ATR_DROME
ID ATR_DROME Reviewed; 2517 AA.
AC Q9VXG8; Q24135;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Serine/threonine-protein kinase ATR;
DE EC=2.7.11.1;
DE AltName: Full=Ataxia telangiectasia and Rad3-related protein homolog;
DE Short=ATR homolog;
DE Short=dATR;
DE AltName: Full=Meiotic protein 41;
GN Name=mei-41; ORFNames=CG4252;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=7671309; DOI=10.1016/0092-8674(95)90478-6;
RA Hari K.L., Santerre A., Sekelsky J.J., McKim K.S., Boyd J.B., Hawley R.S.;
RT "The mei-41 gene of D. melanogaster is a structural and functional homolog
RT of the human ataxia telangiectasia gene.";
RL Cell 82:815-821(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH MUS304.
RX PubMed=14729967; DOI=10.1128/mcb.24.3.1219-1231.2004;
RA Brodsky M.H., Weinert B.T., Tsang G., Rong Y.S., McGinnis N.M., Golic K.G.,
RA Rio D.C., Rubin G.M.;
RT "Drosophila melanogaster MNK/Chk2 and p53 regulate multiple DNA repair and
RT apoptotic pathways following DNA damage.";
RL Mol. Cell. Biol. 24:1219-1231(2004).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10209095; DOI=10.1016/s0960-9822(99)80138-9;
RA Sibon O.C.M., Laurencon A., Hawley R., Theurkauf W.E.;
RT "The Drosophila ATM homologue Mei-41 has an essential checkpoint function
RT at the midblastula transition.";
RL Curr. Biol. 9:302-312(1999).
RN [6]
RP FUNCTION.
RX PubMed=11676920; DOI=10.1016/s0960-9822(01)00483-3;
RA Garner M., van Kreeveld S., Su T.T.;
RT "mei-41 and bub1 block mitosis at two distinct steps in response to
RT incomplete DNA replication in Drosophila embryos.";
RL Curr. Biol. 11:1595-1599(2001).
RN [7]
RP FUNCTION.
RX PubMed=12361566; DOI=10.1016/s0960-9822(02)01165-x;
RA Abdu U., Brodsky M., Schuepbach T.;
RT "Activation of a meiotic checkpoint during Drosophila oogenesis regulates
RT the translation of Gurken through Chk2/Mnk.";
RL Curr. Biol. 12:1645-1651(2002).
RN [8]
RP FUNCTION.
RX PubMed=12689597; DOI=10.1016/s1534-5807(03)00085-6;
RA Zhou L., Steller H.;
RT "Distinct pathways mediate UV-induced apoptosis in Drosophila embryos.";
RL Dev. Cell 4:599-605(2003).
RN [9]
RP MUTAGENESIS OF TRP-253; ALA-647; SER-810; THR-815; LEU-818; HIS-2032 AND
RP PRO-2322.
RX PubMed=12807779; DOI=10.1093/genetics/164.2.589;
RA Laurencon A., Purdy A., Sekelsky J., Hawley R.S., Su T.T.;
RT "Phenotypic analysis of separation-of-function alleles of MEI-41,
RT Drosophila ATM/ATR.";
RL Genetics 164:589-601(2003).
RN [10]
RP FUNCTION.
RX PubMed=14711410; DOI=10.1016/j.cub.2003.12.032;
RA Jaklevic B.R., Su T.T.;
RT "Relative contribution of DNA repair, cell cycle checkpoints, and cell
RT death to survival after DNA damage in Drosophila larvae.";
RL Curr. Biol. 14:23-32(2004).
RN [11]
RP PHOSPHORYLATION OF GRP.
RX PubMed=15860729; DOI=10.1242/jcs.02309;
RA de Vries H.I., Uyetake L., Lemstra W., Brunsting J.F., Su T.T.,
RA Kampinga H.H., Sibon O.C.M.;
RT "Grp/DChk1 is required for G2-M checkpoint activation in Drosophila S2
RT cells, whereas Dmnk/DChk2 is dispensable.";
RL J. Cell Sci. 118:1833-1842(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1569; TYR-1570; SER-1573 AND
RP THR-1575, 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 [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=29746464; DOI=10.1371/journal.pbio.2005687;
RA Seller C.A., O'Farrell P.H.;
RT "Rif1 prolongs the embryonic S phase at the Drosophila mid-blastula
RT transition.";
RL PLoS Biol. 16:E2005687-E2005687(2018).
