TR61B_HUMAN
ID TR61B_HUMAN Reviewed; 477 AA.
AC Q9BVS5; Q9H0Q9; Q9NWS7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial;
DE EC=2.1.1.220 {ECO:0000269|PubMed:23097428};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase {ECO:0000303|PubMed:29107537};
DE EC=2.1.1.- {ECO:0000269|PubMed:29107537};
DE Flags: Precursor;
GN Name=TRMT61B;
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 MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=23097428; DOI=10.1261/rna.035600.112;
RA Chujo T., Suzuki T.;
RT "Trmt61B is a methyltransferase responsible for 1-methyladenosine at
RT position 58 of human mitochondrial tRNAs.";
RL RNA 18:2269-2276(2012).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-335.
RX PubMed=27631568; DOI=10.1371/journal.pbio.1002557;
RA Bar-Yaacov D., Frumkin I., Yashiro Y., Chujo T., Ishigami Y., Chemla Y.,
RA Blumberg A., Schlesinger O., Bieri P., Greber B., Ban N., Zarivach R.,
RA Alfonta L., Pilpel Y., Suzuki T., Mishmar D.;
RT "Mitochondrial 16S rRNA is methylated by tRNyA methyltransferase TRMT61B in
RT all vertebrates.";
RL PLoS Biol. 14:E1002557-E1002557(2016).
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 CAUTION.
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 (2.5 ANGSTROMS) OF 144-477 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RG Structural genomics consortium (SGC);
RT "Human putative tRNA(1-methyladenosine)methyltransferase.";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Methyltransferase that catalyzes the formation of N(1)-
CC methyladenine at position 58 (m1A58) in various tRNAs in mitochondrion,
CC including tRNA(Leu) (deciphering codons UUA or UUG), tRNA(Lys) and
CC tRNA(Ser) (deciphering codons UCA, UCU, UCG or UCC) (PubMed:23097428).
CC Catalyzes the formation of 1-methyladenosine at position 947 of
CC mitochondrial 16S ribosomal RNA and this modification is most likely
CC important for mitoribosomal structure and function (PubMed:27631568).
CC In addition to tRNA N(1)-methyltransferase activity, also acts as a
CC mRNA N(1)-methyltransferase by mediating methylation of adenosine
CC residues at the N(1) position of MT-ND5 mRNA, leading to interfere with
CC mitochondrial translation (PubMed:29107537).
CC {ECO:0000269|PubMed:23097428, ECO:0000269|PubMed:27631568,
CC 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:23097428};
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:29107537};
CC -!- SUBUNIT: Homooligomer; in contrast to TRMT61A, does not form a
CC heterotetramer. {ECO:0000269|PubMed:23097428, ECO:0000269|Ref.10}.
CC -!- INTERACTION:
CC Q9BVS5; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-3197877, EBI-10175124;
CC Q9BVS5; P28799: GRN; NbExp=3; IntAct=EBI-3197877, EBI-747754;
CC Q9BVS5; Q92985: IRF7; NbExp=3; IntAct=EBI-3197877, EBI-968267;
CC Q9BVS5; O76024: WFS1; NbExp=3; IntAct=EBI-3197877, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23097428}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
CC -!- CAUTION: The identity of the enzyme catalyzing mitochondrial mRNA N(1)-
CC methyltransferase is unclear. According to a report, mitochondrial mRNA
CC N(1)-methyltransferase activity is catalyzed by TRMT61B
CC (PubMed:29107537). According to a second report, it is mediated by
CC TRMT10C (AC Q7L0Y3) (PubMed:29072297). As both reports only tested one
CC protein (either TRMT61B or TRMT10C), it is possible that both proteins
CC have this activity. {ECO:0000269|PubMed:29072297,
CC ECO:0000269|PubMed:29107537}.
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DR EMBL; AL136689; CAB66624.1; -; mRNA.
DR EMBL; AK000635; BAA91300.1; -; mRNA.
DR EMBL; CH471053; EAX00524.1; -; Genomic_DNA.
DR EMBL; AC097720; AAY24015.1; -; Genomic_DNA.
DR EMBL; BC000952; AAH00952.1; -; mRNA.
DR EMBL; BC010365; AAH10365.1; -; mRNA.
DR CCDS; CCDS1768.1; -.
DR RefSeq; NP_060380.3; NM_017910.3.
DR PDB; 2B25; X-ray; 2.50 A; A/B=144-477.
DR PDBsum; 2B25; -.
DR AlphaFoldDB; Q9BVS5; -.
DR SMR; Q9BVS5; -.
DR BioGRID; 120338; 283.
DR IntAct; Q9BVS5; 235.
DR MINT; Q9BVS5; -.
DR STRING; 9606.ENSP00000302801; -.
DR iPTMnet; Q9BVS5; -.
DR PhosphoSitePlus; Q9BVS5; -.
DR BioMuta; TRMT61B; -.
DR DMDM; 162416224; -.
DR EPD; Q9BVS5; -.
