ID TRM6_HUMAN Reviewed; 497 AA. AC Q9UJA5; B4DUV6; Q76P92; Q9BQV5; Q9ULR7; Q9Y2Z8; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 26-FEB-2020, entry version 147. DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6; DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase non-catalytic subunit TRM6 {ECO:0000303|PubMed:29072297}; DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6; DE Short=tRNA(m1A58)MTase subunit TRM6; GN Name=TRMT6; Synonyms=KIAA1153, TRM6; ORFNames=CGI-09; 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] (ISOFORM 2), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10574461; DOI=10.1093/dnares/6.5.329; RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.; RT "Characterization of cDNA clones selected by the GeneMark analysis from RT size-fractionated cDNA libraries from human brain."; RL DNA Res. 6:329-336(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLY-299. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT RP GLY-299. 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; 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, AND SUBUNIT. 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-305, AND RP IDENTIFICATION BY 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 [10] RP FUNCTION. 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 [11] RP FUNCTION. 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 [12] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH TRMT61A. 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: Substrate-binding subunit of tRNA (adenine-N(1)-)- CC methyltransferase, which catalyzes the formation of N(1)-methyladenine CC at position 58 (m1A58) in initiator methionyl-tRNA (PubMed:16043508). CC Together with the TRMT61A catalytic subunit, part of a mRNA N(1)- CC methyltransferase complex that mediates methylation of adenosine CC residues at the N(1) position of a small subset of mRNAs: N(1) CC methylation takes place in tRNA T-loop-like structures of mRNAs and is CC only present at low stoichiometries (PubMed:29107537, PubMed:29072297). CC {ECO:0000269|PubMed:16043508, ECO:0000269|PubMed:29072297, CC 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:TRMT61A; NbExp=2; IntAct=EBI-934061, EBI-934042; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41814}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9UJA5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJA5-2; Sequence=VSP_018025; CC Name=3; CC IsoId=Q9UJA5-3; Sequence=VSP_031100, VSP_031101; CC Name=4; CC IsoId=Q9UJA5-4; Sequence=VSP_054740; CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, testis and ovary. CC {ECO:0000269|PubMed:10574461}. CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA86467.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA86467.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB032979; BAA86467.1; ALT_INIT; mRNA. DR EMBL; AF132943; AAD27718.1; ALT_FRAME; mRNA. DR EMBL; AK000613; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK300812; BAG62468.1; -; mRNA. DR EMBL; AL035461; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001262; AAH01262.1; -; mRNA. DR CCDS; CCDS13093.1; -. [Q9UJA5-1] DR CCDS; CCDS63225.1; -. [Q9UJA5-4] DR RefSeq; NP_001268396.1; NM_001281467.1. [Q9UJA5-4] DR RefSeq; NP_057023.2; NM_015939.4. [Q9UJA5-1] DR PDB; 5CCB; X-ray; 2.00 A; B=1-497. DR PDB; 5CCX; X-ray; 2.10 A; B=1-497. DR PDB; 5CD1; X-ray; 3.60 A; B/E=1-497. DR PDBsum; 5CCB; -. DR PDBsum; 5CCX; -. DR PDBsum; 5CD1; -. DR SMR; Q9UJA5; -. DR BioGrid; 119634; 56. DR IntAct; Q9UJA5; 21. DR MINT; Q9UJA5; -. DR STRING; 9606.ENSP00000203001; -. DR iPTMnet; Q9UJA5; -. DR PhosphoSitePlus; Q9UJA5; -. DR BioMuta; TRMT6; -. DR DMDM; 74753354; -. DR EPD; Q9UJA5; -. DR jPOST; Q9UJA5; -. DR MassIVE; Q9UJA5; -. DR PaxDb; Q9UJA5; -. DR PeptideAtlas; Q9UJA5; -. DR PRIDE; Q9UJA5; -. DR ProteomicsDB; 5222; -. DR ProteomicsDB; 84613; -. [Q9UJA5-1] DR ProteomicsDB; 84614; -. [Q9UJA5-2] DR ProteomicsDB; 84615; -. [Q9UJA5-3] DR DNASU; 51605; -. DR Ensembl; ENST00000203001; ENSP00000203001; ENSG00000089195. [Q9UJA5-1] DR Ensembl; ENST00000453074; ENSP00000392070; ENSG00000089195. [Q9UJA5-4] DR GeneID; 51605; -. DR KEGG; hsa:51605; -. DR UCSC; uc002wmh.3; human. [Q9UJA5-1] DR CTD; 51605; -. DR DisGeNET; 51605; -. DR GeneCards; TRMT6; -. DR HGNC; HGNC:20900; TRMT6. DR HPA; HPA047032; -. DR HPA; HPA050408; -. DR neXtProt; NX_Q9UJA5; -. DR OpenTargets; ENSG00000089195; -. DR PharmGKB; PA162407063; -. DR eggNOG; KOG1416; Eukaryota. DR eggNOG; ENOG410XSXD; LUCA. DR GeneTree; ENSGT00390000008327; -. DR HOGENOM; CLU_010916_0_1_1; -. DR InParanoid; Q9UJA5; -. DR KO; K03256; -. DR OMA; MYHGREP; -. DR OrthoDB; 543764at2759; -. DR PhylomeDB; Q9UJA5; -. DR TreeFam; TF314835; -. DR BRENDA; 2.1.1.220; 2681. DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol. DR ChiTaRS; TRMT6; human. DR GenomeRNAi; 51605; -. DR Pharos; Q9UJA5; Tdark. DR PRO; PR:Q9UJA5; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9UJA5; protein. DR Bgee; ENSG00000089195; Expressed in secondary oocyte and 204 other tissues. DR Genevisible; Q9UJA5; 