##gff-version 3 O14746 UniProtKB Chain 1 1132 . . . ID=PRO_0000054925;Note=Telomerase reverse transcriptase O14746 UniProtKB Domain 605 935 . . . Note=Reverse transcriptase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 O14746 UniProtKB Region 1 230 . . . Note=RNA-interacting domain 1 O14746 UniProtKB Region 58 197 . . . Note=GQ motif O14746 UniProtKB Region 137 141 . . . Note=Required for regulating specificity for telomeric DNA and for processivity for primer elongation O14746 UniProtKB Region 210 320 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14746 UniProtKB Region 231 324 . . . Note=Linker O14746 UniProtKB Region 301 538 . . . Note=Required for oligomerization O14746 UniProtKB Region 325 550 . . . Note=RNA-interacting domain 2 O14746 UniProtKB Region 376 521 . . . Note=QFP motif O14746 UniProtKB Region 397 417 . . . Note=CP motif O14746 UniProtKB Region 914 928 . . . Note=Required for oligomerization O14746 UniProtKB Region 930 934 . . . Note=Primer grip sequence O14746 UniProtKB Region 936 1132 . . . Note=CTE O14746 UniProtKB Motif 222 240 . . . Note=Bipartite nuclear localization signal O14746 UniProtKB Motif 328 333 . . . Note=TFLY%3B involved in RNA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q4KTA7 O14746 UniProtKB Binding site 712 712 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 O14746 UniProtKB Binding site 868 868 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 O14746 UniProtKB Binding site 869 869 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00405 O14746 UniProtKB Site 169 169 . . . Note=Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template O14746 UniProtKB Site 867 867 . . . Note=Required for nucleotide incorporation and primer extension rate O14746 UniProtKB Modified residue 227 227 . . . Note=Phosphoserine%3B by PKB/AKT1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22366458;Dbxref=PMID:22366458 O14746 UniProtKB Modified residue 457 457 . . . Note=Phosphoserine%3B by DYRK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23362280;Dbxref=PMID:23362280 O14746 UniProtKB Modified residue 707 707 . . . Note=Phosphotyrosine%3B by SRC-type Tyr-kinases;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808100,ECO:0000269|PubMed:18829466;Dbxref=PMID:12808100,PMID:18829466 O14746 UniProtKB Alternative sequence 711 722 . . . ID=VSP_053369;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14654914;Dbxref=PMID:14654914 O14746 UniProtKB Alternative sequence 764 807 . . . ID=VSP_019587;Note=In isoform 2 and isoform 4. STLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFD->LRPVPGDPAGLHPLHAALQPVLRRHGEQAVCGDSAGRAAPAFGG;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12869302,ECO:0000303|PubMed:14654914;Dbxref=PMID:12869302,PMID:14654914 O14746 UniProtKB Alternative sequence 808 1132 . . . ID=VSP_019588;Note=In isoform 2 and isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12869302,ECO:0000303|PubMed:14654914;Dbxref=PMID:12869302,PMID:14654914 O14746 UniProtKB Alternative sequence 885 947 . . . ID=VSP_021727;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14654914;Dbxref=PMID:14654914 O14746 UniProtKB Natural variant 55 55 . . . ID=VAR_062535;Note=In PFBMFT1%3B impaired telomerase activity. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392301;Dbxref=dbSNP:rs387907247,PMID:17392301 O14746 UniProtKB Natural variant 65 65 . . . ID=VAR_062780;Note=Risk factor for acute myeloid leukemia. P->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19147845,ECO:0000269|PubMed:19760749;Dbxref=dbSNP:rs544215765,PMID:19147845,PMID:19760749 O14746 UniProtKB Natural variant 170 170 . . . ID=VAR_068792;Note=In PFBMFT1%3B the mutant protein is demonstrated to cause decreased telomerase activity. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21436073;Dbxref=dbSNP:rs387907248,PMID:21436073 O14746 UniProtKB Natural variant 202 202 . . . ID=VAR_036863;Note=In PFBMFT1 and AA%3B severe and moderate%3B shorter telomeres. