ID E4TJX1_CALNY Unreviewed; 400 AA.
AC E4TJX1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02007};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02007};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02007};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02007};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02007};
GN OrderedLocusNames=Calni_0309 {ECO:0000313|EMBL:ADR18222.1};
OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Calditerrivibrionaceae.
OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR18222.1, ECO:0000313|Proteomes:UP000007039};
RN [1] {ECO:0000313|EMBL:ADR18222.1, ECO:0000313|Proteomes:UP000007039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1
RC {ECO:0000313|Proteomes:UP000007039};
RX PubMed=21475587; DOI=10.4056/sigs.1523807;
RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Land M.;
RT "Complete genome sequence of Calditerrivibrio nitroreducens type strain
RT (Yu37-1).";
RL Stand. Genomic Sci. 4:54-62(2011).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr). {ECO:0000256|HAMAP-
CC Rule:MF_02007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000069, ECO:0000256|HAMAP-
CC Rule:MF_02007};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02007}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02007}.
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DR EMBL; CP002347; ADR18222.1; -; Genomic_DNA.
DR RefSeq; WP_013450438.1; NC_014758.1.
DR AlphaFoldDB; E4TJX1; -.
DR STRING; 768670.Calni_0309; -.
DR KEGG; cni:Calni_0309; -.
DR eggNOG; COG0162; Bacteria.
DR HOGENOM; CLU_024003_5_0_0; -.
DR OrthoDB; 9804243at2; -.
DR Proteomes; UP000007039; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR HAMAP; MF_02007; Tyr_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02007};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02007}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02007};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02007};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02007}; Reference proteome {ECO:0000313|Proteomes:UP000007039};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 339..400
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT MOTIF 46..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT MOTIF 230..234
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
SQ SEQUENCE 400 AA; 45298 MW; 2B3C0320A70B0E9F CRC64;
MLSVEEQIRV IKRGTEEIIS EEELKQKLEY SIRNNIPLRV KAGFDPTAPD LHLGHTVLIQ
KMKHFQDLGH HVIFLIGDFT GLIGDPTGKS ETRKALTIEE VLKNAETYKE QVFKILDPAK
TEIAFNSHWM GKMTSYDMIK LASSYTVARM LERDDFAKRY SSGKPISIHE FLYPLVQGYD
SVALKSDVEL GGTDQKFNLL VGRDLQRMNG QNPQIALTVP ILEGLDGVQK MSKSLGNYVG
ITEKPTDMFG KIMSISDQLM FRYYLLLSDK SLEEVERIKN GVESGKIHPM DAKKDLAEEI
VKRFHGYVEA KRAREWFEQV FTKKEIPDDI KLFEGKSDEK LIDIIKKLGF APSNSEVRRL
ATAGAITING EKIENVDLSL GAGEFILKVG KRNFAKLKLK
//
