "Cytoplasmic dynein is involved in nuclear migration in Aspergillus
RT nidulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2100-2104(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Cytoplasmic dynein acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules.
CC Dynein has ATPase activity; the force-producing power stroke is thought
CC to occur on release of ADP. Required to maintain uniform nuclear
CC distribution in hyphae.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; U03904; AAA18338.1; -; Genomic_DNA.
DR EMBL; AACD01000004; EAA65296.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF90163.1; -; Genomic_DNA.
DR PIR; A53489; A53489.
DR RefSeq; XP_657722.1; XM_652630.1.
DR SMR; P45444; -.
DR STRING; 162425.CADANIAP00002629; -.
DR EnsemblFungi; CBF90163; CBF90163; ANIA_00118.
DR EnsemblFungi; EAA65296; EAA65296; AN0118.2.
DR GeneID; 2875894; -.
DR KEGG; ani:AN0118.2; -.
DR VEuPathDB; FungiDB:AN0118; -.
DR eggNOG; KOG3595; Eukaryota.
DR HOGENOM; CLU_000038_7_0_1; -.
DR InParanoid; P45444; -.
DR OMA; FIMDEAN; -.
DR OrthoDB; 26380at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IDA:AspGD.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:AspGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0001411; C:hyphal tip; IDA:AspGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:AspGD.
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:0008017; F:microtubule binding; IDA:AspGD.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IMP:AspGD.
DR GO; GO:0015631; F:tubulin binding; ISS:AspGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:AspGD.
DR GO; GO:0051293; P:establishment of spindle localization; IBA:GO_Central.
DR GO; GO:0070789; P:metula development; IMP:AspGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0072382; P:minus-end-directed vesicle transport along microtubule; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IMP:AspGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:AspGD.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 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; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
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; IPR013594; Dynein_heavy_tail.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..4345
FT /note="Dynein heavy chain, cytoplasmic"
FT /id="PRO_0000114638"
FT REGION 1..1895
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1896..2121
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2191..2449
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2554..2803
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2897..3166
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3182..3466
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3552..3781
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3995..4207
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 668..688
FT /evidence="ECO:0000255"
FT COILED 914..934
FT /evidence="ECO:0000255"
FT COILED 1322..1342
FT /evidence="ECO:0000255"
FT COILED 1549..1565
FT /evidence="ECO:0000255"
FT COILED 1628..1657
FT /evidence="ECO:0000255"
FT COILED 3182..3273
FT /evidence="ECO:0000255"
FT COILED 3410..3466
FT /evidence="ECO:0000255"
FT COILED 3701..3799
FT /evidence="ECO:0000255"
FT BINDING 1934..1941
