ID A0A2N1LWD5_TRIHA Unreviewed; 954 AA. AC A0A2N1LWD5; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 10-APR-2019, entry version 6. 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 Name=ALA1 {ECO:0000256|HAMAP-Rule:MF_03133}; GN ORFNames=CI102_1476 {ECO:0000313|EMBL:PKK53690.1}; OS Trichoderma harzianum (Hypocrea lixii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; OC Trichoderma. OX NCBI_TaxID=5544 {ECO:0000313|EMBL:PKK53690.1, ECO:0000313|Proteomes:UP000233603}; RN [1] {ECO:0000313|EMBL:PKK53690.1, ECO:0000313|Proteomes:UP000233603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TR274 {ECO:0000313|EMBL:PKK53690.1, RC ECO:0000313|Proteomes:UP000233603}; RX PubMed=24635846; DOI=10.1186/1471-2164-15-204; RA Steindorff A.S., Ramada M.H., Coelho A.S., Miller R.N., RA Pappas G.J.Jr., Ulhoa C.J., Noronha E.F.; RT "Identification of mycoparasitism-related genes against the RT phytopathogen Sclerotinia sclerotiorum through transcriptome and RT expression profile analysis in Trichoderma harzianum."; RL BMC Genomics 15:204-204(2014). 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 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- 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_03133}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03133}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_03133}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03133}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP- CC Rule:MF_03133}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03133}. 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_03133}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000256|HAMAP-Rule:MF_03133}. 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:PKK53690.1}. 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; NQLC01000036; PKK53690.1; -; Genomic_DNA. DR Proteomes; UP000233603; 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: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 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_03133}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03133}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000233603}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03133}; KW Ligase {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|HAMAP-Rule:MF_03133}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03133}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03133}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_03133}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03133}. FT DOMAIN 5 760 AA_TRNA_LIGASE_II_ALA. FT {ECO:0000259|PROSITE:PS50860}. FT COILED 430 450 {ECO:0000256|SAM:Coils}. FT COILED 754 774 {ECO:0000256|SAM:Coils}. FT METAL 598 598 Zinc. {ECO:0000256|HAMAP-Rule:MF_03133}. FT METAL 602 602 Zinc. {ECO:0000256|HAMAP-Rule:MF_03133}. FT METAL 717 717 Zinc. {ECO:0000256|HAMAP-Rule:MF_03133}. FT METAL 721 721 Zinc. {ECO:0000256|HAMAP-Rule:MF_03133}. SQ SEQUENCE 954 AA; 106657 MW; 7E38A23AB8F963F1 CRC64; MAGNWPEAQV RKTFFDFFEQ RGHTLVPSGS VVPHNDPTLL FTNAGMNQFK PIFLGTVNKS DPMSNLKRAV DTQKVIRAGG KHNDLDDVGK DSYHHTFFEM LGNWSFGDYF KKDAIEMAWE LLTKVYGLDP TRLYVTYFEG NPALNLEPDL EAKDFWLKTG VPEDHIIPGN MKDNFWEMGD QGPCGPCSEV HYDKIGGRNA ASLVNMDDPM VVEIWNLVFM QFDRQKDGSL KPLPAKHIDT GMGFERLVSA LQDTASNYAT DVFTPLFKKI EEVTAARPYT DKYGADDVDG IDTAYRVVAD HIRTMSFAIT DGAVPNNDGR GYVIRRILRR GVRYARKYLN AEIGSFFSKI LPALVEQMGE QFPDLAKKQG DIKEILDEEE EAFSRTLDRG EAQFERYAAK AAKDGVKKLE GDVVWRLYDT FGFPVDLTKL MAEERNLDID EDEVAVAREK AREASKAVKD SVQTFAKLDV HKIAELDSGL KVARTNDDAK YLRGDSKGKV QYIFDGQAFV KTTKDIPANT AIGVLLDKTN FYAESGGQIA DTGRIVIDDV VEFKVMDVQD FGGYVLHSGY IEYGVLSADD EVICEYDELR RSPIRNNHTG THILNHSLRE VLGEDVNQKG SLVDNDKLRF DFSHKTQVKL DELKKIEELS NKYIRANSKI FSKEVDLDLA LKIEGLRAVF GETYPNPVRV VSIGMDVDTL ISDPKNAEWR KYSVEFCGGT HVDQTGLIKD LIIVEESGIA KGIRRIIAYT GEAAHQVQRE AQLFEQKLVD LEALPFGPEK EAQVKAVSQD LSQLVISTLT KDEFNQRFQK IANAVVAEQK KKQKAESKTA VDTVAKHFEA NKESQWFVGR LPISANAKAV GEVIKHYQSK DMSKSVYLFV GSPEEGAVAH GVYVGTHLSS QGVTAEHWAA SVSDVIGGRS GGKEPSRQGQ GTQPEKIDDA VETARKWLSE KLKL //