GenomeNet

Database: UniProt
Entry: Q9VTZ1_DROME
LinkDB: Q9VTZ1_DROME
Original site: Q9VTZ1_DROME 
ID   Q9VTZ1_DROME            Unreviewed;       813 AA.
AC   Q9VTZ1;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Histone acetyltransferase GCN5 {ECO:0000256|ARBA:ARBA00019713};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN   Name=Gcn5 {ECO:0000313|EMBL:AAF49904.1,
GN   ECO:0000313|FlyBase:FBgn0020388};
GN   Synonyms=Ada4 {ECO:0000313|EMBL:AAF49904.1}, anon-WO0172774.89
GN   {ECO:0000313|EMBL:AAF49904.1}, dGCN5 {ECO:0000313|EMBL:AAF49904.1},
GN   dGcn5 {ECO:0000313|EMBL:AAF49904.1}, dGCN5 HAT
GN   {ECO:0000313|EMBL:AAF49904.1}, dGcn5i {ECO:0000313|EMBL:AAF49904.1},
GN   dKAT2 {ECO:0000313|EMBL:AAF49904.1}, Dmel\CG4107
GN   {ECO:0000313|EMBL:AAF49904.1}, dmGCN5 {ECO:0000313|EMBL:AAF49904.1},
GN   dmHAG401 {ECO:0000313|EMBL:AAF49904.1}, dPCAF
GN   {ECO:0000313|EMBL:AAF49904.1}, GCN5 {ECO:0000313|EMBL:AAF49904.1},
GN   gcn5 {ECO:0000313|EMBL:AAF49904.1}, Gcn5/PCAF
GN   {ECO:0000313|EMBL:AAF49904.1}, Gcn5/Pcaf
GN   {ECO:0000313|EMBL:AAF49904.1}, KAT {ECO:0000313|EMBL:AAF49904.1}, KAT2
GN   {ECO:0000313|EMBL:AAF49904.1}, P/CAF {ECO:0000313|EMBL:AAF49904.1},
GN   p/CAF {ECO:0000313|EMBL:AAF49904.1}, PCAF
GN   {ECO:0000313|EMBL:AAF49904.1}, Pcaf {ECO:0000313|EMBL:AAF49904.1},
GN   pCAF {ECO:0000313|EMBL:AAF49904.1};
GN   ORFNames=CG4107 {ECO:0000313|EMBL:AAF49904.1,
GN   ECO:0000313|FlyBase:FBgn0020388}, Dmel_CG4107
GN   {ECO:0000313|EMBL:AAF49904.1};
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:AAF49904.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAF49904.1, 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:AAL39242.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000313|EMBL:AAL39242.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M.,
RA   Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.,
RA   Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA   Rubin G.M., Celniker S.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3] {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   [4] {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   [5] {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   [6] {ECO:0000313|EMBL:AAF49904.1, 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   [7] {ECO:0000313|EMBL:AAF49904.1, 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   [8] {ECO:0000313|EMBL:AAF49904.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA   Svirskas R., Rubin G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:AAF49904.1, 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   [10] {ECO:0000313|EMBL:AAF49904.1, 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).
RN   [11] {ECO:0000313|EMBL:AAF49904.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109357; DOI=.1534/g3.115.018929;
RG   FlyBase Consortium;
RA   Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA   Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA   Gelbart W.M., null;
RT   "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT   Throughput Data.";
RL   G3 (Bethesda) 5:1721-1736(2015).
RN   [12] {ECO:0000313|EMBL:AAF49904.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109356; DOI=.1534/g3.115.018937;
RG   FlyBase Consortium;
RA   Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA   Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA   null;
RT   "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL   G3 (Bethesda) 5:1737-1749(2015).
RN   [13] {ECO:0000313|EMBL:AAF49904.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25589440;
RA   Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA   Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA   Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA   de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA   Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA   Karpen G.H., Celniker S.E.;
RT   "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL   Genome Res. 25:445-458(2015).
RN   [14] {ECO:0000313|EMBL:AAF49904.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Berkeley Drosophila Genome Project;
RA   Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA   Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA   Rubin G.;
RT   "Drosophila melanogaster release 4 sequence.";
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN   [15] {ECO:0000313|EMBL:AAF49904.1}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008607}.
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DR   EMBL; AE014296; AAF49904.1; -; Genomic_DNA.
DR   EMBL; AY069097; AAL39242.1; -; mRNA.
DR   RefSeq; NP_648586.2; NM_140329.3.
DR   AlphaFoldDB; Q9VTZ1; -.
DR   SMR; Q9VTZ1; -.
DR   ComplexPortal; CPX-2644; SAGA complex.