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15814878,ECO:0000269|PubMed:15885610,ECO:0000269|PubMed:19760749;Dbxref=dbSNP:rs121918661,PMID:15814878,PMID:15885610,PMID:19760749 O14746 UniProtKB Natural variant 279 279 . . . ID=VAR_036864;Note=A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15814878;Dbxref=dbSNP:rs61748181,PMID:15814878 O14746 UniProtKB Natural variant 299 299 . . . ID=VAR_062781;Note=Risk factor for acute myeloid leukemia. V->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19147845,ECO:0000269|PubMed:19760749;Dbxref=dbSNP:rs756624928,PMID:19147845,PMID:19760749 O14746 UniProtKB Natural variant 381 381 . . . ID=VAR_084996;Note=R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31355908;Dbxref=dbSNP:rs777343359,PMID:31355908 O14746 UniProtKB Natural variant 412 412 . . . ID=VAR_025149;Note=In PFBMFT1%2C AA and DKCB4%3B severe and moderate%3B risk factor for acute myelogenous leukemia%3B the mutant protein has 36%25 residual activity. H->Y;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15814878,ECO:0000269|PubMed:18042801,ECO:0000269|PubMed:19147845,ECO:0000269|PubMed:19760749,ECO:0000269|Ref.7;Dbxref=dbSNP:rs34094720,PMID:15814878,PMID:18042801,PMID:19147845,PMID:19760749 O14746 UniProtKB Natural variant 441 441 . . . ID=VAR_036865;Note=In AA%3B risk factor for acute myeloid leukemia. Missing;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15814878,ECO:0000269|PubMed:19147845,ECO:0000269|PubMed:19760749;Dbxref=PMID:15814878,PMID:19147845,PMID:19760749 O14746 UniProtKB Natural variant 522 522 . . . ID=VAR_062782;Note=Risk factor for acute myeloid leukemia. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19147845,ECO:0000269|PubMed:19760749;Dbxref=dbSNP:rs1751108994,PMID:19147845,PMID:19760749 O14746 UniProtKB Natural variant 570 570 . . . ID=VAR_062536;Note=In AA%3B abolishes telomerase catalytic activity but no effect on binding to TERC. K->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16990594,ECO:0000269|PubMed:19760749;Dbxref=PMID:16990594,PMID:19760749 O14746 UniProtKB Natural variant 631 631 . . . ID=VAR_062783;Note=In AA. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19760749;Dbxref=dbSNP:rs199422294,PMID:19760749 O14746 UniProtKB Natural variant 682 682 . . . ID=VAR_062537;Note=In AA%3B non-severe%3B abolishes telomerase catalytic activity but little effect on binding to TERC. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627250,ECO:0000269|PubMed:16990594;Dbxref=dbSNP:rs199422295,PMID:16627250,PMID:16990594 O14746 UniProtKB Natural variant 694 694 . . . ID=VAR_036866;Note=In PFBMFT1 and AA%3B moderate. V->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15814878,ECO:0000269|PubMed:19760749;Dbxref=dbSNP:rs121918662,PMID:15814878,PMID:19760749 O14746 UniProtKB Natural variant 704 704 . . . ID=VAR_068793;Note=In DKCB4%3B the mutant protein has 13%25 residual activity. P->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18042801,ECO:0000269|PubMed:21602826;Dbxref=dbSNP:rs199422297,PMID:18042801,PMID:21602826 O14746 UniProtKB Natural variant 716 716 . . . ID=VAR_068794;Note=In PFBMFT1%3B the mutant protein is demonstrated to cause severely compromised telomerase activity. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21436073;Dbxref=dbSNP:rs387907249,PMID:21436073 O14746 UniProtKB Natural variant 721 721 . . . ID=VAR_062538;Note=In DKCB4%3B no effect on telomerase catalytic activity and little effect on binding to TERC. P->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16332973,ECO:0000269|PubMed:16990594;Dbxref=dbSNP:rs199422299,PMID:16332973,PMID:16990594 O14746 UniProtKB Natural variant 726 726 . . . ID=VAR_062539;Note=In AA%3B very severe%3B no effect on telomerase catalytic activity but shortened telomeres. T->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16627250,ECO:0000269|PubMed:16990594;Dbxref=dbSNP:rs149566858,PMID:16627250,PMID:16990594 O14746 UniProtKB Natural variant 772 772 . . . ID=VAR_036867;Note=In PFBMFT1%3B moderate. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15814878;Dbxref=dbSNP:rs121918663,PMID:15814878 O14746 UniProtKB Natural variant 785 785 . . . ID=VAR_062784;Note=In AA. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19760749;Dbxref=dbSNP:rs483352771,PMID:19760749 O14746 UniProtKB Natural variant 791 791 . . . ID=VAR_068795;Note=In PFBMFT1%3B associated with Met-867 in cis on the same allele%3B the double mutant shows severe defects in telomere repeat addition processivity. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21483807;Dbxref=dbSNP:rs141425941,PMID:21483807 O14746 UniProtKB Natural variant 811 811 . . . ID=VAR_062540;Note=In DKCB4%3B 50%25 reduction in telomerase activity. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17785587;Dbxref=dbSNP:rs199422301,PMID:17785587 O14746 UniProtKB Natural variant 841 841 . . . ID=VAR_068796;Note=In PFBMFT1. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21436073;Dbxref=PMID:21436073 O14746 UniProtKB Natural variant 865 865 . . . ID=VAR_036868;Note=In PFBMFT1. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17460043;Dbxref=dbSNP:rs121918666,PMID:17460043 O14746 UniProtKB Natural variant 867 867 . . . ID=VAR_068797;Note=In PFBMFT1%3B associated with Ile-791 in cis on the same allele%3B the double mutant shows severe defects in telomere repeat addition processivity%3B this mutation causes most if not all of the functional defects. