ID A0A059ZTE3_ACIBA Unreviewed; 878 AA. AC A0A059ZTE3; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 02-OCT-2024, entry version 83. 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:CUW34548.1}; GN ORFNames=A6Y97_18720 {ECO:0000313|EMBL:KAA9216850.1}, A7M90_08745 GN {ECO:0000313|EMBL:OIG67468.1}, ABR2091_1143 GN {ECO:0000313|EMBL:CUW34548.1}, AUO97_13275 GN {ECO:0000313|EMBL:APP31728.1}, B9X95_03515 GN {ECO:0000313|EMBL:OTM92370.1}, DOL94_06455 GN {ECO:0000313|EMBL:PZM17994.1}, F2P40_15715 GN {ECO:0000313|EMBL:MQR50747.1}, FQZ15_12845 GN {ECO:0000313|EMBL:QNV31131.1}, FR761_06870 GN {ECO:0000313|EMBL:QFH47199.1}, GNY86_07135 GN {ECO:0000313|EMBL:MVM91291.1}, GSE42_06790 GN {ECO:0000313|EMBL:MYM77633.1}, H0529_08750 GN {ECO:0000313|EMBL:QOJ62109.1}, IAG11_16200 GN {ECO:0000313|EMBL:MBD0221436.1}, IMO23_05860 GN {ECO:0000313|EMBL:QPF15068.1}, JHZ39_002138 GN {ECO:0000313|EMBL:EGY2377750.1}, OMP06_06210 GN {ECO:0000313|EMBL:UZG64037.1}, P9867_12625 GN {ECO:0000313|EMBL:MDK4882510.1}, SAMEA4394745_03680 GN {ECO:0000313|EMBL:SSI70680.1}; OS Acinetobacter baumannii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:PZM17994.1, ECO:0000313|Proteomes:UP000248662}; RN [1] {ECO:0000313|EMBL:APP31728.1, ECO:0000313|Proteomes:UP000072389} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978 {ECO:0000313|EMBL:APP31728.1, RC ECO:0000313|Proteomes:UP000072389}; RX PubMed=25136007; DOI=10.1128/AAC.03074-14; RA Fernando D.M., Xu W., Loewen P.C., Zhanel G.G., Kumar A.; RT "Triclosan can select for an AdeIJK-overexpressing mutant of Acinetobacter RT baumannii ATCC 17978 that displays reduced susceptibility to multiple RT antibiotics."; RL Antimicrob. Agents Chemother. 58:6424-6431(2014). RN [2] {ECO:0000313|EMBL:APP31728.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17978 {ECO:0000313|EMBL:APP31728.1}; RA Singh M.K., Fernando D.M., Kumar A.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CUW34548.1, ECO:0000313|Proteomes:UP000066661} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R2091 {ECO:0000313|EMBL:CUW34548.1}; RA Wibberg D.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:OIG67468.1, ECO:0000313|Proteomes:UP000179937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH647 {ECO:0000313|EMBL:OIG67468.1, RC 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 [5] {ECO:0000313|EMBL:APP31728.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17978 {ECO:0000313|EMBL:APP31728.1}; RA Singh M., Fernando D., Kumar A.; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:MYM77633.1, ECO:0000313|Proteomes:UP000480763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DMS06669 {ECO:0000313|EMBL:MYM77633.1, RC ECO:0000313|Proteomes:UP000480763}; RX PubMed=29137647; RA Si-Tuan N., Ngoc H.M., Hang P.T.T., Nguyen C., Van P.H., Huong N.T.; RT "New eight genes identified at the clinical multidrug-resistant RT Acinetobacter baumannii DMS06669 strain in a Vietnam hospital."; RL Ann. Clin. Microbiol. Antimicrob. 16:0-74(2017). RN [7] {ECO:0000313|EMBL:OTM92370.1, ECO:0000313|Proteomes:UP000194699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR350 {ECO:0000313|EMBL:OTM92370.1, RC ECO:0000313|Proteomes:UP000194699}; RA Song R., Chenine A.L., Ruprecht R.M.; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. RN [8] {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 in RT an hospital from French Polynesia."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:SSI70680.1, ECO:0000313|Proteomes:UP000262697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4300STDY6542375 {ECO:0000313|EMBL:SSI70680.1, RC ECO:0000313|Proteomes:UP000262697}; RG Pathogen Informatics; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:QFH47199.1, ECO:0000313|Proteomes:UP000327158} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E47 {ECO:0000313|EMBL:QFH47199.1, RC ECO:0000313|Proteomes:UP000327158}; RA Phan H.T.T., Stoesser N., Gordon K.A., Crook D., Walker S.A., Mathers A.J., RA Peto T.E.A., George S., Lipworth S.I.; RT "Genomic Dynamics of Species and Mobile Genetic Elements in a Prolonged RT blaIMP-4-associated Carbapenemase Outbreak in an Australian Hospital."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:KAA9216850.1, ECO:0000313|Proteomes:UP000326440} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDA-CDC-AR_0275 {ECO:0000313|EMBL:KAA9216850.1, RC ECO:0000313|Proteomes:UP000326440}; RA Weber K.L., Lesassier D.S., Schulte K.Q., Westfall N., Kappell A.D., RA Albright N.C., Acevedo C.A., Godbold G.D., Palsikar V.S., Ternus K.L., RA Hewitt C.F.; RT "Draft genome sequence of Acinetobacter baumanii (AR Bank 0275)."