ID   UBPE_DROME              Reviewed;        1556 AA.
AC   Q24574; A4V1I7; Q95TM9; Q9VRP1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000250|UniProtKB:Q96K76};
DE            EC=3.4.19.12 {ECO:0000269|PubMed:10949024, ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:26169834};
DE   AltName: Full=Ubiquitin thioesterase 47 {ECO:0000250|UniProtKB:Q96K76};
DE   AltName: Full=Ubiquitin-specific-processing protease 47 {ECO:0000303|PubMed:27552662};
GN   Name=Usp47 {ECO:0000303|PubMed:27552662,
GN   ECO:0000312|FlyBase:FBgn0016756};
GN   Synonyms=Ubp64E {ECO:0000303|PubMed:26169834};
GN   ORFNames=CG5486 {ECO:0000312|FlyBase:FBgn0016756};
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 318-1556 (ISOFORMS A/D), AND FUNCTION.
RC   TISSUE=Embryo;
RX   PubMed=8816485; DOI=10.1128/mcb.16.10.5717;
RA   Henchoz S., de Rubertis F., Pauli D., Spierer P.;
RT   "The dose of a putative ubiquitin-specific protease affects position-effect
RT   variegation in Drosophila melanogaster.";
RL   Mol. Cell. Biol. 16:5717-5725(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-1556 (ISOFORMS A/D).
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   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-405.
RX   PubMed=10949024; DOI=10.1016/s1097-2765(05)00008-0;
RA   Roerth P., Szabo K., Texido G.;
RT   "The level of C/EBP protein is critical for cell migration during
RT   Drosophila oogenesis and is tightly controlled by regulated degradation.";
RL   Mol. Cell 6:23-30(2000).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-173; SER-238;
RP   SER-1131; SER-1132; SER-1140; SER-1141; SER-1199; SER-1201 AND SER-1205,
RP   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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TTK, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=18160715; DOI=10.1128/mcb.01567-07;
RA   Bajpe P.K., van der Knaap J.A., Demmers J.A., Bezstarosti K., Bassett A.,
RA   van Beusekom H.M., Travers A.A., Verrijzer C.P.;
RT   "Deubiquitylating enzyme UBP64 controls cell fate through stabilization of
RT   the transcriptional repressor tramtrack.";
RL   Mol. Cell. Biol. 28:1606-1615(2008).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, ACTIVE SITE, AND
RP   MUTAGENESIS OF CYS-405.
RX   PubMed=26169834; DOI=10.1128/mcb.00373-15;
RA   Shi J., Liu Y., Xu X., Zhang W., Yu T., Jia J., Liu C.;
RT   "Deubiquitinase USP47/UBP64E regulates beta-Catenin ubiquitination and
RT   degradation and plays a positive role in wnt signaling.";
RL   Mol. Cell. Biol. 35:3301-3311(2015).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27552662; DOI=10.1371/journal.pbio.1002539;
RA   Ashton-Beaucage D., Lemieux C., Udell C.M., Sahmi M., Rochette S.,
RA   Therrien M.;
RT   "The Deubiquitinase USP47 Stabilizes MAPK by Counteracting the Function of
RT   the N-end Rule ligase POE/UBR4 in Drosophila.";
RL   PLoS Biol. 14:E1002539-E1002539(2016).
CC   -!- FUNCTION: Ubiquitin-specific protease that deubiquitinates target
CC       proteins to regulate different cellular and developmental pathways
CC       (PubMed:10949024, PubMed:18160715, PubMed:26169834, PubMed:27552662).
