ID A0A091WQM4_OPIHO Unreviewed; 4874 AA.
AC A0A091WQM4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=N306_13121 {ECO:0000313|EMBL:KFR17400.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR17400.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR17400.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR17400.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK736137; KFR17400.1; -; Genomic_DNA.
DR STRING; 30419.A0A091WQM4; -.
DR PhylomeDB; A0A091WQM4; -.
DR Proteomes; UP000053605; Unassembled WGS sequence.
DR GO; GO:0044666; C:MLL3/4 complex; IEA:InterPro.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15696; ePHD1_KMT2C; 1.
DR CDD; cd15697; ePHD2_KMT2C; 1.
DR CDD; cd22026; HMG-box_KMT2C; 1.
DR CDD; cd15509; PHD1_KMT2C_like; 1.
DR CDD; cd15594; PHD2_KMT2C; 1.
DR CDD; cd15511; PHD3_KMT2C; 1.
DR CDD; cd15596; PHD4_KMT2C; 1.
DR CDD; cd15513; PHD5_KMT2C_like; 1.
DR CDD; cd15600; PHD6_KMT2C; 1.
DR CDD; cd19171; SET_KMT2C_2D; 1.
DR Gene3D; 3.30.160.360; -; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 7.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR041967; KMT2C_ePHD1.
DR InterPro; IPR041968; KMT2C_ePHD2.
DR InterPro; IPR047004; KMT2C_PHD2.
DR InterPro; IPR047003; KMT2C_PHD4.
DR InterPro; IPR047005; KMT2C_PHD6.
DR InterPro; IPR037877; PHD3_KMT2C.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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; PTHR45888:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE 2C; 1.
DR PANTHER; PTHR45888; HL01030P-RELATED; 1.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00628; PHD; 4.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 8.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 5.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51805; EPHD; 2.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50016; ZF_PHD_2; 6.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KFR17400.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFR17400.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 172..276
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 286..336
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 333..383
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 395..465
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 910..963
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 960..1010
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1037..1092
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 4362..4470
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 4734..4850
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 4858..4874
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1808..2333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2558..2661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2678..2700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2724..2876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2892..2927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2951..2992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3172..3193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3325..3367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3431..3502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3520..3868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3983..4010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2335..2362
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3197..3234
