ID   B3MTV1_DROAN            Unreviewed;      3708 AA.
AC   B3MTV1;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Histone-lysine N-methyltransferase trithorax {ECO:0000256|PIRNR:PIRNR010354};
DE            EC=2.1.1.355 {ECO:0000256|PIRNR:PIRNR010354};
GN   Name=Dana\GF23177 {ECO:0000313|EMBL:EDV30232.1};
GN   Synonyms=dana_GLEANR_7841 {ECO:0000313|EMBL:EDV30232.1};
GN   ORFNames=GF23177 {ECO:0000313|EMBL:EDV30232.1};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV30232.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV30232.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV30232.1}, and Tucson
RC   14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [2] {ECO:0000313|EMBL:EDV30232.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV30232.1};
RX   PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA   Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT   "Assembly reconciliation.";
RL   Bioinformatics 24:42-45(2008).
RN   [3] {ECO:0000313|EMBL:EDV30232.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV30232.1};
RG   FlyBase;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone methyltransferase that methylates 'Lys-4' of histone
CC       H3 (H3K4me). H3K4me represents a specific tag for epigenetic
CC       transcriptional activation. Functions in segment determination through
CC       interaction with genes of bithorax (BX-C) and antennapedia (ANT-C)
CC       complexes. Acts as an activator of BX-C. Involved in the very early
CC       regulation of homeotic genes expressed only in the posterior region of
CC       the embryo. {ECO:0000256|PIRNR:PIRNR010354}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC         COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH902623; EDV30232.1; -; Genomic_DNA.
DR   EMBL; CH902623; KPU72747.1; -; Genomic_DNA.
DR   RefSeq; XP_001964436.1; XM_001964400.2.
DR   RefSeq; XP_014760807.1; XM_014905321.1.
DR   SMR; B3MTV1; -.
DR   STRING; 7217.B3MTV1; -.
DR   EnsemblMetazoa; FBtr0127877; FBpp0126369; FBgn0100171.
DR   EnsemblMetazoa; FBtr0381836; FBpp0342099; FBgn0100171.
DR   GeneID; 6505823; -.
DR   KEGG; dan:6505823; -.
DR   eggNOG; KOG1084; Eukaryota.
DR   HOGENOM; CLU_000099_0_0_1; -.
DR   OMA; DTKMMEC; -.
DR   OrthoDB; 5490909at2759; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IEA:EnsemblMetazoa.
DR   GO; GO:0044665; C:MLL1/2 complex; IEA:EnsemblMetazoa.
DR   GO; GO:0005704; C:polytene chromosome band; IEA:EnsemblMetazoa.
DR   GO; GO:0008023; C:transcription elongation factor complex; IEA:EnsemblMetazoa.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140949; F:histone H3K9 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IEA:EnsemblMetazoa.
DR   GO; GO:0106363; F:protein-cysteine methyltransferase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001654; P:eye development; IEA:EnsemblMetazoa.
DR   GO; GO:0008354; P:germ cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0007482; P:haltere development; IEA:EnsemblMetazoa.
DR   GO; GO:0007507; P:heart development; IEA:EnsemblMetazoa.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:EnsemblMetazoa.
DR   CDD; cd15664; ePHD_KMT2A_like; 1.
DR   CDD; cd15506; PHD1_KMT2A_like; 1.
DR   CDD; cd15508; PHD3_KMT2A_like; 1.
DR   CDD; cd15489; PHD_SF; 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; 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; IPR016569; MeTrfase_trithorax.
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; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
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; PF00628; PHD; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   PIRSF; PIRSF010354; Methyltransferase_trithorax; 2.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00508; PostSET; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51543; FYRC; 1.
DR   PROSITE; PS51542; FYRN; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   3: Inferred from homology;
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:UP000007801};
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:PRU00146}.
