BN3D2_HUMAN
ID BN3D2_HUMAN Reviewed; 292 AA.
AC Q7Z5W3; A8K829;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=RNA 5'-monophosphate methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:23063121, ECO:0000269|PubMed:28119416, ECO:0000269|PubMed:31329584, ECO:0000269|PubMed:31919512};
DE AltName: Full=BCDIN3 domain-containing protein;
GN Name=BCDIN3D {ECO:0000312|HGNC:HGNC:27050};
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=Cervix;
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 [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DICER1, MUTAGENESIS OF
RP 72-ASP--GLU-74, AND SUBCELLULAR LOCATION.
RX PubMed=23063121; DOI=10.1016/j.cell.2012.08.041;
RA Xhemalce B., Robson S.C., Kouzarides T.;
RT "Human RNA methyltransferase BCDIN3D regulates microRNA processing.";
RL Cell 151:278-288(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF 72-ASP--GLY-74.
RX PubMed=28119416; DOI=10.1093/nar/gkx051;
RA Martinez A., Yamashita S., Nagaike T., Sakaguchi Y., Suzuki T., Tomita K.;
RT "Human BCDIN3D monomethylates cytoplasmic histidine transfer RNA.";
RL Nucleic Acids Res. 45:5423-5436(2017).
RN [6]
RP REVIEW OF SPECIFIC ENZYMATIC ACTIVITY.
RX PubMed=30127802; DOI=10.3389/fgene.2018.00305;
RA Tomita K., Liu Y.;
RT "Human BCDIN3D Is a Cytoplasmic tRNAHis-Specific 5'-Monophosphate
RT Methyltransferase.";
RL Front. Genet. 9:305-305(2018).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31329584; DOI=10.1371/journal.pgen.1008273;
RA Reinsborough C.W., Ipas H., Abell N.S., Nottingham R.M., Yao J.,
RA Devanathan S.K., Shelton S.B., Lambowitz A.M., Xhemalce B.;
RT "BCDIN3D regulates tRNAHis 3' fragment processing.";
RL PLoS Genet. 15:e1008273-e1008273(2019).
RN [8] {ECO:0007744|PDB:6L8U}
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 14-284 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP TYR-37; ARG-46; 72-ASP--GLY-74; ASP-72; GLY-74; ASN-76; ASP-110; ILE-111;
RP ARG-118; ASP-135; PHE-136; SER-165; ILE-166; TRP-169; GLN-198;
RP 201-LYS--ARG-204; LYS-201; ARG-204; 208-ARG-ARG-209; ARG-208; ARG-209;
RP 211-ARG-LYS-212; ARG-211; LYS-212 AND ARG-257.
RX PubMed=31919512; DOI=10.1093/nar/gkz1216;
RA Liu Y., Martinez A., Yamashita S., Tomita K.;
RT "Crystal structure of human cytoplasmic tRNAHis-specific 5'-
RT monomethylphosphate capping enzyme.";
RL Nucleic Acids Res. 48:1572-1582(2020).
CC -!- FUNCTION: O-methyltransferase that specifically monomethylates 5'-
CC monophosphate of cytoplasmic histidyl tRNA (tRNA(His)), acting as a
CC capping enzyme by protecting tRNA(His) from cleavage by DICER1
CC (PubMed:28119416, PubMed:31329584, PubMed:31919512). Also able, with
CC less efficiently, to methylate the 5' monophosphate of a subset of pre-
CC miRNAs, acting as a negative regulator of miRNA processing
CC (PubMed:23063121, PubMed:28119416). The 5' monophosphate of pre-miRNAs
CC is recognized by DICER1 and is required for pre-miRNAs processing:
CC methylation at this position reduces the processing of pre-miRNAs by
CC DICER1 (PubMed:23063121). Was also reported to mediate dimethylation of
CC pre-miR-145; however dimethylation cannot be reproduced by another
CC group which observes a monomethylation of pre-miR-145 (PubMed:23063121,
CC PubMed:28119416). {ECO:0000269|PubMed:23063121,
CC ECO:0000269|PubMed:28119416, ECO:0000269|PubMed:31329584,
CC ECO:0000269|PubMed:31919512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-phospho)-ribonucleoside-RNA + S-adenosyl-L-
CC methionine = a 5'-end (5'-methylphospho)-ribonucleoside-RNA + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:58656, Rhea:RHEA-COMP:15179,
CC Rhea:RHEA-COMP:15181, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:142776;
CC Evidence={ECO:0000269|PubMed:28119416, ECO:0000269|PubMed:31329584,
CC ECO:0000269|PubMed:31919512};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-phospho)-ribonucleoside-RNA + 2 S-adenosyl-L-
CC methionine = a 5'-end (5'-bismethylphospho)-ribonucleoside-RNA + 2 S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:58640, Rhea:RHEA-COMP:15179,
CC Rhea:RHEA-COMP:15182, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:142777;
CC Evidence={ECO:0000305|PubMed:23063121};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 uM for cytoplasmic histidyl tRNA
CC {ECO:0000269|PubMed:28119416};
CC KM=15 uM for pre-miR-145 {ECO:0000269|PubMed:28119416};
CC -!- SUBUNIT: Interacts with DICER1; the interaction may be mediated by RNA.
