ID L5MCJ2_MYODS Unreviewed; 3462 AA.
AC L5MCJ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Histone-lysine N-methyltransferase MLL2 {ECO:0000313|EMBL:ELK36344.1};
GN ORFNames=MDA_GLEAN10022466 {ECO:0000313|EMBL:ELK36344.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36344.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KB101600; ELK36344.1; -; Genomic_DNA.
DR eggNOG; KOG4443; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15695; ePHD1_KMT2D; 1.
DR CDD; cd22027; HMG-box_KMT2D; 1.
DR CDD; cd15509; PHD1_KMT2C_like; 1.
DR CDD; cd15597; PHD3_KMT2D; 1.
DR CDD; cd15513; PHD5_KMT2C_like; 1.
DR CDD; cd15601; PHD5_KMT2D; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 6.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR041961; KMT2D_ePHD1.
DR InterPro; IPR047000; KMT2D_PHD3.
DR InterPro; IPR046999; KMT2D_PHD5.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45888:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE 2D; 1.
DR PANTHER; PTHR45888; HL01030P-RELATED; 1.
DR Pfam; PF00628; PHD; 4.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00249; PHD; 6.
DR SMART; SM00184; RING; 5.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 5.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ELK36344.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:ELK36344.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 136..250
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 258..308
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 261..306
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 305..355
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1364..1417
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1414..1464
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1491..1546
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1785..1878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..1993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2128..2149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2181..2674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2688..2862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2946..3071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3125..3165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3324..3356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..928
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..996
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1039
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1091
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..1992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2181..2197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2198..2217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2399..2418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2432..2467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2536..2555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2561..2595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2603..2617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2715..2741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3031..3049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3126..3165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3462 AA; 367608 MW; E6B30472C95D1391 CRC64;
MSEAVALEDI GTLSPKAGCR SPREGPAQSE RGMDSQKPPG EDKDSEPAAD GHAASEESGA
TEADLPNPHV VEVSVPTSGG LRPQEPPQDC SGGPLRRCAL CNCGEPSLHG QRELRRFELP
FDWPRCPVVS PGGNSEHNEA ALPSEDLSQI GFPEGLTPAH LGEPGGSCWA HHWCAVWSAG
VWGKGGPELC GVDKAIFSGI SQRCSHCTRL GASIPCRSPG CPRLYHFPCA TASGSFLSMK