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21483807;Dbxref=dbSNP:rs201159197,PMID:21483807 O14746 UniProtKB Natural variant 901 901 . . . ID=VAR_062541;Note=In DKCB4%3B severe phenotype overlapping with Hoyeraal-Hreidarsson syndrome%3B very short telomeres and greatly reduced telomerase activity. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17785587;Dbxref=dbSNP:rs199422304,PMID:17785587 O14746 UniProtKB Natural variant 902 902 . . . ID=VAR_036869;Note=In DKCA2%3B abolishes telomerase catalytic activity but no effect on binding to TERC. K->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16247010,ECO:0000269|PubMed:16990594;Dbxref=dbSNP:rs121918665,PMID:16247010,PMID:16990594 O14746 UniProtKB Natural variant 902 902 . . . ID=VAR_068798;Note=In PFBMFT1. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21436073;Dbxref=dbSNP:rs387907250,PMID:21436073 O14746 UniProtKB Natural variant 923 923 . . . ID=VAR_068799;Note=In PFBMFT1. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22512499;Dbxref=dbSNP:rs387907251,PMID:22512499 O14746 UniProtKB Natural variant 948 948 . . . ID=VAR_053726;Note=S->R;Dbxref=dbSNP:rs34062885 O14746 UniProtKB Natural variant 979 979 . . . ID=VAR_062542;Note=In DKCA2%3B shortened telomeres but no effect on telomerase catalytic activity nor on binding to TERC. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15885610,ECO:0000269|PubMed:16990594,ECO:0000269|PubMed:21602826;Dbxref=dbSNP:rs199422305,PMID:15885610,PMID:16990594,PMID:21602826 O14746 UniProtKB Natural variant 1025 1025 . . . ID=VAR_068800;Note=In PFBMFT1. V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21436073;Dbxref=PMID:21436073 O14746 UniProtKB Natural variant 1062 1062 . . . ID=VAR_025150;Note=Increased incidence in sporadic acute myeloid leukemia. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15814878,ECO:0000269|PubMed:19147845,ECO:0000269|PubMed:19760749,ECO:0000269|PubMed:31355908,ECO:0000269|Ref.7;Dbxref=dbSNP:rs35719940,PMID:15814878,PMID:19147845,PMID:19760749,PMID:31355908 O14746 UniProtKB Natural variant 1090 1090 . . . ID=VAR_036870;Note=In PFBMFT1%3B severe. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15814878;Dbxref=dbSNP:rs121918664,PMID:15814878 O14746 UniProtKB Natural variant 1110 1110 . . . ID=VAR_062543;Note=In PFBMFT1%3B uncertain significance%3B impaired telomerase activity. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17392301;Dbxref=dbSNP:rs199422306,PMID:17392301 O14746 UniProtKB Natural variant 1127 1127 . . . ID=VAR_062544;Note=In DKCA2%3B severe%3B shortened telomeres but no effect on telomerase catalytic activity nor on binding to TERC. F->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15885610,ECO:0000269|PubMed:16990594;Dbxref=dbSNP:rs1176273130,PMID:15885610,PMID:16990594 O14746 UniProtKB Mutagenesis 137 141 . . . Note=Reduced catalytic activity and repeat addition processivity. Complete loss of catalytic activity but no loss of binding to telomeric primers%3B when associated with 930-A--A-934. WGLLL->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17296728;Dbxref=PMID:17296728 O14746 UniProtKB Mutagenesis 169 169 . . . Note=About 80%25 loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. Little effect on repeat addition processivity%2C nor on TR interaction nor on protein levels. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19777057;Dbxref=PMID:19777057 O14746 UniProtKB Mutagenesis 169 169 . . . Note=About 85%25 loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. No effect on protein levels nor on TR interaction. Q->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19777057;Dbxref=PMID:19777057 O14746 UniProtKB Mutagenesis 169 169 . . . Note=About 90%25 loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. No effect on protein levels nor on TR interaction. Q->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19777057;Dbxref=PMID:19777057 O14746 UniProtKB Mutagenesis 457 457 . . . Note=Abolishes phosphorylation by DYRK2. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23362280;Dbxref=PMID:23362280 O14746 UniProtKB Mutagenesis 547 547 . . . Note=Defective in high-affinity TERC interactions. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15082768;Dbxref=PMID:15082768 O14746 UniProtKB Mutagenesis 631 631 . . . Note=Abolishes telomerase catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17026956;Dbxref=PMID:17026956 O14746 UniProtKB Mutagenesis 707 707 . . . Note=Abolishes oxidative stress-induced phosphorylation and RAN binding. Impaired nuclear export and enhanced antiapoptotic activity against ROS-dependent apoptosis induction. Impaired interaction with PTPN11. No dephosphorylation by PTPN11. