ID A0AAD9GFV1_BABDI Unreviewed; 983 AA. AC A0AAD9GFV1; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 02-OCT-2024, entry version 3. DE RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_03133}; DE EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_03133}; DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_03133}; DE Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_03133}; GN ORFNames=X943_003921 {ECO:0000313|EMBL:KAK1937692.1}; OS Babesia divergens. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida; OC Babesiidae; Babesia. OX NCBI_TaxID=32595 {ECO:0000313|EMBL:KAK1937692.1, ECO:0000313|Proteomes:UP001195914}; RN [1] {ECO:0000313|EMBL:KAK1937692.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1802A {ECO:0000313|EMBL:KAK1937692.1}; RX PubMed=24799432; DOI=10.1093/nar/gku322; RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E., RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L., RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid A.J., Sanders M., RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N., RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R., RA Pain A.; RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a RT history of genomic innovation underlying host-parasite interaction."; RL Nucleic Acids Res. 42:7113-7131(2014). RN [2] {ECO:0000313|EMBL:KAK1937692.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1802A {ECO:0000313|EMBL:KAK1937692.1}; RA Pain A.; RL Submitted (MAY-2021) 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 tRNA(Ala) via its editing domain. CC {ECO:0000256|HAMAP-Rule:MF_03133}. 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_03133}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03133}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03133}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03133}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03133}. CC Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03133}. 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_03133}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Alax-L subfamily. {ECO:0000256|ARBA:ARBA00008429}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAK1937692.1}. 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; JAHBMH010000033; KAK1937692.1; -; Genomic_DNA. DR Proteomes; UP001195914; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:TreeGrafter. 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:0070143; P:mitochondrial alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00673; AlaRS_core; 1. DR Gene3D; 2.40.30.130; -; 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; 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; 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_03133}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_03133}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03133}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03133}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03133}; KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03133}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_03133}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_03133}; Reference proteome {ECO:0000313|Proteomes:UP001195914}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_03133}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_03133}; Zinc {ECO:0000256|HAMAP-Rule:MF_03133}. FT DOMAIN 23..775 FT /note="Alanyl-transfer RNA synthetases family profile" FT /evidence="ECO:0000259|PROSITE:PS50860" FT BINDING 626 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133" FT BINDING 630 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133" FT BINDING 738 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133" FT BINDING 742 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133" SQ SEQUENCE 983 AA; 108589 MW; E3306A0FF1DA3C46 CRC64; MASSRSDLNA TGKAMNDLGF EVNSSAWVRS EFIRYFESKG HVFWRSSPVL PHNDATLLFA NAGMNQFKDI IVGKADSTTE YGRLKRVCNS QKCIRAGGKH NDLDDVGKDS YHHTFFEMLG NWSFGDYFKK EAIDFAWELL TEVYKLDKSR LYVTYYGGDP KLPACKPDDE AHELWLRYLP PERVLPFGMK DNFWEMADTG PCGPCSEIHY DHIGGRDAAA LVNADDPMVV ELWNLVFMQY NRKASGDVEL LPKPCVDTGM GLERVAAVLK NSNSNYECDL FTDIFAYINK LMPQLPPYGG SDSIVDIAYR VVADHTRCLT VAIADGVEPS NDGRGYVLRR ILRRAVRYGK EHLGSTGPFL SKLVDCVVAS LGAAFPEIQN QNDKIAATIH NEELLFLETL DKGCDRFRKM VAKLQSTSQG GNPPVVSGSD AFLLYSSFGF PLDLTQLMAR EMGLDVDIEG FNEHFKRHQL LSEKKQVKSD DPVEQGLHDV VESLSADVLA TISAAIGNKS TDDSLKYHGI DVAYACDTEF DVEVLAVWSS DGLNKSPKDG EVVAVVLDKT PFYAEQGGQI WDEGLLGPLK VLKILKMGGM VFHFCVYESG RNCIKPGSTV KAKVDYERRV KVACNHTGTH LLNFVLREIY DEQSYQRGSQ LDAEKLKFDI AANKPLTDDV LQKIESRIQT IIDEDWKLEV KEVPFKDAIK IPGIRANFTD VYPEFVRVVC ITKNGQAVDG HANSIEVCGG THVPSTGVLK SVIMVGEEGI SKGIRRLTLA TNEQSENSKA ILASYENSLS ELEGKLFKFT DDMDTALMAQ QANENMRLLT ALRFQMQNEK LLPLLGKRNL KARFDALINA QIDAGKVHQK KLGAIAKNLS TDYVNKFKSG DFCGLKTSRE GVDLIHMEAN ALEGDAKSLN VLTQTIAKAF PKLALLLTSS NKDGSAVSCR CVVPAGSALD ALSLANEAAA NLGHQSDVAR GSRTNASWSV DSQ //