ID   A0A074XME1_AURPU        Unreviewed;       793 AA.
AC   A0A074XME1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   RecName: Full=cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00012832};
DE            EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN   ORFNames=M438DRAFT_373171 {ECO:0000313|EMBL:KEQ86628.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ86628.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ86628.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ86628.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; KL584978; KEQ86628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074XME1; -.
DR   STRING; 1043002.A0A074XME1; -.
DR   HOGENOM; CLU_013528_3_1_1; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000030706; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR   InterPro; IPR015803; Cys-tRNA-ligase.
DR   InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00435; cysS; 1.
DR   PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          37..462
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          751..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   793 AA;  87111 MW;  6746CF4E02A6B0F0 CRC64;
     MAAVQPPWSP PPIPNGGAAK LPKLKLWNSL TRSKVDFVPL KEGKVSWYSC GPTVYDFSHL
     GHARNYVSLD IQRRIMTHLV TDVDDKIILA ARQQHLLSDF MNKHASIDGE VLDTTNAAFK
     AYISKNLPLL PESTSEKLSA YPQEVEKAYG HVLQGKNLAN DGANPGDDEA KIKMHIKTSS
     TAADALAAPA DATGFYAKTS GVLLPYLDFQ FGSTIDGNDH ALFNVLAKKY ENYFFEDMAT
     LNVLPPTTIT RVTEYVPKIV EFVKQIQDNG FAYEHNGSVY FDIGAWEKAG GVYARLAPWS
     KADSSLVAEG EGALAAKGTE FKRSPGDFAL WKATKQKGEP LWQSPWGPGR PGWHIECSAM
     ASDILGSRMD IHSGGIDLCF PHHDGELAQS EAYHCKNPSE QDSTWVSYFL HTGHLGISGA
     KMSKSLKNFT TVRSAISEGT WTPRSLRIVF LLGNWRSSLE ITPAIVGLAS GWEDKISNFM
     LKALDTLKNP TQPAVDTETG LSPDDPLKEA LQSAKIGVED ALLDSFDTPT VMKVLSDLVT
     AYNSETGVSD ELTLEISKYI TSIVTMLGLD ANPPSHGISW SGIEVNPDVA PFVYPLAKIR
     DEVRKQAIAG TIDAPAILSH FDAAALKTPP ATKEGAEAAE ATVGWLSKLN DLIKSDAAPK
     AYMPLCDELR DTTLWNLGIY LEDRASGVAL VRPLNASLRE ERANREALAA MKLEKAKAAK
     EAKEKEEREK LEKGKLSHLE MFRTAEFSEW DEEGLPVKDK EGKEVAKSRS KKLRKDWERQ
     KKLHEAWVAA SEK
//