ID B4M2X2_DROVI Unreviewed; 3142 AA.
AC B4M2X2;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=Dvir\GJ19060 {ECO:0000313|EMBL:EDW65147.1};
GN ORFNames=Dvir_GJ19060 {ECO:0000313|EMBL:EDW65147.1};
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:EDW65147.1, ECO:0000313|Proteomes:UP000008792};
RN [1] {ECO:0000313|EMBL:EDW65147.1, ECO:0000313|Proteomes:UP000008792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW65147.1}, 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:EDW65147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW65147.1};
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:EDW65147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW65147.1};
RG FlyBase;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CH940651; EDW65147.1; -; Genomic_DNA.
DR EMBL; CH940651; KRF82049.1; -; Genomic_DNA.
DR RefSeq; XP_002054946.1; XM_002054910.2.
DR RefSeq; XP_015026575.1; XM_015171089.1.
DR SMR; B4M2X2; -.
DR STRING; 7244.B4M2X2; -.
DR EnsemblMetazoa; FBtr0234985; FBpp0233477; FBgn0206205.
DR EnsemblMetazoa; FBtr0435032; FBpp0392041; FBgn0206205.
DR GeneID; 6632145; -.
DR KEGG; dvi:6632145; -.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_000162_0_0_1; -.
DR InParanoid; B4M2X2; -.
DR OMA; TPNQGMH; -.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15557; PHD_CBP_p300; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:EDW65147.1};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDW65147.1};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 456..542
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 885..964
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1615..1687
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1845..2228
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 2230..2278
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 2292..2373
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 456..542
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 2292..2373
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 32..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2099..2144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2678..2703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2754..2833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2971..3108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3121..3142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2070..2097
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 32..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2114..2130
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2769..2833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2971..2989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2997..3042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3043..3065
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3142 AA; 330336 MW; 6D12EC51E42ADAC9 CRC64;
MMADHLDEPP QKRAKIDQST LRFLEENLPD ELVSSNSGWS DQLSTTGGGV NVVSTATGVG
TGGPNKPPTQ GPGSGVVPPQ MNGAGGGGDD GSGNAGSGAA GSQLRQMQHH QHLQHFLQQQ
QQGNKGAGGG MVVPGMNQLG SKSPSLQSPN TGGIQVTTQM GMVNSMPMSI SNNGNNGMNA
IPGMNSIAQG NLGNMVLTNS GGMGTIGGTG LVNTLKQPVA ASLMNAVPGS VGVSSVSGAA
PSQGMHMQNG PMMGRMVGQQ HLLRGPHLMG AGASGGSGPG GVVGVGGGPR MQNPNMQLGQ
