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Database: UniProt
Entry: A0A091MBT3_CARIC
LinkDB: A0A091MBT3_CARIC
Original site: A0A091MBT3_CARIC 
ID   A0A091MBT3_CARIC        Unreviewed;       343 AA.
AC   A0A091MBT3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=tRNA synthetases class I catalytic domain-containing protein {ECO:0000259|Pfam:PF01406};
DE   Flags: Fragment;
GN   ORFNames=N322_04492 {ECO:0000313|EMBL:KFP68207.1};
OS   Cariama cristata (Red-legged seriema).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX   NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP68207.1, ECO:0000313|Proteomes:UP000054116};
RN   [1] {ECO:0000313|EMBL:KFP68207.1, ECO:0000313|Proteomes:UP000054116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP68207.1};
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; KK526178; KFP68207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091MBT3; -.
DR   Proteomes; UP000054116; Unassembled WGS sequence.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
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; 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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          7..234
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP68207.1"
FT   NON_TER         343
FT                   /evidence="ECO:0000313|EMBL:KFP68207.1"
SQ   SEQUENCE   343 AA;  38739 MW;  72B001CCB590C046 CRC64;
     QMNISPVALA RIYEEDFKQD MAALKVLPPT VYMRVTDNIP QIISFIKTII ASGQAYATPQ
     GNVYFDVKSW GDRYGVLTTI YPDTQDEPVD TDKRHGKDFA LWKAAKPQEL SWTSPWGKGR
     PGWHIECSTI SSAVFGKQLD IHTGGIDLAF PHHENEIAQC EVYHQCEQWG NYFLHSGHLH
     VKGSQEKMSK SLKNYITIKD FLKKFSSDQF RMFCLRSRYS SAVEFSDESM DDAKHLVQAI
     SSFIRDGNAY IKGQLVCDPV REDILWERLA NTKVTVKAAF ADDFDTSRAV AAIMDLIHHG
     NRQLKAVTKD TGSPRSSVVY GSIISYIEGF FNALGMSFGE RQV
//
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