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:MQR50747.1, ECO:0000313|Proteomes:UP000461234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABS103 {ECO:0000313|EMBL:MQR50747.1, RC ECO:0000313|Proteomes:UP000461234}; RA Douraghi M., Aris P., Kenyon J., Hamidian M.; RT "Genetic environment of the oxa23 gene and comparative analysis of RT carbapenem resistant Acinetobacter baumannii isolates belonging to global RT clone 1, lineage 2 recovered in a burns hospital outbreak in 2012-2013."; RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases. RN [13] {ECO:0000313|EMBL:MVM91291.1, ECO:0000313|Proteomes:UP000439424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ac576 {ECO:0000313|EMBL:MVM91291.1, RC ECO:0000313|Proteomes:UP000439424}; RA Fedrigo N.H., Cerdeira L., Fuga B., Marini P.V.B., Shinohara D.R., RA Carrara-Marroni F.E., Lincopan N., Tognim M.C.B.; RT "Multidrug-resistant Acinetobacter baumannii moving toward extensively RT drug-resistant over fifteen years in South of Brazil."; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|EMBL:MYM77633.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DMS06669 {ECO:0000313|EMBL:MYM77633.1}; RA Nguyen S.-T.; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. RN [15] {ECO:0000313|Proteomes:UP000593752} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AC1633 {ECO:0000313|Proteomes:UP000593752}; RA Alattraqchi A.G., Mohd Ranii, F, A Rahmann, NII, Ismail S., Cleary D., RA Clarke S., Yeo C.C.; RT "Complete genome sequencing of Acinetobacter baumannii AC1633 and RT Acinetobacter nosocomialis AC1530 unveils a large multidrug resistant RT plasmid encoding the NDM-1 and OXA-58 carbapenemases."; RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases. RN [16] {ECO:0000313|EMBL:MBD0221436.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A86 {ECO:0000313|EMBL:MBD0221436.1}; RA Abouelfetouh A., Mattock J., Turner D., Li E., Evans B.A.; RT "Diversity of carbapenem-resistant Acinetobacter baumannii and RT bacteriophage-mediated spread of the Oxa23 carbapenemase."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. RN [17] {ECO:0000313|EMBL:QNV31131.1, ECO:0000313|Proteomes:UP000516431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFSAN093707 {ECO:0000313|EMBL:QNV31131.1, RC ECO:0000313|Proteomes:UP000516431}; RA Hoffmann M., Luo Y., Strain E., Rand H., Javkar K.G.; RT "Carbapenem-Resistant Acinetobacter baumannii devoid of typical resistance RT factors."; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. RN [18] {ECO:0000313|EMBL:QPF15068.1, ECO:0000313|Proteomes:UP000594659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Res13-Abat-PEA21-P4-01-A {ECO:0000313|EMBL:QPF15068.1, RC ECO:0000313|Proteomes:UP000594659}; RA Poulin-Laprade D., Brouard J.-S., Gagnon N., Turcotte A., Langlois A., RA Matte J.J., Carrillo C.D., Zaheer R., McAllister T., Topp E., Talbot G.; RT "Resistance determinants and their genetic context in bacteria from a RT longitudinal study of pigs reared under conventional and antibiotic-free RT husbandry practices."; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. RN [19] {ECO:0000313|EMBL:EGY2377750.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2018HL-00813 {ECO:0000313|EMBL:EGY2377750.1}; RG Clinical and Environmental Microbiology Branch: Whole genome sequencing antimicrobial resistance pathogens in the healthcare setting; RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases. RN [20] {ECO:0000313|EMBL:QOJ62109.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AC1633 {ECO:0000313|EMBL:QOJ62109.1}; RA Alattraqchi A.G., Mohd Rani F., A. Rahman N.I., Ismail S., Cleary D.W., RA Clarke S.C., Yeo C.C.; RT "Complete Genome Sequencing of Acinetobacter baumannii AC1633 and RT Acinetobacter nosocomialis AC1530 Unveils a Large Multidrug-Resistant RT Plasmid Encoding the NDM-1 and OXA-58 Carbapenemases."; RL MSphere 6:0-0(2021). RN [21] {ECO:0000313|EMBL:MDK4882510.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CPO519 {ECO:0000313|EMBL:MDK4882510.1}; RA Macesic N.; RT "Genomic dissection of endemic carbapenem resistance: metallo-beta- RT lactamase gene dissemination through clonal, plasmid and integron transfer RT pathways."; RL Submitted (JAN-2023) to the EMBL/GenBank/DDBJ databases. RN [22] {ECO:0000313|EMBL:UZG64037.