ID V5HT18_BYSSN Unreviewed; 953 AA.
AC V5HT18;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=aspartate--tRNA ligase {ECO:0000256|ARBA:ARBA00012841};
DE EC=6.1.1.12 {ECO:0000256|ARBA:ARBA00012841};
GN ORFNames=PVAR5_1218 {ECO:0000313|EMBL:GAD92625.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92625.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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}.
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:GAD92625.1}.
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DR EMBL; BAUL01000032; GAD92625.1; -; Genomic_DNA.
DR AlphaFoldDB; V5HT18; -.
DR eggNOG; KOG0556; Eukaryota.
DR HOGENOM; CLU_004553_1_1_1; -.
DR InParanoid; V5HT18; -.
DR OrthoDB; 382728at2759; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
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: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; IPR024320; LPG_synthase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF2; ASPARTATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09924; LPG_synthase_C; 1.
DR Pfam; PF00152; tRNA-synt_2; 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 Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:GAD92625.1};
KW Ligase {ECO:0000313|EMBL:GAD92625.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT DOMAIN 289..599
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 108785 MW; AB821C76B9FF2E13 CRC64;
MPRGLWAKMS IKRALSKLTP NNKHDDDGSG GSRSPISSPR RSIVGFLRDK DYISSSDDVS
DDSSSGVSKN QQKRLARQQR RQAKSRLSEE HRSESEHRRR EREEEVARQE SPEMKARYGD
LPLLQSRERK GEPRFVLDNV SKDIVGQEIL FTARLHIVRR MSAKLVFLVF RQQLTTFQGV
LHEKPGVTST NMVQWAERLR TGCIVRVRGT IRAPEVPVLG CTIHDVELEI QELHVIVRRE
ETVPFSVYEA EVRTEEEDRA EGRRSHIPDR TRLANRILDL RTPTSQAIFR LQSAISQLFR
EALNDRDFIE IHTPKLQGSA TESGASVFEL NYFGRPAFLA QSPQLAKQMA IASDFGRVYE
IGAVFRAENS NTHRHLTEYT GLDIEMAIDE HYHEMLDTID ATIKHIFKGF YTKYRREVDV
VKHQFPSEDL VWLDETPVIP FVDAIRMLND SGWRTEDGQM LPEDEDLSTR DEIHLGELIK
EKYNTDYYII DKFPVGARPF YTMPDPQDPR YTNSFDIFVR GQEIVSGGQR IHDAKMLEEN
IRKAGIRPDD MEDYLEGFRW GAPPHAGAGI GLERMLMLIL KLGNIRLASL FHRDPRSFPA
KPPVLLLRHP ESSTVEPVWQ KENKSTKAID DDQLQPLEHL IANYGDATST SWGDERYKIW
RDYVTGAAVS YIPINGYAII PGNPLCDPSQ YGRVINAFLG WLRRETKLKP IWLLISPQVE
DILGEKLGWR SLSCIAEERV DPARNLAASD GEISRKIRHA ENEGVKVTAL SQGEMVSEEV
RKKIDKRIQD WLGNRKGTQI HLSEIQPWRD SEHRWYFYAT DKEGNICCFV ALAMLAPQSG
MQVKYSFDFP GAPNGAIEYI VTQAIQTAAK AGVKSLTFGA GATAELRPGH HMTGAKVRML
QHTYEAIVRQ FHLTRKSEFR MKLGAHEEPL YIAYPAHGLG SKGIRAILHF FED
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