DNMT1_BOVIN
ID DNMT1_BOVIN Reviewed; 1611 AA.
AC Q24K09; Q6Y856; Q7YS60;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 1;
DE Short=Dnmt1;
DE EC=2.1.1.37;
GN Name=DNMT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12971987; DOI=10.1016/s1567-133x(03)00121-2;
RA Golding M.C., Westhusin M.E.;
RT "Analysis of DNA (cytosine 5) methyltransferase mRNA sequence and
RT expression in bovine preimplantation embryos, fetal and adult tissues.";
RL Gene Expr. Patterns 3:551-558(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Lee P., Min K.S., Seong H.H., Park J.K., Lee Y.K., Kim S.W., Kim S.J.,
RA Lee H.G., Chung H.K., Chang Y.M., Chang W.K., Kwon M.;
RT "Bovine (Bos taurus) cytosine-5-methyltransferase (Dnmt1) cDNA.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methylates CpG residues. Preferentially methylates
CC hemimethylated DNA. Associates with DNA replication sites in S phase
CC maintaining the methylation pattern in the newly synthesized strand,
CC that is essential for epigenetic inheritance. Associates with chromatin
CC during G2 and M phases to maintain DNA methylation independently of
CC replication. It is responsible for maintaining methylation patterns
CC established in development. DNA methylation is coordinated with
CC methylation of histones. Mediates transcriptional repression by direct
CC binding to HDAC2. In association with DNMT3B and via the recruitment of
CC CTCFL/BORIS, involved in activation of BAG1 gene expression by
CC modulating dimethylation of promoter histone H3 at H3K4 and H3K9.
CC Probably forms a corepressor complex required for activated KRAS-
CC mediated promoter hypermethylation and transcriptional silencing of
CC tumor suppressor genes (TSGs) or other tumor-related genes in
CC colorectal cancer (CRC) cells. Also required to maintain a
CC transcriptionally repressive state of genes in undifferentiated
CC embryonic stem cells (ESCs). Associates at promoter regions of tumor
CC suppressor genes (TSGs) leading to their gene silencing. Promotes tumor
CC growth. {ECO:0000250|UniProtKB:P13864, ECO:0000250|UniProtKB:P26358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC -!- SUBUNIT: Homodimer. Forms a stable complex with E2F1, BB1 and HDAC1.
CC Forms a complex with DMAP1 and HDAC2, with direct interaction.
CC Interacts with the PRC2/EED-EZH2 complex. Probably part of a
CC corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1.
CC Interacts with UHRF1; promoting its recruitment to hemimethylated DNA.
CC Interacts with USP7, promoting its deubiquitination. Interacts with
CC BAZ2A/TIP5. Interacts with PCNA. Interacts with MBD2 and MBD3.
CC Interacts with DNMT3A and DNMT3B. Interacts with UBC9. Interacts with
CC HDAC1. Interacts with CSNK1D. Interacts with SIRT7. Interacts with
CC ZNF263; recruited to the SIX3 promoter along with other proteins
CC involved in chromatin modification and transcriptional corepression
CC where it contributes to transcriptional repression (By similarity).
CC {ECO:0000250|UniProtKB:P13864, ECO:0000250|UniProtKB:P26358}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The N-terminal part is required for homodimerization and acts
CC as a regulatory domain.
CC -!- DOMAIN: The CXXC-type zinc finger specifically binds to unmethylated
CC CpG dinucleotides, positioning the autoinhibitory linker between the
CC DNA and the active site, thus providing a mechanism to ensure that only
CC hemimethylated CpG dinucleotides undergo methylation.
CC {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Sumoylated; sumoylation increases activity.
CC {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates
CC cell cycle G(2)/M transition. Deacetylation of Lys-1346 and Lys-1412 by
CC SIRT1 increases methyltransferase activity.
CC {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Phosphorylation of Ser-154 by CDKs is important for enzymatic
CC activity and protein stability. Phosphorylation of Ser-143 by AKT1
CC prevents methylation by SETD7 therebye increasing DNMT1 stability.
CC {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal
CC degradation. {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts
CC ubiquitination by UHRF1 by promoting deubiquitination and preventing
CC degradation by the proteasome. {ECO:0000250|UniProtKB:P13864}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; AY244709; AAP20551.1; -; mRNA.
DR EMBL; AY173048; AAO44952.1; -; mRNA.
DR EMBL; BC114063; AAI14064.1; -; mRNA.
DR RefSeq; NP_872592.2; NM_182651.2.
DR PDB; 6PZV; X-ray; 3.01 A; C/G=349-594.
DR PDB; 7LMK; X-ray; 2.65 A; A/B/C/D=725-837, A/B/C/D=859-897.
DR PDB; 7LMM; X-ray; 2.80 A; A/B/C/D=725-837, A/B/C/D=859-897.
DR PDBsum; 6PZV; -.
DR PDBsum; 7LMK; -.
DR PDBsum; 7LMM; -.
