ID GATB_STAAM Reviewed; 475 AA. AC P64201; Q99SY7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 113. DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121}; DE Short=Asp/Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121}; DE EC=6.3.5.6 {ECO:0000255|HAMAP-Rule:MF_00121}; DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00121}; DE AltName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121}; DE Short=Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121}; GN Name=gatB {ECO:0000255|HAMAP-Rule:MF_00121}; GN OrderedLocusNames=SAV1899; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu50 / ATCC 700699; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). RN [2] {ECO:0007744|PDB:2DF4, ECO:0007744|PDB:2DQN, ECO:0007744|PDB:2F2A, ECO:0007744|PDB:2G5H, ECO:0007744|PDB:2G5I} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH GATA; GATC; ATP RP ANALOG AND MG(2+), CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AND MUTAGENESIS OF RP 412-ILE--ARG-475; 466-GLN--ARG-475; 472-LEU--ARG-475 AND 473-ASP--ARG-475. RX PubMed=16809541; DOI=10.1126/science.1127156; RA Nakamura A., Yao M., Chimnaronk S., Sakai N., Tanaka I.; RT "Ammonia channel couples glutaminase with transamidase reactions in RT GatCAB."; RL Science 312:1954-1958(2006). RN [3] {ECO:0007744|PDB:3IP4} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH GATA; GATC AND RP MG(2+), FUNCTION, DOMAIN, AND MUTAGENESIS OF 183-LYS--ARG-185 AND RP 437-LYS--LYS-442. RX PubMed=19906721; DOI=10.1093/nar/gkp955; RA Nakamura A., Sheppard K., Yamane J., Yao M., Soll D., Tanaka I.; RT "Two distinct regions in Staphylococcus aureus GatCAB guarantee accurate RT tRNA recognition."; RL Nucleic Acids Res. 38:672-682(2010). CC -!- FUNCTION: Catalytic subunit of the Asp/Glu-tRNA(Asn/Gln) CC amidotransferase complex GatCAB (PubMed:16809541). GatCAB allows the CC formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through CC the multi-step transamidation of misacylated Asp-tRNA(Asn) or Glu- CC tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or CC glutaminyl-tRNA synthetases (By similarity). The reaction takes place CC in the presence of glutamine and ATP through an activated phospho-Asp- CC tRNA(Asn) or phospho-Glu-tRNA(Gln) (Probable). This subunit CC specifically recognizes tRNA(Gln) and tRNA(Asn), and mediates the CC transamidation of misloaded Glu and Asp respectively by catalyzing CC formation of the activated gamma-phospho-intermediate and its CC subsequent aminolysis using ammonia produced by the gatA subunit CC (PubMed:16809541). Recognizes the first base pair and the D-loop of its CC specific tRNA substrates (PubMed:16809541, PubMed:19906721). CC {ECO:0000255|HAMAP-Rule:MF_00121, ECO:0000269|PubMed:16809541, CC ECO:0000269|PubMed:19906721, ECO:0000305|PubMed:16809541}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl- CC tRNA(Gln) + L-glutamate + ADP + phosphate + H(+); CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00121, CC ECO:0000305|PubMed:16809541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartyl-tRNA(Asn) + L-glutamine + ATP + H2O = L- CC asparaginyl-tRNA(Asn) + L-glutamate + ADP + phosphate + 2 H(+); CC Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216; EC=6.3.5.6; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00121, CC ECO:0000305|PubMed:16809541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamyl-tRNA(Gln) + ATP = 5-phospho-L-glutamyl-tRNA(Gln) + CC ADP; Xref=Rhea:RHEA:57908, Rhea:RHEA-COMP:9684, Rhea:RHEA-COMP:15032, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:78520, ChEBI:CHEBI:142449, CC ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_00121, CC ECO:0000305|PubMed:16809541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartyl-tRNA(Asn) + ATP = 4-phospho-L-aspartyl-tRNA(Asn) + CC ADP + H(+); Xref=Rhea:RHEA:57916, Rhea:RHEA-COMP:9677, Rhea:RHEA- CC COMP:15033, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:78516, CC ChEBI:CHEBI:142450, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00121, ECO:0000305|PubMed:16809541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-phospho-L-glutamyl-tRNA(Gln) + NH4(+) = L-glutaminyl- CC tRNA(Gln) + phosphate + H(+); Xref=Rhea:RHEA:57912, Rhea:RHEA- CC COMP:9681, Rhea:RHEA-COMP:15032, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:78521, CC