ID   B4LZS3_DROVI            Unreviewed;      2187 AA.
AC   B4LZS3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|RuleBase:RU271113};
DE            EC=2.1.1.360 {ECO:0000256|ARBA:ARBA00012190, ECO:0000256|RuleBase:RU271113};
DE   AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|ARBA:ARBA00029821, ECO:0000256|RuleBase:RU271113};
GN   Name=Dvir\GJ24607 {ECO:0000313|EMBL:EDW68242.2};
GN   ORFNames=Dvir_GJ24607 {ECO:0000313|EMBL:EDW68242.2};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW68242.2, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW68242.2, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW68242.2}, and Tucson
RC   15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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:EDW68242.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW68242.2};
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:EDW68242.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW68242.2};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC       histone H3 to form H3K79me3. This methylation is required for telomere
CC       silencing and for the pachytene checkpoint during the meiotic cell
CC       cycle by allowing the recruitment of RAD9 to double strand breaks.
CC       Nucleosomes are preferred as substrate compared to free histone.
CC       {ECO:0000256|RuleBase:RU271113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60328, Rhea:RHEA-COMP:15549, Rhea:RHEA-
CC         COMP:15552, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.360;
CC         Evidence={ECO:0000256|ARBA:ARBA00001569,
CC         ECO:0000256|RuleBase:RU271113};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU271113}.
CC   -!- MISCELLANEOUS: In contrast to other lysine histone methyltransferases,
CC       it does not contain a SET domain, suggesting the existence of another
CC       mechanism for methylation of lysine residues of histones.
CC       {ECO:0000256|RuleBase:RU271113}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. DOT1 family. {ECO:0000256|RuleBase:RU271113}.
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DR   EMBL; CH940650; EDW68242.2; -; Genomic_DNA.
DR   EMBL; CH940650; KRF83748.1; -; Genomic_DNA.
DR   EMBL; CH940650; KRF83749.1; -; Genomic_DNA.
DR   EMBL; CH940650; KRF83750.1; -; Genomic_DNA.
DR   RefSeq; XP_002054722.2; XM_002054686.2.
DR   RefSeq; XP_015027756.1; XM_015172270.1.
DR   RefSeq; XP_015027757.1; XM_015172271.1.
DR   RefSeq; XP_015027758.1; XM_015172272.1.
DR   SMR; B4LZS3; -.
DR   STRING; 7244.B4LZS3; -.
DR   EnsemblMetazoa; FBtr0434802; FBpp0391834; FBgn0211685.
DR   EnsemblMetazoa; FBtr0437107; FBpp0393960; FBgn0211685.
DR   EnsemblMetazoa; FBtr0438688; FBpp0395416; FBgn0211685.
DR   EnsemblMetazoa; FBtr0441254; FBpp0397795; FBgn0211685.
DR   GeneID; 6630054; -.
DR   KEGG; dvi:6630054; -.
DR   eggNOG; KOG3924; Eukaryota.
DR   HOGENOM; CLU_001460_1_0_1; -.
DR   InParanoid; B4LZS3; -.
DR   OrthoDB; 146338at2759; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR   CDD; cd20902; CC_DOT1L; 1.
DR   Gene3D; 1.10.260.60; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025789; DOT1_dom.
DR   InterPro; IPR030445; H3-K79_meTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21451; HISTONE H3 METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR21451:SF0; HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC; 1.
DR   Pfam; PF08123; DOT1; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51569; DOT1; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU271113}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU271113};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU271113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU271113};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU271113}.