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12808100,ECO:0000269|PubMed:18829466;Dbxref=PMID:12808100,PMID:18829466 O14746 UniProtKB Mutagenesis 712 712 . . . Note=Loss of telomerase activity. In the absence of TR%2C no loss of binding to telomeric primers. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17026956,ECO:0000269|PubMed:17296728,ECO:0000269|PubMed:9389643,ECO:0000269|PubMed:9443919;Dbxref=PMID:17026956,PMID:17296728,PMID:9389643,PMID:9443919 O14746 UniProtKB Mutagenesis 866 866 . . . Note=Moderate reduction in telomerase activity%2C no change in repeat extension rate nor on nucleotide incorporation fidelity. Little further reduction in activity but 13.5-fold increase in nucleotide incorporation fidelity%3B when associated with M-867. L->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17264120;Dbxref=PMID:17264120 O14746 UniProtKB Mutagenesis 867 867 . . . Note=About 75%25 reduction in telomerase activity%2C about 80%25 reduction in repeat reduction rate and 3.9-fold increase in nucleotide incorporation fidelity. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17264120;Dbxref=PMID:17264120 O14746 UniProtKB Mutagenesis 867 867 . . . Note=About 75%25 reduction in telomerase activity%2C about 50%25 reduction in repeat extension rate and 5.2-fold increase in nucleotide incorporation fidelity. Little further reduction in activity and 13.5-fold increase in nucleotide incorporation fidelity%3B when associated with Y-866. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17264120;Dbxref=PMID:17264120 O14746 UniProtKB Mutagenesis 867 867 . . . Note=Severe reduction in telomerase activity%2C about 50%25 reduction in repeat extension rate and 2.2-fold increase in nucleotide incorporation fidelity. No further reduction in activity but 2.8-fold increase in nucleotide incorporation fidelity%3B when associated with Y-866. V->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17264120;Dbxref=PMID:17264120 O14746 UniProtKB Mutagenesis 868 869 . . . Note=Loss of telomerase activity. DD->AA O14746 UniProtKB Mutagenesis 868 868 . . . Note=Loss of telomerase activity. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15082768,ECO:0000269|PubMed:15857955,ECO:0000269|PubMed:17026956,ECO:0000269|PubMed:9389643,ECO:0000269|PubMed:9443919;Dbxref=PMID:15082768,PMID:15857955,PMID:17026956,PMID:9389643,PMID:9443919 O14746 UniProtKB Mutagenesis 869 869 . . . Note=Loss of telomerase activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9389643,ECO:0000269|PubMed:9443919;Dbxref=PMID:9389643,PMID:9443919 O14746 UniProtKB Mutagenesis 930 934 . . . Note=Completely abolishes telomerase-mediated primer extension and reduced binding to short telomeric primers. Complete loss of catalytic activity but no further loss of binding to telomeric primers%3B when associated with 137-A--A-141. WCGLL->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17296728;Dbxref=PMID:17296728 O14746 UniProtKB Sequence conflict 516 516 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 O14746 UniProtKB Helix 8 14 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 24 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TRD O14746 UniProtKB Helix 45 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 54 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 60 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TRD O14746 UniProtKB Helix 77 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 96 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TRE O14746 UniProtKB Beta strand 99 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 114 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 126 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 135 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 146 154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 157 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 163 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 166 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 171 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 175 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 325 327 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 328 331 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 343 345 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 346 349 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 354 365 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 384 387 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 390 401 