DR   ComplexPortal; CPX-2742; ATAC histone acetyltransferase complex.
DR   ComplexPortal; CPX-2774; CHAT histone acetyltransferase complex.
DR   ComplexPortal; CPX-2824; ADA complex.
DR   IntAct; Q9VTZ1; 6.
DR   STRING; 7227.FBpp0075701; -.
DR   PaxDb; 7227-FBpp0075701; -.
DR   EnsemblMetazoa; FBtr0075969; FBpp0075701; FBgn0020388.
DR   GeneID; 39431; -.
DR   KEGG; dme:Dmel_CG4107; -.
DR   UCSC; CG4107-RA; d. melanogaster.
DR   AGR; FB:FBgn0020388; -.
DR   CTD; 39431; -.
DR   FlyBase; FBgn0020388; Gcn5.
DR   VEuPathDB; VectorBase:FBgn0020388; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   GeneTree; ENSGT00940000168538; -.
DR   HOGENOM; CLU_015901_0_0_1; -.
DR   InParanoid; Q9VTZ1; -.
DR   OMA; YFQTKMR; -.
DR   OrthoDB; 1760108at2759; -.
DR   Reactome; R-DME-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR   Reactome; R-DME-5689880; Ub-specific processing proteases.
DR   Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-DME-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR   BioGRID-ORCS; 39431; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; p; fly.
DR   GenomeRNAi; 39431; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0020388; Expressed in eye disc (Drosophila) and 55 other cell types or tissues.
DR   ExpressionAtlas; Q9VTZ1; baseline and differential.
DR   GO; GO:0140672; C:ATAC complex; IDA:FlyBase.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0070775; C:H3 histone acetyltransferase complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR   GO; GO:0000124; C:SAGA complex; IDA:FlyBase.
DR   GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:FlyBase.
DR   GO; GO:0010484; F:histone H3 acetyltransferase activity; IDA:FlyBase.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:FlyBase.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd05509; Bromo_gcn5_like; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR037800; GCN5.
DR   InterPro; IPR016376; GCN5/PCAF.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR009464; PCAF_N.
DR   PANTHER; PTHR45750; GH11602P; 1.
DR   PANTHER; PTHR45750:SF3; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF06466; PCAF_N; 1.
DR   PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   2: Evidence at transcript level;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Acyltransferase {ECO:0000313|EMBL:AAF49904.1};
KW   Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000313|EMBL:AAF49904.1}.
FT   DOMAIN          481..627
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          721..791
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        546
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003048-1"
SQ   SEQUENCE   813 AA;  92169 MW;  0810EFFB3BC0D2A5 CRC64;
     MSGGPSITIK SQPIDGNNTG NAAAQQQQQA ANGAATAGAS GAAGSAQNPG HGGAASGAGS
     VPAEGTRQNS LQRIQQRKQK VFNLPVPQKL AKLSMYSACQ SEGCRCTGWK TPQENRHRDV
     ESSYCPEFNE ECRNTSCRHS LRSHIAHLDN ISSSSMNELL GAIIDMENLF MSMQRVEDED
     TKKVYQYLFR LLRQCVLTRQ QAVIRGPLGD PPFETPCITK AVLSLVFYKY NHLSTPELQT
     MTEVAKTFLN FLNHYNFESP STRRGDLTHE DASNYKINYT RWLVFCHVPA FCNSLRQCET
     SLVFGRTLLR TVFQCMSQQL KKKCISERDR FPEDKRSIIT LMPKFLETLR AELLKDDSPI
     WDTSYRPSNS FVIQQRKRNQ EVANVPIGPS AASIGGNKRT SVGEPLHKRI KKEPTDRPSS
     ENLDDLPADV VMRAMKSVSE SKTTNKAEIL FPVNVSRDEN VKAEEQKRAI EFHVVGNSLT
     KPVDKQTVLW LLGLQLVFAY QLPEMPREYI SQLVFDTKHK TLALIKENQP IGGICFRPFP
     SQGFTEIVFC AVTMSEQVKG YGTHLMNHLK DYSIQRGIKH LLTFADCDAI GYFKKQGFSK
     DIKLARPVYA GYIKEYDSAT LMHCELHPSI VNTQFIAVIR SQSEILKELI AQRHNEVQKV
     RPGLTCFKEG LPVIPVESIP GLREIGWKPQ NRPARSSRPL EESTDPEKLA TSFASVLQSV
     RQHTTAWPFL RPVTAAEVPD YYDHIKYPMD LKTMGERLKK GYYQTRRLFM ADMARIFSNC
     RFYNSPDTEY YRCANSLERY FQTKMRELGL WDK
//
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