ID D1AXT7_STRM9 Unreviewed; 457 AA.
AC D1AXT7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Cysteine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00041};
DE EC=6.1.1.16 {ECO:0000256|HAMAP-Rule:MF_00041};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00041};
DE Short=CysRS {ECO:0000256|HAMAP-Rule:MF_00041};
GN Name=cysS {ECO:0000256|HAMAP-Rule:MF_00041};
GN OrderedLocusNames=Smon_0635 {ECO:0000313|EMBL:ACZ01113.1};
OS Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS 9901).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Streptobacillus.
OX NCBI_TaxID=519441 {ECO:0000313|EMBL:ACZ01113.1, ECO:0000313|Proteomes:UP000002072};
RN [1] {ECO:0000313|EMBL:ACZ01113.1, ECO:0000313|Proteomes:UP000002072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901
RC {ECO:0000313|Proteomes:UP000002072};
RX PubMed=21304670; DOI=10.4056/sigs.48727;
RA Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA Del Rio T.G., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C.,
RA Ovchinikova G., Pati A., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Streptobacillus moniliformis type strain
RT (9901T).";
RL Stand. Genomic Sci. 1:300-307(2009).
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00041};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00041};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00041};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00041}.
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DR EMBL; CP001779; ACZ01113.1; -; Genomic_DNA.
DR RefSeq; WP_012858665.1; NC_013515.1.
DR AlphaFoldDB; D1AXT7; -.
DR STRING; 519441.Smon_0635; -.
DR GeneID; 29673427; -.
DR KEGG; smf:Smon_0635; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_1_0; -.
DR OrthoDB; 9815130at2; -.
DR Proteomes; UP000002072; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; IPR015273; Cys-tRNA-synt_Ia_DALR.
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:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09190; DALR_2; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SMART; SM00840; DALR_2; 1.
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:0000256|HAMAP-Rule:MF_00041};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00041}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00041};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00041};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00041};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00041}; Reference proteome {ECO:0000313|Proteomes:UP000002072};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00041}.
FT DOMAIN 349..413
FT /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT /evidence="ECO:0000259|SMART:SM00840"
FT MOTIF 29..39
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT MOTIF 266..270
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00041"
SQ SEQUENCE 457 AA; 53145 MW; 043FFE82928F10E6 CRC64;
MKIYNSLNNK LEEFIPINDK KVGIYVCGPT VYNYIHFGNS RPVIVFDTLA RHFINQGYEV
SFVQNFTDID DKIINKSIEE NIPFEEISKK YINAFMEDIS KLNILDIVKR PKVSEYIPDI
IEMIEVLIYN GYAYERDGDV LFRVNKYLEY GKLSNQKLSD LSVGVRINKD EKKENPLDFV
LWKKKKENEP YWNAPFSEGR PGWHIECSAM SRKLLGDNFD IHAGGIDLLF PHHENERAQS
VCFCNEKSSF ANYWMHNGFL EVNGEKMSKS LGNFITLREI LNDYSGDVVR FFMLSTHYRK
PINYSIENLE ISKKTLNSII DTIDRYKQID VTNNSNNEIK KDIIEFELAI NSALNDDLNT
PLAISCIHDL IKKTNKYLNS SIFREITLVV EILEKYIINV LGIKMEKNKN DMLSESLIEL
LNKIREDARM NKNYALSDMI RDELLKLGIK TVDGKVK
//
