ID   A0A0G2IE14_9EURO        Unreviewed;       806 AA.
AC   A0A0G2IE14;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, 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=EMCG_00093 {ECO:0000313|EMBL:KKZ68922.1};
OS   Emmonsia crescens UAMH 3008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ68922.1, ECO:0000313|Proteomes:UP000034164};
RN   [1] {ECO:0000313|Proteomes:UP000034164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KKZ68922.1}.
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DR   EMBL; LCZI01000001; KKZ68922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2IE14; -.
DR   VEuPathDB; FungiDB:EMCG_00093; -.
DR   Proteomes; UP000034164; 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; 2.
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   ECO:0000313|EMBL:KKZ68922.1}; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          46..479
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  90190 MW;  F4E2FC351E829F7F CRC64;
     MSTARQQPPW KQPQPHAGSA SRLPPLKIYN SLTRSKVPFV PLDPSGRKVT WYACGPTVYD
     DAHLGHARNY VSNDILRRIM RDYFKFDVKF IMNITDVDDK VGRQQHFFTE FVHSHPTVDD
     EVIKTVRSAY SAYLEKKLPL LEAGLAPEHY KDEVEKVYAT ILNGGALDGS GKPGDEEAKI
     KMHINTAASA ANALAKVSSA KESTLSEIFY NDVQDVLLEY LDSLHGSSIR GEDRSIFTKL
     TKKYEDRFMQ DVRDLNVLDP DTITRVTEYM PEIVSFVERI VKHKFGYVTS DGSVYFDITA
     FEASGNSYAR LEPWNRNDTK LLAEGEGALT KKTTEKRSAA DFALWKASKA GEPSWPSPWG
     DGRPGWHIEC SAMASAKLGK QMDIHSGGID LAFPHHDNEL AQSEAYWHET CAHDHWVNYF
     LHMGHLSIQG SKMSKSLKNF TTIREALDKG DWTPRSLRIV FLLGGWKDGI EITEDLVKAG
     SAWEEKANNF FIKTKDAVAQ PDVAPGLTDD TLAVALKSAQ DAVYQSLCDS FNTAGAMYAI
     SEFISKYNVA DKSTLPIKDV QEAAIWVTSM VNIFGLNGSA SPVTTEIGWS GIDIPDAAKP
     YLYPLSTMRD SLRDAARSKA GISEDTIKSV VEKGNAAIQQ TSGLSEEEAG VYKNLLSDFC
     TKISSLEQTS TTSKEILTLC DRVRDIDLFD LGIYLEDRDN QPALVRPVTR ELIQAREEKA
     ARAHQKQMEK ENKEKEALKK AEKGKISHLE LFRTNEYSAW DEDGLPTRDV AGEEITKSRS
     KKLRKDWERQ KKLHEAWAAS NKGNLS
//