ID   B4MXM5_DROWI            Unreviewed;      2261 AA.
AC   B4MXM5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=Histone-lysine N-methyltransferase ash1 {ECO:0008006|Google:ProtNLM};
GN   Name=Dwil\GK20252 {ECO:0000313|EMBL:EDW76794.2};
GN   Synonyms=dwil_GLEANR_295 {ECO:0000313|EMBL:EDW76794.2}, GK20252
GN   {ECO:0000313|EMBL:EDW76794.2};
GN   ORFNames=Dwil_GK20252 {ECO:0000313|EMBL:EDW76794.2};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW76794.2, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW76794.2, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
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).
RN   [2] {ECO:0000313|EMBL:EDW76794.2, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CH963876; EDW76794.2; -; Genomic_DNA.
DR   SMR; B4MXM5; -.
DR   FunCoup; B4MXM5; 323.
DR   STRING; 7260.B4MXM5; -.
DR   eggNOG; KOG1083; Eukaryota.
DR   HOGENOM; CLU_229222_0_0_1; -.
DR   InParanoid; B4MXM5; -.
DR   OrthoDB; 79252at2759; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0035097; C:histone methyltransferase complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005700; C:polytene chromosome; IEA:EnsemblMetazoa.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR   GO; GO:0035035; F:histone acetyltransferase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0140954; F:histone H3K36 dimethyltransferase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR   GO; GO:0018991; P:egg-laying behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IEA:EnsemblMetazoa.
DR   GO; GO:0048477; P:oogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:EnsemblMetazoa.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:EnsemblMetazoa.
DR   GO; GO:0141005; P:transposable element silencing by heterochromatin formation; IEA:EnsemblMetazoa.
DR   CDD; cd04717; BAH_polybromo; 1.
DR   CDD; cd15548; PHD_ASH1L; 1.
DR   CDD; cd19174; SET_ASH1L; 1.
DR   FunFam; 2.170.270.10:FF:000011; Histone-lysine N-methyltransferase; 1.
DR   FunFam; 3.30.40.10:FF:000113; Histone-lysine N-methyltransferase; 1.
DR   FunFam; 2.30.30.490:FF:000039; Histone-lysine N-methyltransferase ash1; 1.
DR   Gene3D; 2.30.30.490; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR043319; PHD_ASH1L.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46147; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR   PANTHER; PTHR46147:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1374..1418
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          1421..1537
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1545..1561
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          1961..2099
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          1..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1086..1156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1287..1312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1573..1610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1653..1679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1750..1769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2241..2261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..54
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..123