CC       Functions downstream of Dsor1/MEK to positively regulate the Ras/MAPK
CC       signaling pathway (PubMed:27552662). Likely to modulate the pathway
CC       during various cellular and developmental processes including rl/MAPK
CC       activation by the receptors InR, Egfr and sevenless/sev
CC       (PubMed:27552662). Functions in the post-translational stabilization of
CC       rl/MAPK levels in a mechanism that is independent of rl activity and
CC       opposes the activity of the E2 enzyme Unc6 and the putative E3 ligases
CC       poe, Ufd4 and Kcmf1, which mediate the ubiquitination and proteasomal
CC       degradation of rl (PubMed:27552662). During eye development it may also
CC       act downstream of rl/MAPK to negatively regulate the Ras/MAPK signaling
CC       pathway by stabilizing the transcriptional repressor ttk and
CC       consequently inhibiting photoreceptor cell development
CC       (PubMed:18160715). This suggests that at least during eye development,
CC       it may act in both the positive and negative regulation of the Ras/MAPK
CC       signaling pathway to mediate the development of different cell types
CC       (PubMed:18160715, PubMed:27552662). Positively regulates border
CC       follicle cell migration during oogenesis by mediating the
CC       deubiquitination and stabilization of slbo (PubMed:10949024). In the
CC       wing disks it positively regulates wg signaling by stabilizing arm
CC       (PubMed:26169834). Has an effect on position-effect variegation
CC       (PubMed:8816485). {ECO:0000269|PubMed:10949024,
CC       ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:26169834,
CC       ECO:0000269|PubMed:27552662, ECO:0000269|PubMed:8816485}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:10949024,
CC         ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:26169834};
CC   -!- SUBUNIT: Interacts with ttk. {ECO:0000269|PubMed:18160715}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A {ECO:0000312|FlyBase:FBgn0016756}; Synonyms=B
CC       {ECO:0000312|FlyBase:FBgn0016756};
CC         IsoId=Q24574-1; Sequence=Displayed;
CC       Name=D {ECO:0000312|FlyBase:FBgn0016756};
CC         IsoId=Q24574-2; Sequence=VSP_054033;
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in the embryo (at protein
CC       level). Ubiquitously expressed in the developing eye (at protein
CC       level). {ECO:0000269|PubMed:18160715}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the adult wing results
CC       in the development of wing margin bristles (PubMed:26169834). RNAi-
CC       mediated knockdown in the posterior compartment of the wing reduces
CC       accumulation of arm, resulting in reduced expression of sens and wg
CC       (PubMed:26169834). RNAi-mediated knockdown in larval wing or eye
CC       imaginal disks results in decreased rl protein levels
CC       (PubMed:27552662). {ECO:0000269|PubMed:26169834,
CC       ECO:0000269|PubMed:27552662}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL13901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA67601.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA67601.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE014296; AAF50752.2; -; Genomic_DNA.
DR   EMBL; AE014296; AAN12105.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAS65076.2; -; Genomic_DNA.
DR   EMBL; BT003784; AAO41467.1; -; mRNA.
DR   EMBL; X99211; CAA67601.1; ALT_SEQ; mRNA.
DR   EMBL; AY058672; AAL13901.1; ALT_INIT; mRNA.
DR   RefSeq; NP_523937.2; NM_079213.4. [Q24574-1]
DR   RefSeq; NP_729087.1; NM_168129.4. [Q24574-1]
DR   RefSeq; NP_996001.2; NM_206279.4. [Q24574-2]
DR   AlphaFoldDB; Q24574; -.
DR   SMR; Q24574; -.
DR   BioGRID; 64105; 12.
DR   IntAct; Q24574; 4.
DR   STRING; 7227.FBpp0076802; -.
DR   MEROPS; C19.105; -.
DR   iPTMnet; Q24574; -.
DR   PaxDb; 7227-FBpp0076802; -.
DR   EnsemblMetazoa; FBtr0077095; FBpp0076802; FBgn0016756. [Q24574-1]
DR   EnsemblMetazoa; FBtr0077096; FBpp0076803; FBgn0016756. [Q24574-1]
DR   EnsemblMetazoa; FBtr0306259; FBpp0297369; FBgn0016756. [Q24574-2]
DR   GeneID; 38644; -.
DR   KEGG; dme:Dmel_CG5486; -.
DR   AGR; FB:FBgn0016756; -.
DR   CTD; 55031; -.
DR   FlyBase; FBgn0016756; Usp47.
DR   VEuPathDB; VectorBase:FBgn0016756; -.
DR   eggNOG; KOG4598; Eukaryota.
DR   GeneTree; ENSGT00940000157223; -.
DR   HOGENOM; CLU_002928_0_0_1; -.
DR   InParanoid; Q24574; -.
DR   OMA; DCDWRRY; -.
DR   OrthoDB; 51419at2759; -.
DR   PhylomeDB; Q24574; -.
DR   BioGRID-ORCS; 38644; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Usp47; fly.
DR   GenomeRNAi; 38644; -.
DR   PRO; PR:Q24574; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0016756; Expressed in thoracico-abdominal ganglion (Drosophila) and 31 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR   GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR   GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:FlyBase.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0045874; P:positive regulation of sevenless signaling pathway; IGI:FlyBase.