CC {ECO:0000269|PubMed:23063121}.
CC -!- INTERACTION:
CC Q7Z5W3; Q6ZN57: ZFP2; NbExp=3; IntAct=EBI-10257921, EBI-7236323;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23063121}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- CAUTION: There is some controversy about O-methyltransferase on pre-
CC miR-145, since the dimethylation first described as the specific
CC enzymatic activity cannot be reproduced by a more recent work which
CC observes a monomethylation of pre-miR-145 but two orders weaker than
CC the methylation of cytosolic histidyl tRNA.
CC {ECO:0000269|PubMed:23063121, ECO:0000269|PubMed:28119416}.
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; AK292194; BAF84883.1; -; mRNA.
DR EMBL; CH471111; EAW58101.1; -; Genomic_DNA.
DR EMBL; BC053560; AAH53560.1; -; mRNA.
DR CCDS; CCDS8790.1; -.
DR RefSeq; NP_859059.1; NM_181708.2.
DR PDB; 6L8U; X-ray; 2.92 A; A/B/C/D=14-284.
DR PDBsum; 6L8U; -.
DR AlphaFoldDB; Q7Z5W3; -.
DR SMR; Q7Z5W3; -.
DR BioGRID; 126839; 8.
DR IntAct; Q7Z5W3; 3.
DR STRING; 9606.ENSP00000335201; -.
DR BindingDB; Q7Z5W3; -.
DR ChEMBL; CHEMBL3588740; -.
DR iPTMnet; Q7Z5W3; -.
DR PhosphoSitePlus; Q7Z5W3; -.
DR BioMuta; BCDIN3D; -.
DR DMDM; 74738762; -.
DR EPD; Q7Z5W3; -.
DR jPOST; Q7Z5W3; -.
DR MassIVE; Q7Z5W3; -.
DR MaxQB; Q7Z5W3; -.
DR PaxDb; Q7Z5W3; -.
DR PeptideAtlas; Q7Z5W3; -.
DR PRIDE; Q7Z5W3; -.
DR ProteomicsDB; 69357; -.
DR Antibodypedia; 49296; 48 antibodies from 14 providers.
DR DNASU; 144233; -.
DR Ensembl; ENST00000333924.6; ENSP00000335201.4; ENSG00000186666.6.
DR GeneID; 144233; -.
DR KEGG; hsa:144233; -.
DR MANE-Select; ENST00000333924.6; ENSP00000335201.4; NM_181708.3; NP_859059.1.
DR UCSC; uc001rvh.4; human.
DR CTD; 144233; -.
DR DisGeNET; 144233; -.
DR GeneCards; BCDIN3D; -.
DR HGNC; HGNC:27050; BCDIN3D.
DR HPA; ENSG00000186666; Tissue enhanced (skeletal).
DR MIM; 619601; gene.
DR neXtProt; NX_Q7Z5W3; -.
DR OpenTargets; ENSG00000186666; -.
DR PharmGKB; PA162377410; -.
DR VEuPathDB; HostDB:ENSG00000186666; -.
DR eggNOG; KOG2899; Eukaryota.
DR GeneTree; ENSGT00940000153993; -.
DR HOGENOM; CLU_082749_0_0_1; -.
DR OMA; GNFMNYY; -.
