ID   B3M6Z7_DROAN            Unreviewed;      2257 AA.
AC   B3M6Z7;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDV40862.1};
DE   SubName: Full=Uncharacterized protein, isoform B {ECO:0000313|EMBL:KPU78820.1};
DE            EC=2.1.1.43 {ECO:0000313|EMBL:EDV40862.1, ECO:0000313|EMBL:KPU78820.1};
GN   Name=Dana\GF10724 {ECO:0000313|EMBL:EDV40862.1};
GN   Synonyms=dana_GLEANR_10682 {ECO:0000313|EMBL:EDV40862.1};
GN   ORFNames=GF10724 {ECO:0000313|EMBL:EDV40862.1};
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:EDV40862.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV40862.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV40862.1}, and Tucson
RC   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).
RN   [2] {ECO:0000313|EMBL:EDV40862.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV40862.1};
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).
RN   [3] {ECO:0000313|EMBL:EDV40862.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV40862.1};
RG   FlyBase;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; CH902618; EDV40862.1; -; Genomic_DNA.
DR   EMBL; CH902618; KPU78820.1; -; Genomic_DNA.
DR   RefSeq; XP_001958056.1; XM_001958020.2.
DR   RefSeq; XP_014764459.1; XM_014908973.1.
DR   SMR; B3M6Z7; -.
DR   STRING; 7217.B3M6Z7; -.
DR   EnsemblMetazoa; FBtr0115424; FBpp0113916; FBgn0087764.
DR   EnsemblMetazoa; FBtr0381616; FBpp0341901; FBgn0087764.
DR   GeneID; 6493591; -.
DR   KEGG; dan:6493591; -.
DR   eggNOG; KOG1083; Eukaryota.
DR   HOGENOM; CLU_229222_0_0_1; -.
DR   OMA; LCTPRNM; -.
DR   OrthoDB; 2882778at2759; -.
DR   Proteomes; UP000007801; 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:0046975; F:histone H3K36 methyltransferase 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0048477; P:oogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0010628; P:positive regulation of gene expression; 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   CDD; cd04717; BAH_polybromo; 1.
DR   CDD; cd15548; PHD_ASH1L; 1.
DR   CDD; cd19174; SET_ASH1L; 1.
DR   Gene3D; 2.30.30.490; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 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; IPR036427; Bromodomain-like_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; PF20826; PHD_5; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00249; PHD; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:EDV40862.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDV40862.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1357..1405
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          1408..1524
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1532..1548
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          1978..2098
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          1..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          975..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1171..1242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1270..1293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1549..1603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1642..1671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1849..1868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2147..2180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2237..2257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..760
