GenomeNet

Database: UniProt
Entry: A0A182QTC3_9DIPT
LinkDB: A0A182QTC3_9DIPT
Original site: A0A182QTC3_9DIPT 
ID   A0A182QTC3_9DIPT        Unreviewed;      3067 AA.
AC   A0A182QTC3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Histone-lysine N-methyltransferase {ECO:0000313|EnsemblMetazoa:AFAF016439-PA};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF016439-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF016439-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF016439-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AXCN02001534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 69004.A0A182QTC3; -.
DR   EnsemblMetazoa; AFAF016439-RA; AFAF016439-PA; AFAF016439.
DR   VEuPathDB; VectorBase:AFAF016439; -.
DR   OrthoDB; 5490909at2759; -.
DR   Proteomes; UP000075886; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043933; P:protein-containing complex organization; IEA:UniProt.
DR   CDD; cd19170; SET_KMT2A_2B; 1.
DR   Gene3D; 3.30.160.360; -; 2.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR047219; KMT2A_2B_SET.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45838:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE TRITHORAX; 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; PF00856; SET; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 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.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          812..920
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          2929..3045
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          3051..3067
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1187..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2078..2097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2137..2180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2364..2388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2463..2493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2518..2546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1187..1211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2463..2483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2523..2542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3067 AA;  329389 MW;  ECDC5BC6FB9F2639 CRC64;
     MAATTSTPTA TISGTCEVGS SIGNGHQQSS QQEQQQQQQQ HQQSSQNSNC GARNEKHPAA
     GNGFEMKPST LTSALARRCP PTVASGRVSR QQSPSCEQGA TENSSSGSNP SATGITTSSR
     VPKVDETTEQ STTVGVGGTG STSSKASALM GSKPLTAAST PAAVSTVASI APVKKKSVTF
     HTTLETTDEN IVKKVYNPDT VPLPSIIKKE CLDRPIRLKK SFNRKMKKRL QRAVAAAAAA
     AAAASTSASS AVGGASGAAK TMECLVRPSR LTEIMLKSSN KPSTGGGVAM SLDRSSGSVG
     GLGFGLKALE SAKSGLAFGT SRETGAQAVA ITTEAGSDAI GRNLESGGTQ FGDKRFILPK
     RSVHSSRVIK PNKRFLDEFE LEIKKKNKNL AAAAAVAAAA AAAEACSTTG TGSISSASAS
     KENTTLDSAG ADGNDADSVI GEETRKKKDK KKCEESADKP SSIAIPGVTS TLSSTTTNTT
     NLSAAASIFG KGILRQPRLQ FATSLLNNNN TADKRQRIDL KGPRVKHVCR SASIVLGQPL
     ATFPEDGSAD APSGEVVNIE TPPSDSAAEP GEDLPLIDRE RHASVNDSST VKQDCSDCID