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2224..2231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2593..2600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2935..2942
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 13
FT /note="Missing (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..156
FT /note="QQ -> PK (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="A -> D (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="R -> K (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="G -> R (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="V -> G (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 1727
FT /note="V -> F (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 2683..2684
FT /note="QL -> R (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 2719
FT /note="Missing (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3035
FT /note="A -> P (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3042
FT /note="L -> P (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3234
FT /note="A -> R (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3397
FT /note="A -> P (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3451
FT /note="A -> T (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3627..3633
FT /note="RFGNPIL -> LSETRFI (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3698
FT /note="V -> VWY (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3726
FT /note="R -> L (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 3858
FT /note="Q -> H (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 4035..4036
FT /note="FD -> IPH (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 4049..4053
FT /note="HATCA -> THMP (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 4141
FT /note="A -> G (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 4210
FT /note="D -> H (in Ref. 1; AAA18338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4345 AA; 492082 MW; 3DFC99DA80BC13E8 CRC64;
MEVASSGVPD GAPTAISQGP LVDADAVVEY LADVLRVTLG ALRSELENAG SLLSKTKYSE
TAQRCLRFAS ESQVALYVQK DLVASDHTNG TADSEEPPAE YVYTLSAEIS SSSTTVASVA
FIKRPAAIDP SLPISSQIQV MNLPGPAALN NTQAQQGTSL SPYEILHLLV HHGLSPYFEA
NTRNQDGAAK AKTDSEVKTG VPGTKKKFAE LELGLLHLQQ NVEIPALNLP LHEVVQAALV
EAEKRGVKPS VDLIDSTLLE SSAFINSIQN NVNAWIKSIQ TITKMSRDAD SGSAAQEINF
WLSMETALEG IENQLRGDGV QLTMDILRHA KRYQATLSFV ADTGLREATD LVQKYNQLMR
DFPLDELLSA TSLQKVRESL VLIFNHLNKK LKICPYPIKR ALALVEAISG DLDSQIHSLL
NGRTIMHLDY REFRTLMKTA GSIWRTWDDN LKEFTNVARE STRRRNEKFI PIKINARHDK
TQERLKYINT FRVNHEQLQR TIANVLGPKS YSAEDAAAGA AADGAVIVEE IGDVDAVEEV
AQAYAALKSV DVLDVSPTGT QNWITAEIAY NERTSRVENS IIARLRDRLA TAKNANEMFR
VFSKFNALLV RPKIRGAIGE YQTQLIDNVK QDISALHERF KQQYGHSEAH AMAQLRDLPP
VSGAIVWARQ IERQLDGYMR KVEDVLGEDW HLHTEGQKLQ AESNLFRKKL DTRPVFETWL
HDVQRRRITI SGRLFNIIRN RAAGNTLELA VNFDAQIIAL FKEIRNLIWL NFQVPHAVSN
ISKEAKRVYP YAISLMESVR TLLQTNRSIL SMTDVAILLN GYMNDAQSMI VRGIPLRWES
FVHSYELHVK QAALVNGALD SVIPSRGESK HVQFVREFAA SAAVLQHKTA VLASINDTIQ
KAIHELKTCP YEFSAFKQRL DAIQAAVDKL NLENYVNLGF WVHNLNQKIE GILSERLHKA
IREWMNSFQE SQSGQPMQKV NGNGDTDTTA YNIEFPGLTH EISMRNQVLH LDPPLQYARA
TWFSHFDNWL GIICNLEKIK SSRYQISIEV QKVQLSESCF ADLPQHCTNE LILVYSAIET
RLKEVSEYVD KWLQFQSLWD LQSEQVYDIL GDDLSQWLQL LQEIRKSRAT FDTSEVSRSF
GNIKIDYEQV QTRVNAKYDQ WQHEILLKFG SKLGNRMREV HSEIATARHD LEGKSLDSAS
TAHAVAFITS VQQCKRKAKV WEPEVDLFRQ GQATLVRQRY QFPSDWLHVE NVDGEWAALN
ELLGRKGKIV EEQTEALRAK IAAEDKVIND KITEAIAQWN EEKPVSGTIP PEEASRSLSM