ChEBI:CHEBI:142449; Evidence={ECO:0000255|HAMAP-Rule:MF_00121, CC ECO:0000305|PubMed:16809541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-phospho-L-aspartyl-tRNA(Asn) + NH4(+) = L-asparaginyl- CC tRNA(Asn) + phosphate + H(+); Xref=Rhea:RHEA:57920, Rhea:RHEA- CC COMP:9674, Rhea:RHEA-COMP:15033, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:78515, CC ChEBI:CHEBI:142450; Evidence={ECO:0000255|HAMAP-Rule:MF_00121, CC ECO:0000305|PubMed:16809541}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00121}; CC Note=Binds 2 Mg(2+) ions, a primary Mg(2+) ion involved in positioning CC of the gamma-carbonyl group of the amino acid in Glu-tRNA(Gln), and a CC secondary transient Mg(2+) ion that participates in phosphoryl transfer CC by polarizing the gamma-phosphate group of ATP. {ECO:0000255|HAMAP- CC Rule:MF_00121, ECO:0000269|PubMed:16809541}; CC -!- SUBUNIT: Component of the heterotrimeric GatCAB glutamyl-tRNA(Gln) CC amidotransferase complex composed of GatA, GatB and GatC. CC {ECO:0000255|HAMAP-Rule:MF_00121, ECO:0000269|PubMed:16809541, CC ECO:0000269|PubMed:19906721}. CC -!- DOMAIN: The N-terminal cradle domain recognizes the first base of the CC acceptor tRNA stem. {ECO:0000255|HAMAP-Rule:MF_00121, CC ECO:0000269|PubMed:19906721}. CC -!- DOMAIN: The C-terminal tail domain, an anti-parallel amphiphilic helix CC bundle, is involved in discriminating and binding specific tRNAs. CC Probably recognizes the tRNA(Gln)-specific D-loop structure. CC {ECO:0000255|HAMAP-Rule:MF_00121, ECO:0000269|PubMed:19906721}. CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00121}. 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; BA000017; BAB58061.1; -; Genomic_DNA. DR RefSeq; WP_000545370.1; NC_002758.2. DR PDB; 2DF4; X-ray; 3.20 A; B=1-475. DR PDB; 2DQN; X-ray; 2.55 A; B=1-475. DR PDB; 2F2A; X-ray; 2.30 A; B=1-475. DR PDB; 2G5H; X-ray; 2.50 A; B=1-475. DR PDB; 2G5I; X-ray; 3.35 A; B=1-475. DR PDB; 3IP4; X-ray; 1.90 A; B=1-475. DR AlphaFoldDB; P64201; -. DR SMR; P64201; -. DR KEGG; sav:SAV1899; -. DR HOGENOM; CLU_019240_0_0_9; -. DR PhylomeDB; P64201; -. DR BRENDA; 6.3.5.7; 3352. DR EvolutionaryTrace; P64201; -. DR GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:TreeGrafter. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR FunFam; 1.10.10.410:FF:000001; Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 1. DR FunFam; 1.10.150.380:FF:000001; Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 1. DR Gene3D; 1.10.10.410; -; 1. DR Gene3D; 1.10.150.380; GatB domain, N-terminal subdomain; 1. DR HAMAP; MF_00121; GatB; 1. DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E. DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat. DR InterPro; IPR018027; Asn/Gln_amidotransferase. DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like. DR InterPro; IPR004413; GatB. DR InterPro; IPR042114; GatB_C_1. DR InterPro; IPR023168; GatB_Yqey_C_2. DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS. DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom. DR NCBIfam; TIGR00133; gatB; 1. DR NCBIfam; NF004011; PRK05477.1-1; 1. DR NCBIfam; NF004012; PRK05477.1-2; 1. DR NCBIfam; NF004014; PRK05477.1-4; 1. DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1. DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1. DR Pfam; PF02934; GatB_N; 1. DR Pfam; PF02637; GatB_Yqey; 1. DR SMART; SM00845; GatB_Yqey; 1. DR SUPFAM; SSF89095; GatB/YqeY motif; 1. DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1. DR PROSITE; PS01234; GATB; 1. DR PDBsum; 2DF4; -. DR PDBsum; 2DQN; -. DR PDBsum; 2F2A; -. DR PDBsum; 2G5H; -. DR PDBsum; 2G5I; -. DR PDBsum; 3IP4; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..475 FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase FT subunit B" FT /id="PRO_0000148834" FT REGION 1..294 FT /note="Cradle" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000305|PubMed:19906721" FT REGION 412..475 FT /note="Tail" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000305|PubMed:19906721" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0007744|PDB:2DF4" FT BINDING 12 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0000269|PubMed:19906721, FT ECO:0007744|PDB:2DF4, ECO:0007744|PDB:2DQN, FT ECO:0007744|PDB:2F2A, ECO:0007744|PDB:2G5H, FT ECO:0007744|PDB:2G5I, ECO:0007744|PDB:3IP4" FT BINDING 124 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0000269|PubMed:19906721, FT