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR),
CC ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates various proteins, which collectively inhibits DNA
CC replication and mitosis and promotes DNA repair and recombination.
CC Phosphorylates grp/CHK1. Phosphorylates 'Ser-137' of histone variant
CC H2AX/H2AV at sites of DNA damage, thereby regulating DNA damage
CC response mechanism. Essential for the DNA damage checkpoint in larval
CC imaginal disks and neuroblasts and for the DNA replication checkpoint
CC in the embryo. Has also an essential role during early nuclear
CC divisions in embryos, where it is required to delay mitosis in response
CC to incomplete DNA replication. Also plays an important role during
CC meiosis, where it may monitor double-strand-break repair during meiotic
CC crossing over, to regulate the progression of prophase I, and to
CC enforce metaphase I delay observed at the end of oogenesis.
CC {ECO:0000269|PubMed:10209095, ECO:0000269|PubMed:11676920,
CC ECO:0000269|PubMed:12361566, ECO:0000269|PubMed:12689597,
CC ECO:0000269|PubMed:14711410, ECO:0000269|PubMed:7671309}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with mus304. {ECO:0000269|PubMed:14729967}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:10209095}.
CC -!- DISRUPTION PHENOTYPE: In embryos, during S phase of mid-blastula
CC transition, fails to delay the activation of Cdk1, leads to loss of
CC Rif1 foci, and results in cells entering prematurely into mitosis 13
CC before the completion of replication resulting in chromosome bridging.
CC {ECO:0000269|PubMed:29746464}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Called dATM in some references while it is the ortholog of
CC ATR. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC46881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U34925; AAC46881.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY282465; AAQ22732.1; -; mRNA.
DR EMBL; AE014298; AAF48604.2; -; Genomic_DNA.
DR PIR; T13288; T13288.
DR RefSeq; NP_523369.2; NM_078645.3.
DR AlphaFoldDB; Q9VXG8; -.
DR SMR; Q9VXG8; -.
DR BioGRID; 58948; 34.
DR IntAct; Q9VXG8; 4.
DR STRING; 7227.FBpp0074047; -.
DR iPTMnet; Q9VXG8; -.
DR PaxDb; Q9VXG8; -.
DR PRIDE; Q9VXG8; -.
DR EnsemblMetazoa; FBtr0074271; FBpp0074047; FBgn0004367.
DR GeneID; 32608; -.
DR KEGG; dme:Dmel_CG4252; -.
DR CTD; 32608; -.
DR FlyBase; FBgn0004367; mei-41.
DR VEuPathDB; VectorBase:FBgn0004367; -.
DR eggNOG; KOG0890; Eukaryota.
DR GeneTree; ENSGT00940000155714; -.
DR HOGENOM; CLU_000178_1_0_1; -.
DR InParanoid; Q9VXG8; -.
DR OMA; YTVYSQM; -.
DR OrthoDB; 80538at2759; -.
DR PhylomeDB; Q9VXG8; -.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-69473; G2/M DNA damage checkpoint.
DR SignaLink; Q9VXG8; -.
DR BioGRID-ORCS; 32608; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32608; -.
DR PRO; PR:Q9VXG8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004367; Expressed in egg cell and 11 other tissues.
DR ExpressionAtlas; Q9VXG8; baseline and differential.
DR Genevisible; Q9VXG8; DM.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase.
DR GO; GO:0007349; P:cellularization; TAS:FlyBase.
DR GO; GO:0030261; P:chromosome condensation; IGI:FlyBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:FlyBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR GO; GO:0045002; P:double-strand break repair via single-strand annealing; IMP:FlyBase.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IMP:FlyBase.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; TAS:FlyBase.
DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; TAS:FlyBase.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IDA:FlyBase.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:FlyBase.
DR GO; GO:0030716; P:oocyte fate determination; IMP:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IMP:FlyBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:FlyBase.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IMP:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB.
DR GO; GO:0007348; P:regulation of syncytial blastoderm mitotic cell cycle; TAS:FlyBase.
