ID A0A093DE92_CHAPE Unreviewed; 3854 AA.
AC A0A093DE92;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=[histone H3]-lysine(4) N-methyltransferase {ECO:0000256|ARBA:ARBA00023620};
DE EC=2.1.1.364 {ECO:0000256|ARBA:ARBA00023620};
DE Flags: Fragment;
GN ORFNames=M959_12500 {ECO:0000313|EMBL:KFU83737.1};
OS Chaetura pelagica (Chimney swift) (Hirundo pelagica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes; Apodidae;
OC Apodinae; Chaetura.
OX NCBI_TaxID=8897 {ECO:0000313|EMBL:KFU83737.1, ECO:0000313|Proteomes:UP000031515};
RN [1] {ECO:0000313|EMBL:KFU83737.1, ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M959 {ECO:0000313|EMBL:KFU83737.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25504712; DOI=10.1126/science.1251385;
RG Avian Genome Consortium;
RA Zhang G., Li C., Li Q., Li B., Larkin D.M., Lee C., Storz J.F., Antunes A.,
RA Greenwold M.J., Meredith R.W., Odeen A., Cui J., Zhou Q., Xu L., Pan H.,
RA Wang Z., Jin L., Zhang P., Hu H., Yang W., Hu J., Xiao J., Yang Z., Liu Y.,
RA Xie Q., Yu H., Lian J., Wen P., Zhang F., Li H., Zeng Y., Xiong Z., Liu S.,
RA Zhou L., Huang Z., An N., Wang J., Zheng Q., Xiong Y., Wang G., Wang B.,
RA Wang J., Fan Y., da Fonseca R.R., Alfaro-Nunez A., Schubert M., Orlando L.,
RA Mourier T., Howard J.T., Ganapathy G., Pfenning A., Whitney O., Rivas M.V.,
RA Hara E., Smith J., Farre M., Narayan J., Slavov G., Romanov M.N.,
RA Borges R., Machado J.P., Khan I., Springer M.S., Gatesy J., Hoffmann F.G.,
RA Opazo J.C., Hastad O., Sawyer R.H., Kim H., Kim K.W., Kim H.J., Cho S.,
RA Li N., Huang Y., Bruford M.W., Zhan X., Dixon A., Bertelsen M.F.,
RA Derryberry E., Warren W., Wilson R.K., Li S., Ray D.A., Green R.E.,
RA O'Brien S.J., Griffin D., Johnson W.E., Haussler D., Ryder O.A.,
RA Willerslev E., Graves G.R., Alstrom P., Fjeldsa J., Mindell D.P.,
RA Edwards S.V., Braun E.L., Rahbek C., Burt D.W., Houde P., Zhang Y.,
RA Yang H., Wang J., Jarvis E.D., Gilbert M.T., Wang J.;
RT "Comparative genomics reveals insights into avian genome evolution and
RT adaptation.";
RL Science 346:1311-1320(2014).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KN125664; KFU83737.1; -; Genomic_DNA.
DR Proteomes; UP000031515; Unassembled WGS sequence.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 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; 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; 2.