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 405 412 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 445 453 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 458 472 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 475 478 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 481 496 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 502 504 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 505 508 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 509 511 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TRD O14746 UniProtKB Helix 518 520 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 522 525 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 531 550 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 552 560 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 561 564 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 567 569 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 574 577 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 578 596 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 598 600 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TRD O14746 UniProtKB Helix 603 611 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 612 614 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 617 626 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 629 636 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 647 649 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 650 652 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 654 671 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 673 675 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 676 678 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 683 697 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 700 702 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 709 713 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 714 718 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 722 733 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 738 749 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 755 764 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 766 768 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 773 783 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 788 796 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 802 813 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 815 820 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 823 826 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 835 837 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 838 853 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 855 858 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 861 873 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 877 889 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 892 895 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 904 907 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 913 916 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 919 921 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 924 930 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 933 936 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 937 939 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 942 944 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 947 949 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 952 954 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 955 957 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 963 965 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TRD O14746 UniProtKB Helix 966 983 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Helix 984 986 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Turn 989 991 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Helix 994 1017 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Helix 1025 1027 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Helix 1029 1050 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Turn 1051 1053 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Turn 1059 1061 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Beta strand 1062 1065 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Helix 1067 1082 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Helix 1083 1085 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Helix 1086 1104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Helix 1111 1118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UGW O14746 UniProtKB Beta strand 1121 1123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA O14746 UniProtKB Turn 1125 1129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QXA