ID A0A2U4BVY4_TURTR Unreviewed; 3166 AA.
AC A0A2U4BVY4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 29.
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|RefSeq:XP_019797360.2};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019797360.2};
RN [1] {ECO:0000313|RefSeq:XP_019797360.2}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019797360.2};
RG RefSeq;
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 RefSeq; XP_019797360.2; XM_019941801.2.
DR Proteomes; UP000245320; Chromosome 8.
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; 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; 2.
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:UP000245320};
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 342..390
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 626..677
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 674..728
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 761..825
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 901..946
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1068..1176
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 3026..3142
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 3150..3166
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1474..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1842..1874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1911..1962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2133..2261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2398..2443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2667..2804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2816..2842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2982..3005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1045
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1919..1944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1945..1962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2133..2149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2209..2261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2398..2420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2428..2443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2667..2725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2758..2782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3036
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3038
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3080
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3103..3104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT BINDING 3156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT BINDING 3161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ SEQUENCE 3166 AA; 343224 MW; 6F0AC7009EA6F470 CRC64;
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPLVGGGG PGAPPSPPAV
AAAAAAAAGS GGVGVPGGAA AASAASSSSA SSSSSSSSSA SSGPALLRVG PGFDAALQVS
AAIGTNLRRF RAVFGESGGG GGSGELTTQI PCSWRTKGLI HDKKTEPFRL LAWSWCLNDE
QFLGFGSDEE VRVRSPTRSP SGSMLAQADK LPMTDKRVAS LLKKAKAQLC KIEKSKSLKQ
TDQPKAQGQE SDSSETSVRG PRIKHVCRRA AVALGRKRAV FPDDMPTLSA LPWEEREKIL
SSMGNDDKSS IAGSEDAEPL APPIKPIKPV TRNKAPQEPP VKKGRRSRRC GQCPGCQVPE
