TGT_HUMAN
ID TGT_HUMAN Reviewed; 403 AA.
AC Q9BXR0; B4DFM7; Q96BQ4; Q9BXQ9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_03218};
DE EC=2.4.2.64 {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:20354154};
DE AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_03218};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_03218};
GN Name=QTRT1 {ECO:0000255|HAMAP-Rule:MF_03218}; Synonyms=TGT, TGUT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND PATHWAY.
RC TISSUE=Spleen;
RX PubMed=11255023; DOI=10.1016/s0378-1119(01)00368-7;
RA Deshpande K.L., Katze J.R.;
RT "Characterization of cDNA encoding the human tRNA-guanine transglycosylase
RT (TGT) catalytic subunit.";
RL Gene 265:205-212(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-403 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP MUTAGENESIS OF ASP-279, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20354154; DOI=10.1261/rna.1997610;
RA Chen Y.C., Kelly V.P., Stachura S.V., Garcia G.A.;
RT "Characterization of the human tRNA-guanine transglycosylase: confirmation
RT of the heterodimeric subunit structure.";
RL RNA 16:958-968(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9] {ECO:0007744|PDB:6H42, ECO:0007744|PDB:6H45}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 12-403 IN COMPLEX WITH ZINC AND
RP QUEUINE, COFACTOR, AND SUBUNIT.
RX PubMed=30149595; DOI=10.3390/biom8030081;
RA Johannsson S., Neumann P., Ficner R.;
RT "Crystal Structure of the Human tRNA Guanine Transglycosylase Catalytic
RT Subunit QTRT1.";
RL Biomolecules 8:0-0(2018).
CC -!- FUNCTION: Catalytic subunit of the queuine tRNA-ribosyltransferase
CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:11255023,
CC PubMed:20354154). Catalysis occurs through a double-displacement
CC mechanism. The nucleophile active site attacks the C1' of nucleotide 34
CC to detach the guanine base from the RNA, forming a covalent enzyme-RNA
CC intermediate. The proton acceptor active site deprotonates the incoming
CC queuine, allowing a nucleophilic attack on the C1' of the ribose to
CC form the product (By similarity). {ECO:0000250|UniProtKB:P28720,
CC ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:11255023,
CC ECO:0000269|PubMed:20354154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(34) in tRNA + queuine = guanine + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:16633, Rhea:RHEA-COMP:10341, Rhea:RHEA-
CC COMP:10345, ChEBI:CHEBI:16235, ChEBI:CHEBI:74269, ChEBI:CHEBI:77674,
CC ChEBI:CHEBI:82831; EC=2.4.2.64; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03218, ECO:0000269|PubMed:20354154};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000269|PubMed:30149595};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 uM for tRNA(Tyr) {ECO:0000269|PubMed:20354154};
CC KM=0.41 uM for guanine {ECO:0000269|PubMed:20354154};
CC Note=kcat is 0.0056 sec(-1) with tRNA(Tyr) as substrate and 0.00586
CC sec(-1) with guanine as substrate. {ECO:0000269|PubMed:20354154};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory
CC subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000269|PubMed:20354154, ECO:0000269|PubMed:30149595}.
CC -!- INTERACTION:
CC Q9BXR0; Q9H974: QTRT2; NbExp=2; IntAct=EBI-716832, EBI-1221028;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218}.
CC Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03218};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03218};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03218}. Note=Weakly
CC associates with mitochondria, possibly via QTRT2. {ECO:0000255|HAMAP-
CC Rule:MF_03218}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BXR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXR0-2; Sequence=VSP_056470, VSP_056471;
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03218}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15350.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF302783; AAG60033.1; -; mRNA.
DR EMBL; AF302784; AAG60034.1; -; mRNA.
DR EMBL; AK294166; BAG57488.1; -; mRNA.
DR EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015350; AAH15350.1; ALT_INIT; mRNA.
DR CCDS; CCDS12248.1; -. [Q9BXR0-1]
DR RefSeq; NP_112486.1; NM_031209.2. [Q9BXR0-1]
DR PDB; 6H42; X-ray; 2.45 A; A/B=11-403.
DR PDB; 6H45; X-ray; 2.40 A; A/B=12-403.
DR PDB; 7NQ4; X-ray; 2.88 A; A=1-403.
DR PDBsum; 6H42; -.
DR PDBsum; 6H45; -.
DR PDBsum; 7NQ4; -.
DR AlphaFoldDB; Q9BXR0; -.
DR SMR; Q9BXR0; -.
DR BioGRID; 123623; 37.
DR ComplexPortal; CPX-6662; tRNA-guanine transglycosylase complex.
DR IntAct; Q9BXR0; 18.
DR STRING; 9606.ENSP00000250237; -.
DR BindingDB; Q9BXR0; -.
DR ChEMBL; CHEMBL6004; -.
DR iPTMnet; Q9BXR0; -.
DR PhosphoSitePlus; Q9BXR0; -.
DR BioMuta; QTRT1; -.
DR DMDM; 239938842; -.
DR EPD; Q9BXR0; -.
DR jPOST; Q9BXR0; -.
DR MassIVE; Q9BXR0; -.
DR MaxQB; Q9BXR0; -.
DR PaxDb; Q9BXR0; -.
DR PeptideAtlas; Q9BXR0; -.
DR PRIDE; Q9BXR0; -.
