ID   A0A059ZTE3_ACIBA        Unreviewed;       878 AA.
AC   A0A059ZTE3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036,
GN   ECO:0000313|EMBL:ASF76661.1};
GN   Synonyms=alaS_1 {ECO:0000313|EMBL:SSQ35668.1}, alaS_3
GN   {ECO:0000313|EMBL:SSU38360.1};
GN   ORFNames=A7M79_15050 {ECO:0000313|EMBL:OIH04575.1}, A7M90_08745
GN   {ECO:0000313|EMBL:OIG67468.1}, AB719_03830
GN   {ECO:0000313|EMBL:RDJ61772.1}, B9X91_12675
GN   {ECO:0000313|EMBL:OTL19830.1}, B9X95_03515
GN   {ECO:0000313|EMBL:OTM92370.1}, BGC29_16755
GN   {ECO:0000313|EMBL:ODP71357.1}, C2U32_02220
GN   {ECO:0000313|EMBL:AUT36896.1}, CBI29_01280
GN   {ECO:0000313|EMBL:ASF76661.1}, CEJ63_18835
GN   {ECO:0000313|EMBL:PAM66189.1}, CYQ93_21680
GN   {ECO:0000313|EMBL:RIL13137.1}, DOL94_06455
GN   {ECO:0000313|EMBL:PZM17994.1}, EA677_14030
GN   {ECO:0000313|EMBL:RSR98341.1}, EGM95_14360
GN   {ECO:0000313|EMBL:AYY89888.1}, EHF38_12160
GN   {ECO:0000313|EMBL:QAB42297.1}, SAMEA104305229_03711
GN   {ECO:0000313|EMBL:SSQ35668.1}, SAMEA104305292_02110
GN   {ECO:0000313|EMBL:SSS44900.1}, SAMEA104305325_02884
GN   {ECO:0000313|EMBL:SST96056.1}, SAMEA104305337_09813
GN   {ECO:0000313|EMBL:SSU38360.1};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470 {ECO:0000313|EMBL:PZM17994.1, ECO:0000313|Proteomes:UP000248662};
RN   [1] {ECO:0000313|EMBL:RDJ61772.1, ECO:0000313|Proteomes:UP000254935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMDRAB19 {ECO:0000313|EMBL:RDJ61772.1,
RC   ECO:0000313|Proteomes:UP000254935};
RA   Feng Y., Chiu C.-H.;
RT   "Genome analysis of of clinical invasive Acinetobacter baumannii
RT   isolates in Taiwan.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OIG67468.1, ECO:0000313|Proteomes:UP000179791, ECO:0000313|Proteomes:UP000179937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH639 {ECO:0000313|EMBL:OIH04575.1,
RC   ECO:0000313|Proteomes:UP000179791}, and XH647
RC   {ECO:0000313|EMBL:OIG67468.1, ECO:0000313|Proteomes:UP000179937};
RA   Hua X., Yu Y.;
RT   "The evolution of Acinetobacter baumannii in vivo.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ODP71357.1, ECO:0000313|Proteomes:UP000094982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH198 {ECO:0000313|EMBL:ODP71357.1,
RC   ECO:0000313|Proteomes:UP000094982};
RA   Mu X., Wang N., Li X., Shi K., Zhou Z., Yu Y., Hua X.;
RT   "The effect of colistin resistance-associated mutations on the fitness
RT   of Acinetobacter baumannii.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:OTL19830.1, ECO:0000313|Proteomes:UP000194699, ECO:0000313|Proteomes:UP000194957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR350 {ECO:0000313|EMBL:OTM92370.1,
RC   ECO:0000313|Proteomes:UP000194699}, and PR354
RC   {ECO:0000313|EMBL:OTL19830.1, ECO:0000313|Proteomes:UP000194957};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:PAM66189.1, ECO:0000313|Proteomes:UP000216072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB75 {ECO:0000313|EMBL:PAM66189.1,
RC   ECO:0000313|Proteomes:UP000216072};
RA   Chen Q.;
RT   "Carbapenem-resistant Acinetobacter baumannii strains.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:ASF76661.1, ECO:0000313|Proteomes:UP000197701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A85 {ECO:0000313|EMBL:ASF76661.1,
RC   ECO:0000313|Proteomes:UP000197701};
RA   Hamidian M., Wick R.R., Hawkey J., Holt K.E., Hall R.M.;
RT   "Complete genome sequence of Acinetobacter baumannii strain A85
RT   belonging to global clone 1 (GC1).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:AUT36896.1, ECO:0000313|Proteomes:UP000236385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT36896.1,
RC   ECO:0000313|Proteomes:UP000236385};
RG   NISC Comparative Sequencing Program;
