ID A0A3D1NBV6_9DELT Unreviewed; 878 AA. AC A0A3D1NBV6; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 05-JUN-2019, entry version 5. 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=DEU72_00145 {ECO:0000313|EMBL:HCF04642.1}; OS Desulfomicrobiaceae bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfomicrobiaceae; unclassified Desulfomicrobiaceae. OX NCBI_TaxID=2053547 {ECO:0000313|EMBL:HCF04642.1}; RN [1] {ECO:0000313|EMBL:HCF04642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA12183 {ECO:0000313|EMBL:HCF04642.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:HCF04642.1}. 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; DPEO01000003; HCF04642.1; -; Genomic_DNA. 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}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036, KW ECO:0000256|SAAS:SAAS00250154}; Coiled coil {ECO:0000256|SAM:Coils}; 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:HCF04642.1}; 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 2 713 AA_TRNA_LIGASE_II_ALA. FT {ECO:0000259|PROSITE:PS50860}. FT COILED 736 763 {ECO:0000256|SAM:Coils}. FT COILED 778 798 {ECO:0000256|SAM:Coils}. FT METAL 568 568 Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}. FT METAL 572 572 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; 94304 MW; 35AA8739FD6B1056 CRC64; MLTAKDIRQK FLDFFARHGH SVEPSSSLIP QDDPTLLFTN AGMVQFKKVF LGLEKRPYSR ATTSQKCLRV GGKHNDLENV GRTARHHTFF EMLGNFSFGD YFKREAIAMA WSFVTEELGL DKDRLYITVF RDDDEAAALW QEVAGVPAER IYRLGEKDNF WAMGDTGPCG PCSEIHVDQG ADMACGPDCG IGRCDCDRFL EIWNLVFMQY ERSADGTLTP LPCPSIDTGM GLERIAAVCQ GKRSNFDSDL FQGLIGAMAA KAHVAYGAAE DTDTALRVIA DHSRAIAFLL ADGMLPSNEG RGYVLRRLIR RAFRFGRLLG FTEPFLHAAC AQVVEEMGDV YPELVAARDF LVRAVRQEEE RFGQTLDRGL ALLEEALAAL PAGGTLSGEV VFKLYDTYGF PLDIVNDVAG KSGYAVDEAG FQALMAAQKR QSKEAWAGSG DKGLAQRFAA LTAAGLESTF VGYEALSARS RVTALLDADG APCTRLAQGE TGYVVTARTP FYGESGGQVG DTGRAETVTG ALRVLDAQKP SPGLIVHKVE VVQGEVLADQ EIALTVEEGV RLATARNHTC THLLHAALRR VLGEHVTQAG SLVTPERLRF DFKHFAPLTP EEASRVEDEV NRAILADAPV CATVMAQEEA MARGAMALFG EKYGAEVRVV EVPGESMELC GGTHLQRTGQ AGCFCIVSET GIAAGVRRIE ALSGWGALRH LQAYRSEVEE VAGLLKAAPG ELGRKVTALR EEAKTLEKEV ARLRAEAAKS SCADLTPEVV AGVPLLARQV AAADMDALRE LMDDLRSRTP SGILALAADL GGKAALVVSV SKDLHGRFTA PALIKAMAAA VGGGGGGRPD LAQAGGSRPQ GIPEALETLR RIVSGEQA //