ID H2LU33_ORYLA Unreviewed; 4166 AA.
AC H2LU33;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 81.
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|Ensembl:ENSORLP00000009606.3};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000009606.3, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000009606.3, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000009606.3,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000009606.3}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000009606.3};
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 Ensembl; ENSORLT00000009607.3; ENSORLP00000009606.3; ENSORLG00000007666.3.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000160099; -.
DR HOGENOM; CLU_000208_2_0_1; -.
DR TreeFam; TF319820; -.
DR Proteomes; UP000001038; Chromosome 13.
DR Bgee; ENSORLG00000007666; Expressed in pharyngeal gill and 13 other cell types or tissues.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05493; Bromo_ALL-1; 1.
DR CDD; cd15590; PHD2_KMT2A; 1.
DR CDD; cd19170; SET_KMT2A_2B; 1.
DR Gene3D; 3.30.160.360; -; 1.
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; IPR042025; KMT2A_PHD2.
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; 2.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 3.
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; 2.
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:UP000001038};
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 1292..1340
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1602..1653
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1650..1705
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1880..1924
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 2049..2157
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 4026..4142
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 4150..4166
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1999..2045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2264..2296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2346..2480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2497..2621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2645..2692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2711..2792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2817..2872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2939..3057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3173..3210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3235..3296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3437..3480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3727..3862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1859..1880
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2045
