ID   U4LGI2_PYROM            Unreviewed;       839 AA.
AC   U4LGI2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=PCON_09829 {ECO:0000313|EMBL:CCX31013.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX31013.1};
RN   [1] {ECO:0000313|EMBL:CCX31013.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX31013.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX31013.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; HF935526; CCX31013.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4LGI2; -.
DR   STRING; 1076935.U4LGI2; -.
DR   eggNOG; KOG2007; Eukaryota.
DR   OMA; YEGLGWA; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000018144; 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   CDD; cd00672; CysRS_core; 1.
DR   Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCX31013.1};
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          89..547
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          44..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..782
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  94217 MW;  22862678986D1C1E CRC64;
     MPLPRILASA ATTALRTAIP TTRSLGPTVL FTQRHQTLRH CSSGNMATAQ RREQPPWTRP
     ESSAPLPPLS IYNTLTRQKD PFVPLDKSGK KVTWYCCGPT VYDAAHLGHA RNYVTTDIVR
     RIMRDYFGFN ITFVQNVTDV DDKIILRARQ QHLFEEYKAA NPKITPEVLS ATEKAWTAYF
     TKIAKADEGD LTTVPSTFEA WATRKHEPLM ALIHKELAGE SVEGELLDED ASKLKMHLNT
     LFMASKALQT PPTSAEEFYG TCSSVLLPYI DSLNKDRTYE PAVFSKLSRY WENHFNEDMA
     TLNVLPPTTV TRVSEFIPEN VAFVQKLVDR GYAYPTADGS VYFDIAAYEA AGHHYAKLQP
     WNRGDQSLIA DGEGALTSDK ASTLPTSDSS LPAKKKADQD FALWKASKAG EPSWESPWGQ
     GRPGWHIECS VMCSEVLGGE IDIHSGGIDL AFPHHDNEIA QSEAYWDGCA SHATADGRHQ
     WINYFLHMGH LKIHGSKMSK SLKNFVSVRK ALERGGGWTP RMLRIVFLQG GWKDGIEVRE
     GVLSAAKSWE TAVNKFFTNV KALVTEETAA QAAGTHIPQP WTKLEADLSK ELDSTREKLD
     AALCDSFNTP LAMQLLVDLI STTNIYMSST TNLALVKEIA RWITRITTIF GLDNNSSPDR
     IGWTSEESST GNAEEIAMPY LRLLSSFRDS VRALGISDSK SDSAKELLRL CDKLRDIDLA
     DLGVSLDDRD SANALIKFVP AEELRAAREE KERKAAEREQ KKEEARLKRE EEERKKQEQA
     KVDPVTMFRT EEWSEWDEQG IPTKDKEGEE ITKSRKKALT KAWEQQKKKF EAYQKTVQK
//