ID A0A3D1NBV6_9DELT Unreviewed; 878 AA. AC A0A3D1NBV6; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 11-DEC-2019, entry version 6. 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, ECO:0000313|Proteomes:UP000263277}; RN [1] {ECO:0000313|EMBL:HCF04642.1, ECO:0000313|Proteomes:UP000263277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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 ECO:0000256|SAAS:SAAS00015829}. 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 ECO:0000256|SAAS:SAAS01125460}; 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 ECO:0000256|SAAS:SAAS00832879}. 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|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00575517}. 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: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 Proteomes; UP000263277; 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 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, ECO:0000256|SAAS:SAAS00299154}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00249928, KW 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 FT /note="AA_TRNA_LIGASE_II_ALA" FT /evidence="ECO:0000259|PROSITE:PS50860" FT COILED 736..763 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 778..798 FT /evidence="ECO:0000256|SAM:Coils" FT METAL 568 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT METAL 572 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT METAL 670 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00036" FT METAL 674 FT /note="Zinc" FT /evidence="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 //