ID F6U6A9_HORSE Unreviewed; 3968 AA.
AC F6U6A9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Histone-lysine N-methyltransferase {ECO:0000256|PIRNR:PIRNR010354};
DE EC=2.1.1.364 {ECO:0000256|PIRNR:PIRNR010354};
GN Name=KMT2A {ECO:0000313|VGNC:VGNC:19493};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000006426.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000006426.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000006426.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000006426.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000006426.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000256|ARBA:ARBA00024515};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000256|ARBA:ARBA00024515};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000256|PIRNR:PIRNR010354};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR010354}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000256|PIRNR:PIRNR010354}.
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DR STRING; 9796.ENSECAP00000006426; -.
DR PaxDb; 9796-ENSECAP00000006426; -.
DR Ensembl; ENSECAT00000008563.3; ENSECAP00000006426.3; ENSECAG00000007743.4.
DR VGNC; VGNC:19493; KMT2A.
DR GeneTree; ENSGT00940000160099; -.
DR HOGENOM; CLU_000208_2_0_1; -.
DR InParanoid; F6U6A9; -.
DR OMA; DTKMMEC; -.
DR TreeFam; TF319820; -.
DR Proteomes; UP000002281; Chromosome 7.
DR Bgee; ENSECAG00000007743; Expressed in oviduct epithelium and 23 other cell types or tissues.
DR ExpressionAtlas; F6U6A9; baseline.
DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042800; F:histone H3K4 methyltransferase activity; IBA:GO_Central.
DR GO; GO:0140945; F:histone H3K4 monomethyltransferase activity; IEA:RHEA.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd05493; Bromo_ALL-1; 1.
DR CDD; cd15693; ePHD_KMT2A; 1.
DR CDD; cd15588; PHD1_KMT2A; 1.
DR CDD; cd15590; PHD2_KMT2A; 1.
DR CDD; cd15592; PHD3_KMT2A; 1.
DR CDD; cd19170; SET_KMT2A_2B; 1.
DR Gene3D; 3.30.160.360; -; 2.
DR Gene3D; 6.10.250.2390; -; 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); 3.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR047219; KMT2A_2B_SET.
DR InterPro; IPR041958; KMT2A_ePHD.
DR InterPro; IPR042023; KMT2A_PHD1.
DR InterPro; IPR042025; KMT2A_PHD2.
DR InterPro; IPR044133; KMT2A_PHD3.
DR InterPro; IPR016569; MeTrfase_trithorax.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR002857; Znf_CXXC.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45838:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE 2A; 1.
DR PANTHER; PTHR45838; HISTONE-LYSINE-N-METHYLTRANSFERASE 2 KMT2 FAMILY MEMBER; 1.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR010354};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR010354-51};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR010354};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR010354};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR010354};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR010354};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR010354};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR010354};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR010354-51};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00509}.
FT DOMAIN 1147..1195
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1430..1481
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1478..1532
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1565..1629
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1705..1750
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1872..1980
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 3828..3944
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 3952..3968
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1665..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1807..1871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2083..2135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2147..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2278..2327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2358..2619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2647..2677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2714..2844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2964..3046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3167..3246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3469..3607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3619..3642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3784..3807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2098..2120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2386..2420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2421..2447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2527..2595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2722..2747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2748..2785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2786..2844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3012..3046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3167..3184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3197..3223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3231..3246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3469..3528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3539..3564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3565..3605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3838
