ID   A0A2N1LWD5_TRIHA        Unreviewed;       954 AA.
AC   A0A2N1LWD5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   11-DEC-2019, entry version 9.
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       {ECO:0000256|HAMAP-Rule:MF_03133}.
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}.
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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   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
FT                   /note="AA_TRNA_LIGASE_II_ALA"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
FT   REGION          915..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          430..450
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          754..774
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   METAL           598
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT   METAL           602
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT   METAL           717
FT                   /note="Zinc"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT   METAL           721
FT                   /note="Zinc"
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
//