FQTRLESLQS EFEMVSKAKE ALDLPPSAES SLPAILEEVQ DFMSVWAALS TIWRSLNDLR
DTLWTSIQPR KLRQSIDGLI KMTKEMPSRM RQYAAFEHIQ NVLKQLLKVN PLLSDMKSEA
VRERHWLKIY KALKPGMRFS LVSLTLGDVW DLQLAASETV IRNIIAQAQG EMALEEFLKS
VRETWQNYSL DLVNYQNKCR LIRGFDDLFA KCSENLNSLQ AMRHSPYYKE FEEDASSWED
KLNRVHVLFD VWIDVQRQWV YLEGVFTGNA DIKHLLPLES SRFQNINSEF FAVMKKVYKS
PFVLDVLAIN GVQKSLERLA ELLNKIQKAL GEYLERERVS FPRFYFVGDE DLLEIIGNSN
DIFRVAKHFK KMFAGLSGVL MDDDNNIVGF TSKEGEEVRL KKEVNLVKTP RINDWLTALE
SNMKLTLAEL LAEAIEQFEP IYNSAEVDRT AFDDFIANYP AQIVVLASQV VWTNEVQKSL
ENSGTTLPTL YDAQVRILEL LAVTVLGDLD PISRKKCEHL ITEFVHQRDT ISKLIASNAT
SATHYLWLLQ MRYVYQADGD FLQRLYVHMA NAKLNYGFEY LGVPERLVRT PLTDRCFLTL
TQALCQRLGG SPYGPAGTGK TESVKALGLQ LGRFTLVFCC DDTFDFQAMG RIFLGICQVG
AWGCFDEFNR LEERILSAVS QQIQNIQIGL RNKETDEKSQ IDLVGRRLTV NMNTGIFITM
NPGYAGRSNL PDNLKKLFRS VAMSKPDKEL IAEVMLFSQG FKQAKRLSQQ TVPFFDHCST
RLSKQAHYDF GLRALKSVLV SSGGLKRARI ANSDGDLGPD EIVEPQIIVQ SLRETIAPKL
VREDVATMLQ IQEQDFAGVE YVPANYEALT AAIREIAREQ HFVDSEMWIT KILQLYQIQS
IHHGVMMVGK SGSGKSSAWK ILLQALQRIE GVEGVSHIID SKVMSKEALY GSLDSTTREW
TDGLFTGILR KIVDNLRGED TKRHWIVFDG DVDPEWVENL NSVLDDNKLL TLPNGERLNL
PPNVRIMFEV ESLKYATLAT VSRCGMVWFN EDTVTPSMII TNYVESLKTK TFEDLDDDSV
PSGQSAVKTQ DCQDMLSTIL SQLLQTDELV HKSLGEAKKY NHIMEFTEIR ALNTLFSLLN
KACRNILEYN IQHVDFPLEY EQIESYISKK LLLALVWSFT GDCPLGDRKS FGEFVSGLTT
IDLPIETNSS IIDFDVTLPK GTWSSWQSQV PTIDVNTHSI TQTDVVIPTV DTVRHEDVLY
SWLAEHKPLL LCGPPGSGKT MTLFAALRKL PNMEVVGLNF SSATTPDLLI KTFEQYCEYK
KTLSGVVMSP NQIGRWLVIF CDEINLPAPD KYGTQRAISF LRQLVEQNGF WRTSDKTWVS
LDRIQFVGAC NPPTDAGRTP LAERFLRHSP LVMVDYPGEI SLNQIYGTFN SAILKILPLL
RGYSESLTKA MVQFYLESQQ RFTPKIQPHY VYSPRELTRW VRGVYEAIKP LESLSVEGLV
RIWAHEALRL FQDRLVTEEE RAWTADAVRR IALEHFPTID QEAALKGPIL FSNWLSRNYV
PVEQEQLRDF VKARLKTFCE EEVDVPLVLF NDVLEHALRI DRVFRQPQGH LILIGVSGSG
KTTLSRFVAW MNGLKVFQIK VHGKYSSEDF DDDLRSVLRR AGCKGEKICF IMDESNVLDS
GFLERMNTLL ANAEVPGLFE GDEFSSLMTA CKEGAQRQGL ILDSQEELYK WFTQQIVKNL
HVVFTMNPPE EGLSSKAATS PALFNRCVLN WMGDWSDQAL FQVGSELTQS VDLDKPGFVA
PDSIPVAYRE LSLPASHRDT VINAMVYIHH SLQRFNQRLQ KQQGKTTYLT PRHYLDFVAQ
YVKLFNEKRE DLEEQQRHLN VGLEKLRDTV EKVSDLRGSL AQKKMQLEKK DAEANEKLQR
MVADQREAEQ RKAVSLEVQA ALEKQEKEVA LRKDVVLHDL ARAEPAVLEA QKSVSNIKRQ
HLTEVRSMGN PPAGVRLALE AVCTLLGHKV DSWKTIQGIV RRDDFIASIV NYDNEKQMTK
NHRLKMQNEF FSKEDFTYER VNRASKACGP LVQWVEAQVN YSAILDRVGP LRDEVGQLEE
QALQTKAEAQ AIENTINDLE SSIATYKSEY AALISETQAI KAEMERVQFK VDRSVRLLDS
LSSERTRWEE GSKSFETQIS TLIGDVLIAA AFLAYAGFYD QQFRKAMTED WVQHLVQSGI
SLKPHNPITE YLSNADERLA WQAHSLPVDD LSTENAIFLK RYNRYPLIID PSGRVTEFLQ
KESSDRKLTV TSFLDDSFVK QLESALRFGN PILIQDAEHL DPILNHVLNK EYQKTGGRVL
IQLGKQEIDF SPSFKLFLST RDPSATFAPD VCSRTTFVNF TITQSSLQIQ SLNEVLKSER
DDVDRRRSDL VKAQGEFNVH LRQLEKRLLQ ALNESHGNIL DDDNVIETLE TLKKEAAEIS
RKMAETEGVM TEVEEITQRY SIIARSCSAV FAVLEQLHHI NHFYQFSLQY FTDIFESVLH
GNPHLENSGL RKMEDYQQRI QIILRDLFVT TYQRTSLGVI QKDRITLAML LAQAAPYPMD
KSIIDTILDE SVEGTDLSAN PEAKVQVMSA FGNMSLFKAH LPSVTAEQWD QFLGEELAEN
FVPKVWDENT SELDKLLRSL LLVKLCRMDR FVPAAERFIV AVFGRELYEG STDLKDIVGQ
VTATAPISLS SSPGFDASYK VDALVERTHA TCANIAMGSN EGLESADKAI SNAASAGTWV
LVKNVHLAPS WLQSLEKRLA SLKPHKDFRL FLSMESSPKI PVNLIRASRV LMYEQPAGVR
ANMKDSLSSL STRASKAPVE KARVYLLLCF LHAVVQERLR YAPSLGWKGF WEFNDSDYEC
SANIIDHWVD VVAQGRSNVA PQKLPWDMIR TLITEMYGGK VDDSDDFQQL ERLVHSFLTP
ATFEADYKLV EGVENDECLI LPGETGLPAF VEWVNKLPER EPPTYLGLPA NAEKLLLVGH
GKKMISDLAR ITSLLDEGEQ LMIDA
