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Database: UniProt
Entry: M4RY99_9SPHN
LinkDB: M4RY99_9SPHN
Original site: M4RY99_9SPHN 
ID   M4RY99_9SPHN            Unreviewed;       409 AA.
AC   M4RY99;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02006};
DE            EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02006};
DE   AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02006};
DE            Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02006};
GN   Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02006};
GN   ORFNames=G432_03845 {ECO:0000313|EMBL:AGH48496.1};
OS   Sphingomonas sp. MM-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH48496.1, ECO:0000313|Proteomes:UP000011816};
RN   [1] {ECO:0000313|EMBL:AGH48496.1, ECO:0000313|Proteomes:UP000011816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MM-1 {ECO:0000313|EMBL:AGH48496.1};
RX   PubMed=23682148;
RA   Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT   "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT   Bacterium Sphingomonas sp. Strain MM-1.";
RL   Genome Announc. 1:E00247-13(2013).
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_02006}.
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_02006};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02006}.
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DR   EMBL; CP004036; AGH48496.1; -; Genomic_DNA.
DR   RefSeq; WP_015457511.1; NC_020561.1.
DR   AlphaFoldDB; M4RY99; -.
DR   STRING; 745310.G432_03845; -.
DR   KEGG; sphm:G432_03845; -.
DR   PATRIC; fig|745310.14.peg.789; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_0_3_5; -.
DR   Proteomes; UP000011816; 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_02006; Tyr_tRNA_synth_type1; 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; IPR024107; Tyr-tRNA-ligase_bac_1.
DR   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11766:SF0; TYROSINE--TRNA LIGASE, MITOCHONDRIAL; 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   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_02006};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02006};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02006};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02006};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02006,
KW   ECO:0000256|RuleBase:RU363036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011816};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          352..390
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|Pfam:PF01479"
FT   MOTIF           44..53
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   MOTIF           236..240
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         39
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         176
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         180
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   409 AA;  44230 MW;  28577859BBCB18EB CRC64;
     MTEYASDLLR LLDSRGYIHQ LTDAAGLDAL AARQVVPGYI GFDPTAPSLH VGHLVSIMML
     RQLQRAGHKP IVVMGGGTGK IGDPSFKDEA RSLLTTETIA ANVASIRRVF ERFLTFGDGP
     SDAIMVDNAE WLDRLEYIPF LRDIGQHFSV NRMLSFDSVK LRLDREQSLS FLEFNYMILQ
     AYDFLELSRR VGCRLQMGGS DQWGNIVNGV ELARRVDGTQ VFGLTTPLLT NADGTKMGKT
     VGGAVWLNED QLSHFDYWQF WRNTDDRDVA SRLRLFTDLP LDEIDRLAAL QGAEINEAKI
     VLANAATALC RGAEAAAQAA ETARRTFEEG AAGDALPSFA VAGGSIAIVD ALVGLGLAAS
     KGEARRLIKG GGARVDGEKV TDEALVVSVG ADPVRISSGK KHHGVLTAG
//
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