ID A0A091HB99_BUCRH Unreviewed; 490 AA.
AC A0A091HB99;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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};
DE Flags: Fragment;
GN ORFNames=N320_03755 {ECO:0000313|EMBL:KFO93131.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO93131.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO93131.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO93131.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KL532057; KFO93131.1; -; Genomic_DNA.
DR RefSeq; XP_010139893.1; XM_010141591.1.
DR AlphaFoldDB; A0A091HB99; -.
DR GeneID; 104498236; -.
DR KEGG; brhi:104498236; -.
DR CTD; 79587; -.
DR OrthoDB; 2140072at2759; -.
DR Proteomes; UP000054064; 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; 1.20.120.640; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW 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:UP000054064};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..272
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO93131.1"
FT NON_TER 490
FT /evidence="ECO:0000313|EMBL:KFO93131.1"
SQ SEQUENCE 490 AA; 55226 MW; 18822522D846EBD8 CRC64;
SYVRFDILRR IMTRFFGIEV IMVMGITDID DKIIKRANEM NISPVALALI YEEDFKQDMA
ALKVLPPTVY MRVTDNIPQI ISFIKKIIAS GQAYATSQGN VYFDVKSWGK RYGVLTTICP
DTQDEAVDTD KRHGRDFALW KAARPQELSW TSPWGKGRPG WHIECSTISS AVFGKQLDIH
TGGIDLAFPH HENEIAQCEV YHQCEQWGNY FLHSGHLHVK GSQEKMSKSL KNYVTIKDFL
KKFSSDQFRM FCLRSRYSSA VEFSDESMDD AKHHLQAISS FIRDANAYIK GQLVCDPVRE
DILWERLANT KVTVKAAFAD DFDTSRAVAA IMDLIHHGNR QLKAVTKDAA SPRSSVVYGS
IISYIEGFFN ALGMSFGERQ VALRGDSSAL LSNVIDQLVS FRAKVRHYAL ALPEADVVPM
EGAVETKGPK QEQKERRQRL MQERKPLLEA CDSLRGDLAA FGIHIKDRAA VSTWEVEEGG
PAEQLTGKKS
//
