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Database: UniProt
Entry: A0A0K3CMW0_RHOTO
LinkDB: A0A0K3CMW0_RHOTO
Original site: A0A0K3CMW0_RHOTO 
ID   A0A0K3CMW0_RHOTO        Unreviewed;       779 AA.
AC   A0A0K3CMW0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   Name=FGENESH: predicted gene_11.147 {ECO:0000313|EMBL:CTR09790.1};
GN   ORFNames=AAT19DRAFT_9855 {ECO:0000313|EMBL:PRQ71740.1}, BN2166_0056510
GN   {ECO:0000313|EMBL:CTR09790.1};
OS   Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR09790.1, ECO:0000313|Proteomes:UP000199069};
RN   [1] {ECO:0000313|EMBL:CTR09790.1, ECO:0000313|Proteomes:UP000199069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Single colony {ECO:0000313|EMBL:CTR09790.1};
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PRQ71740.1, ECO:0000313|Proteomes:UP000239560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ71740.1,
RC   ECO:0000313|Proteomes:UP000239560};
RX   PubMed=29521624;
RA   Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA   Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA   Arkin A.P., Skerker J.M.;
RT   "Functional genomics of lipid metabolism in the oleaginous yeast
RT   Rhodosporidium toruloides.";
RL   Elife 7:0-0(2018).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CWKI01000011; CTR09790.1; -; Genomic_DNA.
DR   EMBL; LCTV02000011; PRQ71740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K3CMW0; -.
DR   STRING; 5286.A0A0K3CMW0; -.
DR   OMA; FHNDMKS; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000199069; Unassembled WGS sequence.
DR   Proteomes; UP000239560; 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   ECO:0000313|EMBL:PRQ71740.1}; 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:UP000199069};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          23..474
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          711..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..761
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  86520 MW;  7B0EDF8400AD4526 CRC64;
     MQNSWRIPQP SAPEPKLKVD FVTKKPGIVT WYNCGPTVYD ASHMGHARNY MAQDIMRRIL
     RDYFGYEVNF VMNITDVDDK IIVRARQSHL LKKYLAELAT SSTPLSSRVL QEVSTAWTAY
     FTKAFAASLP SPVAADDFAA AEAGWAQVQD LAKDANWVEA QKTANEKFPM YFAAVEAGYT
     ALKLAQKQEA AGATGLTDAE ALIEANKDAV GLWLDKQLGA SVTDPAVFRD LAAFWEDSYF
     KSMAALHVER PTTLTRVSEY IPEIVTFVEG IVKRGFAYEG GGSVWFDTVK FEGAKGEGEG
     DDEWRHTYAK LQPWSKGNRE LLEDGEGSLT STTGKRSAAD FALWKSSKPG EPAWPSPWGP
     GRPGWHIECS VMASAVLGEG MDVHSGGVDL AFPHHDNEIA QSEAFHNCRQ WVNYFLHTGH
     LHIEGLKMSK SLKNFITIDD ALEKHTARQL RFAFLSQNWN ARLDFKESSM QEVKSAETVL
     NNFFTNVKAL ATEAKERSVA SDGQHHYEQA EKDLLAQLEQ AQLAFRTALC DSFDTPTALQ
     ILLDIVSKTN IYLARGRRQV NFAVILAVSE WVTRMLRMFG LGEGSPVDGN GDKVIGWGVA
     AAKGDEQSVD RESILMPYLR ALSGFRDQVR QLAMSGAASS DILALTDKLR DHDLVDLGVA
     LDDQEDGRAM VKLVPPEILR EARDAKAAAV REKAAKKAAA AAAAEAKRLE RLEKGRVPPT
     EMFRSNTAEY SAWDEQGLPT KDKDGNELPK SRGKKLKKEW DMQKKLHDEF LKEQEKQSA
//
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