DR ProteomicsDB; 4060; -.
DR ProteomicsDB; 79483; -. [Q9BXR0-1]
DR Antibodypedia; 25490; 156 antibodies from 20 providers.
DR DNASU; 81890; -.
DR Ensembl; ENST00000250237.10; ENSP00000250237.4; ENSG00000213339.9. [Q9BXR0-1]
DR Ensembl; ENST00000421333.6; ENSP00000389126.2; ENSG00000213339.9. [Q9BXR0-2]
DR GeneID; 81890; -.
DR KEGG; hsa:81890; -.
DR MANE-Select; ENST00000250237.10; ENSP00000250237.4; NM_031209.3; NP_112486.1.
DR UCSC; uc002mpr.4; human. [Q9BXR0-1]
DR CTD; 81890; -.
DR DisGeNET; 81890; -.
DR GeneCards; QTRT1; -.
DR HGNC; HGNC:23797; QTRT1.
DR HPA; ENSG00000213339; Low tissue specificity.
DR MIM; 609615; gene.
DR neXtProt; NX_Q9BXR0; -.
DR OpenTargets; ENSG00000213339; -.
DR PharmGKB; PA134963074; -.
DR VEuPathDB; HostDB:ENSG00000213339; -.
DR eggNOG; KOG3908; Eukaryota.
DR GeneTree; ENSGT00530000063679; -.
DR HOGENOM; CLU_022060_0_1_1; -.
DR InParanoid; Q9BXR0; -.
DR OMA; GIDLFDC; -.
DR PhylomeDB; Q9BXR0; -.
DR TreeFam; TF300732; -.
DR BioCyc; MetaCyc:HS05270-MON; -.
DR BRENDA; 2.4.2.29; 2681.
DR BRENDA; 2.4.2.64; 2681.
DR PathwayCommons; Q9BXR0; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q9BXR0; -.
DR BioGRID-ORCS; 81890; 25 hits in 1079 CRISPR screens.
DR ChiTaRS; QTRT1; human.
DR GenomeRNAi; 81890; -.
DR Pharos; Q9BXR0; Tbio.
DR PRO; PR:Q9BXR0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BXR0; protein.
DR Bgee; ENSG00000213339; Expressed in mucosa of transverse colon and 139 other tissues.
DR ExpressionAtlas; Q9BXR0; baseline and differential.
DR Genevisible; Q9BXR0; HS.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:1990234; C:transferase complex; IPI:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; TAS:UniProtKB.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IDA:UniProtKB.
DR Gene3D; 3.20.20.105; -; 1.
DR HAMAP; MF_00168; Q_tRNA_Tgt; 1.
DR InterPro; IPR004803; TGT.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Glycosyltransferase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW Transferase; tRNA processing; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..403
FT /note="Queuine tRNA-ribosyltransferase catalytic subunit 1"
FT /id="PRO_0000135565"
FT REGION 260..266
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT REGION 284..288
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 279
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 105..109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218,
FT ECO:0000269|PubMed:30149595, ECO:0007744|PDB:6H45"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218,
FT ECO:0000269|PubMed:30149595, ECO:0007744|PDB:6H45"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218,
FT ECO:0000269|PubMed:30149595, ECO:0007744|PDB:6H45"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218,
FT ECO:0000269|PubMed:30149595, ECO:0007744|PDB:6H45"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218,
FT ECO:0000269|PubMed:30149595, ECO:0007744|PDB:6H45"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218,
FT ECO:0000269|PubMed:30149595, ECO:0007744|PDB:6H45"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218,
FT ECO:0000269|PubMed:30149595, ECO:0007744|PDB:6H45"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 178..225
FT /note="SIRWLDRCIAAHQRPDKQNLFAIIQGGLDADLRATCLEEMTKRDVPGF ->
FT PLGLVTGALLQVNPLAGPVHCSPSAAGQAEPLRHYPGWAGRRSPGHLP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056470"
FT VAR_SEQ 226..403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056471"
FT MUTAGEN 279
FT /note="D->N: Loss of transglycosylase activity."
FT /evidence="ECO:0000269|PubMed:20354154"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:7NQ4"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7NQ4"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 169..187
FT /evidence="ECO:0007829|PDB:6H42"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6H42"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 338..365
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:6H42"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:6H42"
SQ SEQUENCE 403 AA; 44048 MW; 1E30F3C7BF47A106 CRC64;
MAGAATQASL ESAPRIMRLV AECSRSRARA GELWLPHGTV ATPVFMPVGT QATMKGITTE
QLDALGCRIC LGNTYHLGLR PGPELIQKAN GLHGFMNWPH NLLTDSGGFQ MVSLVSLSEV
TEEGVRFRSP YDGNETLLSP EKSVQIQNAL GSDIIMQLDD VVSSTVTGPR VEEAMYRSIR
WLDRCIAAHQ RPDKQNLFAI IQGGLDADLR ATCLEEMTKR DVPGFAIGGL SGGESKSQFW
RMVALSTSRL PKDKPRYLMG VGYATDLVVC VALGCDMFDC VFPTRTARFG SALVPTGNLQ
LRKKVFEKDF GPIDPECTCP TCQKHSRAFL HALLHSDNTA ALHHLTVHNI AYQLQLMSAV
RTSIVEKRFP DFVRDFMGAM YGDPTLCPTW ATDALASVGI TLG
