GenomeNet

Database: UniProt
Entry: A0A194RF85_PAPMA
LinkDB: A0A194RF85_PAPMA
Original site: A0A194RF85_PAPMA 
ID   A0A194RF85_PAPMA        Unreviewed;       509 AA.
AC   A0A194RF85;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=RR48_06069 {ECO:0000313|EMBL:KPJ16114.1};
OS   Papilio machaon (Old World swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ16114.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ16114.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ16114.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ16114.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
CC   -!- FUNCTION: Mitochondrial cysteine-specific aminoacyl-tRNA synthetase
CC       that catalyzes the ATP-dependent ligation of cysteine to tRNA(Cys).
CC       {ECO:0000256|ARBA:ARBA00043868}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC         cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC         Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC         ChEBI:CHEBI:456215; EC=6.1.1.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00043713};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17775;
CC         Evidence={ECO:0000256|ARBA:ARBA00043713};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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; KQ460313; KPJ16114.1; -; Genomic_DNA.
DR   RefSeq; XP_014357050.1; XM_014501564.1.
DR   AlphaFoldDB; A0A194RF85; -.
DR   STRING; 76193.A0A194RF85; -.
DR   GeneID; 106709711; -.
DR   KEGG; pmac:106709711; -.
DR   InParanoid; A0A194RF85; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000053240; 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; 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:SF27; CYSTEINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 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:KPJ16114.1}; 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:UP000053240};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          57..343
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
SQ   SEQUENCE   509 AA;  58431 MW;  955C3E1F588BAE9F CRC64;
     MIKVLPVISR KLSHICSLKP FKETKWLMPN GNPIGVYVYN CIADQKVPVI LNDPTIATWY
     SCGPTVYDSA HIGHACCYVK LDILQRIMKS FFNIKLVTAM GITDIDDKII KKAKETNTDF
     RIVAKNFEHE FWLDLSSLNI EKPMIITRVS EYMPTIQSFV KNLIDSEMAY IASDGSVYFD
     TSKFPSYGKL QNMQDNGEPT SNEKRNKMDF ALWKGFKPGE PFWETSWGKG RPGWHIECSA
     MVSKVFGSQI DFHAGGIDLQ FPHHENEEAQ SCAFHNTTQW ANYWIHVGHL SLKDVKMSKS
     LQNTLSIPDF LKIYTSDIFR MACLMSNYRY PMEYTDEIMK TAESVLKKFK FFLNDVLLYV
     NKSDTGHGDY DKKLLNELQK VEINNLEALK NDFDTSSCIN SLLNLVAVTN KIIKADTKDH
     YPVPVILIAQ YITNILSNFG LKLQDNTEND LSNLLIDTLV DFRHIVRNNA LQRKDKELLT
     ACDMVRDKMK TMKVQINDSN KTASWVFTK
//
DBGET integrated database retrieval system