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2387..2403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2419..2467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2508..2528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2529..2574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2578..2603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2604..2621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2659..2692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2724..2784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2845..2859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2943..2969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3017..3057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3258..3279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3454..3468
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3727..3760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3762..3776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3777..3808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4036
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 4038
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 4080
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 4103..4104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 4106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 4154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 4155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 4156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 4161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ SEQUENCE 4166 AA; 448653 MW; EFE0159AC4A03B46 CRC64;
MAHSCRWRFP ARPGGSSNSG TGKRAGRIRV TASLRSIPGA QSNTAGLGPG FDAALQVSSV
IGSNLQKFRD VLGESSDSSS AEVSTRQAGT GTAAQEKKPR GRPPRGLTTQ RTAASLSPHS
SLPSPTQAKL EGPELPAEKE KRLPGRPPGT GEKRRGRPPS SSNKKAWSSG NHAADEDSRL
AESELGLDTE GEKDKKAAKK PPAGSAQPHD MEARLSKAGR SEPKVNKLKR LTETKMTPLN
PHLKTVPGVP RRRPGRPPSA ERLKAMTAAA QLCTLVEGGE GKHKAFRVRG GDSSTDQLTS
QQAILKNVDG SDDQVPSSAA ASPPPSKLGK PVGLRKSPRH VKPVRIVPPS KRTDATIAKQ
LLQRAKKGAQ KRLEKEAVAT GGSVVSSSEA GIRKTQLKNI RQFIMPVVST VSLRIIKTPK
RFIEDEGSFG TSTPLAKMPR LETPTSALST SAQTTSATSS SPSPALVSVT VATASSGMTA
PIVSPPHTAS PEPIHAVPSA APSLLNSSSN TANGRFSSSA PSCGSSAVSQ HSSQLSSAES
SRSSSPSLDD SSCDSQASEA TQTLSDQEDN SPSSHGERES SLLQGSQPLS PPSETEPEHV
LSDRSRRGRR AQGVGRGSHK QRVKERLTTR VKKPIISPPT GLLMPSSTIG NSQQASSTAS
SPSSPPPPPS SLLTLTQPPQ SSSSSAAAIS EHLSQPSWMP HPIPPFLPGS PVLSNLSDKR
NRSILREPTF RWTSMSNPKL PCFSSAKYAK EGLIRKPIFD NFRPPPLTLE DVGLLPQGVL
GAGGATAGAF RLPGAGAGTG TRLFGPLHTH HQHPSSTRFD APHAKRSPLL RAPCFTPSEA
HSRIFESVTL PSSSGSSPGS LSPHQNSSSS AQNLRPRRRP VSVAQRSNPR SPSHSMTRRS
SQMGGHVSVG KVTSEMSVLS SSVSSGNPSS LASSLATSAL VPAPFSTFSS VSLSLPAQGT
PESRRGANGT PSLSTPPAAP SPLFSAFPSS AQDTGRGAGK GGKEKAPPEP ATKEKENDFE
KNREKEKENK RDGRKDFEKR NKTIALDDSP NPPSSLFGVD KRDSEGGVLH LSPKKTPGRK
KSTSVDTISD TASSDGRGLH HSSIGKGRPP KKGRLSEKVA ETENVEKDKE KRSMPNQQTP
SLPGQPSGKH QLPVSLLVKQ TEQHPLPDKR IVGLLKKAKD QLIAIKKNKQ KPAEQNKVQG
QESDSSEASV RGPRIKHVCR RAAVALGRNR AVFPDDMPTL SALPWEEREK ILSSMGNDDK
SSVAGSEEAE PQSPPIKPRE TRQKAVQEAP LKKGRRSRRC GQCSGCQVPE DCGVCTNCLD
KPKFGGRNIK KQCCKMRKCQ NLQWMPSKMF LQKQSKDKKD KKKIKLPDKN PVKGPVTESA
PKATPAPPKE DPPCKKSESP PRKLGEEKSK QLPLSKQSSP IPLSTPSPVE PSQASNTVTF
EAESPSLTKE GPKQLPVSSN TSAHSSPSQS TPPQMAQPSQ PSQMAQQQPW PPASQPALTK
