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Database: UniProt
Entry: A0A1V6QTI0_9EURO
LinkDB: A0A1V6QTI0_9EURO
Original site: A0A1V6QTI0_9EURO 
ID   A0A1V6QTI0_9EURO        Unreviewed;       266 AA.
AC   A0A1V6QTI0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Alanyl-transfer RNA synthetases family profile domain-containing protein {ECO:0000259|PROSITE:PS50860};
GN   ORFNames=PENSOL_c043G05082 {ECO:0000313|EMBL:OQD92236.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD92236.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OQD92236.1}.
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DR   EMBL; MDYO01000043; OQD92236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QTI0; -.
DR   STRING; 60172.A0A1V6QTI0; -.
DR   OrthoDB; 5490212at2759; -.
DR   Proteomes; UP000191612; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.30.130; -; 1.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR   PANTHER; PTHR43462:SF2; THREONYL AND ALANYL TRNA SYNTHETASE SECOND ADDITIONAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   SMART; SM00863; tRNA_SAD; 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   Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT   DOMAIN          1..266
FT                   /note="Alanyl-transfer RNA synthetases family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50860"
SQ   SEQUENCE   266 AA;  29367 MW;  F9BF6B342F580B51 CRC64;
     MTSPRTILVF QHDASLHILE TTVTAIIPFN DLEESSRVFF KDASEEYHVI VTEKTIFHPQ
     GGGQPSDTGV LKGLSGTFTV TAVRTDANGQ VLHLGLFENS SSAFKKGETV QQAIDVGKRL
     LYSRLHTAGH VLGASVRHLL EKEIENFDEL KASHFPDSAA CEFQGSIDGK WKDSIQNKLD
     TYVAAKMPVQ IEWWDEEDFR SRGLERLIPD RSLVPAGEKS RVVNIVGAEV YPCGGTHVDT
     TDLCGPVTVK KISRKQGNSR VSYVVK
//
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