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 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
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:0000313|EMBL:KFU83737.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000031515};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR010354-50};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFU83737.1};
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 1008..1056
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 1290..1341
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1338..1392
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1425..1486
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1568..1613
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1735..1843
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 3714..3830
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 3838..3854
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1672..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1946..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2051..2181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2223..2462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2513..2540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2581..2630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2818..2921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3082..3128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3370..3519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3670..3693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..2002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2011..2031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2054..2105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2118..2165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2237..2262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2269..2285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2331..2345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2391..2412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2423..2462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2587..2612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2613..2630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2818..2833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2899..2921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3370..3414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3423..3443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3467..3513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3724
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3726
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3768
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3791..3792
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3794
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3842
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3843
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3844
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3849
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFU83737.1"
FT NON_TER 3854
FT /evidence="ECO:0000313|EMBL:KFU83737.1"
SQ SEQUENCE 3854 AA; 419906 MW; 4FC7DDCD3478C842 CRC64;
QDEQFLGFGS DEEVKVQSPT RSPTVKSSPR KPRGRPRSSS DRSSAVLSDS SSVCSPSSKS
ETTSMEKVKK KDLKSGEKRR GRPPTLTSVK FKLSQVKDAS DIQKGSKEEK ESLKKIKRSP
STTFQQATKI KKLRTSKLSP LKSKFKPGAK LQIGRNVQIV RRRGRPPSSE RLKTSSTLVI
SSQLEKPQRI RKEKDGTPPP TKEEKTAVRQ SPRRIKPVRI IPSTKRTDAA IAKQLLQRAK
KGAQKKIEKE AAKLQGRKGR TQLKNIRQFI MPVVSAISSR IIKTPKRFIE DEDYDPPIKI
SRLESTPNSR FSATSCGSSE KSSAASQHSS QMSSDSSRSS SPSVDTSTDS QASEEMQTLS
EERSNTPEVH APLPVSQSPE NDNGDRRNRR FSITEGSFGQ RTAKKLSALP SVPQQQSSSS
PPPPLLTPPP PLQPTSSISD HTPWLMPPTI PLASPFLPAS AAPMQEKRKS ILREPTFRWT
SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN FRPPPLTPED VGFTSGFSTP GATAPARLFS