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1675..1695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1696..1723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1833..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1881..1932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1980..1994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2017..2032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2093..2112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2113..2139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2281..2329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2573..2602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2626..2644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2685..2700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2725..2769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2770..2792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2793..2808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2843..2876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2892..2917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3325..3340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3431..3465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3520..3551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3581..3610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3620..3664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3665..3683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3700..3718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3752..3770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3771..3799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3800..3835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3840..3854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR17400.1"
FT NON_TER 4874
FT /evidence="ECO:0000313|EMBL:KFR17400.1"
SQ SEQUENCE 4874 AA; 535418 MW; 364BE93B22BDF24E CRC64;
PRSRGKTAVE DEDSMDGLEA AETENTVETE VKEQSAEEDA QTELDSTKQL TPVLQRSVSE
ESASSTASVG VEAKTSEQLC AFCYCGERSS LGQGDLKQFS PTPGYVIPWK NQPLNKSEAS
DSTDGACERT PRQNSVPRRQ RGQKKSRSSI ASCTSVSTQT ASDDQVVKFW DELSLVGLPD
DIDVQALFEP TGHCWAHHRC AEWSLGVCQT EEQLSVNVDK AVVSGSTERC AYCKHLGATI
KCCEEKCTQM YHYPCAAGAG TFQDFSNLSL LCPDHIDQAP ERSKEEANCA VCDSPGDLLD
QLFCTTCGQH YHGMCLDIQV TPLKRAGWQC PDCKVCQNCK HSGEDNKMLV CDTCDKGYHT
FCLQPVMDAV PTNGWKCKNC RVCAECGTRT SCQWHHNCLV CDSCYQQQDN LSCPFCEKLC
LQDFQKDMLH CHMCKRWIHI ECDRSPGGEL ESQLKDYICT LCKQGEGDQT QSCDVMDTSE
LIPEPGSITA CTNEMEIESG DDATFQEQPI TDDGPGQESA VGCVTDGKKE FCSLRKCRYR
ILQRPLPFTK VCGLAPEEKT TELEAEVSAE INSAEMEMSP KKTPASGDSQ TEKMMEVVEG
VQAVTQQELD KQVEETQLPQ GSVEASEVST VDCRSLSSVP ETVTVTPEIQ ETESKGDICI
PVEQQLEIIK VQKDVEKGET HEKSETPALL EVETTSANEV VANNSPVGDK LIKSPAETYP
SLPPSVNINK TNVSSSPDVS LDLHSARDVQ HSQPPALPSA AGSALPTTYI SVTPKIGMGK
PAITKRKFSP GRPRSRQGAW STNNTVSPPS WSPDISEGRD IFKSRQLPGS AIWSIKVGRG
SGFPGKRRPR GAGLSGRGGR GRSKLKNGVG TVVIPGVTTM DVSSNKDEEE NSMHNTVVLF
SNSDKFTLHQ DMCVVCGSFG QGAEGRLLAC SQCGQCYHPY CVSIKITKVV LSKGWRCLEC
TVCEACGKAT DPGRLLLCDD CDISYHTYCL DPPLQTVPKG GWKCKWCVWC RHCGATSPGL
RCEWQNNYTQ CAPCASLSTC PICYRTYRDE ELIIQCRQCD RWMHAICQNL NTEEEVENIA
DMGFDCTICR PYIPPTNVPS LDCCDSSGGA QIISKSKELD PPKTYTQDGV CLTESGMSQL
QSLTVTVPRR KRTKPKLKLK IINQNSVAVL QTPPDAQSEH SRDGEMDDSR EGDLMDCDGK
SDSSPEREAV DDDTKVAEGA DGIKKRKRKP YRPGIGGFMV RQRSRTGQGK TKRSLTRKDS
SGSVSEQLPG RDEGWTEQLP DTPVEESTPA AESTEKIKKR YRKKKNKLEE TFPAYLQEAF
FGKDLLDTSR QNKMSLDNLP EESLPLSCKT NLTTSFLDPS SDPLLSSTSA AAQAKLGPQG
STDDPLADLS EVLNTDDDIL GILSDDLVKS GDHSAGLDIG PISDDPSSLP QPSVNQSSRP
LSEEQLDGIL SPELDKMVTD GAILGKLYKI PELGGKDVED LFTAVLSPAT TQPAPLPQPP
PPPQLMSLHS QAENAFPRVP LMNGLIGPNP HLPHTALAAG GGLGTFSPIT QQPYTDTRDK
NPAFNPMVND PNSSWAPSAP PLEGEGDTMS NAQRSTLKWE KEEALGEMAT VAPVLYTNIN