RA   Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA   Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA   Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT   "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT   Bacterial Plasmids Conferring Carbapenem Resistance.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:AUT36896.1, ECO:0000313|Proteomes:UP000236385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT36896.1,
RC   ECO:0000313|Proteomes:UP000236385};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:RIL13137.1, ECO:0000313|Proteomes:UP000266418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APC25 {ECO:0000313|EMBL:RIL13137.1,
RC   ECO:0000313|Proteomes:UP000266418};
RA   Freitas D.Y., Araujo S., Folador A.R.C., Ramos R.T.J., Azevedo J.S.N.,
RA   Tacao M., Silva A., Henriques I., Barauna R.A.;
RT   "Extended spectrum beta-lactamase-producing Gram-negative bacteria
RT   recovered from an Amazonian mesotrophic lake.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [10] {ECO:0000313|EMBL:PZM17994.1, ECO:0000313|Proteomes:UP000248662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R10 {ECO:0000313|EMBL:PZM17994.1,
RC   ECO:0000313|Proteomes:UP000248662};
RA   Bonnin R.A., Levy M., Cuzon G., Dortet L., Naas T.;
RT   "Carbapenemase-producing Acinetobacter spp. from environmental sources
RT   in an hospital from French Polynesia.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [11] {ECO:0000313|Proteomes:UP000262639, ECO:0000313|Proteomes:UP000263147, ECO:0000313|Proteomes:UP000263963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4300STDY7045733 {ECO:0000313|EMBL:SSQ35668.1,
RC   ECO:0000313|Proteomes:UP000263963}, 4300STDY7045797
RC   {ECO:0000313|EMBL:SSS44900.1, ECO:0000313|Proteomes:UP000262639},
RC   4300STDY7045830 {ECO:0000313|EMBL:SST96056.1,
RC   ECO:0000313|Proteomes:UP000264417}, and 4300STDY7045842
RC   {ECO:0000313|EMBL:SSU38360.1, ECO:0000313|Proteomes:UP000263147};
RG   Pathogen Informatics;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [12] {ECO:0000313|EMBL:RSR98341.1, ECO:0000313|Proteomes:UP000282466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TG15473 {ECO:0000313|EMBL:RSR98341.1,
RC   ECO:0000313|Proteomes:UP000282466};
RA   Sahl J.W.;
RT   "GWAS and RNA-Seq identify cryptic mechanisms of antimicrobial
RT   resistance in Acinetobacter baumannii.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [13] {ECO:0000313|EMBL:AYY89888.1, ECO:0000313|Proteomes:UP000273577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSN15313 {ECO:0000313|EMBL:AYY89888.1,
RC   ECO:0000313|Proteomes:UP000273577};
RA   Sorenson N.M., Snesrud E., Xavier D.E., Cacci L.C., Oeleman W.,
RA   Iavarone A.T., Mc Gann P., Riley L.W., Moreira B.M.;
RT   "A novel plasmid carries a functional mcr-4.3 gene in a colistin-
RT   resistant Acinetobacter baumannii clinical strain.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [14] {ECO:0000313|EMBL:QAB42297.1, ECO:0000313|Proteomes:UP000287737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A52 {ECO:0000313|EMBL:QAB42297.1,
RC   ECO:0000313|Proteomes:UP000287737};
RA   Ruan Z., Jia H.;
RT   "Carbapenem-resistant Acinetobacter baumannii strain harboring blaOXA-
RT   72 from China.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a
CC       two-step reaction: alanine is first activated by ATP to form Ala-
CC       AMP and then transferred to the acceptor end of tRNA(Ala). Also
CC       edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its
CC       editing domain. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00015829}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-
CC         alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657,
CC         Rhea:RHEA-COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497,
CC         ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00036, ECO:0000256|SAAS:SAAS01125460};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00832879}.