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..283
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..324
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..460
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..760
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1586..1598
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1752..1769
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1536
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   2261 AA;  249718 MW;  424049FE988AFC15 CRC64;
     MNSDQNGATR AADKTKDQEQ QNPGPGPETG GSENEETTDT SQSQTQSIKS SATQFSVVQR
     TDTDGLRMRI SAIRPLAPPP SLKTNCKMST TTTDSLSCFR QEEITTNKSN KTSKKIKVKR
     KKLSHTDAVN PSKVRKSGGV AAASMGGIFS SDSDDDLPLK VHQQRAPRLL LTAIAGHQAS
     GQAPPPPDSI GISSSDNELP SLVQAAIKRV ESDTEDTSVS LGATGKSKHL PQYQSTLLQD
     FMEKTQMLGQ HQLVGGGDRV KPKEETQPPA NPRKRRGRPK KLNPHIGSNL RAGSVVTARP
     AAVNESADSG VISTTSTTQS TTPSPKMPNS SDPPQAQARG LDSAAGNSST KIDMSYLDKR
     MYATERVLYP PPRNKRRQIK NPKNIKDAEQ VDPLWREIDV NKKFRLRSMS VGASGGGGGS
     GRGGSGGVAS AICSKVLVAN SGYVSDYGSV RHPHSSHSRS NHNSGYKSDA SCKSRYSVKS
     CVSRRSRAKS CGYRSDCKEG GKSSIRLRRR RRPSTMIATT ADVEDQDILQ LAGLSLGQSS
     EESNEYISKP SLQSLPSTSA SKKYGEINRY ITTGQYFSRE PNPSQNQNQP EAPFMSKMLL
     NHRKDSSQAA SNAQSSCRFP CKIKSRRSSA ASMCSSYVSG VSRMLRRRHR RNKSLQIDSK
     LLTEIEILTS TFHGRCRIQE DRLTGSSGKE KLLAEATKLK ATTLNAAAPA STLAQPLKRA
     MKKRKLSEPL VDFAMLSASA NANGDGVGGA SNAQSSGAGS SKRRHKKSQG SSTSSSPDDH
     KLPLKKRHYL LTPGERPPAD SSNFANGKLN AEAWAAAAAT AKTTASTKSQ AQFNARSAKS
     LLTPKKRHLL EHQSGGVTTT SASNSPLRIV VDSNSSISGG KLLDISPSSL GSLKQQKRAS
     VASSNKQKRD PATQLHSPAP SGSGSCPPPP PGIFEPSVEL EIQIPLSKLN ESVIITKSEV
     ASPLLSLDIK EDTKKEMGQR VVESLLHKTG GNLLFKRKRK KINRTGFPTV RRKKRKVSLE
     QLQTEKSSEQ MDQEQEQQEQ DPLSRETRST NSNNPVQNCE RVPLVGEARE TFVARSNARM
     TPRLSVVALE RLQRPQTPSR GRPRGRKPKD KLEQVTESSA VASSAPPPPP PSEKTVAKKR
     GRRQVAKPEE EQEPAIAIPT PAKNKLLVEP NIKLPAGVDP NTNFSCKIRL KRRRNLEEIT
     SKEIVSQEEL DKEAEAKRLD VIPSEHDPLP MQECTSSSTL AIHSQQDYAS CSESSEDKLS
     TASRNKISKL KKNYLVAGLL SNYYKQATKP PPVKHQGGGK DSIAPSSGQR LMPPPPYCER
     YHRRTQIDFE LPYDIWWAYT NAKLPLRHQV PSWNYRKIRT NVYAESVRPN LAGFDHPVCN
     CKESCMDNCL NRMVYTECSA TNCPSGDKCH NQKIHRHEVA PGVERFMTAD KGWGVRTKLP
     IAKGTYILEY VGEVVTEREF KQRMASIYLN DTHHYCLHLD GGLVIDGQRM GSDCRFVNHS
     CEPNCEMQKW SVNGLSRMVL FAKRQIRQGE ELTYDYNFSL FNPSEGQPCR CGMPQCRGVI
     GGKSQRVKPL PPIAAVSADA SPQRGGRQRK HKAKKHPQKG GTAAGGSGSM PLVNKLVQQL
     SERERKLAKQ FNVFLVRNYE KIRRYKVKRS HKASSAIGAS AASTSQGSLG GRRPSTPSSS
     SLLAAQISAL CTPRNIKTRG LAQAVQDPEL EKMARMAVVL RDICQTIEGM NMTEILSLSA
     AACKQSKRKN AKNTNSAVSS SSSSSSTTAG ALQAGRLEFK GIQSMVEQGH YKSPQEFDAH
     MQQLFDEARK TYTDDESKIN LLQSLVECYE QQKVSSYEQL VEILGDSVDL HGFKAKQVEP
     QPTVEPAIKE TQITPLPPPV ATDDEDVISC ICGLYKDEGL MIQCSKCMVW QHTECTKADI
     NAENYQCERC EPRKVDREIP LDEFTEEGHR YYLSLMRGND LQVRQGDAVY VLRDIPIKDN
     EEQKKHTYET IGKIDYQECD IFRVEHLWKN ETGKRFIFGH HFLRPHETFH EPTRRFYPNE
     VVRVSLYEVV PIELVIGRCW VLDRTTFCKG RPIECHDESH CYICELRVDK SARFFSKTKA
     SYPACTKSYA FRKFPERVKI SKTYAPHDVD ASMLKTKKQK TELEVATTAK QQRITVREGR
     RRQPRTAEPS YVATKSIGGV GTSNATAAVQ VLTPTLPNGQ LLKRKRSRLE NVLITMKLKC
     LDAQTAQEQP IDLSYLLSGR GARQRKTNNN QTTTTSDLGH N
//