ID M9MS40_DROME Unreviewed; 3282 AA.
AC M9MS40;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=nej {ECO:0000313|EMBL:ADV37657.1,
GN ECO:0000313|FlyBase:FBgn0261617};
GN Synonyms=anon-WO0147981.11 {ECO:0000313|EMBL:ADV37657.1},
GN anon-WO03040301.89 {ECO:0000313|EMBL:ADV37657.1}, CBP
GN {ECO:0000313|EMBL:ADV37657.1}, Cbp {ECO:0000313|EMBL:ADV37657.1}, cbp
GN {ECO:0000313|EMBL:ADV37657.1}, CBP/p300 {ECO:0000313|EMBL:ADV37657.1},
GN CBP_ {ECO:0000313|EMBL:ADV37657.1}, CG15321
GN {ECO:0000313|EMBL:ADV37657.1}, Crbp {ECO:0000313|EMBL:ADV37657.1},
GN dCBP {ECO:0000313|EMBL:ADV37657.1}, dKAT3
GN {ECO:0000313|EMBL:ADV37657.1}, dmCBP {ECO:0000313|EMBL:ADV37657.1},
GN Dmel\CG15319 {ECO:0000313|EMBL:ADV37657.1}, l(1)G0112
GN {ECO:0000313|EMBL:ADV37657.1}, l(1)G0350
GN {ECO:0000313|EMBL:ADV37657.1}, l(1)G0470
GN {ECO:0000313|EMBL:ADV37657.1}, Nej {ECO:0000313|EMBL:ADV37657.1}, nej
GN CBP {ECO:0000313|EMBL:ADV37657.1}, Nejire
GN {ECO:0000313|EMBL:ADV37657.1}, P300 {ECO:0000313|EMBL:ADV37657.1},
GN p300 {ECO:0000313|EMBL:ADV37657.1}, p300/CBP
GN {ECO:0000313|EMBL:ADV37657.1};
GN ORFNames=CG15319 {ECO:0000313|EMBL:ADV37657.1,
GN ECO:0000313|FlyBase:FBgn0261617}, Dmel_CG15319
GN {ECO:0000313|EMBL:ADV37657.1};
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 {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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 [4] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:ADV37657.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; AE014298; ADV37657.1; -; Genomic_DNA.
DR RefSeq; NP_001188575.1; NM_001201646.2.
DR SMR; M9MS40; -.
DR STRING; 7227.FBpp0291862; -.
DR PaxDb; 7227-FBpp0291862; -.
DR EnsemblMetazoa; FBtr0302722; FBpp0291862; FBgn0261617.
DR GeneID; 43856; -.
DR KEGG; dme:Dmel_CG15319; -.
DR AGR; FB:FBgn0261617; -.
DR CTD; 43856; -.
DR FlyBase; FBgn0261617; nej.
DR VEuPathDB; VectorBase:FBgn0261617; -.
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000166210; -.
DR InParanoid; M9MS40; -.
DR OMA; TPNQGMH; -.
DR OrthoDB; 5490807at2759; -.
DR PhylomeDB; M9MS40; -.
DR Reactome; R-DME-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DME-3214847; HATs acetylate histones.
DR Reactome; R-DME-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-DME-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DME-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-DME-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR Reactome; R-DME-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-DME-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-DME-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR Reactome; R-DME-9759194; Nuclear events mediated by NFE2L2.
DR BioGRID-ORCS; 43856; 1 hit in 3 CRISPR screens.
DR ChiTaRS; nej; fly.
DR GenomeRNAi; 43856; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0261617; Expressed in cleaving embryo and 21 other cell types or tissues.
DR ExpressionAtlas; M9MS40; baseline and differential.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:FlyBase.
DR GO; GO:0043993; F:histone H3K18 acetyltransferase activity; IDA:FlyBase.
DR GO; GO:0044017; F:histone H3K27 acetyltransferase activity; IDA:FlyBase.
DR GO; GO:1990226; F:histone methyltransferase binding; IPI:FlyBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:FlyBase.
DR GO; GO:0030707; P:follicle cell of egg chamber development; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0007464; P:R3/R4 cell fate commitment; IMP:FlyBase.
DR GO; GO:0045466; P:R7 cell differentiation; IMP:FlyBase.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
DR GO; GO:0007416; P:synapse assembly; IMP:FlyBase.
