KDM5_DROME
ID KDM5_DROME Reviewed; 1838 AA.
AC Q9VMJ7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Lysine-specific demethylase lid;
DE EC=1.14.11.67 {ECO:0000269|PubMed:17311883, ECO:0000269|PubMed:17351630, ECO:0000269|PubMed:17351631};
DE AltName: Full=Histone demethylase lid;
DE AltName: Full=Jumonji/ARID domain-containing protein lid;
DE AltName: Full=Protein little imaginal disks;
DE AltName: Full=Retinoblastoma-binding protein 2 homolog;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase lid {ECO:0000305};
GN Name=lid; ORFNames=CG9088;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=11014813; DOI=10.1093/genetics/156.2.645;
RA Gildea J.J., Lopez R., Shearn A.;
RT "A screen for new trithorax group genes identified little imaginal discs,
RT the Drosophila melanogaster homologue of human retinoblastoma binding
RT protein 2.";
RL Genetics 156:645-663(2000).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH MYC,
RP IDENTIFICATION IN COMPLEX WITH MYC AND ASH2, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF HIS-637 AND GLU-639.
RX PubMed=17311883; DOI=10.1101/gad.1523007;
RA Secombe J., Li L., Carlos L., Eisenman R.N.;
RT "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase
RT required for dMyc-induced cell growth.";
RL Genes Dev. 21:537-551(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1474, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17351631; DOI=10.1038/nsmb1216;
RA Lee N., Zhang J., Klose R.J., Erdjument-Bromage H., Tempst P., Jones R.S.,
RA Zhang Y.;
RT "The trithorax-group protein Lid is a histone H3 trimethyl-Lys4
RT demethylase.";
RL Nat. Struct. Mol. Biol. 14:341-343(2007).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17351630; DOI=10.1038/nsmb1217;
RA Eissenberg J.C., Lee M.G., Schneider J., Ilvarsonn A., Shiekhattar R.,
RA Shilatifard A.;
RT "The trithorax-group gene in Drosophila little imaginal discs encodes a
RT trimethylated histone H3 Lys4 demethylase.";
RL Nat. Struct. Mol. Biol. 14:344-346(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-323; SER-1422; SER-1433;
RP SER-1635 AND SER-1640, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [10]
RP FUNCTION.
RX PubMed=21960634; DOI=10.1126/science.1206022;
RA DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J.,
RA Panda S.;
RT "Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences
RT the circadian clock.";
RL Science 333:1881-1885(2011).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of
CC histone H3, thereby playing a central role in histone code. Does not
CC demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79'
CC or H4 'Lys-20'. Specifically demethylates trimethylated H3 'Lys-4'.
CC Required for the correct regulation of homeotic genes during
CC development. Plays a role in the regulation of the circadian rhythm and
CC in maintaining the normal periodicity of the circadian clock. Regulates
CC the expression of clock-controlled genes including tim, per and cry.
CC {ECO:0000269|PubMed:11014813, ECO:0000269|PubMed:17311883,
CC ECO:0000269|PubMed:17351630, ECO:0000269|PubMed:17351631,
CC ECO:0000269|PubMed:21960634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000269|PubMed:17311883, ECO:0000269|PubMed:17351630,
CC ECO:0000269|PubMed:17351631};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by Myc. {ECO:0000269|PubMed:17311883}.
CC -!- SUBUNIT: Interacts with Myc. Part of a complex containing Lid, Myc and
CC Ash2. {ECO:0000269|PubMed:17311883}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:17311883}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; AE014134; AAF52319.1; -; Genomic_DNA.
DR EMBL; AY095051; AAM11379.1; -; mRNA.
DR EMBL; AE014134; AAN10569.1; -; Genomic_DNA.
DR RefSeq; NP_001245908.1; NM_001258979.2.
DR RefSeq; NP_001245909.1; NM_001258980.1.
DR RefSeq; NP_001245910.1; NM_001258981.2.
DR RefSeq; NP_001285649.1; NM_001298720.1.
DR RefSeq; NP_523486.1; NM_078762.6.
DR RefSeq; NP_723140.1; NM_164671.1.
DR PDB; 2LM1; NMR; -; A=214-320.