TLQLLCPEHS EGAAHLEEAR CAVCEGPGEL CDLFFCTSCG HHYHGACLDT ALTARKRAGW
QCPECKVCQA CRKPGNDSKM LVCETCDKGY HTFCLKPPME ELPAHSWKCK ACRVCRSCGA
GSAELNPNSE WFENYSLCYR CHKTQGGQPI SSVAEQRSAV CSRFSPPEPG DTPTGEPDAL
YVACQGQPKG GHVTSMQPKE PGPLQCEAKP LGRAGAQLEP QLEAPLNEEM PLLPPPEESP
LSPPPEESPT SPPPEASRLS PPPEESPLSP PPEESPLSPP PESSPFSPLE ESPFSPPEES
PPSPPLETPL SPPPEASPLN PPFEESPLSP PPEELPTSPP PEASRLSPPP EESPMSPPPE
ASRMFPPFEE SPLSPPPEES PLSPPPEASR LSPPPEDSPM SPPPEDSPMS PPPEVSRLSL
LPEVSRLSPP PEESPLSPPP EESPTSPPPE ASRVSPPPED SPTSPPPEDS PASPPPEDLL
VSLPLEESPL SPLPEELQFC PPLEESHLSP TTEERRLSPR PEEPRLSPKP EEPRLSPKPE
EPRLSPRPEE PHLSPGPKEP CLSPKPEELR LSPRREEPCL SPRREEPRLS PRPEELRPSP
RPEEPCLSPR PEEPLGEPSL CSAPEELPLF LPPGEPPLSP VLGEPALSEP GEPPLSPLPE
ELPLSPTREP SLSPQLMPPD PLPPPLSPII TAVAPPALSP LGELEYPFGA KGDSDPESPL
AAPILETPIS PPPEANCTDP EPVPPMILPP SPGSPMGLAS PILMEPLPPR CSPLLQHSLP
PQNSPPSQCS PPALPLSIPS PLSPVEKSME VSHEAEPPEM EVEKAPDPEC PALEPSPTSP
LPSPMGNLSC PAPSPAPALE DFSGLGEDTA PLDGTDTPDS QPEAGQTPGS LASELKGSPV
LLDPEELAPV TPMEVYGPEC KQTGQGSPCE EQEEPRAPVA PIPPVLIKSD IVNEISNLSQ
GDASASFPGS EPLLGSPDPE GGGSLSMELG VSTDVSPARD EGSLRLCTDS LPETDDSLLC
DTGAAVGGGK AEGDKGKRRS SPARSRIKQG RSSSFPGRRR PRGGAHGGRG RGRARLKSTT
SSIETLVVAD IDSSPSKEEE DDDDDTMQNT VVLFSNTDKF VLMQDMCVVC GSFGRGAEGH
LLACSQCSQC YHPYCVNSKI TKVMLLKGWR CVECIVCEVC GQASDPSRLL LCDDCDISYH
TYCLDPPLLT VPKGGWKCKW CVSCMQCGAA SPGFHCEWQN SYTHCGPCAS LVTCPICHAP
YVEEDLLIQC RHCERWMHAG CESLFTEDDV EQAADEGFDC VSCQPYVIKP AAPVAPPELV
PMKVKEPEPQ YFRFEGVWLT ETGMAVLRNL TMSPLHKRRQ RRGRLGLPGE AGLEGSEPSD
ALGPDDKKDG DLDTEELLKG EGGVEHMECE IKLEGPISPD VEPGKEETEE SKKRKRKPYR
PGIGGFMVRQ RKSHTRVKKG PAAQAEVLSG DGQPDEGETV MPADLPAEGP VEQSPADAEE
KKKQQRRGRK KSKLEDMFPA YLQEAFFGKE LLDLSRKALF AVGVGRPSFA LGTPKAKGDG
GSDRKELPTL QKGDDGTEVA DEESRGAEGK ADTPGPEDGG VKASPVPSDP EKPGTPGEGM
LSSDLDRIPT EELPKIESKD LQQLFKDVLG SEREQHLGCG TPGLDGSRTP LQRPFLQGGL
PLGNLPSSSP MDSYPGLCQS PFLDSRERGG FFSPEPGEPD SPWTGSGGTT PSTPTTPTTE
GEGDGLSYNQ RSLQRWEKDE ELGQLSTISP VLYANINFPN LKQDYPDWSS RCKQIMKLWR
KVPAADKAPY LQKAKDNRAA HRINKVQKQA ESQINKQTKV GDMARKTDRP ALHLRIPPQP
GALGSPPPAA APTIFIGSPT TPAGLSTSAD GFLKPPAGTV PGPDSPGELF LKLPPQVPAQ
VPSQDPFGLA PAYALEPRFP TAPSTYPPYP SPTGAPVQPP TLGTSSRPGT GQPGEFHTTP
PGTPRHQPST PDPFLKPRCP SLDNLAVPES PGVGGGKASE PLLSPPPFGE SRKALEVKKE
ELGAASPSYG PPNLGFVDSP SSGPHLGSLE LKAPDVFKAP LTPRASQVEP QSPGLGLRPQ
EPSPAQALAP SPPSHSDIFR PGPYPDPYAQ PPLTPRPQPP APESCCALPP RSLPSDPFSR
VPASPQSQSS SQSPLTPRPL SAEAFCPSPV TPRFQSPDPY SRPPSRPQSR DPFAPLHKPP
RPQPPEVAFK SGPLAHTPLG AGGFPAALPS GPAGELHAKV PSGQPPNFAR SPGTGAFVGT
PSPMRFTFPQ AVGEPSSLKP PVPQPGLPPP HGINSHFGPG PTMGKPQSTN YSVATGNFHP
SGSPLGPSSG STGEGYGLSP LRPQSVLPPP VPDGSLPYPP HGASQRAGIT SPVDKREDPG
AGMAGSLAAP ELPGTQDPGI SSLSQTELEK QRQRQRLREL LIRQQIQRNT LRQEKETAAA
AAGAVGPPGN WGTEPSNPAF EQLSRGQTPF SGTQDKSNLG LPSNKLGGPI LGPGAFPSDD
RLSRPPPPAT PSSMDVNSRE DSHRLAPEGL RGLTASGLPP QKPSAPLAPE LNNSLHPAPN
TKGPTLPPGL DLVSRPPSST ELGRPPPLVL EAGKLPCEDP ELDDDFDAHK ALEDDELAHL
GLGVDVAKGD DELGTLENLE TNDPHLDDLL NGDEFDLLAY TDPELDTGDK KDIFNEHLRL
VESANEKAER EALLRGVEPG PLGPEERPPP AADASEPRLA PVLPEVKPKV EEGGRHPSPC
QFTITNPKVE PAPATTSLGL GLKPGQSVMG SRDTRMGTGP FSSSGHTGAT GGPPAHLLTP
NPLSGPGGSS LLEKFELESG ALTLPGGHAA SGDELDKMES SLVASELPLL IEDLLEHEKK
ELQKKQQLSA QLQPAQQQQQ HSLLSTPGPA QAMSLPHEGS SSTLAGPQQQ LALGLGGSRQ
PGLAQPLMPT QPPAHALQQR LAPSLAMVSN QGHMISGQHG GQAGLVSQQS PQPVLAQKPM
GTMPPSMCMK PQQLAMQQQL ANSFFPDTDL DKFAAEDIID PIAKAKMVAL KGIKKVMAQG
SIGVAPGMNR QQVSLLAQRL SGGTGSDLQN HVAAGSGQER NAGDPSQARP NPPTFAQGVI
NEADQRQYEE WLFHTQQLLQ MQLKVLEEQI GVHRKSRKAL CAKQRTAKKA GREFPEADAE
KLKLVTEQQS KIQKQLDQVG KAGFSLETRS WEEGWHGGQA RG
//
