TRM61_HUMAN
ID TRM61_HUMAN Reviewed; 289 AA.
AC Q96FX7; A6NN78; Q8N7Q9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A;
DE EC=2.1.1.220 {ECO:0000269|PubMed:16043508};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase catalytic subunit TRMT61A {ECO:0000303|PubMed:29072297};
DE EC=2.1.1.- {ECO:0000269|PubMed:29072297, ECO:0000269|PubMed:29107537};
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRMT61A;
DE Short=tRNA(m1A58)MTase subunit TRMT61A;
GN Name=TRMT61A; Synonyms=C14orf172, TRM61;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-282.
RC TISSUE=Testis;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND VARIANT ALA-66.
RX PubMed=16043508; DOI=10.1261/rna.5040605;
RA Ozanick S., Krecic A., Andersland J., Anderson J.T.;
RT "The bipartite structure of the tRNA m1A58 methyltransferase from S.
RT cerevisiae is conserved in humans.";
RL RNA 11:1281-1290(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
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 SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29107537; DOI=10.1016/j.molcel.2017.10.019;
RA Li X., Xiong X., Zhang M., Wang K., Chen Y., Zhou J., Mao Y., Lv J., Yi D.,
RA Chen X.W., Wang C., Qian S.B., Yi C.;
RT "Base-resolution mapping reveals distinct m1A methylome in nuclear- and
RT mitochondrial-encoded transcripts.";
RL Mol. Cell 0:0-0(2017).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29072297; DOI=10.1038/nature24456;
RA Safra M., Sas-Chen A., Nir R., Winkler R., Nachshon A., Bar-Yaacov D.,
RA Erlacher M., Rossmanith W., Stern-Ginossar N., Schwartz S.;
RT "The m(1)A landscape on cytosolic and mitochondrial mRNA at single-base
RT resolution.";
RL Nature 551:251-255(2017).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH TRMT6;
RP S-ADENOSYL-L-METHIONINE AND TRNA SUBSTRATE, AND SUBUNIT.
RX PubMed=26470919; DOI=10.1016/j.jmb.2015.10.005;
RA Finer-Moore J., Czudnochowski N., O'Connell J.D. III, Wang A.L.,
RA Stroud R.M.;
RT "Crystal structure of the human tRNA m(1)A58 methyltransferase-tRNA(3)(Lys)
RT complex: refolding of substrate tRNA allows access to the methylation
RT target.";
RL J. Mol. Biol. 427:3862-3876(2015).
CC -!- FUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase,
CC which catalyzes the formation of N(1)-methyladenine at position 58
CC (m1A58) in initiator methionyl-tRNA (PubMed:16043508). Catalytic
CC subunit of mRNA N(1)-methyltransferase complex, which mediates
CC methylation of adenosine residues at the N(1) position of a small
CC subset of mRNAs: N(1) methylation takes place in tRNA T-loop-like
CC structures of mRNAs and is only present at low stoichiometries
CC (PubMed:29107537, PubMed:29072297). {ECO:0000269|PubMed:16043508,
CC ECO:0000269|PubMed:29072297, ECO:0000269|PubMed:29107537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00952,
CC ECO:0000269|PubMed:16043508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;
CC Evidence={ECO:0000269|PubMed:29072297, ECO:0000269|PubMed:29107537};
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two copies
CC of TRMT61A. {ECO:0000269|PubMed:26470919, ECO:0000305|PubMed:16043508}.
CC -!- INTERACTION:
CC Q96FX7; P56279: TCL1A; NbExp=3; IntAct=EBI-934042, EBI-749995;
CC Q96FX7; Q9UJA5: TRMT6; NbExp=2; IntAct=EBI-934042, EBI-934061;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46959}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05168.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AL133367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010167; AAH10167.1; -; mRNA.
DR EMBL; AK097771; BAC05168.1; ALT_SEQ; mRNA.
DR CCDS; CCDS41994.1; -.
DR RefSeq; NP_689520.2; NM_152307.2.
DR PDB; 5CCB; X-ray; 2.00 A; A=1-289.
DR PDB; 5CCX; X-ray; 2.10 A; A=1-289.
DR PDB; 5CD1; X-ray; 3.60 A; A/D=1-289.
DR PDBsum; 5CCB; -.
DR PDBsum; 5CCX; -.
DR PDBsum; 5CD1; -.
DR AlphaFoldDB; Q96FX7; -.
DR SMR; Q96FX7; -.
DR BioGRID; 125450; 66.
DR ComplexPortal; CPX-6269; tRNA (adenine(58)-N(1))-methyltransferase complex.
DR IntAct; Q96FX7; 25.
DR MINT; Q96FX7; -.
DR STRING; 9606.ENSP00000374399; -.
DR GlyGen; Q96FX7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96FX7; -.