DR PDB; 2MIQ; NMR; -; A=414-504.
DR PDBsum; 2LM1; -.
DR PDBsum; 2MIQ; -.
DR AlphaFoldDB; Q9VMJ7; -.
DR BMRB; Q9VMJ7; -.
DR SMR; Q9VMJ7; -.
DR BioGRID; 60002; 44.
DR DIP; DIP-29330N; -.
DR IntAct; Q9VMJ7; 11.
DR MINT; Q9VMJ7; -.
DR STRING; 7227.FBpp0297914; -.
DR iPTMnet; Q9VMJ7; -.
DR PaxDb; Q9VMJ7; -.
DR PRIDE; Q9VMJ7; -.
DR DNASU; 33837; -.
DR EnsemblMetazoa; FBtr0079231; FBpp0078862; FBgn0031759.
DR EnsemblMetazoa; FBtr0079232; FBpp0078863; FBgn0031759.
DR EnsemblMetazoa; FBtr0307069; FBpp0297912; FBgn0031759.
DR EnsemblMetazoa; FBtr0307070; FBpp0297913; FBgn0031759.
DR EnsemblMetazoa; FBtr0307071; FBpp0297914; FBgn0031759.
DR EnsemblMetazoa; FBtr0345336; FBpp0311492; FBgn0031759.
DR GeneID; 33837; -.
DR KEGG; dme:Dmel_CG9088; -.
DR CTD; 33837; -.
DR FlyBase; FBgn0031759; lid.
DR VEuPathDB; VectorBase:FBgn0031759; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000168915; -.
DR HOGENOM; CLU_000991_3_0_1; -.
DR InParanoid; Q9VMJ7; -.
DR OMA; KWAPVAP; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q9VMJ7; -.
DR BRENDA; 1.14.11.67; 1994.
DR BRENDA; 1.14.99.66; 1994.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DME-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR SignaLink; Q9VMJ7; -.
DR BioGRID-ORCS; 33837; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 33837; -.
DR PRO; PR:Q9VMJ7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031759; Expressed in egg cell and 27 other tissues.
DR ExpressionAtlas; Q9VMJ7; baseline and differential.
DR Genevisible; Q9VMJ7; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070822; C:Sin3-type complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0033749; F:histone H3-methyl-arginine-3 demethylase activity; IMP:FlyBase.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IMP:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0016577; P:histone demethylation; IMP:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IMP:FlyBase.
DR GO; GO:0034721; P:histone H3-K4 demethylation, trimethyl-H3-K4-specific; IMP:FlyBase.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IMP:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0070193; P:synaptonemal complex organization; IMP:FlyBase.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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 Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF57903; SSF57903; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Chromatin regulator; Coiled coil;
KW Developmental protein; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1838
FT /note="Lysine-specific demethylase lid"
FT /id="PRO_0000292421"
FT DOMAIN 161..202
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 226..316
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 591..757
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 448..498
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1293..1354
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1753..1808
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 960..1049
FT /evidence="ECO:0000255"
FT COMPBIAS 1..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 637
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 640
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 725
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1422
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1474
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 1635
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1640
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 637
FT /note="H->A: Abolishes enzymatic activity; when associated
FT with A-536."
FT /evidence="ECO:0000269|PubMed:17311883"
FT MUTAGEN 639
FT /note="E->A: Abolishes enzymatic activity; when associated
FT with A-534."