DR OrthoDB; 1185441at2759; -.
DR PhylomeDB; Q7Z5W3; -.
DR TreeFam; TF324061; -.
DR BRENDA; 2.1.1.B140; 2681.
DR PathwayCommons; Q7Z5W3; -.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR SignaLink; Q7Z5W3; -.
DR BioGRID-ORCS; 144233; 37 hits in 1075 CRISPR screens.
DR ChiTaRS; BCDIN3D; human.
DR GenomeRNAi; 144233; -.
DR Pharos; Q7Z5W3; Tbio.
DR PRO; PR:Q7Z5W3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7Z5W3; protein.
DR Bgee; ENSG00000186666; Expressed in islet of Langerhans and 117 other tissues.
DR Genevisible; Q7Z5W3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008171; F:O-methyltransferase activity; EXP:Reactome.
DR GO; GO:0070883; F:pre-miRNA binding; IDA:ARUK-UCL.
DR GO; GO:0008173; F:RNA methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; IBA:GO_Central.
DR GO; GO:2000632; P:negative regulation of pre-miRNA processing; IDA:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:ARUK-UCL.
DR GO; GO:0001510; P:RNA methylation; IDA:ARUK-UCL.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR039772; Bin3-like.
DR InterPro; IPR010675; Bin3_C.
DR InterPro; IPR024160; BIN3_SAM-bd_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12315; PTHR12315; 1.
DR Pfam; PF06859; Bin3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51515; BIN3_SAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..292
FT /note="RNA 5'-monophosphate methyltransferase"
FT /id="PRO_0000289265"
FT DOMAIN 53..274
FT /note="Bin3-type SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00848"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31919512,
FT ECO:0000312|PDB:6L8U"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31919512,
FT ECO:0000312|PDB:6L8U"
FT BINDING 110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31919512,
FT ECO:0000312|PDB:6L8U"
FT BINDING 135..136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31919512,
FT ECO:0000312|PDB:6L8U"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:31919512,
FT ECO:0000312|PDB:6L8U"
FT VARIANT 288
FT /note="S -> R (in dbSNP:rs11169172)"
FT /id="VAR_032614"
FT MUTAGEN 37
FT /note="Y->A,F: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 46
FT /note="R->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 72..74
FT /note="DVG->AVA: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23063121,
FT ECO:0000269|PubMed:28119416, ECO:0000269|PubMed:31919512"
FT MUTAGEN 72
FT /note="D->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 74
FT /note="G->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 76
FT /note="N->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 110
FT /note="D->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 111
FT /note="I->G: Decreased O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 118
FT /note="R->A: Slightly decreased O-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 135
FT /note="D->A: Decreased O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 136
FT /note="F->G: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 165
FT /note="S->A: Decreased O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 166
FT /note="I->G: Decreased O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 169
FT /note="W->F: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 198
FT /note="Q->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 201..204
FT /note="KCYR->ACYA: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 201
FT /note="K->A: Decreased O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 204
FT /note="R->A: Decreased O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 208..209
FT /note="RR->AA: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 208
FT /note="R->A: Strongly decreased O-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 209
FT /note="R->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 211..212
FT /note="RK->AA: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 211
FT /note="R->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 212
FT /note="K->A: Decreased O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT MUTAGEN 257
FT /note="R->A: Abolished O-methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31919512"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:6L8U"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 167..187
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6L8U"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:6L8U"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:6L8U"
SQ SEQUENCE 292 AA; 33200 MW; 361EF0BBAAC0CCAF CRC64;
MAVPTELDGG SVKETAAEEE SRVLAPGAAP FGNFPHYSRF HPPEQRLRLL PPELLRQLFP
ESPENGPILG LDVGCNSGDL SVALYKHFLS LPDGETCSDA SREFRLLCCD IDPVLVKRAE
KECPFPDALT FITLDFMNQR TRKVLLSSFL SQFGRSVFDI GFCMSITMWI HLNHGDHGLW
EFLAHLSSLC HYLLVEPQPW KCYRAAARRL RKLGLHDFDH FHSLAIRGDM PNQIVQILTQ
DHGMELICCF GNTSWDRSLL LFRAKQTIET HPIPESLIEK GKEKNRLSFQ KQ
