ID G7KHW7_MEDTR Unreviewed; 578 AA.
AC G7KHW7; A0A0C3VXQ1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 2.
DT 24-JAN-2024, entry version 64.
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 OrderedLocusNames=MTR_6g072080 {ECO:0000313|EMBL:AES76149.2};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES76149.2, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES76149.2, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES76149.2}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES76149,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:AES76149.2, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:AES76149.2}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES76149,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:AES76149}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES76149};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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DR EMBL; CM001222; AES76149.2; -; Genomic_DNA.
DR RefSeq; XP_003619931.2; XM_003619883.2.
DR AlphaFoldDB; G7KHW7; -.
DR STRING; 3880.G7KHW7; -.
DR PaxDb; 3880-AES76149; -.
DR EnsemblPlants; AES76149; AES76149; MTR_6g072080.
DR Gramene; AES76149; AES76149; MTR_6g072080.
DR eggNOG; KOG2007; Eukaryota.
DR HOGENOM; CLU_013528_0_1_1; -.
DR Proteomes; UP000002051; Chromosome 6.
DR ExpressionAtlas; G7KHW7; differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
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:SF26; CYSTEINE--TRNA LIGASE 1, CYTOPLASMIC-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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002051};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 64..357
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 382..409
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 65907 MW; EB557E698E4D820E CRC64;
MESFLSKIDK PQPFGTSGAN NGGKGSETPG NGVVKQNNVK PKRKKKRVES LQLYNSKNNE
MEVFEPEVKG KVSMYVCGVT SYDYSHLGHA RAAISFDILV RYLKHLKYEV TYVRNFTDII
IIYLFIYFFE EAKLIIKRAN EKGVDPLELS RHFCDEYNVD MSDLLCERPT KEPRVSDHID
QIKDMITKII NNDFAYEVDG DVFYSVEKFP NYGALSGQRK RHPADFALWK AAKPGEPSWD
SPWGPGRPGW HIECSAMSAC YLSHKFDIHG GGIDLIFPHH ENEIAQNRAA DKESRIKYWL
HNGHVTNNNE KMSKSLGNFF TVREITERYH PLALRHFLIS AHYRAPLNYS IAQLETSSDA
IYYIFQTLED CRDALSSFLQ EDSEKKDQIN AAEKCINKLK EEFQTEMNDD LQTHVILKGA
LLEALKFMNR SLQFKQSLLK VEQEVREVLK VLGLLSSLSY AEVLQQLKDK ALKRAGLTEK
EVLKLIEERK QARINKDFAK SDNIRTDLTA KGIALEDVDN EMIWRPCIPS KPLVAQAVST
DNKVPEVEEK LSTLAVSQKV EEIPADREGK GSHASSST
//