ID A0A024GCV3_9STRA Unreviewed; 973 AA.
AC A0A024GCV3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Aminoacyl-transfer RNA synthetases class-II family profile domain-containing protein {ECO:0000259|PROSITE:PS50862};
GN ORFNames=BN9_049460 {ECO:0000313|EMBL:CCI44162.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI44162.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI44162.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI44162.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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:CCI44162.1}.
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DR EMBL; CAIX01000063; CCI44162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GCV3; -.
DR STRING; 65357.A0A024GCV3; -.
DR InParanoid; A0A024GCV3; -.
DR OrthoDB; 1046261at2759; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd02035; ArsA; 1.
DR CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR025723; Anion-transp_ATPase-like_dom.
DR InterPro; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR016300; ATPase_ArsA/GET3.
DR InterPro; IPR018793; Cyt_c_oxidase_assmbl_Pet191.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00459; aspS_bact; 1.
DR NCBIfam; TIGR00345; GET3_arsA_TRC40; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02374; ArsA_ATPase; 1.
DR Pfam; PF10203; Pet191_N; 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; SSF55261; GAD domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 485..940
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 973 AA; 110292 MW; 61A081A56E6D195E CRC64;
MEREKVLIVS TDPAHNLSDA FGQKFTREPT LVHGFSNLFV MEIDPTVDLE EMNPDGLQET
SGMASFMKDL TNSIPGIDEA MSFAELMKQV QTMDFSIIVF DTAPTGHTLR LLSFPTALNK
AFDKILSLKN QFSGMFSQVS ALLGGALPSQ EHLLGKLEQT QEIIQKVNQQ FKDPERTTFV
CVCIPEFLSL YETERLVQEL TKYEIDVHNI VVNQVLYRES GSTCSNCTAR QKMQQKYIDQ
IYDLYEDFHV VEMPLLNEEM GKSCHDMALA LRDCMIQQEC MNTGERTLKE CLHERQYANE
CHAYRVAYFE CKRGQLDMRT RCSNAAVEHD NHSTKFSSYR TRTCGELRNA NQHLNQYVRL
CGWVHGIREL GSITFLSLRD RYGITQLVVD KDSTAAHAAS NLRLESIVRV AGSVRQRPDK
MKNSSMSTGD IEVIVESIEE VSHIDHGKSF PIRLEAPADN ANDETRLRYR YLDLRRPQLQ
KNILLRSKIT FEARKFLHDL DFAEIETPTL FKSTPEGARE FIVPTRTPGM FYALTQSPQQ
YKQLLMVGGM DRYFQIARCY RDENGRADRQ PEFTQLDLEM SFVTQDDIMQ LMELLVRHLW
ATAGQTLCSE PFHRISYAEA IRRFGIDKPD TRYGLELHDL TDLMRDSVLL ETPCEKSSNG
VVARGLNAKG LAASTPKGFS RKHMDAFMQV AHAYSIEKEA VKFALVKIEG ERKEWKSYFT
AKVSPEARAA INERLSVEEG DVLLVAIGTY ASTSKLLGRM RIHAANVLRA NGLLEEEMSA
NRYNMLWVTD FPLFSVEEGT LLCGQKKQSI CSTHHPFTAP LEDEISVLAD LSAKIQNRKE
WKKDPNLLSS VLSLRAQHMD LVCNGWELGG GSIRLHSTVL QRAVFESILQ LSPSQRESFA
HLLEAFSYGA PPHGGIALGL DRLMTILCGA KSLREVIAFP KSATGKELMT CAPGLVENTQ
LREYHLSRIN HKC
//