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3840
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3882
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3905..3906
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3908
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3956
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3957
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3958
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3963
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ SEQUENCE 3968 AA; 431089 MW; BAA727A61E9DE97E CRC64;
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRIPALLL PPGPPVGGGG PGAPPSPPAV
AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA
AIGTNLRRFR AVFGESGGGG GSGEDEQFLG FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR
SGSDRNPAIL SDPSVFSPLS KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD
ISELPKGNKE DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QLGRKGVQIV
RRRGRPPSTE RVKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ SPRRIKPVRI
IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK TQVKNIRQFI MPVVSAISSR
IIKTPRRFIE DEDYDPPIKI ARLESTPNSR FSATSCGSSE KSSAASQHSS QMSSDSSRSS
SPSVDTSTDS QVSEEIQVLP EERSDTPEVR PPLPISQSPE NDGNDRRSRR YSVSERSFGS
RTAKKLSALQ SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS
AAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN FRPPPLTPED
VGFASGFSTS GTAASARLFS PLHSGTRFDM HKRSPLLRAP RFTPSEAHSR IFESVTLPSN
RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS PSHSMRTRSG RLSTSELSPL TPPSSVSSSL
SISVSPLATS ALNPTFTFPS HSLTQSGESA EKNQRPRKQT SAPTEPFSSS SPTPLFPWFT
SGSQTERGRN KDKAPEELSK DRDADKSMEK DKSRERDRER EKENKRESRK EKRKKGSEIQ
SSSALYPVGR VSKEKVVGED VATSSSAKKT TGRKKSSSLD SGTDIASVTL GDTTAVKTKI
LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK HSTSSIGSML AQADKLPMTD
KRVASLLKKA KAQLCKIEKS KSLKQTDQPK AQGQESDSSE TSVRGPRIKH VCRRAAVALG
RKRAVFPDDM PTLSALPWEE REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA
PQEPPVKKGR RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM
PSKAYLQKQA KAVKKKEKKS KTSEKKENKE SSVVKNLVDS SQKPTPSARE DPAPKKSNNE
PARKPVEDKS EEGNASAPGP EPKQVTTPTA RKSGKQVSQP APVIPPQPPS TAPPRKEVPK
TTPSEPKKKQ PPPPEAGPEQ SKQKKVAPRP SIPVKQKPKE KEKPPPVNKQ ENAGTLNILS
TLSNGNSSKQ KVPADGVHRI RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG
HVEFVYCQVC CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC
RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK
LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCEN LSGTEDEMYE ILSNLPESVA
YTCVNCTERH PAEWRLALEK ELQISLKQVL TALLNSRTTS HLLRYRQAAK PPDLNPETEE
SIPSRSSPEG PDPPVLTEVS KQEDQQPLDL EGVKRKMDQG SYTSVLEFSD DIVKIIQAAI
NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSSNSGM LPNAVLPPSL
DHNYAQWQER EEDSHTEQPP LMKKIIPAPK PKGPGEPDSP TPPHPPTPPI LSTDRSREDS
PELNPPPGIE DNRQCALCLT YGDDSANDAG RLLYIGQNEW THVNCALWSA EVFEDDDGSL
KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR
DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS
DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIVECRPPV VEPDINSTVE HDENRTIAHS
PSSLAEISSK ESHNTAENIS PPSPDRPPHS QTSGSCFYHV ISKVPRIPTP SYSPTQRAPG
CRPLPSAGSP TPTTHEIVTV GDPLLSSGLR SIGSRRHSTS SLSPQRSKLR IMSPMRTGST
YSRNSVSSVS TVGTATDLES STKAVDHVLG PLNSNTNLGQ NTPTSSNLQR TVVTMGTKTS
HLDGSSSSEM KHSTASDLAS KSSSLKGEKT KMLSSKSSEG SAHNVAYPGI PKLAPQVHNT
TSGELNVSKI STYVEHSSAP FSSKETLSFP PVHLRGQRND RDQHTDSNQS ANPPPSEDTE
VKTLKLSGVS NRSSITNEHV GSSSRDRRQK GKKSSKETFK EKHSSKSFLE PGQVTTGEEG
NLKPESVDEV LTPEFMGRPC NNVSSDKIGD KVLSIPGVPK APSLQVEGSA KELQTPRKRT
VKVTLTPLKM ESESQSKNTL KESSPVSPLQ IESASPTEPI SASESPGDGP VAQPSPNNTS
SQDSQSNNYQ NLPVQDRNLM LPDGPKPQED GSFKRRYPRR SARARSNMFF GLTPLYGVRS
YGEEDIPFYS SSTGKKRGKR SAEGQVDGAD DLSTSDEDDL YYYNFTRTVI SSGGEERLAS
HNLFREEEQC DLPKISQLDG VDDGTESDTS VTATTRKSSQ IPKRNGKENG TENLKIDRPE
DAGEKEHVIK SSVGHKNEPK MDNCHSVSRV KTQGQDSLEA QLSSLESSRR VHTSTPSDKN
LLDTYNPELL KSDSDNNNSD DCGNILPSDI MDFVLKNTPS MQALGESPES SSSELLNLGE
GLGLDGNREK DMGLFEVFSQ QLPPTEPVDS SVSSSISAEE QFELPLELPS DLSVLTTRSP
TVPSQNPSRL AVISDSGEKR VTITEKSVAS SEGDSALLSP GVDPTPEGHM TPDHFIQGHM
DADHISSPPC GSVEQGHGNN QDLTRNSSTP GLQVPVSPTV PIQNQKYVPN STDSPGPSQI
SNAAVQTTPP HLKPATEKLI VVNQNMQPLY VLQTLPNGVT QKIQLTSSVS STPNVMETNT
SVLGPMGGGL TLTTGLNPSL PTSQPLFPPA SKGLLPMPHH QHLHSFPAAT QSSFPPNISS
PPSGLLIGVQ PPPDPQLLVS EASQRTDLST TVATPSSGLK KRPISRLQTR KNKKLAPSST
PSNIAPSDVV SNMTLINFTP SQLPNHPNLL DLGSLNTSSH RTVPNIIKRS KSGIMYFEQA
PLLPQRVGGS AATAAGTSTI SQDSGHLTSG PVSGLASGSS VLNVVSMPTT TAPASSASVP
GHVALTNPRL LGAPDIGSIS NLLIKASQQS LGIQDQPVAL PPSSGMFPQL GTSQTPSTAA
MTAASSICVL PSTQTTGITA ASPSGEAGEH YQLQHVNQLL ASKTGLLSSQ RDLDSAPGTQ
GSNFTQTVDA PNSMGLEQNK ALSSAMQASS ASPGGSPSSG QQSASPSVPG PTKPKPKIKR
IQLPLDKGNG KKHKVSHLRT SSEAHIPDQE ANTTPLTSVT GTPGAEPEQQ DTANVEQSSQ
KECGQPAGQV AALPEIQMTQ NPANEQESTE PKTVEEEESN FSSPLMLWLQ QEQKRKESIA
EKKPKKGLVF EISSDDGFQI CAESIEDAWK SLTDKVQEAR SNARLKQLSF AGVNGLRMLG
ILHDAVVFLI EQLSGAKHCR NYKFRFHKPE EANEPPLNPH GSARAEVHLR QSAFDMFNFL
ASKHRQPPEY NPNDEEEEEV QLKSARRATS MDLPMPMRFR HLKKTSKEAV GVYRSPIHGR
GLFCKRNIDA GEMVIEYAGN VIRSIQTDKR EKYYDSKGIG CYMFRIDDSE VVDATMHGNA
ARFINHSCEP NCYSRVINID GQKHIVIFAM RKIYRGEELT YDYKFPIEDA SNKLPCNCGA
KKCRKFLN
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