ID G8BZK6_TETPH Unreviewed; 557 AA.
AC G8BZK6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033155};
GN Name=TPHA0K02010 {ECO:0000313|EMBL:CCE65334.1};
GN OrderedLocusNames=TPHA_0K02010 {ECO:0000313|EMBL:CCE65334.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65334.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE65334.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000225};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000256|ARBA:ARBA00005312}.
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DR EMBL; HE612866; CCE65334.1; -; Genomic_DNA.
DR RefSeq; XP_003687768.1; XM_003687720.1.
DR AlphaFoldDB; G8BZK6; -.
DR STRING; 1071381.G8BZK6; -.
DR GeneID; 11533402; -.
DR KEGG; tpf:TPHA_0K02010; -.
DR eggNOG; KOG0556; Eukaryota.
DR HOGENOM; CLU_004553_2_1_1; -.
DR OMA; WVHEIRD; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000005666; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04320; AspRS_cyto_N; 1.
DR CDD; cd00776; AsxRS_core; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT DOMAIN 246..549
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 63728 MW; CB624807C8427F21 CRC64;
MSEQAATATE VPKEEQPVVL GEDGQPLSKK ALKKLQKEQE KQKKKEETAR RLQLEKEQRE
KDEASAPDSA AANYGKLPLV QSLPSARTNE SRIKFEDLTE DMNDKEVLFR ARVHNTRQQG
ATLAFLTLRQ QSQLIQALLR VNKEGSVSKK MTKWAGSLHL ESIVLVRGVV KKVDEPIKSA
TVQNLEVHVT QIHIISETPE NLPILLEDAS RSEEEAERAG LPVVNLDTRL DARVIDLRTA
TNQAIFKIQS GVCQLFREFL YQKKFMEVHS PKLLGAPSEG GASVFEVAYF KDTKAYLAQS
PQFHKQQLMV ADFERVFEIA PVFRAENSNT HRHMTEFTGL DLEMTFEENY HEVLDTLSEL
FVFIFIELNK RYKKEIDVVR KQYPVEEFKL PKDGKMIKLT FKEGIEMLRA SGKTEVGDYD
DLSTENEKLL GKLVREKYDT DFYILDKFPL AVRPFYTMPD PEDPNYSNSY DFFMRGEEIM
SGAQRIHDYD LLLTRLKAHG LSPEDPGLKD YVDAFSYGCA PHAGGGIGLE RVLMFFLDLK
NIRRASLFPR DPKRLRP
//