DR GO; GO:0009314; P:response to radiation; TAS:FlyBase.
DR GO; GO:0000723; P:telomere maintenance; IGI:FlyBase.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR012993; UME.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; DNA damage; DNA repair; DNA-binding;
KW Kinase; Manganese; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2517
FT /note="Serine/threonine-protein kinase ATR"
FT /id="PRO_0000225630"
FT REPEAT 1178..1214
FT /note="HEAT"
FT DOMAIN 1509..2066
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2184..2508
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2485..2517
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2190..2196
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2360..2368
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2380..2404
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOD_RES 1569
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1570
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 253
FT /note="W->T: In mei-41D12; induces a weak sensitivity to
FT methanesulfonate."
FT /evidence="ECO:0000269|PubMed:12807779"
FT MUTAGEN 647
FT /note="A->V: In mei-41D3; induces a very strong sensitivity
FT to methanesulfonate and female infertility."
FT /evidence="ECO:0000269|PubMed:12807779"
FT MUTAGEN 810
FT /note="S->F: In mei-41D9; induces some sensitivity to
FT methanesulfonate."
FT /evidence="ECO:0000269|PubMed:12807779"
FT MUTAGEN 815
FT /note="T->P: In mei-41D15; induces some sensitivity to
FT methanesulfonate."
FT /evidence="ECO:0000269|PubMed:12807779"
FT MUTAGEN 818
FT /note="L->F: In mei-41D14; induces some sensitivity to
FT methanesulfonate."
FT /evidence="ECO:0000269|PubMed:12807779"
FT MUTAGEN 2032
FT /note="H->Y: In mei-41D12; induces a weak sensitivity to
FT methanesulfonate."
FT /evidence="ECO:0000269|PubMed:12807779"
FT MUTAGEN 2322
FT /note="P->L: In mei-41D5; induces a strong sensitivity to
FT methanesulfonate."
FT /evidence="ECO:0000269|PubMed:12807779"
FT CONFLICT 22
FT /note="N -> I (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="M -> L (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="H -> Y (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="L -> M (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="R -> Q (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="Y -> H (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="S -> G (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="T -> A (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
FT CONFLICT 1125
FT /note="N -> D (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
FT CONFLICT 1350
FT /note="R -> K (in Ref. 1; AAC46881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2517 AA; 289330 MW; 8ABE2499EA477B88 CRC64;