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic
CC       domain, the editing domain and the C-terminal C-Ala domain. The
CC       editing domain removes incorrectly charged amino acids, while the
CC       C-Ala domain, along with tRNA(Ala), serves as a bridge to
CC       cooperatively bring together the editing and aminoacylation
CC       centers thus stimulating deacylation of misacylated tRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00575517}.
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DR   EMBL; CP021782; ASF76661.1; -; Genomic_DNA.
DR   EMBL; CP026125; AUT36896.1; -; Genomic_DNA.
DR   EMBL; CP033869; AYY89888.1; -; Genomic_DNA.
DR   EMBL; MDWM01000084; ODP71357.1; -; Genomic_DNA.
DR   EMBL; LYKI01000067; OIG67468.1; -; Genomic_DNA.
DR   EMBL; LYKQ01000058; OIH04575.1; -; Genomic_DNA.
DR   EMBL; NGCH01000812; OTL19830.1; -; Genomic_DNA.
DR   EMBL; NGEL01000030; OTM92370.1; -; Genomic_DNA.
DR   EMBL; NKKG01000086; PAM66189.1; -; Genomic_DNA.
DR   EMBL; QKWF01000059; PZM17994.1; -; Genomic_DNA.
DR   EMBL; CP034092; QAB42297.1; -; Genomic_DNA.
DR   EMBL; LFHE01000033; RDJ61772.1; -; Genomic_DNA.
DR   EMBL; PYSX01000042; RIL13137.1; -; Genomic_DNA.
DR   EMBL; RFDR01000387; RSR98341.1; -; Genomic_DNA.
DR   EMBL; UFJW01000100; SSQ35668.1; -; Genomic_DNA.
DR   EMBL; UFLY01000010; SSS44900.1; -; Genomic_DNA.
DR   EMBL; UFNA01000142; SST96056.1; -; Genomic_DNA.
DR   EMBL; UFNQ01000059; SSU38360.1; -; Genomic_DNA.
DR   RefSeq; WP_000199457.1; NZ_ULHD01000017.1.
DR   STRING; 470.IX87_04765; -.
DR   EnsemblBacteria; AKQ27505; AKQ27505; ACX60_12345.
DR   EnsemblBacteria; AMN00940; AMN00940; AZE33_07035.
DR   EnsemblBacteria; OBE58331; OBE58331; A7934_11960.
DR   EnsemblBacteria; ODP71357; ODP71357; BGC29_16755.
DR   KEGG; abaa:IX88_07955; -.
DR   KEGG; abw:BL01_15570; -.
DR   PATRIC; fig|470.1288.peg.2973; -.
DR   KO; K01872; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000094982; Unassembled WGS sequence.
DR   Proteomes; UP000179791; Unassembled WGS sequence.
DR   Proteomes; UP000179937; Unassembled WGS sequence.
DR   Proteomes; UP000194699; Unassembled WGS sequence.
DR   Proteomes; UP000194957; Unassembled WGS sequence.
DR   Proteomes; UP000197701; Chromosome.
DR   Proteomes; UP000216072; Unassembled WGS sequence.
DR   Proteomes; UP000236385; Chromosome.
DR   Proteomes; UP000248662; Unassembled WGS sequence.