DCGVCTNCLD KPKFGGRNIK KQCCKMRKCQ NLQWMPSKAY LQKQAKAVKK KEKKSKTSEK
KESKESSVVK SLADSSQKST PSAREDPAPK KSNSEPPPRK PPEDKSEEGN ASTPGAEAKQ
VATPSSRKSS KQVSQPAPAI PLQPPSTAPP RKEVPKTTPS EPKKKQPPPP ESGPEQSKQK
KVAPRPSIPV KQKPKEKEKP PPVNKQENAG TLNILSTLSN GNSSKQKVPA DGVHRIRVDF
KEDCEAENVW EMGGLGILTS VPITPRVVCF LCASSGHVEF VYCQVCCEPF HKFCLEEHER
PLEDQLENWC CRRCKFCHVC GRQHQATKQL LECNKCRNSY HPECLGPNYP TKPTKKKKVW
ICTKCVRCKS CGSTTPGKGW DAQWSHDFSL CHDCAKLFAK GNFCPLCDKC YDDDDYESKM
MQCGKCDRWV HSKCENLSGT EDEMYEILSN LPESVAYTCV NCTEQHPAEW RLALEKELQI
SLKQVLTALL NSRTTSHLLR YRQAAKPPDL NPETEESIPS RSSPEGPDPP VLTEVSKQED
QQPLDLEGVK RKMDQGNYTS VLEFSDDIVK IIQAAINSDG GQPEIKKANS MVKSFFIRQM
ERVFPWFSVK KSRFWEPNKV SSNSGMLPNA VLPPSLDHNY AQWQEREENS HTEQPPLMKK
IIPAPKPKGP GEPDSPTPLH PPTPPILSTD RSREDSPELN PPPGIEDNRQ CALCLTYGDD
SANDAGRLLY IGQNEWTHVN CALWSAEVFE DDDGSLKNVH MAVIRGKQLR CEFCQKPGAT
VGCCLTSCTS NYHFMCSRAK NCVFLDDKKV YCQRHRDLIK GEVVPENGFE VFRRVFVDFE
GISLRRKFLN GLEPENIHMM IGSMTIDCLG ILNDLSDCED KLFPIGYQCS RVYWSTTDAR
KRCVYTCKIV ECRPPVVEPD INSTVEHDEN RTIAHSPTSF AEISPKESQN TAEIVNPPSP
DRPPHSQTSG SCFYHVISKV PRIRTPSYSP TQRSPGCRPL PSAGSPTPTT HEIVTVGDPL
LSSGLRSIGS RRHSTSSLSP QRSKLRIMSP MRTGSAYSRN SVSSVATIGT AADLESSAKA
VDHVLGPLNS NTNLGQNTPT SSHLQRTVVT MGTKTSHFDG SSSSEMKHSS ASDSTSKSSS
SKGEKTKMPS SRNSEGSAHN VAYPGLPKLA PQVHNATAGE LNVSKTGTFA ELSSVPFSSK
EALPFPPLHL RGQRNDRDQQ TDSNQSANSP PDEDTEVKTL KLSGVSNRSS IINEHVGSSS
RDRRQKGKKS CKEMFKEKHS SKSFLEPGQV ATGEEGNLKP EFVDEVLPPE FMGQRPCNNV
SSDKIGDKVH SIPGVPKAPS MQVEGSAKEL QTPRKRTVKV TLTPLKMEGE SQSKNTLKES
SPLSPLQIES ASPTEPISTS EGPGDGPVAQ ASPNNTSSQD SQSNNYQNLP VQDRNLMLPD
GPKPQEDGSF KRRYPRRSAR ARSNMFFGLT PLYGVRSYGE EDIPFYSSST GKKRGKRSAE
GQVDGADDLS TSDEDDLYYY NFTRTVISSG GEERLTPHNL FREEEQCDLP KISQLDGVDD
GTESDTSVTA TTRKGSQIPK RNSKENGTEN LKMDRPEDTG EKEHVIKSSV GHKNEPKMDN
CHAVSRVKTQ GQDSLEAQLS SLESSRRVHT STPSDKNLLD TYNTELLKSD SDNNNSDDCG
NILPSDIMDF VLKNTPSMQA LGESPESSSS ELLNLGEGLG LDSNREKDMG LFEVFSQQLP
TTEAVDSSVS SSISAEEQFE LPLELPSDLS VLTTRSPTVP SQNPSRLAVI SDSGEKRGAI
PEKSVASSEG DSSLLSPGVD PSPEGHMTPD HFIQGHMDAD HISSPPCGSV EQGHGNNQDL
TRNSSTPGLQ VPVSPTVPIQ NQKYVPNSTD SPGPSQISNA AVQTTPPHLK PATEKLIVVN
QNMQPLYVLQ TLPNGVTQKI QLTSSVSSAP SVMETNTSVL GPMGSGLTLT TGLSPSLPTS
QSLFPPASKG LLPMPHHQHL HSFPAATQSS FPPNISSPPS GLLIGVQPPP DPQLLVSEAS
QRTDLSTTVA TPSSGLKKRP ISRLQTRKNK KLAPSSTPSN IAPSDVVSNM TLINFTPSQL
PNHPNLLDLG SLNTSSHRTV PNIIKRSKSG IMYFEQAPLL PQSVGGTAAP AAGAATMSQD
TGHLTSGPVS GLASGSSVLN VVSMQTTTAP TSSASVPGHV ALTNPRLLGS PDIGSISNLL
IKASQQSLGI QDQPVALPPS SGMFPQLGTS QTPTTAAMTA ASSICVLPST QTAGITAASP
SGEAEEHYQL QHVNQLLASK TGILSSQRDL DSAPGTQGSN FTQTVDAPNS MGLEQNKALS
SAMQASSTSP GGSPSSGQQS ASPSVPGPMK PKPKIKRIQL PLDKGSGKKH KVSHLRTSSS
EAHIPDQEAS TTPLTSVTGA PGAEAEQQDI ANVEQSPQKE CGQPAGQVAV LPEIQTTQNP
ADEQENSEPK TAEEEESNFS SPLMLWLQQE QKRKESIAEK KPKKGLVFEI SSDDGFQICA
ESIEDAWKSL TDKVQEARSN ARLKQLSFAG VNGLRMLGIL HDAVVFLIEQ LSGAKHCRNY
KFRFHKPEEA NEPPLNPHGS ARAEVHLRKS AFDMFNFLAS KHRQPPEYNP NDEEEEEVQL
KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL FCKRNIDAGE MVIEYAGNVI
RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR FINHSCEPNC YSRVINIDGQ
KHIVIFAMRK IYRGEELTYD YKFPIEDASN KLPCNCGAKK CRKFLN
//