ESSPKVSPCE HKKKPQQHSA QQQSPLPTGE RPGRTFPLNT KPTSSSTLNL LSTPSTRDQV
KPRAPCDGVH RIRVDFQRDH DVEKVWEAGG LSLLTSVPIT PRVLCFLCAS SGNVEFVYCR
VCCEPFHLFC LGESERPLQE QFENWCCRLC RFCQACGRQH QKAKQQLVEC DKCRNSYHPE
CLGPNYPTKP TKKKRIWICT KCVRCKSCGA TKPGKSWDAQ WSHDFSMCHD CAKLFAKGNF
CPLCDKSYSD DYYDSKMMEF YSITWHMVAN LSCYCLSDEM FELLSKLPEN IAYTCMKCAE
CHPAEWRSAL EMELQGCIRN VLNALLNSRT STHLLRYRQA VKPPELNPEM EESLPSRRSP
EGPDPPVLTE VAPTTPPGDS PPDLESVEKK MDQGHYRSLL DFNDDIVRII QTAIKGDGGQ
PEGRKANSMV KSFFIRQMER NFPWFKVKES RFWESQKVSA NSGLLPNAVL PPSLDHNYAQ
WQERQELSRA EHPHFMKKII PAPQPKTPGE PDLPASSPPQ PPVLPPPPSL LPDLDDGPEP
PPPPGVTDNR KCVFCFKYGD EKINECGRLL YIGQNEWTHV NCALWSAEVF EDDDASLKNV
HMAVLRGKKM CCERCQKTGA TVSCCFTSCT RNYHFMCARQ CQCTFLEDKK IYCPKHRDVV
SGFEVTRRIL VDMEGINFKR KFLAGLEPES VHMMIGSMKI DCLGILTELS DCKRKLFPLG
YQCSRVYWST LDARKRCVYT CRIIVCDPPV RDSDLKSAMT PEENYTIAHS PPPNADVDFP
DPFESPRRSD TLSPANTPKL RVYTRNRHPS YPPCPRSLGP KLMPSAGTDV EPLECFMSST
FTDNTPHLIK ETGSGKEVNP GSQCKPMSTE NKSSRLAPAG CGQSSPPVGT AVLSGLQRSG
SNKQVDKQGK HGGKDQDVSA SLNFLSHHRP SFNSNTTSIP PPLQKDSVVG KSCSPQKSIT
RKSNEHASGP ATAAAAKTQW LSKASADEDV IKRGTMPLAS PNAASTAKDK HPKVKAAGSR
DVSKDREKNI PNSNSSNKMP LLNNNTKASG SSNTHASSTS FYNSSNNKVL GNSTKAHGKA
QGEKHFNLEG DRSSSKSRDN YSCPERKNSS SLESSLQQLQ QTSLAAETGG NTTVQSYIKQ
AANQLPLASR EKKRSVRLST PTPLKTDKMT DPNGTITAAG ISPSSCHTGT TSSAAAAGQT
THCSVLSALF SSPSASSSDS SESDTRTQAE EHELHKDYSS NKLRDHHSLL TECADDDGPE
DDHNRSLDDK HHEDDSDGSG SAKRRYPRRS ARARSNTFFG LTPLYGVRSY GEEDLPFYGS
GDGAGPVVKR RTGSRKKSAE GQVDGADDIS TSSSSGESGE DDDSGMKQRG KDPYYYNFTR
TIINPGEGLP SIEGLDQCLG RGSQLQRFLK DEEQQQQRVQ EKTETDMLGS LLQQIGQLDG
VDDGSESDTS ICTTSNTTTT ATSTSTPHKI TPKRRGRERH TEKTAAHVSS KEADSCGGAV
SSNTRESRRN QKENCLPLGG SVKSQPQSQA QDPLDTPLTL STDLLKSDSD NNNSDDCGNI
LPSDIMEFVL NTQSMSLPTL GQQSEPLLDE SYVGVDVNRP KDMLFGDFPQ PLASGESGGV
VESSVNSSIS VEEPYLPLEL PSDLSVLTTR SPTVGTSQNH SAGTLISNTS NRTILGLNSD
SETISGEKSG GKKTAGPALS PSENQHNSTA LGNRETQVTE GHMTPEQFIA SPAVGPVNEA
PASQDVPRNP GTPGLPSSPS MPLQGQKYLP ASVTTAGSPS PVPGPGPSQT QVSSPAVIKS
GPDKLIVVHQ QFQPLYVLQT VPNGVTQKIS ATGVMDTASP TVLSSMTLTT GLNTGLSSGQ
PMFPGGGKVL GTIPHPSQIH AFTGPTQTGF QTGIPSTTSG LLIGLPSQAH DQSQILVSEA
GRPHELGPSV AIVSSPSSMN SSPAVLASAH GKKRPISRLP RKSKKASRSR SQPTLAPSDV
APANMTLINL SSPQITASIP GQPSGLVELS TLSSSQRKVP NIIKRKSGGF MYLDPTTLLQ
QRIPGTTQSG IMGHESSTHL IPCTVSGLSP SQSVLNVVSV PPSGSAGLLA PGSVSLSTPV
LGSTEITGPI SNLLFKAGPH GLGLSDQPVV IQSAGTGTLM SQLSSPVQTS IASSICVLPT
QQTITMAVNR QGETEVNNLY LQHQSQPVSR AQTVDSCANN TVALSPSPST PQSPAKGRVV
GVFTQALPSA HSQSSRTTPI VRSSEQRPLN STTAGSGALS EKSKQKVKRS RQSLDSSSGK
KLKASQAEDQ VNKPAGSKDL SSPEPMDTAN VLGNKKSPEG TAAPGKPVGK DKACPVGRGV
SVPVSLPPNK DSNVEDPSTD SKPKKGIIFE ICSEDGFHIR SESIEDAWKC LTDKVKEARS
HARLSDLSFD GVNGLRMLGI VHEAVVFLLE QLCGSKHCRS YSFRFHKPEE SEDPPLNPHG
SARAEIHHRR SVFDMFNFLA SKHRQPPEYR PQEEEEDEGQ LRIIRRASME LPLAVRFKQL
KAMSKETVGV YRSPIHGRGL FCKKTIEAGE MVIEYSGNVI RSVLTDKREK YYDAKGIGCY
MFRIDDYEVV DATVHGNAAR FINHSCEPNC YSRVLTVDGQ KHIVIFASRR ICCGEELTYD
YKFPIEDASN KLPCNCGTKK CRKFLN
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