ID B3MXV4_DROAN Unreviewed; 4064 AA.
AC B3MXV4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
DE Flags: Fragment;
GN Name=Dana\GF19366 {ECO:0000313|EMBL:EDV38569.2};
GN Synonyms=dana_GLEANR_21408 {ECO:0000313|EMBL:EDV38569.2};
GN ORFNames=GF19366 {ECO:0000313|EMBL:EDV38569.2};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV38569.2, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV38569.2, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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; CH902630; EDV38569.2; -; Genomic_DNA.
DR RefSeq; XP_001966160.2; XM_001966124.2.
DR SMR; B3MXV4; -.
DR STRING; 7217.B3MXV4; -.
DR EnsemblMetazoa; FBtr0391381; FBpp0350836; FBgn0096376.
DR GeneID; 6502126; -.
DR KEGG; dan:6502126; -.
DR eggNOG; KOG3595; Eukaryota.
DR HOGENOM; CLU_000038_0_0_1; -.
DR InParanoid; B3MXV4; -.
DR OrthoDB; 166463at2759; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005930; C:axoneme; IEA:UniProt.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0036126; C:sperm flagellum; IEA:EnsemblMetazoa.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:EnsemblMetazoa.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.287.2620; -; 1.
DR Gene3D; 1.10.472.130; -; 1.
DR Gene3D; 1.10.8.1220; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.1270.280; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.20; -; 1.
DR Gene3D; 1.20.920.30; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 6.10.140.1060; -; 1.
DR Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
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; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR PANTHER; PTHR45703:SF34; DYNEIN HEAVY CHAIN, CYTOPLASMIC; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 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; PF12777; MT; 1.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Hydrolase {ECO:0000313|EMBL:EDV38569.2};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801}.
FT DOMAIN 1425..1562
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1704..1845
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2045..2194
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 747..785
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2858..2909
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 4064