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; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; IEA:InterPro. DR GO; GO:0006400; P:tRNA modification; TAS:Reactome. DR InterPro; IPR017423; TRM6. DR PANTHER; PTHR12945; PTHR12945; 1. DR Pfam; PF04189; Gcd10p; 1. DR PIRSF; PIRSF038170; tRNA_m1A_mtfrase; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; tRNA processing. FT CHAIN 1..497 FT /note="tRNA (adenine(58)-N(1))-methyltransferase non- FT catalytic subunit TRM6" FT /id="PRO_0000233098" FT REGION 94..104 FT /note="Substrate binding" FT /evidence="ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919" FT REGION 145..154 FT /note="Substrate binding" FT /evidence="ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919" FT REGION 175..182 FT /note="Substrate binding" FT /evidence="ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919" FT REGION 415..423 FT /note="Substrate binding" FT /evidence="ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919" FT REGION 434..441 FT /note="Substrate binding" FT /evidence="ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919" FT BINDING 349 FT /note="Substrate" FT /evidence="ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919" FT BINDING 377 FT /note="Substrate" FT /evidence="ECO:0000244|PDB:5CD1, FT ECO:0000269|PubMed:26470919" FT MOD_RES 107 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:17525332" FT MOD_RES 298 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT VAR_SEQ 1..170 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054740" FT VAR_SEQ 344..365 FT /note="QEKQRRQEEQRKRHLEAAALLS -> SGKNRGRQGRSSGKDFWGCRFA (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:10810093" FT /id="VSP_031100" FT VAR_SEQ 366..497 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10810093" FT /id="VSP_031101" FT VAR_SEQ 372..497 FT /note="LIVASRFHPTPLLLSLLDFVAPSRPFVVYCQYKEPLLECYTKLRERGGVINL FT RLSETWLRNYQVLPDRSHPKLLMSGGGGYLLSGFTVAMDNLKADTSLKSNASTLESHET FT EEPAAKKRKCPESDS -> CVDGRRQETPQCMWALLQTDWHSLSPCL (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:10574461" FT /id="VSP_018025" FT VARIANT 293 FT /note="E -> K (in dbSNP:rs6139876)" FT /id="VAR_053789" FT VARIANT 299 FT /note="E -> G (in dbSNP:rs451571)" FT /evidence="ECO:0000269|PubMed:10810093, FT ECO:0000269|PubMed:14702039" FT /id="VAR_053790" FT VARIANT 333 FT /note="P -> L (in dbSNP:rs35203742)" FT /id="VAR_053791" FT STRAND 25..30 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 33..38 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 44..46 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 51..53 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 54..56 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 59..61 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 64..74 FT /evidence="ECO:0000244|PDB:5CCX" FT HELIX 108..116 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 122..130 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 132..134 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 135..137 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 140..154 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 159..161 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 165..175 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 177..180 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 185..194 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 202..207 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 212..221 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 225..232 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 239..243 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 248..251 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 254..258 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 259..261 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 262..267 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 342..365 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 369..375 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 380..387 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 388..390 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 396..404 FT /evidence="ECO:0000244|PDB:5CCB" FT HELIX 405..417 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 420..434 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 441..446 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 448..450 FT /evidence="ECO:0000244|PDB:5CCB" FT STRAND 452..458 FT /evidence="ECO:0000244|PDB:5CCB" SQ SEQUENCE 497 AA; 55799 MW; 920800D0722A6CBB CRC64; MEGSGEQPGP QPQHPGDHRI RDGDFVVLKR EDVFKAVQVQ RRKKVTFEKQ WFYLDNVIGH SYGTAFEVTS GGSLQPKKKR EEPTAETKEA GTDNRNIVDD GKSQKLTQDD IKALKDKGIK GEEIVQQLIE NSTTFRDKTE FAQDKYIKKK KKKYEAIITV VKPSTRILSI MYYAREPGKI NHMRYDTLAQ MLTLGNIRAG NKMIVMETCA GLVLGAMMER MGGFGSIIQL YPGGGPVRAA TACFGFPKSF LSGLYEFPLN KVDSLLHGTF SAKMLSSEPK DSALVEESNG TLEEKQASEQ ENEDSMAEAP ESNHPEDQET METISQDPEH KGPKERGSKK DYIQEKQRRQ EEQRKRHLEA AALLSERNAD GLIVASRFHP TPLLLSLLDF VAPSRPFVVY CQYKEPLLEC YTKLRERGGV INLRLSETWL RNYQVLPDRS HPKLLMSGGG GYLLSGFTVA MDNLKADTSL KSNASTLESH ETEEPAAKKR KCPESDS //