ID A0A2N1LWD5_TRIHA Unreviewed; 954 AA. AC A0A2N1LWD5; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 22-FEB-2023, entry version 18. 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; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; 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., Pappas G.J.Jr., RA Ulhoa C.J., Noronha E.F.; RT "Identification of mycoparasitism-related genes against the phytopathogen RT Sclerotinia sclerotiorum through transcriptome and expression profile RT analysis in Trichoderma harzianum."; RL BMC Genomics 15:204-204(2014). 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: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 AlphaFoldDB; A0A2N1LWD5; -. 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 CDD; cd00673; AlaRS_core; 1. DR Gene3D; 2.40.30.130; -; 1. DR Gene3D; 3.10.310.40; -; 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 PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1. DR PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1. 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; 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 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_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}; 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 5..760 FT /note="Alanyl-transfer RNA synthetases family profile" FT /evidence="ECO:0000259|PROSITE:PS50860" FT REGION 915..940 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 598 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133" FT BINDING 602 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133" FT BINDING 717 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03133" FT BINDING 721 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="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 //