FT /evidence="ECO:0000313|EMBL:EDV38569.2"
SQ SEQUENCE 4064 AA; 466681 MW; 2E26F82092D21CC3 CRC64;
MSSRDSDDEE DEDRIFGRED GLRVSGGGGD GDGGGSGDGI EIGRRLRSGN GIELTDRKRR
VKRKSKTRRS DAGGSGGMTD RDSEINTPRM TNDDRASGMS MERLGSDATG LGDRASDNLD
GSIGGPSPGD GERSGGKQKK TKHRLNFQST KNTTIVGGKS RNPSSTKITT GASLIPDLNL
VINRMRNMPD DSFVYMDYML PHDSEYFTPY SLRLVEYRDL NTYEPFYTVT RHGVTFWHCS
ENFFTPLDQW QQEFEQFLSI IQIRSFSIFR LWKGFKVWEK TIKWRKLNEA RDFLQNNLFI
VIPQLAKAIL RMRSDIVQME RLNFVNVSNV ENWHPFYFLE THMRIYEQLH RIFTDFREFI
GKTIFRACTD AIQARGFYPD DEINYYPSLK KMREAHSFMD RARKRAFCKT LTNFLTYCDM
MVYQMLYRIT IKSFADLAWA FEVHDEVGPS EADISKHERV DKKIEKPRPP DKPQSPFFLA
MLRLLPDRID VEPSEDVIRI IFQRITGLIL ETVLEIHPFT TDPFFTQYTQ PSIMGRQEEV
LYEGAPDLHY LLRADIKFQY NRKNMFVLIR RAYERARLYT MRFHSIRENF EVDNSTDPTV
LNTERDLELL RAYCDRYCNN VRALDGILEY IYLGLLKLTQ TNFKETVTPV CSRLQNILAT
YLPKLAEEET TRLYEEAQDF YGRICYEPHE TLEIVAHIRF LDTCDSELDD IFKGIDYVHD
LLLIIKDFSI PIDDESKEDY MDTEDYLNRT RETLAEIKEK RQEFINRLED AMQDDIAQLK
EEIHEVAIMA LEPWLLDAKS NRHTVTTKLD MMLDRLNGCR ERADEFLGYQ KEFQIDLTMY
EEMASGFYDI RMRQNLYRTQ TEWEESLAEW IAADFNTLNV ADMLDLNAKT IKNCLQFAKY
LPENNIVPVL HASAEAFKEK LPVIGYLRNP NLRARHWTEI EDLLNRKFFQ EKDIIIQTYE
DVHAFDDLAI GEALMQISSQ ATGEVQLENM LKAIETIWKE TELSIVSHHD AKDVFILAGT
EELQAVLDDS NVNINTIAAS KFVGPIKGKV DEWITAMDQF AKTFESWMDC QGAWIYLEAI
FASADIQRQL PHEAKMFFTV DKSFKETVRQ AKKVALALPT MSSVDVYKTL VENNRLLDLI
SRGLEAYLEV KRVVFPRFYF LSNDELLEIL AQTRIPQAVQ PHLRKCFDAI YRLEFGQKEG
GDGKMVATND IIAFLSPEGE KLQFGKGLKA RGAVEEWLSK VEEAMFVSVK RYMRFGYQCY
PAKEREDWFQ DHPNQVVLTV SQVQWAADIH RIYEGKERNP LNILEKMAKF EMKCLKDLGA
LAALTRKSIS SLLRKILCAL ITIDVHAKDS VHMLIEKEVA KPTDFNWLKM LRFYWADETE
TVYSRMAAAN IPYYYEYLGA GGVLVLTPLT DRCYLCLMGA FQMDLGGAPA GPAGTGKTET
TKDLAKALAK QCVVFNCSDG LDYKMMGRFF SGLAQCGAWC CFDEFNRIDI EVLSVIAQQL
ITIRTAKAMK VKRFIFEGRE IKINRSCCVF ITMNPGYAGR TELPDNLKAL FRPISMMVPD
YALISEVILY SEGFEDPKIL ARKMVQMYQL CSQQLSQQNH YDFGMRAVKS VLVMAGALKR
ASPNQREDIT LIAALRDSNI PKFLADDAVL FRGILSDLFP GVELPDSEHP HLEVSLRLGL
RNKFLQPVPT TIRKCLQLYE TMCVRWGVML VGPTGGGKSV VLHALEFALS HLFENEIQDP
NFRPVVIQTM NPKAVTMNEL YGYVDAKTLE WQDGLLGLAV RTATLVEDEI HQWIMCDGPV
DAVWIENLNT VLDDNKMLCL ANSERIKLTA WIHMLFEVQD LLQASPATVS RCGMVYVDPG
DLGWIPLIDT WREVDMGKKL PAPMADFLYQ LFIGYFDKAL KIERKRAVYT IHQVLGSKVR
LCCNLTSSQL EAVNWKTMGE EPSKELLTKI FAWTVLWAIA SNLKDAEKVS FEEQWSKAMS
