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Database: UniProt
Entry: A0A3P9QJF1_POERE
LinkDB: A0A3P9QJF1_POERE
Original site: A0A3P9QJF1_POERE 
ID   A0A3P9QJF1_POERE        Unreviewed;       577 AA.
AC   A0A3P9QJF1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00015745, ECO:0000256|RuleBase:RU003748};
DE            EC=6.1.1.6 {ECO:0000256|ARBA:ARBA00013166, ECO:0000256|RuleBase:RU003748};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563, ECO:0000256|RuleBase:RU003748};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000034229.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000034229.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000034229.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC         tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC         COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000204,
CC         ECO:0000256|RuleBase:RU003748};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   RefSeq; XP_008403547.1; XM_008405325.1.
DR   AlphaFoldDB; A0A3P9QJF1; -.
DR   Ensembl; ENSPRET00000034610.1; ENSPREP00000034229.1; ENSPREG00000023179.1.
DR   GeneID; 103462488; -.
DR   CTD; 3735; -.
DR   GeneTree; ENSGT01030000234618; -.
DR   OrthoDB; 648039at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000023179; Expressed in head and 1 other cell type or tissue.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00775; LysRS_core; 1.
DR   CDD; cd04322; LysRS_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 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; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR034762; Lys-tRNA-ligase_II_bac/euk.
DR   InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00499; lysS_bact; 1.
DR   PANTHER; PTHR42918:SF9; LYSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PIRSF; PIRSF039101; LysRS2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
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:UP000242638}.
FT   DOMAIN          232..563
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  65705 MW;  C20B8F8C0B7D1B38 CRC64;
     MADVTAVGDE KLSKNELKRR MKAEKKAAEK ESKAKDLGEQ ADSNNADAQN ANALDDETLD
     PNQYFKIRTQ AIQELKGTAE DPYPHKYHVD LSLTDFIQKY NHLQSGDQLS DVVLAVSGRV
     HAKRASGAKL IFYDLRSEGV KLQVMANSRN YKSEEAFVAI NNKLRRGDII GVRGNPGKTK
     KGELSIIPIE ITLLSPCLHM LPHLHFGLKD KETRFRQRYL DLILNDYVRQ KFLTRAKIIT
     YLRNFLDQMG FLEIETPMMN IIPGGAVARP FVTYHNELDM NLFMRIAPEL YHKMLVVGGL
     DRVYEVGRQF RNEGIDLTHN PEFTTCEFYM AYADYHDLME ITESLLSGMV KHITGGYKVT
     YHPDGPEGQA YEIDFTPPFK RVSMTHDLEK IMGVKFPPTD SYDSDETRKF FDDLCAQKGV
     ECPPPRTTAR LLDKLVGDFL EVTCISPTFI CDHPQIMSPL AKWHRSEKGL TERFELFVMK
     KEICNAYTEL NDPIRQRELF EQQAKAKAEG DDEAMFIDET FCTALEYGLP PTAGWGMGID
     RLTMFLTDSN NIKEVLLFPA MKPDDNKKSA PSEETSS
//
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