     PTMALSPPAT PDEVTGAVRA SPAKPEIVPS FDPDTSGSTE KELMIDEDQL PDVEDEKECS
     RKTGGDISLV DIKQKINANE YYSLQDFHYD MNTLLQAVSS EELTVAYKEF LSETFPWFQN
     ETKACTDALE EAMRGEVDQS SSLDRYHSST RTGAMGGDRG GSTDSHNGTS HQLRNNMYPF
     ATTLDQKVPQ VDIPLDDLSD YFHGSEEELL DTRICMLCKQ QGEGMPLHES RLLYCGQNNW
     IHTNCALWSA EVFEEIDGSL QNVHSAVSRG RLIKCCHCGV KGATVGCNVK NCGEHYHFPC
     ARHIGCVFML DKTVYCTSHA IEAQKKRCPE ERNFEIARSV YVELDRRKKR FVEPSRVQFM
     IGSLNVRRLG HVVPTFSDHT DVLIPTDFEC TRLYWSAKEP WKIVSYRIKT SIQSSNYCYG
     TDLGKNFTVD HSSNSSTVQW GLTQIARWHT SLQYCEDQQE EMVDTLDNEA LQQHLISSMS
     STATTMTTTT TTQLLASSRC EPNTVCVGTG DDTNDEEPQN TNDLLPPEIK DAIFEDLPHD
     ILDGISMLDI LPKLMTYEDL LAMDLKSDST FNIDILKDPG ILQGLGNGAG SSTGGSSTTA
     NNVGQSAKNN DHSGMDVEDM TSLHEAIGST VGSELSNDSW AKTIGTPGVE DALLSGLTKP
     ATPSVTNTAV HHRELKRSKS DILEAIAAAG QQQPRGQRSG SFSWNTKQLE STAAAVAKRR
     KIASPITLPH SLASGTGPMT TTTLSTAQGL GGVFSQQPQI FSIGPNGQPQ LMTIAAPQHQ
     QTILQAGVSQ PIGMQQGAKK IVYTTASPKK VMTKLAQQQQ GLKSKRTLAS NGVSKPGIQI
     KTKQQQHQEQ TVTLHPTTNV IGGQSTASQL QTTLTAAPQQ QQQQQIQLIN TSYPLIQRAT
     APTGPHQTSG NVIFQTQSPS NQPILVQQVG GNQISYLADQ GTLTANPVQY QLAPANVLTQ
     NGFAMATTGP DAGTLAAATA NNILIPNGTG GYSLIPAGAL QIATQPQVIG TIVQPQAAAI
     QCGMMATEQM VLGATAAATA SAQPTLEMMV TDPASGCMYL TSPSMYYGLE TIVQNTVMSS
     QQFVSATAMQ GVLSQNSSFS ATTTQVFAAS KIEPIVEMPT GYVVLNNDGT TAQQMQIGTS
     TASVVSQAPT PVQMQTSTSV GANGGQAIFQ QAQLQPTAAV VSSSASGSLP TAHQTTPVVS
     IQQQQQQQQL WKLECSTPST ISIQPNTIAT SSSNSTTSIV TPLKPTMKTI VPKSQPQLVN
     KVMPNTAMKV LSSGNEQTST GTGSMVSVSQ QQKSACFQSI VSSSVYTTAT ALTTSTKVSN
     VIKPITKTTN YTKPKIVAKP VKQKTSPALL SPTSHSPVYQ LSQQQPPTVM ISTQPVQQQQ
     QQLLQNGITL IPATSTSTPV NNASQLVPIK PNVNANGLQT ITANQLTVSA IAQQPPIVIE
     KLPQQVQSVT SSTSVTPISN GISLNNGQMM IIQPNSASVA KKPTQVNGQG SGHVKKQKTM
     LPMNQISYTT AQQLPQQQQQ QQQQQAQPYQ QLMNVSTTQQ QLSGIPQQQQ QQQGQQQQIQ
     SQPIGISQGG KGPLSKKTSS NVGQITLSLA NIGTTNTIGP VPVSMPASTI TITPSQPASI
     TLPTAPYPMP LYSNIPTNVV NPIQQQTNQN TQSSTGNSRP TNRVLPMQAS VMQQKNPEVP
     QTPPPPPLKM LHQQCSEKLD HEFSIIPSPA PFGVSTPSSS PNDVDRMKMS GNEKLLTTGK
     NTNRLEIEIK PIEITPLTSA MMTPTTTNGS CTPSPLPPSS ISQQQEESSL QTELPLEQAT
     MMMEIEEQHQ QQQLHQLNTE QQINETPSFQ FSLSFDGTSG TLIPLDSQQQ TMTAQIEIKP
     ILTSSPRCND GEMQSPQPIL TSNDSIEDDR DTETQRIDEL KHSLEAETQE MLAEGHETSM
     CGDSAGAGSS SGTASPSLND GESDSPEIKD KISEILDNLE QQTNQEVEMQ MQAFDSLGGS
     KEHCSAVTER LVAELREEFH SAVSSPSTAT PAATVPIMSV EQSQTTANLS DQQNLLTMSD
     SMFDNSKKES NINACYRDNI DRSNYAGNTS GDDLNSLLQD GDAESVLFGK IRQPEPSPLS
     QPSPTEHHHQ LHQLDEELQQ FTVQAPTPAP PSAATKPPRS TSPKLLYEIQ SQDGFTYKST
     SIVEIWDKLF EAVQTARRAH GLTPLPEGQL KEMAGVQMLG LKTNAIRYLL EQLPGVEKCS
     QYSPLYHKKQ SSGLGGLGVG ETGTGLAGCN GVADYFDELQ ENVNGTARCD PYKTRSEYDM
     FSWLASRHRK QPMPIVAQNI DDTIIPRRGS GSNLPMAMRY RTLKESSKES VGVYRSHIHG
     RGLFCNRDIE AGEMVIEYAG ELIRSTLTDK RERYYDSRGI GCYMFKIDEN FVVDATMRGN
     AARFINHSCE PNCYSKVVDI LGHKHIIIFA LRRIVQGEEL TYDYKFPFED VKIPCSCGSK
     KCRKYLN
//
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