DR AlphaFoldDB; Q24K09; -.
DR SMR; Q24K09; -.
DR BioGRID; 158481; 1.
DR STRING; 9913.ENSBTAP00000003549; -.
DR REBASE; 7406; M.BtaDnmt1AP.
DR PaxDb; Q24K09; -.
DR PRIDE; Q24K09; -.
DR GeneID; 281119; -.
DR KEGG; bta:281119; -.
DR CTD; 1786; -.
DR eggNOG; ENOG502QPKK; Eukaryota.
DR HOGENOM; CLU_003040_0_0_1; -.
DR InParanoid; Q24K09; -.
DR OrthoDB; 898916at2759; -.
DR TreeFam; TF328926; -.
DR BRENDA; 2.1.1.37; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010216; P:maintenance of DNA methylation; ISS:UniProtKB.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR017198; DNMT1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002857; Znf_CXXC.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF12047; DNMT1-RFD; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR PIRSF; PIRSF037404; DNMT1; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 2.
DR SMART; SM01137; DMAP_binding; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Chromatin regulator; DNA-binding;
KW Isopeptide bond; Metal-binding; Methylation; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1611
FT /note="DNA (cytosine-5)-methyltransferase 1"
FT /id="PRO_0000239845"
FT DOMAIN 16..109
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT DOMAIN 752..877
FT /note="BAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 969..1097
FT /note="BAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REPEAT 1106..1107
FT /note="1"
FT REPEAT 1108..1109
FT /note="2"
FT REPEAT 1110..1111
FT /note="3"
FT REPEAT 1112..1113
FT /note="4"
FT REPEAT 1114..1115
FT /note="5; approximate"
FT DOMAIN 1136..1595
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ZN_FING 643..689
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 1..334
FT /note="Interaction with the PRC2/EED-EZH2 complex"
FT /evidence="ECO:0000250"
FT REGION 1..148
FT /note="Interaction with DNMT3A"
FT /evidence="ECO:0000250"
FT REGION 1..120
FT /note="Interaction with DMAP1"
FT /evidence="ECO:0000250"
FT REGION 123..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..216
FT /note="Interaction with DNMT3B"
FT /evidence="ECO:0000250"
FT REGION 163..174
FT /note="Interaction with PCNA"
FT /evidence="ECO:0000250"
FT REGION 306..603
FT /note="Interaction with the PRC2/EED-EZH2 complex"
FT /evidence="ECO:0000250"
FT REGION 329..548
FT /note="DNA replication foci-targeting sequence"
FT /evidence="ECO:0000250"
FT REGION 594..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..751
FT /note="Autoinhibitory linker"
FT REGION 695..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1115
FT /note="5 X 2 AA tandem repeats of K-G"
FT REGION 1118..1611
FT /note="Interaction with the PRC2/EED-EZH2 complex"
FT /evidence="ECO:0000250"
FT REGION 1136..1611
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT MOTIF 177..204
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 150..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 653
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 656
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 667
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 688
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 1143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1147..1148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1165..1166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1187..1188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1574
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1576
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT SITE 507
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT MOD_RES 70
FT /note="N6,N6-dimethyllysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT MOD_RES 142
FT /note="N6-methyllysine; by SETD7"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 143
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 160
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 257
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 746
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 888
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 954
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 958
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 972
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1051
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT MOD_RES 1346
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1412
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT CROSSLNK 1605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT CONFLICT 655
