ID   CLA4_CLACD              Reviewed;         594 AA.
AC   A0A120HYZ1;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Lysine--tRNA ligase cla4 {ECO:0000305};
DE            EC=6.1.1.6;
DE   AltName: Full=Cladosporin biosynthesis cluster protein 4 {ECO:0000303|PubMed:26783060};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000303|PubMed:26783060};
DE            Short=LysRS {ECO:0000305};
GN   Name=cla4 {ECO:0000303|PubMed:26783060};
OS   Cladosporium cladosporioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Cladosporium.
OX   NCBI_TaxID=29917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=26783060; DOI=10.1002/anie.201509345;
RA   Cochrane R.V., Sanichar R., Lambkin G.R., Reiz B., Xu W., Tang Y.,
RA   Vederas J.C.;
RT   "Production of new cladosporin analogues by reconstitution of the
RT   polyketide synthases responsible for the biosynthesis of this antimalarial
RT   agent.";
RL   Angew. Chem. Int. Ed. 55:664-668(2016).
CC   -!- FUNCTION: Involved in self-resistance to cladosporin since this product
CC       is an inhibitor of lysyl-tRNA synthetase. Cla4 may not be inhibited by
CC       cladosporin, thereby imparting cladosporin resistance
CC       (PubMed:26783060). When cladosporin biosynthesis is switched on,
CC       transcription of cla4 will then be necessary for continued protein
CC       synthesis in C.cladosporioides (PubMed:26783060).
CC       {ECO:0000269|PubMed:26783060}.
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:0000250|UniProtKB:P15180};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P15180}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; KT037693; AMB51801.1; -; mRNA.
DR   AlphaFoldDB; A0A120HYZ1; -.
DR   SMR; A0A120HYZ1; -.
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; -; 1.
DR   Gene3D; 3.30.930.10; -; 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   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PIRSF; PIRSF039101; LysRS2; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..594
FT                   /note="Lysine--tRNA ligase cla4"
FT                   /id="PRO_0000437073"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  67601 MW;  83F8506AC921AB07 CRC64;
     MADPGAVKET VLLLDEPTGE KVSKTELKKR LKSRAKEAEK QKKAATAPTK IQKETSSEQD
     EANLSAHQYF EIRSNRINKL RETKNSYPYP HKFEVTNDLR DFLTVYKNLA KGEERTDVPI
     RIAGRIYTKR VSGNKLVFYD IRAEGVKVQV MCQAQNSTTG FEEQHEVLRR GDIVGIVGFP
     GRTSPKTRDN GELSIFATQV VLLSPCLHAL PSEHYGFQDK EQRFRQRYLD LIINDRPRQI
     FRTRAKIVSY LRSYLDSRDF TEVETPMMNA IAGGATASPF VTHHNDLKRD LFMRVAPELY
     LKMLVVGGLE RVYEIGKQFR NEGIDLTHSP EFTTCEFYQA YADYNDLMAM TEDLISSMVK
     HITGGYETTF ESQTGQVYTI NWQSPWKRID MIPALEEACG DKFPPGDQLH TPEAGTFLKE
     MLKKMKVECT PPLTNARMLD KLVGEFVEDK CINPTFVTGH PQMMSPLAKA HRDTPGICER
     FEVFVTTKEL LNAYTELNDP FDQRMRFEEQ ANQKAQGDDE AQMVDENFCQ ALEYGLPPTG
     GWGMGIDRLT MFLTNNYSIK EVLAFPMMKD DKADGEKKEA IVKTGTAEDG SVQL