FT   DOMAIN          739..849
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          1264..1344
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1341..1390
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1418..1479
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1724..1832
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          3570..3686
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          3692..3708
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1203..1227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1542..1561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1984..2010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2060..2102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2168..2193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2639..2658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2865..2884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3039..3086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3332..3369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3462..3488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..553
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        965..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1063
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1120..1155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1203..1224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1542..1560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1984..2004
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3039..3071
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3072..3086
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3462..3485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         3580
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         3582
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         3624
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         3647..3648
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         3650
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         3696
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         3698
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         3703
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ   SEQUENCE   3708 AA;  397280 MW;  299F76CCBF9F853E CRC64;
     MGRSKFPGKP SKSINRKRIS VLQLEDDQPQ QQPETQPDSQ PDTQQQQQQQ TSSGSGAGSL
     TAREKGNNCD KDEDDNAPGG ASSTGGNNAS SSSASSSEST GNGNSSASGS SSGSTNGGSV
     NGASSHKNAA NSDKEHQGEA KDGDKGRTKT APLGGAASLG GKSSRTSSGS SASGAAFEKC
     AGGKGAKPPT GTASGKSCGS GSVISIEISS GKQSEAASPR ALAGLSPGAS SASSSGLASP
     GGSSSGSFAL SAALLRARKG SNKKFKNLNL ARAEVMLPST SKLKMQQQQE LNGPGAAGSG
     SSSAPSPSSA ETAGMGLANP FAGEAGEDAA LKRRLADMPH EVASETASTS SGSAGNDAAA
     GATTTAGAGP SGSAAGCSPK PGQAAAATGS GPGPAKQKKT VTFRNVLETS DDKSVVKRFY
     NPDNRIPLVS IMKKDSLNRP LNYSRGGECI VRPSILSKIL NKSSNIDKLN SLKFRSAPSS
     SGKSSESPNV FGLSRAFGAP MDEDEEESGG VTFRRNDSPP GQKIDDDDDD MDEDEDEEEG
     NLDEEDNEQE DIDEGVSEKS AETDRNGRES EERDSEEKQL VMDSHFVLPK RSTRSSRIIK
     PNKRLIEDGA ISKKSAPSSS DSKSKSLFGA PAPSTSSTSA AGFSSFGSLK LNSNTSGSGS
     GSGSGSGSGS FVLRQPRLRF QTDSKPVPFG SAAATKSSCP TSPSAIQTPA SSLAMTSFGT
     LATSSSSPNP NPAAGSAGSS TCSVCSTSVS SKEVAQPRKY GVVACDVCRK FMSKMTKKSI
     SANSSSPNAA GSSGGQQHLQ CKGAEGSACS ILTAKSQLKN FKKLYKERCT ACWLKKCVNS