ECO:0007744|PDB:2DF4, ECO:0007744|PDB:2DQN, FT ECO:0007744|PDB:2F2A, ECO:0007744|PDB:2G5H, FT ECO:0007744|PDB:2G5I, ECO:0007744|PDB:3IP4" FT BINDING 150 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0000269|PubMed:19906721, FT ECO:0007744|PDB:2DF4, ECO:0007744|PDB:2DQN, FT ECO:0007744|PDB:2F2A, ECO:0007744|PDB:2G5H, FT ECO:0007744|PDB:2G5I, ECO:0007744|PDB:3IP4" FT BINDING 153 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0007744|PDB:2G5I" FT BINDING 192 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0007744|PDB:2DF4" FT BINDING 196 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0007744|PDB:2G5I" FT BINDING 206 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0007744|PDB:2G5I" FT BINDING 208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0007744|PDB:2G5I" FT BINDING 210 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00121, FT ECO:0000269|PubMed:16809541, ECO:0007744|PDB:2DF4" FT MUTAGEN 183..185 FT /note="Missing: 17-fold reduction in enzyme efficiency and FT altered tRNA substrate preference." FT /evidence="ECO:0000269|PubMed:19906721" FT MUTAGEN 412..475 FT /note="Missing: Loss of tRNA(Gln) binding." FT /evidence="ECO:0000269|PubMed:16809541" FT MUTAGEN 437..442 FT /note="KNGKGK->GMGAMGP: Reduces affinity for tRNA." FT /evidence="ECO:0000269|PubMed:19906721" FT MUTAGEN 466..475 FT /note="Missing: Loss of tRNA(Gln) binding." FT /evidence="ECO:0000269|PubMed:16809541" FT MUTAGEN 472..475 FT /note="Missing: Loss of tRNA(Gln) binding." FT /evidence="ECO:0000269|PubMed:16809541" FT MUTAGEN 473..475 FT /note="Missing: No effect on tRNA(Gln) binding." FT /evidence="ECO:0000269|PubMed:16809541" FT STRAND 3..14 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 21..28 FT /evidence="ECO:0007829|PDB:3IP4" FT TURN 39..43 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 53..65 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 89..93 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 99..125 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 136..140 FT /evidence="ECO:0007829|PDB:3IP4" FT TURN 142..145 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 147..153 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 160..177 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 188..199 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:2F2A" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 217..237 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 243..248 FT /evidence="ECO:0007829|PDB:3IP4" FT TURN 250..252 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 255..261 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:2DF4" FT HELIX 282..289 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 296..305 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 311..317 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:2DF4" FT HELIX 321..331 FT /evidence="ECO:0007829|PDB:3IP4" FT TURN 332..334 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 337..343 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 344..348 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 349..354 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 359..361 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 366..378 FT /evidence="ECO:0007829|PDB:3IP4" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:2F2A" FT HELIX 383..396 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 400..405 FT /evidence="ECO:0007829|PDB:3IP4" FT TURN 406..408 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 415..428 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 430..437 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 443..454 FT /evidence="ECO:0007829|PDB:3IP4" FT HELIX 461..474 FT /evidence="ECO:0007829|PDB:3IP4" SQ SEQUENCE 475 AA; 53657 MW; 96805EE591658154 CRC64; MHFETVIGLE VHVELKTDSK MFSPSPAHFG AEPNSNTNVI DLAYPGVLPV VNKRAVDWAM RAAMALNMEI ATESKFDRKN YFYPDNPKAY QISQFDQPIG ENGYIDIEVD GETKRIGITR LHMEEDAGKS THKGEYSLVD LNRQGTPLIE IVSEPDIRSP KEAYAYLEKL RSIIQYTGVS DVKMEEGSLR CDANISLRPY GQEKFGTKAE LKNLNSFNYV RKGLEYEEKR QEEELLNGGE IGQETRRFDE STGKTILMRV KEGSDDYRYF PEPDIVPLYI DDAWKERVRQ TIPELPDERK AKYVNELGLP AYDAHVLTLT KEMSDFFEST IEHGADVKLT SNWLMGGVNE YLNKNQVELL DTKLTPENLA GMIKLIEDGT MSSKIAKKVF PELAAKGGNA KQIMEDNGLV QISDEATLLK FVNEALDNNE QSVEDYKNGK GKAMGFLVGQ IMKASKGQAN PQLVNQLLKQ ELDKR //