ID   A0A2N1LWD5_TRIHA        Unreviewed;       954 AA.
AC   A0A2N1LWD5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   23-MAY-2018, entry version 2.
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=.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: ATP + L-alanine + tRNA(Ala) = AMP +
CC       diphosphate + L-alanyl-tRNA(Ala). {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}.
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DR   EMBL; NQLC01000036; PKK53690.1; -; Genomic_DNA.
DR   Proteomes; UP000233603; Unassembled WGS sequence.
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
//