QHPNMKLPKL SMWNYRIDLE KQDWGTWNQI MQKFHFDPEI SYYDMQVPTV DTTKYGYVAD
LLFKRNMPVM VTGDTGVGKT VLAISCMKRL QSEGKVIPVI LNFSAQTSSV RTQEMIEGPL
EKRKRTQLGA PVGKTVIVFI DDVNMPKLDT YGAQPAIELL RQFLDFTGFY DREKLFWKEI
LDVVLGCACA PPGGGRNPLT PRFVRHFALF SLPKPNEETL TQIFNGILRG FLQTFSASIR
ALSEPMVNAC VDVYMRVANV MLPTPDRSHY IFNLRDLSKC IQGILQASNL HYNQESQILR
LFYHETTRVF HDRLINQDDK NLFKRLMKDV CMDHFHRQVI GDDEPEILFG DFMVFGKPKN
ERIYDEIKDH TKLESVLNDY IVDYNSIAVG KGMKLILFQD AMEHTVRLAR LLRSDRGNGL
LVGVAGMGKQ SLTRLASHVN EYNCWQIEMR RNYDLNAFHE DLRVLYRIAG IDNQPVTFLL
IDSQIVEEEF LEDINNILNS GEVPNLFEGD EYEKIILDAR DACNENRKDE PCNRDEIYKY
FINRVRNNLH VVMSMSPVGD AFRRRCRMFP SLVNCTTIDW FTSWPTEALY SVALGLLNKI
APKMEDRVAL ASTTVFMHKT VEDASVRFYK EMKRHYYTTP SSYLELLKLY QNLLKLKNME
IIAKRKRIAN GLNKLLETNE VIAVMGKELE VMVPQLDEKS ALMKSLVDNL TKETKQADAV
KQSVMEDETN AKEKAAVAQA ISEDASKDLE IAMPALREAE DALKGLTKAD INELKSFTTP
PALVQFCMEA VCILLGAKPT WASAKAIMAD INFIKRLFEY DKEHMKEDTL KKVKKYIDHK
DFVPAKFEKV SKVAKSVSMW VIAMDKFSKV YKVVEPKIKR KEAAEAELKE VMTVLRQKQK
ELAAVEAKIQ ALRDSLEEKQ REFQVIQDNV DLTYGRINRA GRLTSALSDE QVRWRETVKS
LTGDLACVPG DVLVAAACVA YLGAFSHEYR RDMSALWVTK CREYKIPSSG DFNLLKVLGD
PYEMRQWNVD GLPKDNISIE NGIYATRALR WALMIDPQEQ ANRWIRNMEG GNNLQVIKMT
DPSMMRVLEN SVRQGYPVLL EEINETIDPS LRPILQRETY KFEGRVYLKL GDQVIDYDDN
FKLYMTTKLP NPHYLPEVCI NVTLVNFLVT ESGLEDQLLA DIVAIELPAM EIQRNDLVVK
INADKQQLLA LEDKVLKLLF NSEGNILDDE ELVETLNDAK ETSLIIAARL IDTEETEKII
TASRERYRIL ASRGAILYFV VAGLAEIDPM YQYSLKYFTQ VFCNVLRLDH PVQTVEVRIA
NLMVDELKAI FDNISRGLFE NHKIIFSFLL ALSVERQEKR VTDEEFNFLT RGAVGNIRPK
KMPPNLKLSQ MQWDTCIYLE DNFPDVFSGF TNDLDKPFFL QLMDNREEFD FAGTNQPPTD
KWNKRLRIFS KLMFVAVFRK PRFLLNIVCY LNATVGKYFT EAGAGTQLST VYLDTSAITP
LIFVLSTGSD PMSSFLKFTT QMQFTDKYYS ISLGQGQGPL AENLIEKSLR LGHWVFLQNC
HLATSFMQTL ETIVRNLTLG ITKANPEFRL YLSSMPIATF PISVLQNSVK ITNEPPKGIK
ANVMGALADL KPDFFEQHIQ NGNWRAIVFG LCMFHAVLLE RRKFGPLGWN ITYEFSESDR
DCGLKTLDFF IDREVAEDIP WEAILYINGE ITWGGRVTDY WDLRCLRTIL MIFSSKRIIH
PEYKYCRGES NYRDPRKKTL VEYATFVQNF PVLEDPEIFG MNQNANIVFQ TKETDFFIST
LLLGQPRSAA DEGQAAENEI AQQVIARIQK ALVTKIQREP LHDTLSVLDS KGQVPSLTIV
LVQEIDRFNI SLGIIHDSLA NLSKAIKGLV VMSEELENVF KALLANLVPA SWAKRSFLSI
KPLPSYIADF QRRIDFIQQW AENGAPRSYW ISGFFFPQSF LTGILQTYAR RRILPIDSLK
IDFEIVEKEL VQQDFFEMHT SNKSDAKLYG NLPECTDAVI HVHGIFIEAA RWDLSKGGLC
DANFGELYTR LPVVKFKPCL EMSPQIRYEA PLYKTQQRSG VLST
//