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1029
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1113..1131
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2154..2180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2257 AA;  248444 MW;  895FF1B7CEED5D0A CRC64;
     MSSGQNETAA AAKVLETQES GSENEETDSI TDQSSQSKST KSATQFSVQR SDTDGLRMRI
     SAIRPLPVAT PVESKPPKKP VVSKSRNMSA QDTESGCSEA KNKAVSKKIR VKRKKISSGN
     SGISKTEREK PHGSGFSSDS EDDLPLKVHQ QRAPRLLLTA ISQAAQSIEK PCLDIGISSS
     DNELPSLVQA AINRVESDTE DTTVEGSFRK AAKAKNLPRY QSTLLQDFME RTQMLGQSGN
     AGKLPEETVV KAKEEVAVLQ TATPRKRRGR PKKVVAVLPA ANSGPAINES ADSGVISTTS
     TTQSTTPSPK MQSETVLPAG TAPVASTSKP KIDMAYLDKR MYATERVLYP PPRSKRRQNN
     KKPTSSSSNK EELQLDPLWR EIDVNKKFRL RSMSVGAASA TGAGTTTICS KILAAKSGYV
     SDYGSVRQPR SAHNHNSGYK SDASCKSRYS TKSCMSRRSR AKSCGYRSDC KESGKSGLRM
     RRKRRASMLL KTAADDPTED QDILQLAGLS LGQSSEESNE YISKPSLQSL PTTSASKKYG
     EINRYVTTGQ YFGRGGSLTA TNPENFISKM MNQRKETPAP SKSSCKIKSR RSSAASMCSS
     YVSGMSRVRR RHRRKSFSHN KSLNIDSKLL TEIEIITSTF HSRCRIQDDR LTGSSGKEKL
     MADANKLQAT LTAPSPAQQL VLNGGGSGGV GALAAPLPKP VKRGLKKRKL SEPLVDFAML
     SASASGAPNG SGSSTGTAKR RHKKSQSNDS SSPDDHKLPL KKRHYLLTPG ERPLAETAFA
     NGKLNAEAWA AAAAAAKSTA STKSQAQFNA KSAKSALTPK KRHLLEQSTP SGRQGASSAS
     NSPLRIVVDN NSISGGKLLD ISPSSLCSLK QQRRVGGGKQ KAIATRELVQ MPSPAGSYPP
     PGVFEPSVEL EIQIPIGKLN ESVITKAEVE SPLLSALDIK EDTKKEIGQR VVESLLHKTG
     GNLLLKRKRK KINRTGFPTV RRKKRKVSVE QQPAVLMDEA GQAPDPDDEP LQSIRETRSS
     SSAQVQVPPT NPPMDCERVP QAGEARETFV ARSNQRAPRL SVVALERLQR PQTPARGRPR
     GRKPKDKTVV PPPPPEPEVK VAKKRGRHPK KPPVEVAPPP PTPPAPAPRP TKTKLQPNIK
     LPAGIDPNTN FSCKIRLKRR KNLDAVHQDL ARTIKSKPAA PPPPPPAEDE ITASQEEIDA
     EAEAKRLDSI PTEHDPLPAG ESLNPGPFDY ASCSDTSEDK SSTVSTKKLS KVKKTYLVAG
     LFSNHYKQSL MPPPAKVNKK PAQPEEQPVA PASLLPPPPY CEKYLRRSKI DFELPYDIWW
     AYTNSKLPTR HVVPSWNYRK IRTNVYAESV RPNLAGFDHP TCNCKNHGEI ACQDNCLNRM
     VYTECSPSNC PAAEKCRNQK IQRHEVAPGV ERFMTEDKGW GVRTKLPIAK GTYILEYVGE
     VVTEREFKQR MASIYLNDTH HYCLHLDGGL VIDGQRMGSD CRFVNHSCEP NCEMQKWSVN
     GLSRMVLFAK RAIAQGEELT YDYNFSLFNP SEGQPCRCRM PQCRGVIGGK SQRVKPLPAA
     EAKPSESSPG RNGRQRKHKA KKHQQQQRAQ AKDAASSVAV AKMQPLSDKE KKLVKQFNTF
     LVRNFEKIRK FKAKRAAAQA SSALTASASS PVQGATNGDI PGRRPSTPSS TSLLATQISA
     LCTPRNMKTR GLAQAVQDPE LEKMAKMAVI LRDICSTLES RKMSDLLTTV SSKKKKAMKS
     SLGGKQGSSA GSGRVEFRSI QAQVEQGHYK SPLEYDEHMQ QLFADAKQQH GDDEGKAKAL
     QSLMDCYEQQ KTSSYSQLVE ILGESESLQS FKPKEEELMV PTVELQKDVK KSPGTGDATP
     PPTVPSIPIN VLPPIEGSSD EDVIRCICGL YKDEGLMIQC AKCMVWQHTE CTKADIDADN
     YQCERCEPRE VDREIPLEEF TEEGHRYYLS LMRGDLQVRQ GDAVYVLRDI PIKDEAGKVL
     PTKKHTYETI GAIDYQECDI FRVEHLWKNE TGKRFIFGHH FLRPHETFHE PSRRFYPNEV
     VRVSLYEVVP IELVIGRCWV LDRTTFCKGR PMECTDEDHC YICELRVDKT ARFFSKAKAN
     HPACTKSYAF RKFPEKLKIS KSYAPHDVDP SLLKTRRQKT DLEVAGGVPA TAQKTPGRQE
     QQQQKAAGRK QRGVNAVTSE SSSVRVLQPV APNGQILKKK RSRLENVLIT MKLKCLDAQT
     AQEQPIDLSY LLSGRGARQR KTQQHSGNGN NSSNCSN
//