MSTQRKDMWK LLYNHVNRNV SNFSGVYSVI EDILCQEPSL ISCSLVRELH NKFQDTFLLW
LLNKLAKCLS ESPDSSECIN LQRKILSSCC SNHPKLFERL VLAYVEAIEE THLQLSSLDL
GQLSNERKPA ITVRIFRCDV ECLQEFDPHC AIEDIKVPLE QADMYAKSLL EVLQHAHHIG
YATHGDIFSG SLHQALLILK ECDMDTKLAS LNYCHNVLRS QSASSWITNP DVGHYAQLTL
EATAIMWSAV AKWLDMGCMT RQELKRLNIT TKLLLEVLHM RARPAHHLGY LLLNEILSLP
TAIELDDGLL ETLSSYIQGQ LEHSVVPLEQ LVHLQQLMLS HWHCHPTHLV PILALMGLKQ
TEMRSGVVQV LTQSLVEILK KEEVLSKDWQ KLIAILRGFK QLEKLILSQS QHKIAEHEGH
IDSSVLAMLP LQCEIIKVAD TNWNNLSMQL VELESKCSAD RRHIHLEICS LLMQITFIRH
FLKTQTQHQL LAILQRHLKL SYLCAIRLET PSSVHTQMQS FYAQQYMRLF QSEETQEIFC
SNLPQLYISG FIKPEQLMKA LPTINNRSGR AQVIRLLLCS QPGKLSVFKV KDRIELYCPK
CRPLPKKLPG IYLGKCKQQL PCPDFSSTNL EMIANDLLFY PDFECIAQHL DLLCFEPNVI
LGLLRETEAL QKVSVKVIGQ LVSAMRVRSP EFLEQLANLV LAAIKAMLAK PLTEQNVLQQ
RSMLNVLTAI AHMEDNEIWL FHWFKMTFFF LVHTRSLVAQ EAVLAATEMC ASQGLQTIHL
WNWYKRDALD LTVRLALNVY LLDGVRFTRS LRALTKMLGF TCVQEFTCKY HRLLTAMVLP
HCIVNPLCKG VLVLIAKQMQ KHIGTLFSIS FLRIYTHVFL TEEPELANSC IELVVSCTQS
SLQQLMNADV KQTVAELLIY FNRNPTFVMR SFQSLLQLSI GSLEELSSQT ANAEFANFIA
ERFLGVITYF ESCLSEPSFE KPLKEETLYS LGQIMRFVGS QHVTQFRFKI IAMLSFVHTL
QEPRLQRICL KIWHIFLHVV NVQELGPSLG RIVATLQPLL ADNESVKQVN DLYEFIILRN
ASMLGTFITD LYFLDRMENV SPSIQKCIRR HTAHLDLKGL AEEENQSPPL VDQLRFLQKH
ITDECLQVRV YALQHLGDLF GRRRPKLNST ILSELPLEPM LEQIVNVLMA GCQHDDSQLQ
MASAKCLGEL GAIDASYLPS NYNFASPQHL PLNILSDDFA VLALTSLCRG YQFQQNTKHV
DSFSLAIQET LAICGISPKE QKKVQLWQSL PARMRQLMEP MLHSCYTCVH RPSTCLQQPL
FGSHYSHNYY EEWAFLWASR LIDYLPSSGR RHLLSSYKPC IKRDSNMLST FYPYILLHAL
LECTTEQRNH IQEEFMAVLQ ANEESSSSVR GRQELGAIKE NAFKQFESRK YAAGIKPLAS
TLVSDRKEDS SRVPRLAGKL CAELLDFLQR WLREWQRIHG RSTGGKPPET IDSNYRKIHE
FLNLIPKLLV SRASYNCGEY ARALSYLESY LEEGEDKSQR LLEQFTFLVE VYGSLRDPDS
VEGAVQVRSY DMSVTQDILV NRLVERQQDM ITSYEQLLSS TDQMQPDHVR AMIDAYLRDT
PKTAQLIADG LWQRLSDRYS DQCFAECKSE LLWRLGSYDE MEELQSNWPA QCSQGCLKLR
RPLTTRIEFD SLLDGMRESV LEELRSCSAV QQHSYANAYD AVLKLHLVHE LHCSQELVEK
LEQDRDEDNQ EKLMKNYFDD WQYRLQIVQP QVRIQESIYS FRRNILAELQ RRLTDRNHLL
PHLKTELARI WLNSAQINRN AGQLQRAQLY ILKAAEYQPS GLFIERAKLL WQKGDQVMAM
NYLEEQLSIM RSGCQGNVKQ LAAEQRHLFF RGKYLQAVYS AESMHLCADA VLKYFQEAIA
VHRQSESCHV QMAQFLEKIL EARQGGKSEP TGEQDDMLIN VMVNYAKSLR YGSEHVYQSM
PRLISLWLDT TESSTNTEQV KKMNDLLTNC CTALPTAVFY TVYSQMLSRL CHPVNDVFTV
LRNVIIKLVE AYPQQSLWML LPHFKSAKAH RIKRCKLVLT DSRLQNSTFQ KLLQDFNSLT
ERLMDLTNKE VTLDRTYKLS DLDTRLSKLC KQPEFSQILL PFEKYMQPTL PLNSDSNSSE
GSHLPANQST VNWFPYQQIY ISGFQESVLI LRSAAKPKKL TIRCSDGKDY DVLVKPKDDL
RRDARLMEFN GLVKRYLHQD APARQRRLHI RTYAVLPFNE ECGLVEWLPN LASYRSICMN
LYAQRRLVMS TRQLQSLAVP LHESIERKRE VFTKQLVPAH PPVFQEWLRQ RFATPHSWYE
ARNTYIRTVA VMSMVGYILG LGDRHGENIL FAEGNGDAVH VDFNCLFNQG ELLPYPEVVP
FRLTHNMIVA MGPLGVEGSF RKCCEITLRL LKQESKTLMS ILRPFVYDVG AQTRKGAATA
KITKDVQRIA DRLQGHVKRQ QANSIPLSTE GQVNFLINEA TKVDNLASMY IGWGAFL