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RBH2 {ECO:0000313|EMBL:UZG64037.1}; RA Ambrose S.J., Hall R.M.; RT "Acinetobacter baumannii RBH2 complete genome."; RL Submitted (FEB-2023) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two- CC step reaction: alanine is first activated by ATP to form Ala-AMP and CC then transferred to the acceptor end of tRNA(Ala). Also edits CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing CC domain. {ECO:0000256|HAMAP-Rule:MF_00036}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl- CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA- CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00036}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00036}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00036}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036}. CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the CC editing domain and the C-terminal C-Ala domain. The editing domain CC removes incorrectly charged amino acids, while the C-Ala domain, along CC with tRNA(Ala), serves as a bridge to cooperatively bring together the CC editing and aminoacylation centers thus stimulating deacylation of CC misacylated tRNAs. {ECO:0000256|HAMAP-Rule:MF_00036}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00036}. 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; CP018664; APP31728.1; -; Genomic_DNA. DR EMBL; LN997846; CUW34548.1; -; Genomic_DNA. DR EMBL; AAYLMQ010000023; EGY2377750.1; -; Genomic_DNA. DR EMBL; VYVC01000047; KAA9216850.1; -; Genomic_DNA. DR EMBL; JACSVK010000052; MBD0221436.1; -; Genomic_DNA. DR EMBL; JARTMM010000048; MDK4882510.1; -; Genomic_DNA. DR EMBL; WIOC01000023; MQR50747.1; -; Genomic_DNA. DR EMBL; WPIP01000038; MVM91291.1; -; Genomic_DNA. DR EMBL; WWCH01000001; MYM77633.1; -; Genomic_DNA. DR EMBL; LYKI01000067; OIG67468.1; -; Genomic_DNA. DR EMBL; NGEL01000030; OTM92370.1; -; Genomic_DNA. DR EMBL; QKWF01000059; PZM17994.1; -; Genomic_DNA. DR EMBL; CP042556; QFH47199.1; -; Genomic_DNA. DR EMBL; CP061521; QNV31131.1; -; Genomic_DNA. DR EMBL; CP059300; QOJ62109.1; -; Genomic_DNA. DR EMBL; CP062919; QPF15068.1; -; Genomic_DNA. DR EMBL; UFDJ01000034; SSI70680.1; -; Genomic_DNA. DR EMBL; CP110462; UZG64037.1; -; Genomic_DNA. DR RefSeq; WP_000199457.1; NZ_WYAO01000019.1. DR STRING; 1096995.BJAB07104_01324; -. DR KEGG; abw:BL01_15570; -. DR PATRIC; fig|470.1288.peg.2973; -. DR eggNOG; COG0013; Bacteria. DR OrthoDB; 9803884at2; -. DR Proteomes; UP000066661; Chromosome I. DR Proteomes; UP000072389; Chromosome. DR Proteomes; UP000179937; Unassembled WGS sequence. DR Proteomes; UP000194699; Unassembled WGS sequence. DR Proteomes; UP000248662; Unassembled WGS sequence. DR Proteomes; UP000262697; Unassembled WGS sequence. DR Proteomes; UP000326440; Unassembled WGS sequence. DR Proteomes; UP000327158; Chromosome. DR Proteomes; UP000439424; Unassembled WGS sequence. DR Proteomes; UP000461234; Unassembled WGS sequence. DR Proteomes; UP000480763; Unassembled WGS sequence. DR Proteomes; UP000516431; Chromosome. DR Proteomes; UP000593752; Chromosome. DR Proteomes; UP000594659; Chromosome. DR Proteomes; UP000634608; Unassembled WGS sequence. DR Proteomes; UP001156386; 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 CDD; cd00673; AlaRS_core; 1. DR Gene3D; 2.40.30.130; -; 1. DR Gene3D; 3.10.310.40; -; 1. DR Gene3D; 3.30.54.20; -; 1. DR Gene3D; 6.10.250.550; -; 1. DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. 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; IPR050058; Ala-tRNA_ligase. 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 NCBIfam; TIGR00344; alaS; 1. DR PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1. DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1. 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; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1. DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00036}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00036}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00036}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00036}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00036}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00036}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00036}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00036}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00036}. FT DOMAIN 1..713 FT /note="Alanyl-transfer RNA synthetases family profile" FT /evidence="ECO:0000259|PROSITE:PS50860" FT COILED 344..386 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 736..763 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 562 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT BINDING 566 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT BINDING 670 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT BINDING 674 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="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 //