DR GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15557; PHD_CBP_p300; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF1; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ADV37657.1};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9MS40};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADV37657.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 514..600
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 944..1023
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1721..1793
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1951..2334
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 2336..2384
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 2398..2479
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 514..600
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 2398..2479
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 33..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1636..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2211..2250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2686..2741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2861..2963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3005..3034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3096..3240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2176..2203
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 112..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1473..1487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2220..2236
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2727..2741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2878..2948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3096..3145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3154..3173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3174..3196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3282 AA; 341431 MW; 3A5A472BB9EF3918 CRC64;
MMADHLDEPP QKRVKMDPTD ISYFLEENLP DELVSSNSGW SDQLTGGAGG GNGGGGASGV
TTNPTSGPNP GGGPNKPAAQ GPGSGTGGVG VGVNVGVGGV VGVGVVPSQM NGAGGGNGSG
TGGDDGSGNG SGAGNRISQM QHQQLQHLLQ QQQQGQKGAM VVPGMQQLGS KSPNLQSPNQ
GGMQQVVGTQ MGMVNSMPMS ISNNGNNGMN AIPGMNTIAQ GNLGNMVLTN SVGGGMGGMV
NHLKQQPGGG GGGMINSVSV PGGPGAGAGG VGAGGGGAVA ANQGMHMQNG PMMGRMVGQQ
HMLRGPHLMG ASGGAGGPGN GPGGGGPRMQ NPNMQMNFRP FAAQLNSLPY GVGQYGGPGG
GNNPQQQQQQ QQQQLLAQQM AQRGGVVPGM PQGNRPVGTV VPMSTLGGDG SGPAGQLVSG
NPQQQQMLAQ QQTGAMGPRP PQPNQLLGHP GQQQQQQQQP GTSQQQQQQQ GVGIGGAGVV
ANAGTVAGVP AVAGGGAGGA VQSSGPGGAN RDVPDDRKRQ IQQQLMLLLH AHKCNRRENL
NPNREVCNVN YCKAMKSVLA HMGTCKQSKD CTMQHCASSR QILLHYKTCQ NSGCVICYPF
RQNHSVFQNA NVPPGGGPAG IGGAPPGGGG AGGGAAGAGG NLQQQQQQQQ QQQQNQQPNL
TGLVVDGKQG QQVAPGGGQN TAIVLPQQQG AGGAPGAPKT PADMVQQLTQ QQQQQQQQVH
QQQVQQQELR RFDGMSQQVV AGGMQQQQQQ GLPPVIRIQG AQPAVRVLGP GGPGGPSGPN
