ID   B4PT97_DROYA            Unreviewed;      3750 AA.
AC   B4PT97;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Histone-lysine N-methyltransferase trithorax {ECO:0000256|PIRNR:PIRNR010354};
DE            EC=2.1.1.355 {ECO:0000256|PIRNR:PIRNR010354};
GN   Name=Dyak\GE26459 {ECO:0000313|EMBL:EDW97596.2};
GN   ORFNames=Dyak_GE26459 {ECO:0000313|EMBL:EDW97596.2};
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW97596.2, ECO:0000313|Proteomes:UP000002282};
RN   [1] {ECO:0000313|EMBL:EDW97596.2, ECO:0000313|Proteomes:UP000002282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01
RC   {ECO:0000313|Proteomes:UP000002282};
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:EDW97596.2, ECO:0000313|Proteomes:UP000002282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01
RC   {ECO:0000313|Proteomes:UP000002282};
RX   PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA   Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA   Ashburner M., Bergman C.M.;
RT   "Principles of genome evolution in the Drosophila melanogaster species
RT   group.";
RL   PLoS Biol. 5:E152-E152(2007).
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}.
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DR   EMBL; CM000160; EDW97596.2; -; Genomic_DNA.
DR   RefSeq; XP_002097884.2; XM_002097848.2.
DR   KEGG; dya:Dyak_GE26459; -.
DR   eggNOG; KOG1084; Eukaryota.
DR   HOGENOM; CLU_000099_0_0_1; -.
DR   OrthoDB; 5490909at2759; -.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0035097; C:histone methyltransferase complex; IEA:InterPro.
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:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 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; IPR013088; Znf_NHR/GATA.
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; 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; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00508; PostSET; 2.
DR   SMART; SM00184; RING; 4.
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   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR010354};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR010354};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
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          775..900
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          1281..1362
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1359..1408
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1436..1497
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1749..1857
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   DOMAIN          3612..3728
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          3734..3750
