GenomeNet

Database: UniProt
Entry: A0A1Y2EZK4_9BASI
LinkDB: A0A1Y2EZK4_9BASI
Original site: A0A1Y2EZK4_9BASI 
ID   A0A1Y2EZK4_9BASI        Unreviewed;       788 AA.
AC   A0A1Y2EZK4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=BCR35DRAFT_267332 {ECO:0000313|EMBL:ORY76907.1};
OS   Leucosporidium creatinivorum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX   NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY76907.1, ECO:0000313|Proteomes:UP000193467};
RN   [1] {ECO:0000313|EMBL:ORY76907.1, ECO:0000313|Proteomes:UP000193467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=62-1032 {ECO:0000313|EMBL:ORY76907.1,
RC   ECO:0000313|Proteomes:UP000193467};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY76907.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MCGR01000033; ORY76907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2EZK4; -.
DR   STRING; 106004.A0A1Y2EZK4; -.
DR   InParanoid; A0A1Y2EZK4; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000193467; 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; 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   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:ORY76907.1}; 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   Reference proteome {ECO:0000313|Proteomes:UP000193467};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          35..487
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          727..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..771
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  87548 MW;  8FE7CCC533D5486B CRC64;
     MASTQDASRS KATQDSWILP TRTVEEPKLK VDFVTKKPGV VTWYNCGPTV YDASHMGHAR
     NYMAQDIMRR ILRDYFGYEV HFVMNITDVD DKIILRARQS HLLDKYTADV TSSSTPLSPT
     FLAEVQAAWS AYVFKTMKDS LAAPTSDDYA AAKLAWEEIL TSEKDLKWVE AQKAKEEKFG
     MYLSAVRAGL VGLVEAEKAA KEGRIGVEEA KALITANHDA ISLWLDKKLG STVNDPTIFR
     DLAAYWEDSY FKSMAALHVE RPTTLTRVSE YLPEIVTFVE GIVNRGLAYE AGGSVWFDTT
     KFEGAKGEES KDGDDGWKHT YAKLQPWSKG NRELLEDGEG SLTSTTGKRS ASDFALWKAS
     KPGEPEWPST WGPGRPGWHI ECSVMASAVL GEGMDVHSGG VDLAFPHHDN EIAQSEAFHN
     CRQWVNYFLH TGHLHIEGLK MSKSLKNFVT IDDALLKYSA RQLRFSFLLQ TWNAKLDFKE
     SAMQEVRAAE TLLNNFFAIV NALAAEAKAD SVASDGQHHF NQPELDLLDK LEQAQLAFRV
     ALCDSFDTPK GLQIILDLVS ATNVYLARGR AEVNISSVVA VADWVTRMLR MFGLGEGAPT
     NVRGERLIGW GTAAAPGQEG AGDRQEILMP YLRALSAFRD SVRKLAMEGA PASEILALSD
     QFRDYDAVEL GIALDDQADG RALFKLMPPE SLRQARDAKL AAANEKAARK AATAAAAEVK
     RLERLEKGRT PPTELFRSSP EYSAWDEQGI PTLDKEGVEV PKSRKKKCQK EWDAQKKLHD
     EFLKESSK
//
DBGET integrated database retrieval system