ID A0A087V6A4_BALRE Unreviewed; 822 AA.
AC A0A087V6A4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00039362};
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=N312_09413 {ECO:0000313|EMBL:KFO08146.1};
OS Balearica regulorum gibbericeps (East African grey crowned-crane).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO08146.1, ECO:0000313|Proteomes:UP000053309};
RN [1] {ECO:0000313|EMBL:KFO08146.1, ECO:0000313|Proteomes:UP000053309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO08146.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent ligation of cysteine to
CC tRNA(Cys). {ECO:0000256|ARBA:ARBA00037196}.
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:ARBA00036537};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17774;
CC Evidence={ECO:0000256|ARBA:ARBA00036537};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; KL481478; KFO08146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087V6A4; -.
DR Proteomes; UP000053309; 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 CDD; cd10310; GST_C_CysRS_N; 1.
DR Gene3D; 1.20.1050.130; -; 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; IPR036282; Glutathione-S-Trfase_C_sf.
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; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KFO08146.1};
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:UP000053309};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 116..526
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 730..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO08146.1"
FT NON_TER 822
FT /evidence="ECO:0000313|EMBL:KFO08146.1"
SQ SEQUENCE 822 AA; 94813 MW; 9D388EA1DD73CCFA CRC64;
ASSYSFILSI SEEEARVKAL NEYLSTRSYI QGFTFSHADV EVFRKFSGPP VDQYIHVVRW
YRHIEAIYDG SCEKNEPCKL QTSKGKRVQP PWSPPEGTKH SRLCLYNSLT RNKEIFQPQN
GKKVLWYCCG PTVYDASHMG HARSYISFDI LRRILRDYFK YDIFYCMNIT DIDDKIIKRA
RQNYLFERYK ENKSAPTQLL EDVKTASELF SVKLNETTDP DKKQMLERIQ NAVRSAFDPL
QEAVQAKLPA EEINRCHEIL LEEAKDLLSD WLDTKFGSQV TDNSIFSKLP KFWEGEFHKD
MEALNVLPPD VLTRVSEYVP EIVDFVKKIV DNGYGYVSNG SVYFDTMKFD CSEKHSYAKL
VPEAVGDQKA LQEGEGDLSI SADRLSEKHS PNDFALWKSS KPGEPSWDSP WGKGRPGWHI
ECSAMAGSIL GESMDIHGGG FDLRFPHHDN ELAQSEAYFE NDHWVRYFLH TGHLTIAGCK
MSKSLKNFIT IKDALKKHTA RQLRLAFLMH SWKDTLDYSN NTMESAIQYE KFMNEFFLNV
KDILRAPTDV TGQFQKWENQ EAELNKNFYD KKAAIHEALC DNIDTRSVLE EMRSLISQSN
SYIAAKKSSR QMPNRLLLEN ISSYLTQMLK IFGAIESDDA IGFPVGGNSQ NINIESTVMP
YLQVLSEFRE GVRQIAREKK VTEVLQLSDA LRDDVLPELG VRFEDHEGLP TVVKLVDKDT
LLKEREEKKK IEEEKKRKKE EAARKKQEQE AAKLAKMKIP PHELFKSECD KYSMFDENGF
PTHDTEGKEL SKGQIKKLKK LYETQEKLYK EYLQMVQNGS AN
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