LHSGTRFDMH KRSPLLRAPR FTPSEAHSRI FESVTLPSSV GRTTTGTSAA GVSSRKRKRR
VFSPIRSEPR SPSHSMRTRS GRLSTSDLAT LTPQSSVSSS LTSISVSSLA TSALNSTFTF
PSHSLTQSGE SAERSQRPKK QTSTPAEPFS SGSPTPLFPW FTPSSQTERG RNKDRAAEEL
SKDKDADKSL EKDKSREKDR EREKENKRES RKEKRRKGSE IQSSSALFPV GKMPKDKVVS
EDVAASSSAK KTAGRKKSAA IDPAADVSTA ALVDTATIKT KTSKKGRGGL DKSDLDLSPT
VPPVEKEKAL HLSAASSSTV KHSASSISSM LAQADKLPMT DKRVASLLKK AKAQLYKIEK
SKSLKQADQP KAQGQESDSS ETSVRGPRIK HVCRRAAVAL GRKRAVFPDD MPTLSALPWE
EREKILSSMG NDDKSSIAGS EEAEPLAPPI KPIKPVTRNK AQQEPPVKKG RRSRRCGQCS
GCQVPEDCGV CTNCLDKPKF GGRNIKKQCC KMRKCQNLQW MPSKAYLQKQ AKAAKKKEKK
SKTNEKKESH SGKNQLDSGQ KQAPQTVVSR EDNAVKKSSE PAARKPVEEK HEDGNSSIPV
SEPKQVPASS TRKTGKQASQ PVQLPPSQPL SSGPLKKEAP KLSTSEPKKK QTPQPEIGTE
QSKQKKIAPR PTFPVKQKPK EKEKPPPISK PESSTLNLLS TLTNGSSSKQ KPPTDGVHRI
RVDFKEDCEV ENVWEMGGLG IVTSVPITPR VVCFLCASSG HVEFVYCQVC CEPFHKFCLE
ESERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC RNSYHPECLG PNYPTKPTKK
KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK LFAKGNFCPL CDKCYDDDDY
ESKMMQCGKC DRWVHSKCEN LSDEMYEILS NLPESVAYTC INCTEQHPAE WRLALEKELQ
VSLKQVLTAL LNSRTTSHLL RYRQGSWSLM SPKPPDLNPE TEESIPSRSS PEGPDPPVLT
EVSKQEEQQP LDLEGVKRKM DQGGYISVLE FSDDIVKIIQ AAINSDGGHP EVKKANSMVK
SFFIRQMERV FPWFSVKKSR FWEPNKVTSN SGMLPNAVLP PSLDHNYAQW QEREENNRTE
QPPLMKKIIP APKPKGPGEP DSPTPLHPPT PPISGSDRSR EDSPELNPPP DVEDNRQCAL
CLKYGDDSAN DAGRLLYIGQ NEWTHVNCAL WSAEVFEDDD GSLKNVHMAV IRGKQLRCEF
CQKSGATVGC CLTSCTSNYH FMCSRAKNCV FLDDKKVYCQ RHRDLIKGEV VPENGFEVLR
RVFVDFEGIS LRRKFLSGLE PENIHMMIGS MTIDCLGILN DLSDCEDKLF PIGYQCSRVY
WSTTDARKRC VYTCKIMECR PPVIEPDINS TVEHDDNRTI AHSPVPLTET LPKDSQNTPE
IVNPPSPDRP LHSQTSSSCY YPVVSKGPRI RTPSYPSTQR SPGSRPLPSA GSPTPVTHEI
VTVGDPLLSS GLKSIGSRRH STSSLSQQQS KLRMISPTRA GNAYSRHSVS SVSSMGSSSE
QEPSIKSPDH FVGSLNAGTP SAPVQSCSAS SGSQKTAAAS GSKTYQLDTS QSTEGKHSSS
SDFVAKGVPS KGEKVKTLTS KDPDYSAHGF ASEGNSKMST QATISSGTEI NIKIGTFQES
SGSFSSKEAI SFPPLHQRGP RKDRDQHVEP IQPEKTSVVD EMDAKTFKSA GVNSRSPAAS
EQVVSASRDR RQKGKKLMKD SFKEKHSLKS LTESSQAGGS DEGNLKPEFG NQALATEQMS
QRLCNNIPAE KAGEKSPPLQ GPLKGSSALA DAAPKESQAP RKRTVKVTLT PLKMESENQT
KNAPQESDTE PQSAGAELAG LVEPSSTSGS PEDNSTAQGS PNEAPAQESQ NNAYENLPVQ
DSSLMLQDGT KAQEEGSYKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED IPFYSNSTGK
KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVVSSNTE ERLASHSLFR EEEQCDLPKI
SQLDGVDDGT ESDTSVTATT RKVSQVSKRS GKENGTENLK LDRTEEAGEK VQVTKSSAVH
KTDPKIDNCH PVSRVKAQGQ DSLEAQLSSL ETGRRAHAST PSDKNLLDTF NTELLKSDSD
NNNSDDCGNI LPSDIMDFVL KNTPSMQALG ESPESSSSEL LTLGEGLGLD SNRGKDMGLF
EVFSQQLPTA EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ NHNRLAVISE
SSLSSSGERS MLALPSSESG EKRVTVTEKS ASGEGDSALL SPGVDPSPEG HMTPDHFIQG
HIDAEHIASP PCGPVEQGHG TNQELTRNSG TPGIQVPVSP TVPLQSQKYV PNSTDSPGPS
QISNAAVQTT PPHLKPAAEK LLVVNQNMQP LYVLQTLPNG VTQKIQLTPS VSSAQSVMET
NASVLGPMGS GLTLTTGLNP SLPSSQSLFP PTSKGLLPMS HHQHMHPFTA TQTGFPPNIS
SPSPGLLIGV QPPPDPQLLV SEASQRTDLG TTVSTPAALG KKRPISRLQS RKNKKLAPSG
TPSAIAPPDM VSNMTLINFA PSQISNHPLD LGTLANSTSH RTVPNIIKRS KPGVMYFEQT
PLLPQGGTTS AVGTSPSVIG PDAGHLPAGP VSGLASSSSV LNVVSMQATT APTTGGSVPS
HVLGQSSVTL TSPGLLGDLG SISNLLIKAS QQSLGVQEQH MTLPPSSGMF SQLGASQTPS
TAAMTAASSV CVLPSTQTMG MTVAPSSADP EGSYQLQHMT QLLARKTGLT SSQLDLGAAS
ATTQLSSFPQ LVDAPNNTGL EQNKASSSVM HASSASPGGS PSSGQQSASS SLLGPTKVKP
KIKRIQPSLD KGSGKKHKLS HLWTSSSEAH VPDRGAVAVP QASATGTPPV KADTQDAGSI
DQPSQKQCVQ SAGQTAVLPE SQSTENLANE QESAGSKALE EEESTFSSLL LFWLQQEQKR
KGLGEKKPKK GLVFEISSDD GFQICAESIE DAWKSLTDKV QEARSNARLK QLSFAGVNGL
RMLGIIHDTV VFLIEQLYGA KHCHNYKFRF HKPEEANEPP LNPHGSARAE VHLRQVKSAF
DMFNFLASKH RQPPEYNPND EEEEEVQLKS ARRATSMDLP MPMRFRHLKK TSKEAVGVYR
SPIHGRGLFC KRNIDAGEMV IEYSGNVIRS ILTDKREKYY DSKGIGCYMF RIDDSEVVDA
TMHGNAARFI NHSCEPNCYS RVINIDGQKH IVIFAMRKIY RGEELTYDYK FPIEDASNKL
PCNCGAKKCR KFLN
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