DR   Proteomes; UP000254935; Unassembled WGS sequence.
DR   Proteomes; UP000262639; Unassembled WGS sequence.
DR   Proteomes; UP000263147; Unassembled WGS sequence.
DR   Proteomes; UP000263963; Unassembled WGS sequence.
DR   Proteomes; UP000264417; Unassembled WGS sequence.
DR   Proteomes; UP000266418; Unassembled WGS sequence.
DR   Proteomes; UP000273577; Chromosome.
DR   Proteomes; UP000282466; Unassembled WGS sequence.
DR   Proteomes; UP000287737; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR   InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR   InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR   InterPro; IPR003156; DHHA1_dom.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF02272; DHHA1; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF101353; SSF101353; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   TIGRFAMs; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00249969, ECO:0000313|EMBL:RDJ61772.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250154}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000094982,
KW   ECO:0000313|Proteomes:UP000179791, ECO:0000313|Proteomes:UP000179937,
KW   ECO:0000313|Proteomes:UP000194699};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00299154};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00249928, ECO:0000313|EMBL:PZM17994.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423853};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250206};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250204};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250135};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250194};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00423813}.
FT   DOMAIN        1    713       AA_TRNA_LIGASE_II_ALA.
FT                                {ECO:0000259|PROSITE:PS50860}.
FT   COILED      344    364       {ECO:0000256|SAM:Coils}.
FT   COILED      366    386       {ECO:0000256|SAM:Coils}.
FT   COILED      736    763       {ECO:0000256|SAM:Coils}.
FT   METAL       562    562       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       566    566       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       670    670       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       674    674       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
SQ   SEQUENCE   878 AA;  96528 MW;  48DC937CBAF0C6F6 CRC64;
     MTSAEIREAF LRYFETQGHT RVASSSLVPA NDPTLLFTNA GMNQFKDCFL GLEKRDYVRA
     TTSQKCVRAG GKHNDLDNVG YTARHHTFFE MLGNFSFGDY FKRDALKFAW EFLTSEQWLA
     LPKDKLYVTV YHTDDEAYDI WNKEIGLAPE RIIRIGDNKG EKYASDNFWA MGDTGPCGPC
     SEIFFDHGEH IWGGLPGSPE EDGDRFIEIW NNVFMQFNRT ADGVLHPLPA PSVDTGMGLE
     RISAVLQHVN SNYDIDLFQH LLKAAANIIG IEDEGQPSLR VVADHARSCC FLIADGVNPS
     NEGRGYVLRR IIRRAVRHGN KLGATGTFFY KMLQPLIEVM GQAYPELEAR REVIEATLIR
     EEEQFAKTLE QGLKLLEGEL AQLKDKTIPG ATVFKLYDTY GFPTDLTADI ARERGFIIDE
     AGFEVEMAAQ RQRARDAGKF AVDYNNIVKV EGETQFDGYT NTTGQGQIVA IYKDGVQVDE
     VSEGDEALIV LNQTPFYAES GGQIGDTGIF KNETGIFEVQ DTKKSGGAFV HQGIVTVGNL
     KTSQNVEAIV KADIREATAR NHSATHLLHA ALRQILGSHV QQKGSLVASD ILRFDFANDQ
     PVSFEQLQQV ERLVNAEIIA NTAVTTELLD IETAKAKGAM MLFGEKYGDE VRVLSMGSVI
     DEKNFSIELC GGIHVKRTGD IGLFKITSEG GVAAGVRRIE AVTGTKALEV VQKADHDIQH
     INSLLKAQKD QTVERVQANV ELVSALQKQI EQLNQKLANF QAADLIDQVQ TIAGRQTLIT
     TVQGVDAKAL RNLHDSVKSK LENAVIVLAG VEGDKVSLLA SVASQYTANL KAGDIIKHLA
     TELGGKGGGK PDLAQGGAPL NEKFGQVMAA LPAWLEQK
//