DR   GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR   GO; GO:0050821; P:protein stabilization; IGI:FlyBase.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR045578; USP47_C.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF702; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 47; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF19718; USP47_C; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q24574; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..1556
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 47"
FT                   /id="PRO_0000080687"
FT   DOMAIN          396..779
FT                   /note="USP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT   REGION          117..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1087..1148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1124..1143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        405
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093,
FT                   ECO:0000305|PubMed:10949024, ECO:0000305|PubMed:26169834"
FT   ACT_SITE        720
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         272..289
FT                   /note="Missing (in isoform D)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054033"
FT   MUTAGEN         405
FT                   /note="C->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10949024"
FT   MUTAGEN         405
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:26169834"
FT   CONFLICT        437..439
FT                   /note="NIP -> KS (in Ref. 4; CAA67601)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        513
FT                   /note="D -> A (in Ref. 4; CAA67601)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        519
FT                   /note="E -> G (in Ref. 4; CAA67601)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525..526
FT                   /note="TR -> NDC (in Ref. 4; CAA67601)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        645
FT                   /note="D -> DS (in Ref. 5; AAL13901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        791
FT                   /note="A -> R (in Ref. 4; CAA67601)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        910
FT                   /note="Missing (in Ref. 4; CAA67601)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1556 AA;  173794 MW;  F70AE5BB2914E8BE CRC64;
     MTDKESEQCT VSVFDQTPGS EQKKINVVVR SHFTVKRVID LIGTQFSYEK FELLLQPHDN
     KDLVNLNALE SQLMYEVAGF EPQLKNHLIL LPSGSWDGDV TKRFELPIKR VVVKKVMKSD
     GEKAKSPATG EKKKRVVGEK TKKKPASGSS SPSKAKTTSE DSLAKTSISS ESSPEKTSKI
     KTTAAKISKP GSEKAPRASP EECPELSTEI NSKNTSSESP VAKKTAKVTS KPTLELLSPI
     KPSSPIKELD CEPVDTLSKQ QLSEQLQLYP QGRNLISPVD DAPSDLFISD AEQLSDDDLA
     LGASASPTML GPGYDYGAPT GDSDVEGVTG VTDPSTIGTD DGTYPALSNF YRRKYGGDEL
     RAWQRVNTTG ADFVSSATTE TEAEARQASL GPRGYVGLVN QAMTCYLNSL LQALFMTPEF
     RNALYRWEFD NDNEAKNIPY QLQKLFLNLQ TSPKAAVETT DLTRSFGWDS TEAWQQHDIQ
     ELCRVMFDAL EHKFKNTKQA NLISNLYEGK MNDYVKCLEC NTEKTREDTF LDIPLPVRPF
     GSSSAYGSIE EALRAFVQPE TLDGNNQYLC EKCKKKCDAH KGLHFKSFPY ILTLHLKRFD
     FDYQTMHRIK LNDRVTFPQT LNLNTFINRS GNSGEQNSQL NGTVDDCSTA DSGSAMEDDN
     LSSGVVTTAS SSQHENDLND EDEGIDMSSS TSKSAKQGSG PYLYELFAIM IHSGSASGGH
     YYAYIKDFDN NEWFCFNDQN VTSITQEDIQ RSFGGPNGSY YSSAYTSSTN AYMLMYRQVD
     AKRNELVAKV ADFPEHIKTL LPKLHSEEET RVSRLGRHIT VTDLALPDLY KPRVYFYNPS
     LKKMKITRVY VSQSFNINLV LMSAYEMLNV EQFAPLSRCR LVAYNSSMDT IIQSLESCTD
     PALTELRAAQ NYSLDFLLEY RAEDQEFEVY PPNGITWYVF KVDLSTMAMD GPFLVYSAAR
     EREASDVLRR SIALRLHISE QQFLLATVRA TVPKAFVSYD PHPTPEALQH LQNMANTQFK
     SITYFYLNVP NTDAATLEML GVPTVESVEC ASGGDVVDAA MMNGVAPGHM SSSNDYDWRR
     YKRDLVEPMS QPSPSHGHES NSEDSSLSDG DRTLVETDNM AHRGGGDSQV SSTSHSPQLS
     SPEDEAASHD AMMRVHAYCN GNGSYAAADV VDPLLLPTST NHFFYATKVE CVDVVGTGSS
     SGHQSDEEAQ LRKPTRAYKL LVGTHMRMGA FKKHIEQLIQ VPAAHFKLQR KHDNNLSNNQ
     NNSLVHLIEG ETLTVELGKT LEPDEFKAKI HFLRLADIDN ETSKLPCVCE WVYNANTTAE
     QAKKELVAKL HRIDAKYATL SVQNCRIWLK GGRIPIKILS DDETLYCDMR SSIAAEFIVQ
     ECEEEVDPQP KDDSLTLFVR RWCPAKLEFG KFQEITLDQD SEIRLSLSQI SDIPIDKLSY
     MKLNSNFPCT SISALSVNES SSWYSVPTTL DKYPLNSTQT GNIYLYKDRT VPARELTLEE
     RRLMNAREKA RLDRVGCVST TRYAQRRERA LKIYLDSPEK SSNVTASAPM DVHVNN
//