DR jPOST; Q9BVS5; -.
DR MassIVE; Q9BVS5; -.
DR MaxQB; Q9BVS5; -.
DR PaxDb; Q9BVS5; -.
DR PeptideAtlas; Q9BVS5; -.
DR PRIDE; Q9BVS5; -.
DR ProteomicsDB; 79231; -.
DR Antibodypedia; 14029; 78 antibodies from 20 providers.
DR DNASU; 55006; -.
DR Ensembl; ENST00000306108.10; ENSP00000302801.5; ENSG00000171103.11.
DR GeneID; 55006; -.
DR KEGG; hsa:55006; -.
DR MANE-Select; ENST00000306108.10; ENSP00000302801.5; NM_017910.4; NP_060380.3.
DR UCSC; uc002rmm.5; human.
DR CTD; 55006; -.
DR DisGeNET; 55006; -.
DR GeneCards; TRMT61B; -.
DR HGNC; HGNC:26070; TRMT61B.
DR HPA; ENSG00000171103; Low tissue specificity.
DR MIM; 619404; gene.
DR neXtProt; NX_Q9BVS5; -.
DR OpenTargets; ENSG00000171103; -.
DR PharmGKB; PA164726796; -.
DR VEuPathDB; HostDB:ENSG00000171103; -.
DR eggNOG; KOG2915; Eukaryota.
DR GeneTree; ENSGT00940000154239; -.
DR HOGENOM; CLU_025402_1_1_1; -.
DR InParanoid; Q9BVS5; -.
DR OMA; HTAFLIK; -.
DR OrthoDB; 1074728at2759; -.
DR PhylomeDB; Q9BVS5; -.
DR TreeFam; TF315053; -.
DR BRENDA; 2.1.1.220; 2681.
DR PathwayCommons; Q9BVS5; -.
DR Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
DR SignaLink; Q9BVS5; -.
DR BioGRID-ORCS; 55006; 22 hits in 1078 CRISPR screens.
DR ChiTaRS; TRMT61B; human.
DR EvolutionaryTrace; Q9BVS5; -.
DR GenomeRNAi; 55006; -.
DR Pharos; Q9BVS5; Tbio.
DR PRO; PR:Q9BVS5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BVS5; protein.
DR Bgee; ENSG00000171103; Expressed in secondary oocyte and 186 other tissues.
DR ExpressionAtlas; Q9BVS5; baseline and differential.
DR Genevisible; Q9BVS5; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central.
DR GO; GO:0061953; F:mRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; IDA:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
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 SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51620; SAM_TRM61; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..477
FT /note="tRNA (adenine(58)-N(1))-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000311814"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..79
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 92..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..179
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 206..207
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 228..232
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 253..260
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 334..337
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 358..365
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT COMPBIAS 43..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|Ref.10"
FT BINDING 278..279
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.10"
FT BINDING 317
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|Ref.10"
FT BINDING 335
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00952,
FT ECO:0000269|Ref.10"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT MUTAGEN 335
FT /note="D->A: Loss of ability to catalyze the formation of
FT 1-methyladenosine at position 947 of mitochondrial 16S
FT ribosomal RNA."
FT /evidence="ECO:0000269|PubMed:27631568"
FT CONFLICT 132
FT /note="T -> I (in Ref. 5; AAH00952)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="S -> F (in Ref. 2; BAA91300)"
FT /evidence="ECO:0000305"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2B25"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2B25"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:2B25"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:2B25"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:2B25"
FT HELIX 281..298
FT /evidence="ECO:0007829|PDB:2B25"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:2B25"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:2B25"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:2B25"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 350..362
FT /evidence="ECO:0007829|PDB:2B25"
FT HELIX 363..376
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2B25"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:2B25"
SQ SEQUENCE 477 AA; 52965 MW; AE538B72413DED63 CRC64;
MLMAWCRGPV LLCLRQGLGT NSFLHGLGQE PFEGARSLCC RSSPRDLRDG EREHEAAQRK
APGAESCPSL PLSISDIGTG CLSSLENLRL PTLREESSPR ELEDSSGDQG RCGPTHQGSE
DPSMLSQAQS ATEVEERHVS PSCSTSRERP FQAGELILAE TGEGETKFKK LFRLNNFGLL
NSNWGAVPFG KIVGKFPGQI LRSSFGKQYM LRRPALEDYV VLMKRGTAIT FPKDINMILS
MMDINPGDTV LEAGSGSGGM SLFLSKAVGS QGRVISFEVR KDHHDLAKKN YKHWRDSWKL
SHVEEWPDNV DFIHKDISGA TEDIKSLTFD AVALDMLNPH VTLPVFYPHL KHGGVCAVYV
VNITQVIELL DGIRTCELAL SCEKISEVIV RDWLVCLAKQ KNGILAQKVE SKINTDVQLD
SQEKIGVKGE LFQEDDHEES HSDFPYGSFP YVARPVHWQP GHTAFLVKLR KVKPQLN