INNMPYGVGN YGTPSSNNPQ QQQQLLAQQM AQRGGGGVVA PNMSAGMPQG NRPIGTVVPM
SSLGGDGPPP GSGGLVGNPQ QQQQLAAANA QMNPQQQQQP PSAQQSALGP RAPQPNQLLG
HSQQQQQQPG TSQQQAISSG VASSVSGPAP APGSMSDERK KQIQQHLMLL LHAHKCNRRE
NMNPNREVCS VNYCKAMKAV LAHMATCKQS KDCTMQHCTS SRQILLHYKT CQRSDCIICY
PFRQNHSLFQ NASGAGGGPT GAANASPLQQ QQQQQQLAQG QPQVSQNPSG VGVGVGVGVD
SKQVAQSTGT GGTQNTAIVL PQQQTPGATN VPKSNTDLAQ QQQQQVQQQE LRRFESVGSI
GQVGPVSAGM LGVPGQGMPP GIRMQGTPSV RVLGVQPGAG GAISGGVPVP GQNVLPGAND
VTSLQQQQAQ AAQQGGQLML QGCNTSTGRR RAIPNMVEQQ PNAQQSVQQQ QQLGNIPAPL
SVNVGFNNAN FVGVGEKQQL GSQSDQMAKL KLQAQSQAQV QAHVSVVSAG APGTGNSTAG
ASVLMPADTT GVANSSSSGS NSSNAGAGSA GSAGGAGGAP GSGSDSEKDW RESVTADLRN
HLVHKLVQAI FPTSDPTTMQ DKRMHNLVSY AEKVEKDMYE MAKSRSEYYH LLAEKIYKIQ
KELEEKRLKR KEQHQQQMLQ MQQGGPNSGV VNPTSVPNNS LQQQPGQGVR PIISPMGSGG
GGPSGMVQQQ MRPQAPGMGS GASQQQTAAG QANMVAVAAS MRSHSPGGNM LAIQQQQQRM
QFPQQQQPVQ GNMLVGPSGP SPGGMVANPV LSPFNTQQTM QSASSVGGGP GILTSPVTAQ
QQQQQQQQQQ QQQQQQQFIN ANGSSGGQNS QISEIMKQRL LQQHQQQTNA AMLLPQSPFS
NATPIQQPQQ LQQQSNAFNS PMQQKAQQPP GSVLNNMPPT PTSLDALTAG APNAGAGGIG
SGTVTAPSPS PSFMSNGPIG TPSNNPPSVS SLMQPLSNRA ATPPYIPTSP VPATSASGLA
ASSTPASAAA TCANSGSSSN ISSTSSSVIT TTAVTAVVST PISCASGATQ TSTTATSGNV
NSTPVSSTVL LVARSNSDNT ATGRVMSTSS SLSSQMAALE AAARDNDDET PSPAGANDTN
GSNGGGSSGG GGMSSKGKLD SIKQEDEIKK EFMDDSCGGN GDSSQMDCST GGKGKNVNND
GTSMLKIDLK SEDGAAGDVK IKSEPMDVDE SAVVGGIATG ANGDGGGGSD GKDDINGAID
GVSAGIASDI KIKSETKPMV PEPLAPNAGD KKKKCQFNPE ELRTALLPTL DKLYRQEPES
VPFRYPVDPQ ALGIPDYFEI VKKPMDLGTI RNNILNGKYS DPWEYVDDVW LMFDNAWLYN
RKTSRVYRYC TKLSEVFEAE IDPVMQALGY CCGRKYTFNP QVLCCYGKQL CTIPRDAKYY
SYQNSLKEYG VASNRYTFCQ KCFNDIQGDT VTLGDDPLQS QTQIKKDQFK EMKNDHLELE
PFVDCQECGR KQHQICVLWL DSIWPGGFVC DNCLKKKNSK RKENKFNAKR LPTTKLGVYI
ETRVNNFLKK KEAGAGEVHI RVVSSSDKCV EVKPGMRRRF VEGGEMMQEF PYRAKALFAF
EEVDGIDVCF FGMHVQEYGS ECPAPNTRRV YIAYLDSVHF FRPRQYRTAV YHEILLGYMD
YVKQLGYTMA HIWACPPSEG DDYIFHCHPT DQKIPKPKRL QEWYKKMLDK GMIERIIQDY
KDILKQAMED KLGSAAELPY FEGDFWPNVL EESIKELDQE EEEKRKQAEA AEAAAAANLF
SAEDNEVSGD GKKKGQKKAK KSNKSKAAQR KNSKKSNEHQ SGNDLSAKIY ATMEKHKEVF
FVIRLHSAQS AASLAPIQDP DPLLTCDLMD GRDAFLTLAR DKHYEFSSLR RAQFSTLSML
YELHNQGQDK FVYTCNNCKT AVETRYHCTV CDDFDLCTVC KEKVGHPHKM EKLGFDLDDG
SAPADLKQAN PQEARKQSIQ RCIQSLVHAC QCRDANCRLP SCQKMKRVVQ HTKNCKRKTN
GGCPICKQLI ALCCYHAKHC QEQKCPVPFC PNIKLKLKQQ QLQQKLQQQQ LLRRRVALMS
RTAAPTALPG PAVSGPVVAA GGVGVGVPVV GMSGVAVSQQ VMSGPASILP SSGGGMSPST
VPVPSPVSGA VIAGMTSPHP HQPGIGMKPG GHSPSPNVLQ VVKQVQEEAA RQQVPHGGSF
GKGVPMAPPV MQRPMGVGVP NQGAMGGMVG NQLTGNVGVV PGGGQMPSGG NCNNVLNSNN
LLPMDQWGGG GGPQQRYANN TPNQQGMRQP NQLMQQNIQQ QQMLGIPSNQ LGVGVGVGGS
VGTGQMPVVG AGVSMGGGGA AHGIGLGAPI GAATSGGGVR PPGAQGVGGG GTGGAGPNMV
NGPPLNTQTL AQIMQKIKNN PTNESNQHIL SILKQNPQIM AAIIKQRQQS QINAAAGGAG
GAGGALQAGN GPQTPQQQQQ QQQVMQQQQM QHMMNQQQQG PGPGPQQMGP GQQQQVSLMQ
GAQQPQQGPP HQRMANMQNT AMMLPNLPPG ITNQGGMVPN QNWTKMRYMQ MNQYPPPYPQ
RQRGPHMGVA GQPQFPGGTT GNFNAGSAGN VTGVQVAGTT VGSGAAGTVS DQYSMANAAA
SNMLQQQQTV GGAGVKPVPQ QQQQQMGVIP PGMQQQPMQQ QQQQQMMQAV AAGGGGMTGT
NPQNALPGGS SGPTGPGSNV MGPPTPHTLQ QQLMQTARSS PPIRSPQPTP SPRSAPSPRG
PSASPRAQPS PHHVMSSHSP APQGPHDGLH NHGMHHQSPL PAVPQDVGVS GVSVGVNAGN
VGNAGGSLPD ASDQLSKFVE RL
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