FT /note="I -> V (in Ref. 2; AAO44952)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="H -> R (in Ref. 2; AAO44952)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="T -> A (in Ref. 2; AAO44952)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176
FT /note="L -> F (in Ref. 1; AAP20551)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186
FT /note="E -> K (in Ref. 1; AAP20551)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="L -> V (in Ref. 1; AAP20551)"
FT /evidence="ECO:0000305"
FT CONFLICT 1209
FT /note="P -> L (in Ref. 1; AAP20551)"
FT /evidence="ECO:0000305"
FT CONFLICT 1287
FT /note="M -> R (in Ref. 1; AAP20551)"
FT /evidence="ECO:0000305"
FT CONFLICT 1387
FT /note="G -> R (in Ref. 1; AAP20551)"
FT /evidence="ECO:0000305"
FT CONFLICT 1405
FT /note="I -> T (in Ref. 2; AAO44952)"
FT /evidence="ECO:0000305"
FT CONFLICT 1466
FT /note="S -> T (in Ref. 2; AAO44952)"
FT /evidence="ECO:0000305"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6PZV"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:6PZV"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 402..411
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:6PZV"
FT TURN 424..428
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:6PZV"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:6PZV"
FT HELIX 494..516
FT /evidence="ECO:0007829|PDB:6PZV"
FT HELIX 522..531
FT /evidence="ECO:0007829|PDB:6PZV"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:6PZV"
FT HELIX 545..549
FT /evidence="ECO:0007829|PDB:6PZV"
FT HELIX 552..564
FT /evidence="ECO:0007829|PDB:6PZV"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:6PZV"
FT STRAND 728..733
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 739..749
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 752..755
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 759..762
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 772..782
FT /evidence="ECO:0007829|PDB:7LMK"
FT TURN 783..785
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 786..795
FT /evidence="ECO:0007829|PDB:7LMK"
FT HELIX 797..799
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 812..821
FT /evidence="ECO:0007829|PDB:7LMK"
FT HELIX 822..824
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 825..829
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 865..867
FT /evidence="ECO:0007829|PDB:7LMK"
FT TURN 868..871
FT /evidence="ECO:0007829|PDB:7LMK"
FT STRAND 872..875
FT /evidence="ECO:0007829|PDB:7LMK"
FT TURN 883..885
FT /evidence="ECO:0007829|PDB:7LMK"
FT HELIX 886..888
FT /evidence="ECO:0007829|PDB:7LMK"
FT HELIX 891..896
FT /evidence="ECO:0007829|PDB:7LMK"
SQ SEQUENCE 1611 AA; 182842 MW; A7F0D9B24A18771C CRC64;
MPARTAPARV PALASRAFSL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH EFLRTEIKNQ
LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGAHAFS REANGCLENG SQTSGEDCRV
VMAEKGKPPK PVSRLYTPRR SKSDGETKSE VSSSPRITRK TTRQTTITSH FPRGPAKRKP
EEEPEKVKSD DSVDEEKDQE EKRRRVTSRE RVAGLLPAEE PGRVRPGTHM EEEGRDDKEE
KRLRSQTKEP TPKHKAKEEP DRDVRPGGAQ AEMNEGEDKD EKRHRSQPKD LASKRRPEEK
EPERVKPQVS DEKDEDEKEE KRRRTTYREL TEKKMTRTKI AVVSKTNPPK CTECLQYLDD
PELRYEQHPP DAVEEIQILT NERLSIFDAN ESGFESYEDL PQHKLTCFSV YCKRGHLCPI
DTGLIEKDVE LLFSGSAKPI YEDDPSPEGG INGKNFGPIN EWWIAGFDGG EKALLGFSTS
FAEYILMDPS PEYAPLFSVM QEKIYISKIV VEFLQSNPDS TYEDLINKIE TTVPPCMLNL
NRFTEDSLLR HAQFVVEQVE SYDRAGDSDE QPIFLSPCMR DLIKLAGVTL GKRRAERRQT
IRQPAKEKDK GPTKATTTKL VYQIFDTFFA EQIEKDDKED KENAFKRRRC GVCEICQQPE
CGKCKACKDM VKFGGSGRSK QACQKRRCPN MAMKEADDDE EVDDNIPEMP SPKKMHQGKK
KKQNKNRISW VGDAVKTDGK KSYYKKVCID SETLEVGDCV SVIPDDSSKP LYLARVTALW
EDSSNGQMFH AHWFCAGTDT VLGATSDPLE LFLVDECEDM QLSYIHSKVQ VIYKAPSENW
AMEGGVDPEA LMSEDDGKTY FYQLWYDQDY ARFESPPKTQ PTEDNKYKFC ASCARLAEMR
QKEIPRVVEQ LQDLEGRVLY SLATKNGVQY RVGDGVYLPP EAFTFNIKLS SPVKRPRKEP
VDEALYPEHY RKYSDYIKGS NLDAPEPYRI GRIKEIFCSK KSNGRPNETD IKIRVNKFYR
PENTHKSTPA SYHADINLLY WSDEEAVVDF KAVQGRCTVE YGEDLPQCLQ DFSAGGPDRF
YFLEAYNAKS KSFEDPPNHA RSTGNKGKGK GKGKNRTKSQ TCEPSELETE IKLPKLRTLD
VFSGCGGLSE GFHQAGISET LWAIEMWDPA AQAFRLNNPG STVFTEDCNV LLKLVMAGEV
TNSRGQKLPQ KGDVEMLCGG PPCQGFSGMN RFNSRTYSKF KNSLVVSFLS YCDYYRPRYF
LLENVRNFVS FKRSMVLKLT LRCLVRMGYQ CTFGVLQAGQ YGVAQTRRRA IILAAAPGEP
LPLFPEPLHV FAPRACQLSV VVDDKKFVSN ITRLSSGPFR TITVRDTMSD LPEIRNGASA
LEISYNGEPQ SWFQRQLRGS QYQPILRDHI CKDMSALVAA RMRHIPLAPG SDWRDLPNIE
VRLSDGTLAR KLRYNYHDKK NGCSSSGALR GVCSCVEGKP CEPAARQFNT LIPWCLPHTG
NRHNHWAGLY GRLEWDGFFS TTVTNPEPMG KQGRVLHPEQ HRVVSVRECA RSQGFPDTYR
LFGNILDKHR QVGNAVPPPL AKAIGLEIKR CMLAKARESA SAKIKEEAAK D
