ID A0A3S0QNR7_STEMA Unreviewed; 882 AA. AC A0A3S0QNR7; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 19-JAN-2022, entry version 7. 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 ORFNames=EKL94_15555 {ECO:0000313|EMBL:RTQ87505.1}; OS Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas OS maltophilia). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group. OX NCBI_TaxID=40324 {ECO:0000313|EMBL:RTQ87505.1, ECO:0000313|Proteomes:UP000271705}; RN [1] {ECO:0000313|EMBL:RTQ87505.1, ECO:0000313|Proteomes:UP000271705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDMC339 {ECO:0000313|EMBL:RTQ87505.1, RC ECO:0000313|Proteomes:UP000271705}; RA Kartti S., Manni A., Chemao El Fihri M.W., Laamarti M., Temsamani L., RA El Jamali J.E., Ouadghiri M., Ibrahimi A., Filati-Maltouf A.; RL Submitted (DEC-2018) 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|ARBA:ARBA00001676, ECO:0000256|HAMAP- CC 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 -!- 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:RTQ87505.1}. 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; RXLZ01000047; RTQ87505.1; -; Genomic_DNA. DR Proteomes; UP000271705; Unassembled WGS sequence. 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 Gene3D; 3.30.930.10; -; 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; 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 SUPFAM; SSF55681; SSF55681; 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|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 7..716 FT /note="AA_TRNA_LIGASE_II_ALA" FT /evidence="ECO:0000259|PROSITE:PS50860" FT COILED 732..759 FT /evidence="ECO:0000256|SAM:Coils" FT METAL 571 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT METAL 575 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT METAL 673 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT METAL 677 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" SQ SEQUENCE 882 AA; 94943 MW; F037F347E54D84E3 CRC64; MNASAKFTTS QIRSDFLEFF KGKGHTIVPS APLVPGNDPT LLFTNSGMVQ FKDVFLGAEK RSYVRAADVQ RCLRAGGKHN DLDQVGYTAR HHTFFEMLGN WSFGDYFKKD AIAWAWELLT QVWKLPPERL LVTVYQTDDE AYELWRDMVG IPEARIVRIG DNKGAPFASD NFWQMADTGP CGPCTEIFYD HGDHIAGGPP GSPDEDGDRF IEIWNLVFMQ FDRQPDGTLV PLPAPCVDTG MGLERLAAIL QHVHTNYEID LFQALIRKAS ELTGTADLEN KSLRVIADHI RACSFLIVDG VLPSNEGRGY VLRRIIRRAL RHGWMLGVRQ PFFSKLVPTL VEQMGEAYPE LPAAVDTVTR ALQAEEERFA ETLDAGMKIF EDVAGKASNG VIPGVDAFRL YDTYGFPLDL TQDIARERDL TVDIAGFDAA MEQQRETARA AGKFGGGVTL PAELVATLSP TRFLGYDRLQ ADGLTVLALL KDGRPVQSAD AGDAVIVITN QTPFYAESGG QVGDTGVLTG NGVRLVVDDT QKFAGQFHGH VGTLSEGGLK VGDVLSGQVD GERRGATILN HSATHLLHAA LREVLGTHVQ QKGSLVAPDR LRFDFSHFQP ISAEELAVIE RKVNQQVRAN NAAEVHNMGM QEALDFGAMA LFGEKYGEHV RVLKMGDYST ELCGGTHVNR TGDIGLFKIT SEGGVSAGVR RIEAVTGQGA LDYVDAEEAR LAEAAELLGG SAADVVEKIR ALGQRQKQLE RELEAVKAKV AAGATADLSG QAVEVAGVKV LAARLEGFDA KALRDAMDRL KQQLGDAVIV LAGVQDGKAA LVAGVNGSAM GKVKAGELLS HIAGQIGGKG GGRPDLAQGG GEDGPALATA LAAVVEWVSP RL //