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          998..1086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1108..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1224..1244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1560..1600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2006..2035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2107..2127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2499..2523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2661..2686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2899..2923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3050..3097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3107..3126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..607
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1015
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1065
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1148..1172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1224..1238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2107..2122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2899..2921
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3112..3126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         3622
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         3666
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         3689..3690
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-50"
FT   BINDING         3692
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         3738
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         3740
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
FT   BINDING         3745
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR010354-51"
SQ   SEQUENCE   3750 AA;  402114 MW;  911CA37C92DB657D CRC64;
     MGRSKFPGKP SKSINRKRIS VLQLEDEAAN PAETQQPPPE SQQPSGSGSG SPAAREKGNN
     CDNDEDDNAP GGASTSGNTA SSSAGSENSG NGSSSGSGSG SGSSGSGSSG SGTTNGGSVN
     GGTHHKSAAN LDKEAVTKDQ NGDGDKTRGN VSRSDASMSS APSGKLSAAA SGKASSKSPR
     TFSASNSGSS SGRSSGSSPE GNSGASSDGA SSGISCGKST AKFPETSSGT SSSGKLAKTT
     AAGTCSSGKT SKASSGTTCE ATTSGLSSSC LKALFVATPA TSTGLACALV SPGGSSQGGA
     FPISAALLRA RKNSNKKFKN LNLARGEVML PSTSKLKQLN SPVVDNPFPS APNTSGSPPS
     VEGGTGVGGV VSPGEDAALK RVLSEMPNEV ARDPSPSSCP AAPNGAASGK GSVPNGPPAV
     ATSADGSSPK SGADAGPTTS SSSAAAKQKK TVTFRNVLET SDDKSVVKRF YNPDIRIPIV
     SIMKKDSLNR PLNYSRGGEC IVRPSILSKI LNKNSNIDKL NSLKFRSAAA SSSSSNQESG
     SSSNVFGLSR AFGAPMDEDD EGGVTFRRND SPYDQNNAED DDMEDDEDDE EAEEDDDNED
     DNDEAASEKS AETEKSDERD SEEKQLVMDS HFVLPKRSTR SSRIIKPNRR LLEEGAISTK
     KPLTLVDSKA KNVFGAASSS ASSTASTFSA SASLKLGKET FFNFGTLKPS SSAAGNFVLR
     QPRLQFQADT QQAPFTAPKA CPTSPSAIPK PANPLATSSF GSLASTSSST VTPTPSACSV
     CSAMVSSKEV AQARKYGVVA CDVCRKFFSK MTKKSISANA STANTSSGSQ QYMQCKGTEG
     SSCSIHSAKS QLKNFKKFYK DRCTACWLKK CMNSFQLPVA HRSRLSGILP PGMRGESSSR
     EEKSAELLSP TGSLRFTSTA SSSSSSVVAS SSVKWKSSGD STSALTSIKP NPLAENNVTF
     GSTPLLRPAI LEKPLFLKIS NAADQKLTAA EAISPSLTKK TSKQEKEKVK ESELSEKPLS
     PTLAATKKSG SAEPPVVEAQ APKEEAPSIS AATQPTASNG TSQGVPPADL AGEANATGDT
     LKRQRIDLKG PRVKHVCRSA SIVLGQPLAT FGEDQQPEEG DMQQEIAAPV PSAISEPSPE
     KPAQIVTDIN DNCASCKTSP VGDESKPSKS AGSAQAEAKK VTAGGKEGTA SAAAGSSAKV
     TTRNAAVASN LIVAASKKQR NGDIVTSSSI TQSSNQTQGR KTKEHRQQRT LISIDFWENY