     FQLPAAHRSR LSAILPAAMR VDVSSREDKS TELLSPTGSI RFTAPSALSS SSVAASTSVK
     WKSSGDSSSS ALASIKSNPL AENNVTFGST PLLRPAILEK PLFLKISNAA DQKLGANEVG
     CPSPSRKAKQ DEEKEKEKEK EKEKAKDQDV GDKLLSPTLS ASKKPPSAEN PIPEAQKEEA
     QSSTTTMQAG TLNGTSQATN QSEANGDSNP NSNANATSSG ETLKRQRIDL KGPRVKHVCR
     SASIVLGQPL ATFGEDQEAE EEAEVQKEAV VPVPSESSAQ KPEPVVTDEN DNCASCKTHP
     SDGSNASQAS GSNQGEARKV APAGKENVTV AKAEPAAPSV PAKVATRNAT VASNMNVVAT
     KKQRNGDITS SSVTQTSNLS QGRRTKEQRQ QRTLISIDFW ENYDPAEVCQ TGFGLIVTET
     VAQRALCFLC GSTGLDPLIF CACCCEPYHQ YCVQDEYNLK HSSFEETTLM GSLLETSVTA
     VGSSSSLNQL TQRLNWLCPR CTVCYTCNMS SGSKVKCQKC QKNYHSTCLG TSKRLLGADR
     PLICVNCLKC KSCSTTKVSK FVGNLPMCTN CFKLRKKGNF CPICQKCYDD NDFDLKMMEC
     GDCRQWVHSK CEGLSDEQYN LLSTLPESIE FICKKCARRN ESSKMKAEEW RQAVMEEFKV
     SLYSVLKLLS KSRQACALLK LSPRKKLRCT CGAAGKLQPK ALQFSSGSDN GLGSDGESQN
     SDDVYEFKEQ QQRNMNQNKS RVGKSLSCSC QQPISQPQSF SLVDIKQKIA NNSYVSLAEF
     NYDMSRVIQQ SNCDELDIAY KELLSEQFPW FQNETKACTD ALEEDMFESC AGGNYEDLPD
     GAGGSSVYND HSTSQGESRS GVLDIPIEEV DDLGSCGIKM RLDSRVCLFC RKSGEGLSGE
     EARLLYCGHD CWVHTNCAMW SAEVFEEIDG SLQNVHSAVA RGRMIKCTVC GNRGATVGCN
     VRSCGEHYHY PCARSIECAF LTDKSMYCPT HAKNGNALKA NGSPSVTYES NFEVSRPVYV
     ELDRKRKKLI EPVRVQFHIG SLEVRQLGTI VPRFSDSYEA VVPINFLCSR LYWSSKEPWK
     IVEYTVRTTI QNSSSSTLTA LDVGRNYTVD HSNPNGKEVQ LGLAQIARWH STLARSDLLE
     SNGTDWNGDF ANQNSCVPPD ENTEEEPQQQ ADLLPPEIKD AIFEDLPHEI LDGISMLDIF
     MYDDLADKSD LFAISEQSKD GTQAMTSHQA QSQQGQQAGG GSVSICDEDT RNSNTSLGNA
     WPASNPVEDA MLSAARNSSQ VQMLKTLAWP KLDGNCAMAT AIKRRKLSKN LAEGVILTLS
     SQQRSKKEMA TVAGVSRRQS ISETSTEASS SSSVRSKSFT WSAAKRYFEK SEGREEAAKM
     RIMQMDGVDD SITEYRIIAD GNLSTAQFTG QLKCERCQCT YRNYDAFQRH LPGCEPAMST
     NDTESEVNAT GTTTNATHLS AESLNELQKQ LLANAGGLNY LQTAAAATTF PQVQSLGSLG
     QFGLQGLQPL QLQPQSLGNG FFLSQPNPAP SQSNGTEELQ IYANSLQSLA ANLGGGFTLA
     QPTVTAAPQP QLIAVSTNPD GTQQFIQIPQ TTAPAATYQT LQATNTDKKI VLPLSTAGKP
     LKTVATKAAQ QAAAKQKQLK SGHQVKPIQA KLQPHPQQQA TQVQQAQPIT VMGQNLLQPQ
     LLFQSSAQAQ TPQLILPQTQ PQNIISFVTG DGSQGQPLQY ISIPTGGEYK PQPQPTATPT
     FLTTAAPGAG ATFLQTDASG NLMLTTAPTN SGLQMLTAAP LQSQPQVIGT LIQPQTLQLS
     GATDGSQPGA SQQSLILGGT SGGGTTGLEF ATTTPQVILA TQPMYYGLET IVQNTVMSSQ
     QFVSTAMPGV LSQNASFSAT TTQVFQASKI EPIVDLPAGY VVLNNPTDGT GAGTFLNAAS
     VLQQQQSQDD LLQNANFQFQ AVPSSSSSAT LDYSAPLVVT AKIPPVTQMK RANSNAGKAA
     GVSGVSKVPP QVVNKVLPTS IAAQQSQVQL KNTTSGNLKH TVKGKAVSQT GTNCGAPPSI
     ASKPLQKKTN LIRPIHKLEV KPKVMKPAPK VHVQNHAILQ QQQQQQTVPQ QQPAAPKITI
     TQQRIPVQTQ QQQPQPTQLL QISQPLHQQP QPVHVPQQQL QVQVQPSMPI ITIAEAPALQ
     TQFVIDQQEL VNQQEMVNRA QHFAGSSTSN SLPTNVVNPL QQQAPPTTNI STTRPTNRVL
     PMQQRQDPNP PTIESPVMPS PTPPKPLEQQ VIQQITSASA PKCYMPKTVS PIYEAELKTV
     TGLDSIVPSN VDCEIMEQPV TESIYTEGLY EKHSPSDAKT EQLIIQQQQR EQLTQHLANN
     SFLLEKHTFE VDAMDTDSYR DDDLEDEDDE EDDFSLKMAA SVGNDHEMSD TEEPAVKDKI
     SKILDNLTND DCADSIATAT TAEVEASAAG YQQMVEDVLA TTAAASSAPT EEFEGTLETA
     AVEAAASYIN EMAEAHVLEL KQLENGVELE LTRRKGEPQK QESVAKQQVK VPTAAAPEPP
     PPIREPKKIS GPHLLYEIQS EDGFTYKSSS ISEIWEKVFE AVQVARRAHG LTPLPEGPLA
     DMGGIQMIGL KTNALKYLIE QLPGVEKCSK YTPKYHKRNG NVSTAANAGH GGSTGGGNAS
     LASNGDPQAL LDYGSDQDEL QENAFECARC EPYSSRSDYD MFSWLASRHR KQPIQVFVQP
     SDSELVPRRG TGSNLPMAMK YRTLKETYKD YVGVFRSHIH GRGLYCTKDI EAGEMVIEYA
     GELIRSTLTD KRERYYDSRG IGCYMFKIDD NLVVDATMRG NAARFINHSC EPNCYSKVVD
     ILGHKHIIIF ALRRIVQGEE LTYDYKFPFE EEKIPCSCGS KRCRKYLN
//