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Database: UniProt
Entry: A0A1F5LTH2_9EURO
LinkDB: A0A1F5LTH2_9EURO
Original site: A0A1F5LTH2_9EURO 
ID   A0A1F5LTH2_9EURO        Unreviewed;       958 AA.
AC   A0A1F5LTH2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=PENARI_c003G02817 {ECO:0000313|EMBL:OGE56488.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE56488.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE56488.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE56488.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT   high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
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|ARBA:ARBA00008226, 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:OGE56488.1}.
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DR   EMBL; LXJU01000003; OGE56488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5LTH2; -.
DR   STRING; 1835702.A0A1F5LTH2; -.
DR   OrthoDB; 3639120at2759; -.
DR   Proteomes; UP000177622; 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   NCBIfam; TIGR00344; alaS; 1.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000177622};
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          8..763
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
FT   BINDING         601
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT   BINDING         605
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT   BINDING         720
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
FT   BINDING         724
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03133"
SQ   SEQUENCE   958 AA;  106493 MW;  F06E86E03CEABC82 CRC64;
     MTSVGSEWTA LRVRETFLDY FKQNGHTFVP SSPVAPLSDP TLLFTNAGMN QFKSIFLGTV
     DPSSDFGKLK RAANSQKCLR AGGKHNDLDD VGKDSYHHTF FEMLGNWSFG DYFKKEAITY
     SWTLLTKVYG LNPDRLYVTY FEGNEAGGLE PDLEAKELWK SVGVPESHIL PGDMKDNFWE
     MGDQGPCGPC SEVHYDRIGG RNAAHLVNQD DPNVLEIWNN VFIQYNREPD SSLRSLPNKH
     VDTGMGFERL VSILQDKSSN YDTDVFTPIF QAIQTVTGAR EYRGNFGADD ADGIDTAYRV
     VADHVRTLMF AISDGVIPNN EGRGYVIRRV LRRGARYARK YFQVDIGNFF AKLVPTVVDQ
     LGDMFPELKR KQQDVIEILD EEELSFAKTL DRGERQFEQY AQQAKVKGTD KLHGADVWRL
     YDTFGFPVDL TRIMAEERGL RIDDVEFEEA RLKAKEASKG QKKAAETTVK LDVHDLGKLE
     KMNDVQKTDD SAKFGRGNIT AHVKAIYHAK RFYDNTDNVP DGAQLGVILD CTNFYAEQGG
     QENDTGKIII DGQAELEVGD VQSYAGYVLH TGFMKYGSFA VGDSVICEYD ELRRWPIRNN
     HTGTHILNFA LKVILGDGVD QKGSLVAAEK LRFDFSHKSA ISDAELEKIE AKATEYIRQN
     CSVYSKDIPL ATAQEISGVR AVFGETYPDP VRVVSVGVEL EEILQNVKDP RWQEVSIEFC
     GGTHVQKTGD IKDLIILEES GIAKGIRRII AVTGEEAHEV QRVAQDFGKR LDRLNALPLG
     SEKEQEAKQV QVDLNQLSIS AVEKAKFRER FAKINKQVLD GQKAQQKLES KKAVDTITSY
     FEAPENKDKS WLVIQLPISA NAKAVSESLN HVKSKLQGKS VYLLAADSEQ GRVSHGCYIS
     QDLSTQGASA SDWAAVVSGA VGGKAGGKGP TSIGNGTNSD KVEEAIALAS DYLSKFKL
//
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