FT   DOMAIN          19..336
FT                   /note="DOT1"
FT                   /evidence="ECO:0000259|PROSITE:PS51569"
FT   REGION          361..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1081
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1106..1191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1259..1297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1310..1348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1371..1427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1495..1518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1572..1592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1624..1672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1724..1754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1783..1822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1860..2034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2087..2187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          687..721
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        362..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..913
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..1004
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1063..1081
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1107..1131
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1183
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1259..1279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1799..1819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1867..2005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2130..2144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2166..2187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2187 AA;  239479 MW;  E6C6C16FCD3201EA CRC64;
     MATPQVKDLV LRSPAGSSDT ITFAWPLQIG HGQDKHDNGI DIIDTIKFVC DELPSISSAF
     EEINLNHIDT ACYKTMTNLV DRFNKAVDSI VALEKGTSLP AERLNKFAHP SLLRHILQLV
     YNAAVLDPDK LNQYEPFSPE VYGETSYELV QQMLKHVNVS KEDTFIDLGS GVGQVVLQMA
     GSFPLKTCIG IEKADTPARY AERMDQIFRQ YMSWFGKRYC EYKLIKGDFL VDEHREKITS
     STLVFVNNFA FGPTVDHQLK ERFADLRDGA RVVSSKSFCP LNFRITDRNL SDIGTIMHVS
     EIPPLKGSVS WTCKPVSYYL HVIDRTILER YFQRLKTKGG DHEHVGTVRT TRDRAKREAN
     IGHQNNNHNN NNNHNNNHQR EQREQQRERE RDLFNGPAQQ RNQSQSPANV SGGGGLAASK
     TRQQLASAQH QQQQQQQQQQ MQQRSLDMDS STESDGEGEA TNGNGGNTTT ATTSTSNGPM
     TRKVWSDWCS SKGKSSQSDD EENNNSNSNN SNSHQGRGPR AITTLKKRKK LTRKAAIASK
     SAAAAQREAE EAAAVAAVTA SATSASASKD SSSKEDQPRA ASAGPGRKGR LKKGQRGRKC
     LKIAGLDVLH KQTVLSTSLD AMTKKLPAAP GTVDQQLTSL LTGDMSHREL DIPTAPQDTP
     YALQILLDVF RSQYMTMIEH MRSSAYLPQV QKQIAQEQER MARLKNRANQ LDKQIKVLID
     DSVTLLKVRM NELGINVNSP NDLIAQAKEI VGRHKDLQHA VSKMRNEVTV YESEQKLLLS
     KQLKHLPEYQ KLCAVANGGN GKVKLELPHE LSETAAQELV LKEIANTLSQ RKKLYAQVST
     IEQETSSLQK SAEERSTANV LLAQGTNISL ASSAPTVATN AATTATLANC NKLVNNKSSR
     RSREHRARSQ EWPEVPEVGK IQESNPEVLA QKILETCRQV EAGKFQPPPS TISAVNFING
     QKPKMEPKTT PAPYKDSTLM PAPKQQSQPQ QQQQQLQQQQ QQQHHAVLLP KCELPGLGRK
     QESPKVANFE DRLKSIITSA LNEDQEQRSK AMPIMETPAV PLQSPVSKRS KQMGQTTTTT
     GNSLHNIITV STQGLMHLNA NTTISPITPP LPGPRAAAAA STAPPPPANL PYGSAYMSSK
     QQQLQHLSGK YGQTVSLKES KYSPARPGAS APPPPPPPPP TSSSASSSSS SSSAAHMATL
     YAGHGSTAAT APTVADLGFH RRRASVSANS YEHFMVQQQQ QQQHALMLAH VAQQRLQHQQ
     QQQQQQQQQQ QQQQQHAQHA PIGHLHHHHH QAAGTSAEFK APAENLLQRS GSREQLSEQQ
     QQQQQQQQQL QQQHQHQHQQ SQQQQPHSLD LLPRASSANS DYAGYRVERL SVRPPSRPSS
     NSSQPDYTQV SPAKMALRRH LSQEKLSQPP QALPTPPPMS LAPPVTAGKT IGDLVNGEIE
     RTLEISHQSI INAAVNMSTG SSSSSSSAHF MERAFLAERT NDRLLINLNA QRPERVHVRP
     LGEDAPDPQP TNYSQAASSS NNNLATLAHV AYAHKTQPGA RASSSSRSGR DYQPVALPRA
     EMMGCIEAYF HEEQQQQQQQ QQQHQKSKST VGGASALRAP RLNGANPPLE GLAASLQDHV
     RARKYKEENE ERQRRAAAAS SSSSLELAPH FAHQAPPAHS YHQPQQQPHH HTAASIINGT
     PHKVELGVKR SSPLAPHQQP SRPAKLAHFE QQPLAHAHQH LYVNSNGVSG LPPPAHDATT
     PSPTPSSSSS SCGRRSKLLV EPPLLMSPEI NSLMGDERPL QLSTSHQQLH HHQQKPHQQQ
     LRGSHQSGHS ITPTIVGGQR SNAADDDDVI AADEESHWQH RVSSGFDRLV AFASTELDKT
     RRSIDGDTVP ASISCNTSPD SGITHSSSNS DAVRTFLSTS SSSSQLELPI NNSSSSSSSN
     NSSSLYASQV HNLSHHTYQH GHQQLQQQQQ QLPLQQQQQQ QQAQQQHPQQ QQQQHLADHL
     SDSSMKSTAS SSLHASSSLK TVSPVDSGAI ESPPLSDVGL PRTPSPSAAS VATPPLAHAP
     SLVNELRIPL KYQRKSKSGS EKHYKKKFCE RNWEYDCDEL LAYSNSSAPP TAADAAGNGP
     PALDVTGGVS ATPPVGLSKS GKSPKEKSSP HHGINTNANA NASFHHHHKS SKFRPKGKDW
     DWSLDSRSNT GEPTANGAGG GANTTSN
//