     DPAEVCQTGF GLIVTETVAQ RALCFLCGST GLDPLIFCAC CCEPYHQYCV QDEYNLKHGS
     FEDTTLMGSL LETTVNASTG PSSSLNQLTQ RLNWLCPRCT VCYTCNMSSG SKVKCQKCQK
     NYHSTCLGTS KRLLGADRPL ICVNCLKCKS CSTTKVSKFV GNLPMCTGCF KLRKKGNFCP
     ICQRCYDDND FDLKMMECGD CAQWVHSKCE GLSDEQYNLL STLPESIEFI CKKCARRNES
     SKIKAEEWRQ AVMEEFKASL YSVLKLLSKS RQACALLKLS PRKKLRCTCG ASSNQGKLQP
     KALQFSSGSD NGLGSDGESQ NSDDVYEFKD QQQQQQQRNV SLNKPRVKSL PCSCQQHISH
     SQSFSLVDIK QKIAGNSYVS LAEFNYDMSQ VIQQSNCDEL DIAYKELLSE QFPWFQNETK
     ACTDALEEDM FESCSGANYE DLQDAGGGSA SVYNEHSTSQ AESRSGVLDI PLEEVDDFGS
     CGIKMRLDTR VCLFCRKSGE GLSGEEARLL YCGHDCWVHT NCAMWSAEVF EEIDGSLQNV
     HSAVARGRMI KCTVCGNRGA TVGCNVRSCG EHYHYPCARS IDCAFLTDKS MYCPAHAKNG
     NALKANGSPS VTYESNFEVS RPVYVELDRK RKKLIEPARV QFHIGSLEVR QLGAIVPRFS
     DSYEAVVPIN FLCSRLYWSS KEPWKIVEYT VRTTIQNSSS TLTALDVGRN YTVDHSNPNS
     KEVQLGMAQI ARWHTSLARS EFLENGGADW SGEFPNPNSC VPPDENTEGE PQQQADLFPP
     EIKDAIFEDL PHELLDGISM LDIFLYDDKT DLFAISEQSK DGTQAMTSNQ AQNQQAGGAA
     SVSICDEDTR NSNTSLGNGW PSSNPVEDAM LSAARNSSQV QMLKTLAWPK LDGNSAMATA
     IKRRKLSKNL AEGVFLTLSS QQRNKKEMAT VAGVSRRQSI SETSAEGVAT TSGSVRSKSF
     TWSAAKRYFE KSEGREEATK MRIMQMDGVD DSITEFRIIS GDGNLSTAQF SGQVKCDRCQ
     CTYRNYDAFQ RHLPSCGPSM SSNETESDVS GQGITNNATQ ISAESLNELQ KQLLANAGGL
     NYLQSATSFP QVQSLGSLGQ FGLQGLQQLQ LQPQSLGNGF FLSQPNPATQ ANTDDLQIYA
     NSLQSLAANL GGGFTLAQPT VTAPAQPQLI AVSTNPDGTQ QFIQIPQTMQ ATTTPTATYQ
     TLQATNTDKK IMLPLTAAGK PLKTVATKAA QQAAVKQRQL KSGHQVKPIQ AKLQPHPQQH
     QQQQQTQVQQ PITVMGQNLL QPQLLFQSSA QSQAPQLILP QAQPQNIISF VTGDGSQGQP
     LQYISIPTAG EYKPQPQPTA TPTFLTTAPG GGATYLQTDA SGNLVLTTTP ANSGLQMLTA
     QSLQPQPQVI GTLIQPQTIQ LGGGADGNQS GGNQQPLILG GTGGGSTGLE FATTSPQVIL
     ATQPMYYGLE TIVQNTVMSS QQFVSTAMPG MLSQNASFSA TTTQVFQASK IEPIVDLPAG
     YVVLNNTGDA SSAGTFLNAA SVLQQQTQDD TTTQILQNAN FQFQSVPTSS GASTSMDYTA
     PVMVTAKIPP VTQVKRTNAQ AKAAGISGVR NMYXQGGEFK GERGILCTPR GHNKSLFNCN
     ELNVLHXXXX NLKQSQVKGK AASGTGTSCG APPSIASKPL QKKTNMIRPI HKLEVKPKVM
     KPTPKVQNQN HSLLQQQQQQ QAQLQQQIPA VVVNQVPKVT ISQQRIPAQP QQQQQQLQQA
     QMLHIPQQQQ PLQQQQVQVQ PSMPIITLAE APVPQSQFVM EPQVLEQQEM ANRVQHFSTS
     STSSSSNCSL PTNVVNPMQQ QAPPTTSSST TRPTNRVLPM QQRQEPAPLS NECPVVPSPT
     PPKPVEQPMI QQLTSASVSK CYAQKATLPS PVYEAELKAS SVLESIVPAV TMDAILEEQP
     VTESIYTEGL YEKNSPAESK TEQLLLQQQQ REQLSQQFAN GYLLDKHAFQ VEPMDTDVYR
     EEDLDEEEDE DDDFSLKMAT SACNDHEMSD SEEPAVKDKI SKILDNLTND DCTDSIATAT
     TMEVEATAGY QQMVEDVLAT TAAASAPTEE FEGALETAAV EAAATYINEM ADAHVLELKQ
     LQNGVELELR RKEEQRTVPQ EPEPSKAAIV PTAAAPEPPP PIQEPKKMSG PHLLYEIQSE
     DGFTYKSSSI TEIWEKVFEA VQVARRAHGL TPLPEGPLAD MGGIQMIGLK TNALKYLIEQ
     LPGVEKCSKY TPKYHKRNGN VSTAANGVHG GNLGGSSASA ALSLSGVDSH GLLDYGSDQD
     ELQENAYDCA RCEPYANRSE YDMFSWLASR HRKQPIQVFV QPSDNELVPR RGTGSNLPMA
     MKYRTLKETY KDYVGVFRSH IHGRGLYCTK DIEAGEMVIE YAGELIRSTL TDKRERYYDS
     RGIGCYMFKI DDNLVVDATM RGNAARFINH CCEPNCYSKV VDILGHKHII IFALRRIVQG
     EELTYDYKFP FEEEKIPCSC GSKRCRKYLN
//