FT /evidence="ECO:0000269|PubMed:17311883"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2LM1"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:2LM1"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:2LM1"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2LM1"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:2LM1"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:2LM1"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:2LM1"
FT HELIX 294..315
FT /evidence="ECO:0007829|PDB:2LM1"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:2MIQ"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:2MIQ"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:2MIQ"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:2MIQ"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:2MIQ"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:2MIQ"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:2MIQ"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:2MIQ"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:2MIQ"
SQ SEQUENCE 1838 AA; 203993 MW; E01BDB89027F9F50 CRC64;
MSAKTEADNT TAANSGGGGV GSGTSSGGGA SANGTATPAR RLRTRNSTGN GTNSGSESVK
KSNANDEPST PVTPAGATGS HTHAPPGISP AVMERPMPSV PMNHASSSVS ASKKYHNSCP
HPTPTPAPTG HKKSVHTQPH SSNKFDQGKN EEFHFDTPPE CPVFRPTTEE FKNPLAYISK
IRSIAEKCGI AKILPPATWS PPFAVDVDKL RFVPRVQRLN ELEAKTRVKL NFLDQIAKFW
ELQGSSLKIP MVERKALDLY TLHRIVQEEG GMEQTTKDRK WAKVANRMQY PSSKSVGATL
KAHYERILHP FEVYTSGKVL GPTPTSSGSG STPVKLEDGG GTDYKAHEIP TRQQIAPPNE
TNTRRSKRFG NSNASCGLSG VTPTTKPSAG VFVKTETKEE FKRDLLSSFN AVNSGGSPLA
TGTTANTRGA SQKKGGEPPA LIVDPLMKYI CHICNRGDVE ESMLLCDGCD DSYHTFCLLP
PLTSIPKGEW LCPRCVVEEV SKPQEAFGFE QAEREYTLQQ FGQMADQFKQ EYFRKPVHLV
PTEMVEREFW RIVSSIDEDV TVEYGADLHT MDHGSGFPTK SSLYLLPGDQ EYAESSWNLN
NLPLLEDSIL GHINADISGM NAPWMYVGMC FAAFCWHNED HWSYSINYLH WGEPKTWYGV
PGSCAEQFEE TMKQAAPELF SSQPDLLHQL VTIMNPNILM NNRVPVFRTD QHAGEFVITF
PRAYHAGFNQ GYNFAEAVNF APADWLKMGR ECVNHYSMLR RFCVFSHDEL VCKMALEPAK
LTFGIATACY IDMAEMVDTE KKLRKSLLEW GVTRAERRAF ELVNDDERHC QECNTTCFLS
AVACECNDKL IVCLRHYTVL CGCAPEKHTL IYRYTLDEMP LMLQKLKVKA HSFERWLSRC
RDIVDAHTPT SVTLQELQEL CKEAETKKFP SSLLIDRLNA AAVEAEKCVT VIQQLGINKV
RTRSDHNQEA AQYKLTMEEL ELFVQEIDNL CCIIDEGASV RELLVLGKQF VERSESQLQL
SLESLEESEL ETLINEGSSL RIELQQLDLL QKRLKQCKWY KRSQGLRETS SKLTYQDVKN
LLHIAAADLD PTDPYVDKEM RKLQQIGADI EAWESQAAKY FRRLTQQHEL GEIEQFLKSA
SDINGQVPSH GLLKDALRKA REWLRAVEQL QQNNHVTYCH TLEAMIERGL NIPIQLEELS
RMQGHLNSAH QWKDNTACAF LKKGTFYTLL EVLMPRSDAI NIDSDLKPRF QDDFLKEKNP
AEIVASFKHA EEQELLDMRE LRRQNMNKNP MRDMFCLCKS EFRNLMFNCQ LCRDWFHEDC
VPPPSATNQN GIVNGGSGPG TNRPKWLCPS CVRSKRPRLE TILPLLVQLQ QLPIRLPEDE
ALRCLAERAM NWQDRARKAL SSPDVSAAQE AIMAQQQQKR RSEGGAGVGN ISSPRKPRRR
GSLTKEASGS TESDADDDDD EDECRLRIVE DNFSNDEDEP RTAPATSTVN SDLLKLLSDS
EIENLLDLMM EGDLLEVSLD ETQELWRILE TMPPTLLQAE AMERVVQYMQ RQRQQHTNPL
PTSGAEDSND SLMVQNSPNS NSNSGGATGS ASNSGRNKKR RSNDTGGNSA VPRKKQSTPK
QTPGKKGSAA AARKSDAKAS PAASTTPGAD ADAENKQANG GNTNSSTGSG GGNSATTTPT
PGSTHKKRKR TSTTATNNNN NNNNNSTNNS NSSTNLNSNT TSGQGAATGG NNATGGQKKH
AQRSQQAAQE DDEEECRAEN CHKPTGREVD WVQCDGGCNE WFHMYCVGLN RSQIKPDDDY
ICIRCTKTVA IGTQGSGHSM SVASTTTPGK QRAVQSAR