DR PhosphoSitePlus; Q96FX7; -.
DR BioMuta; TRMT61A; -.
DR DMDM; 74760827; -.
DR EPD; Q96FX7; -.
DR jPOST; Q96FX7; -.
DR MassIVE; Q96FX7; -.
DR MaxQB; Q96FX7; -.
DR PaxDb; Q96FX7; -.
DR PeptideAtlas; Q96FX7; -.
DR PRIDE; Q96FX7; -.
DR ProteomicsDB; 76570; -.
DR Antibodypedia; 6565; 74 antibodies from 20 providers.
DR DNASU; 115708; -.
DR Ensembl; ENST00000389749.9; ENSP00000374399.4; ENSG00000166166.13.
DR GeneID; 115708; -.
DR KEGG; hsa:115708; -.
DR MANE-Select; ENST00000389749.9; ENSP00000374399.4; NM_152307.3; NP_689520.2.
DR UCSC; uc001yng.4; human.
DR CTD; 115708; -.
DR DisGeNET; 115708; -.
DR GeneCards; TRMT61A; -.
DR HGNC; HGNC:23790; TRMT61A.
DR HPA; ENSG00000166166; Low tissue specificity.
DR neXtProt; NX_Q96FX7; -.
DR OpenTargets; ENSG00000166166; -.
DR PharmGKB; PA164726783; -.
DR VEuPathDB; HostDB:ENSG00000166166; -.
DR eggNOG; KOG2915; Eukaryota.
DR GeneTree; ENSGT00940000154239; -.
DR HOGENOM; CLU_025402_4_1_1; -.
DR InParanoid; Q96FX7; -.
DR OMA; VVYPKDA; -.
DR OrthoDB; 1032689at2759; -.
DR PhylomeDB; Q96FX7; -.
DR TreeFam; TF315053; -.
DR BRENDA; 2.1.1.220; 2681.
DR PathwayCommons; Q96FX7; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q96FX7; -.
DR BioGRID-ORCS; 115708; 256 hits in 1081 CRISPR screens.
DR ChiTaRS; TRMT61A; human.
DR GenomeRNAi; 115708; -.
DR Pharos; Q96FX7; Tbio.
DR PRO; PR:Q96FX7; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96FX7; protein.
DR Bgee; ENSG00000166166; Expressed in type B pancreatic cell and 202 other tissues.
DR ExpressionAtlas; Q96FX7; baseline and differential.
DR Genevisible; Q96FX7; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0061953; F:mRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:ComplexPortal.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR PANTHER; PTHR12133; PTHR12133; 1.
DR Pfam; PF08704; GCD14; 1.
DR PIRSF; PIRSF017269; GCD14; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51620; SAM_TRM61; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..289
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit TRMT61A"
FT /id="PRO_0000233094"
FT REGION 245..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20..22
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 35..42
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 64..65
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 85..89
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CCB, ECO:0007744|PDB:5CCX,
FT ECO:0007744|PDB:5CD1"
FT BINDING 110..117
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 114..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CCB, ECO:0007744|PDB:5CCX,
FT ECO:0007744|PDB:5CD1"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|PubMed:26470919, ECO:0007744|PDB:5CCB,
FT ECO:0007744|PDB:5CCX, ECO:0007744|PDB:5CD1"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CCB, ECO:0007744|PDB:5CCX,
FT ECO:0007744|PDB:5CD1"
FT BINDING 163..164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CCB, ECO:0007744|PDB:5CCX,
FT ECO:0007744|PDB:5CD1"
FT BINDING 180..183
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|PubMed:26470919, ECO:0007744|PDB:5CCB,
FT ECO:0007744|PDB:5CCX, ECO:0007744|PDB:5CD1"
FT BINDING 205..212
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470919,
FT ECO:0007744|PDB:5CD1"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VARIANT 66
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:16043508"
FT /id="VAR_026053"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:5CCB"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:5CCB"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:5CCB"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 226..243
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:5CCB"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:5CCB"
SQ SEQUENCE 289 AA; 31382 MW; 5DCD6437A0B6F54D CRC64;
MSFVAYEELI KEGDTAILSL GHGAMVAVRV QRGAQTQTRH GVLRHSVDLI GRPFGSKVTC
GRGGWVYVLH PTPELWTLNL PHRTQILYST DIALITMMLE LRPGSVVCES GTGSGSVSHA
IIRTIAPTGH LHTVEFHQQR AEKAREEFQE HRVGRWVTVR TQDVCRSGFG VSHVADAVFL
DIPSPWEAVG HAWDALKVEG GRFCSFSPCI EQVQRTCQAL AARGFSELST LEVLPQVYNV
RTVSLPPPDL GTGTDGPAGS DTSPFRSGTP MKEAVGHTGY LTFATKTPG