VLPNDVNSLH QQQQQMLQQQ QQQGQNRRRG GLATMVEQQQ QHQQQQQQPN PAQLGGNIPA
PLSVNVGGFG NTNFGGAAAG GAVGANDKQQ LKVAQVHPQS HGVGAGGASA GAGASGGQVA
AGSSVLMPAD TTGSGNAGNP NQNAGGVAGG AGGGNGGNTG PPGDNEKDWR ESVTADLRNH
LVHKLVQAIF PTSDPTTMQD KRMHNLVSYA EKVEKDMYEM AKSRSEYYHL LAEKIYKIQK
ELEEKRLKRK EQHQQMLMQQ QGVANPVAGG AAGGAGSAAG VAGGVVLPQQ QQQQQQQQQQ
QGQQPLQSCI HPSISPMGGV MPPQQLRPQG PPGILGQQTA AGLGVGVGVT NNMVTMRSHS
PGGNMLALQQ QQRMQFPQQQ QQQPPGSGAG KMLVGPPGPS PGGMVVNPAL SPYQTTNVLT
SPVPGQQQQQ QFINANGGTG ANPQLSEIMK QRHIHQQQQQ QQQQQQQGML LPQSPFSNST
PLQQQQQQQQ QQQQQQQATS NSFSSPMQQQ QQGQQQQQQK PGSVLNNMPP TPTSLEALNA
GAGAPGTGGS ASNVTVSAPS PSPGFLSNGP SIGTPSNNNN NSSANNNPPS VSSLMQQPLS
NRPGTPPYIP ASPVPATSAS GLAASSTPAS AAATCASSGS GSNSSSGATA AGASSTSSSS
SAGSGTPLSS VSTPTSATMA TSSGGGGGGG GNAGGGSSTT PASNPLLLMS GGTAGGGTGA
TTTTSTSSSS RMMSSSSSLS SQMAALEAAA RDNDDETPSP SGENTNGSGG SGNAGGMASK
GKLDSIKQDD DIKKEFMDDS CGGNNDSSQM DCSTGGGKGK NVNNDGTSMI KMEIKTEDGL
DGEVKIKTEA MDVDEAGGST AGEHHGEGGG GSGVGGGKDN INGAHDGGAT GGAVDIKPKT
ETKPLVPEPL APNAGDKKKK CQFNPEELRT ALLPTLEKLY RQEPESVPFR YPVDPQALGI
PDYFEIVKKP MDLGTIRTNI QNGKYSDPWE YVDDVWLMFD NAWLYNRKTS RVYRYCTKLS
EVFEAEIDPV MQALGYCCGR KYTFNPQVLC CYGKQLCTIP RDAKYYSYQN SLKEYGVASN
RYTYCQKCFN DIQGDTVTLG DDPLQSQTQI KKDQFKEMKN DHLELEPFVN CQECGRKQHQ
ICVLWLDSIW PGGFVCDNCL KKKNSKRKEN KFNAKRLPTT KLGVYIETRV NNFLKKKEAG
AGEVHIRVVS SSDKCVEVKP GMRRRFVEQG EMMNEFPYRA KALFAFEEVD GIDVCFFGMH
VQEYGSECPA PNTRRVYIAY LDSVHFFRPR QYRTAVYHEI LLGYMDYVKQ LGYTMAHIWA
CPPSEGDDYI FHCHPTDQKI PKPKRLQEWY KKMLDKGMIE RIIQDYKDIL KQAMEDKLGS
AAELPYFEGD FWPNVLEESI KELDQEEEEK RKQAEAAEAA AAANLFSIEE NEVSGDGKKK
GQKKAKKSNK SKAAQRKNSK KSNEHQSGND LSTKIYATME KHKEVFFVIR LHSAQSAASL
APIQDPDPLL TCDLMDGRDA FLTLARDKHF EFSSLRRAQF STLSMLYELH NQGQDKFVYT
CNHCKTAVET RYHCTVCDDF DLCIVCKEKV GHQHKMEKLG FDIDDGSALA DHKQANPQEA
RKQSIQRCIQ SLAHACQCRD ANCRLPSCQK MKLVVQHTKN CKRKPNGGCP ICKQLIALCC
YHAKNCEEQK CPVPFCPNIK HKLKQQQSQQ KFQQQQLLRR RVALMSRTAA PAALQGPAAV
SGPTVVSGGV PVVGMSGVAV SQQVIPGQAG ILPPGAGGMS PSTVAVPSPV SGGAGAGGMG
GMTSPHPHQP GIGMKPGGGH SPSPNVLQVV KQVQEEAARQ QVSHGGGFGK GVPMAPPVMN
RPMGGAGPNQ NVVNQLGGMG VGVGGVGGVG VGGVGGVGVN QLNSGGGNTP GAPISGPGMN
VNHLMSMDQW GGGGAGGGGA NPGGGNPQAR YANNTGGMRQ PTHVMQTNLI PPQQQQQMMG
GLGGPNQLGG GQMPVGGQHG GMGMGMGAPP MAGTVGGVRP SPGAGGGGGS ATGGGLNTQQ
LALIMQKIKN NPTNESNQHI LAILKQNPQI MAAIIKQRQQ SQNNAAAGGG APGPGGALQQ
QQAGNGPQNP QQQQQQQQQQ QVMQQQQMQH MMNQQQGGGG PQQMNPNQQQ QQQQVNLMQQ
QQQGGPGGPG SGLPTRMPNM PNALGMLQSL PPNMSPGVST QGGMVPNQNW NKMRYMQMSQ
YPPPYPQRQR GPHMGGAGPG PGQQQFPGGG GGAGNFNAGG AGGAGGVVGV GGVPGGAGTV
PGGDQYSMAN AAAASNMLQQ QQGQVGVGVG VGVKPGPGQQ QQQMGVGMPP GMQQQQQQQQ
PLQQQQMMQV AMPNANAQNP SAVVGGPNAQ VMGPPTPHSL QQQLMQSARS SPPIRSPQPT
PSPRSAPSPR AAPSASPRAQ PSPHHVMSSH SPAPQGPPHD GMHNHGMHHQ SPLPGVPQDV
GVGVGVGVGV GVNVNVGNVG VGNAGGALPD ASDQLTKFVE RL
//