FPNLKEEFPA YFLVADWATR VKQIAKLWRK ASSQERAPYV QKARDNRAAL RINKVQMSND
SMKRQQQQDS IDPSSRIDSD LFKDPLKQRE SEHEQEWKFR QQMRQKSKQQ AKIEATQKLE
QVKNEQQQQQ QQQQQQQFGS QQLLNQSGSD TPSSGIQSPL TPQTSNGSMS PAQQTFHKDL
FTKQQLPAMP TSASSDDVFL KPQAPPPTPT RVPVHDSLSQ SQTPQTSSQQ MFSPGSTNTR
PPSPMDPYAK MVGTPRPAPI NQNFVRRNTV APLDTCAPQP SISRAIQVTE PSGSRPSPVR
DSCSSSPGSS DPYAKPPDTP RPVMASEQFS KPLGVPRSPM VMEQSGKVPL AAGSSDPFTK
PAPRTDTFQR QRVTSADAYA RPPLTPTPTP VDGSSGPFKT PMPPPQSPQD PYASMPTTPR
RVAVDPYERP ALTPRPVDNF SHNQPNDPYS QPPFTPHPAI KETFAHPPRV VRQQSDSFPQ
SGPVSRPASQ DPYSQPPGTP RPTTVDPYMQ QPPTPRPAQP ADLFAHSPAN QRHSDPYAQP
PGTPRPVLSD PYSQQPATPR PGIPEGFNRP AMTRPGLIPN RDPFLQAPRN RLQGTFVRPS
DPCSQTPRPA GPAITDSFSH SPAAPAHDPY DQPPMTPRPQ PESFGTGQLA HDAAEQPRPG
SEGSFNASGN SPMSSQGQQF PKVSQVPGPA PTTGVTDTQN TMNMSQADTE KLRQRQKLRE
IILQQQQQKK NAVRQEKALQ DAAAPTHATP LQHWQQDNLN QIFNRPPPPY PGNIRSSVVP
PGGPRFPVYP KDQRGPFPGD GQFNRPQFPG DMNAMGMRPH GLRYGFPGGG HGPPSGQERF
LSPQQPMQRP GVPPQLRRSL SIDMPRPVNN PQINNTSGIS QHFPPQGIPV QQHNILGQAF
IELRHRAPDG RPRLPFNPSA ANIMDAAAQH QRHAGFIPRQ EFPGPRQAEP MRHNSQGIPN
QLQMSTSLEH MSQSQQDQIN PDNPPPLVIR SLSHPPIADA FPGPSLSTPA PSNESANLQL
PNQPSDGLEE KLDPDDPAVK DLDVKDLDGV EVKDLDDEDL ENLNLDTEDG KGDELDTLDN
LETNDPHLDD LLRSGEFDII AYTDPDLDVG DKKGMFNEEL DLSVPIDDKL DIQGKTEEPK
QKEQDDKTVS PSETQSPQKK SATENEIKTE VLSPNTQEEK KNENEKSDGN AESTSTQQAA
EVELKDGEKA SAQPPNPECP DRTTPVPSQE TTVPSPDAQG STPLPVQGAV SSCSISGSTP
VLSSLLANES SDNAEARTLG SPSQSLPTPQ MNHAPGIPQT LMTPGGQILE NTLNSNLTMV
PRINHNFSQG SPNPGFIQGQ SSNHSFGTGQ TSNQTVAVTN RPGPSGISGP QQIMLPQPLA
QQQNRERPLL LEEQPLLLQD LLDQERQEQQ QQRQMQAMIR QRSEPFFPNI DFDAITDPIM
KAKMVALKGI NKVMAQSNMG MPPMVMNRFP FMGQPVPGAQ TSEGQNHMQQ AITQDGSLTP
QISRPNPPNF GPGFVNDSQR KQYEEWLQET QQLLQMQQKY LEEQIGAHRK SKKALSAKQR
TAKKAGREFP EEDAEQLKHV TEQQSMVQKQ LEQIRKQQKE HAELIEEYRI KQQQQCGMAP
HAMMPGVQAQ PPMVPAGTSP AMNQQNFPMV AQQLQHQQHA VVIPGQSNPT RMPNLSGWQS
ANAPASHISI NPARMQPPMT PMPITPGTPA PVPGPNTTAQ SGPPPRVEFE DNNPFSESFQ
ERERKERLRE QQERQRIQLM QEVDRQRALQ QRMELEQHSM IGPELNNKTS LSQIPFFNSD
LPCDFIQTPR PLQQSPQHQQ QQMGQILQQG AVTSPPATNF VQSSERRPGG PAAFGPDASA
VPGGAPSFHN VKQTHGNLPG ATFTQNQVRP LLVPAVPSST VLSSGAPCGS DTSVPQAANF
PGSSQSLIQL YSDIIPEEKG KKKRTRKKKK DDDAESIKAP STPHSDITAP STPTISDSTS
TPAVNTPNEL SHHQDEQDSV ELTGPSTSNA AESQTSPELE CKLPDSSLPQ KQPSVNTETE
KAKADTPTSI QEVKLEKAET DQCSGQAEPK PENTNSIKVE EDKVTSQPAS SAQSPAQPAS
VPAAKGESGN ELLKHLLKNK KSSSLLSQKS ENSSRTEEEA SGDKKLTEKQ NPAEGMQTAG
NQMQGAFGCS NSQLQRADVG PETKKQRNKR TQRTGEKAAP RSKKRKKEEE EKQAVYPNAD
TFIQLKQQNN LSNPPTPPAS LPPTPPPVAC QKLVNGFATT EELAGKAGML GGHDVTKALG
PKQFQLPFRP QDDLLARAMA QGPKTVDVPA SLPTPPHNNQ EELRVQDHCE DRDTPDSFVP
SSSPESVVGM EISRYPDLSV IKEENPEPVP SPIIPILPSS TGKGSEAKRN YVKSEPGSGA
LPGSGLFASQ LGPSQNGPKS GLISVAITLH PTAAENISSV VAAFSNLLHV RIPNSYEVSN
APDIPSSMAT VSSHRVNPSM EYRQHLLLQG PQAGAVGPAR IVGSYGLKQP NVTFPANSNG
VAGYKDHSQN VTEGSALRPR WCSHCKVVVL GSGVRKSFKD LPFLKQDSQE GSDKMKDIVF
CSNNCFVLYS AAVQAKNSEN KESVPSLPQS PMKERPPKAF HQYSNNISAL DVHCLPQLQE
KVSPPSSPPI MFPPAFEAAK VEAKPDELKV TVKLKPRLKA IHSSLDDCRP PSKKWKGMKW
KKWSIQIVIP KGSFKPPCEE EIDEFLKKLG TTLKPDPVPK DYRKCCFCHE EGDGLTDGPA
RLLNLDLDLW VHLNCALWST EVYETQAGAL INVELALRRG LQMKCMFCHK MGATSGCHRL
RCTNIYHFTC AIKAQCMFFK DKTMLCPMHK PKGTHEQELS YFAVFRRVYV QRDEVRQIAS
IVQRGERDHT FRVGSLIFHA VGQLLPQQMQ AFHSSKALFP VGYEASRLYW SMRYANRRCR
YLCSIEEKDG LPLFVIKVVE QGHEDLVLTD TTPKGVWDKI LEPVASVRKE SEMLQLFPGY
LKGEDLFGLT VSAVARIAES LPGVEACENY TFRYGRNPLM ELPLAINPTG CARAEPKMST
HVKRFVLRPH TLNSTSTSKS FQSTVTGELN APYSKQFVHS KSSQYRKMKT EWKSNVYLAR
SRIQGLGLYA ARDIEKHTMV IEYIGTIIRN EVANRKEKLY ESQNRGVYMF RIDNDHVIDA
TLTGGPARYI NHSCAPNCVA EVVTFERGHK IIISSSRRIQ KGEELCYDYK FDFEDDQHKI
PCHCGAVNCR KWMN
//
