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Database: UniProt
Entry: A8IFI5_AZOC5
LinkDB: A8IFI5_AZOC5
Original site: A8IFI5_AZOC5 
ID   A8IFI5_AZOC5            Unreviewed;       437 AA.
AC   A8IFI5;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 110.
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   OrderedLocusNames=AZC_3619 {ECO:0000313|EMBL:BAF89617.1};
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF89617.1, ECO:0000313|Proteomes:UP000000270};
RN   [1] {ECO:0000313|EMBL:BAF89617.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=17720818; DOI=10.1128/AEM.01514-07;
RA   Suzuki S., Aono T., Lee KB., Suzuki T., Liu CT., Miwa H., Wakao S., Iki T.,
RA   Oyaizu H.;
RT   "Rhizobial factors required for stem nodule maturation and maintenance in
RT   Sesbania rostrata-Azorhizobium caulinodans ORS571 symbiosis.";
RL   Appl. Environ. Microbiol. 73:6650-6659(2007).
RN   [2] {ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BAF89617.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=18522759; DOI=10.1186/1471-2164-9-271;
RA   Lee KB., Backer P.D., Aono T., Liu CT., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T.T., Ussery D.W., D'Haeze W., Herder J.D., Gevers D.,
RA   Vereecke D., Holsters M., Oyaizu H.;
RT   "The genome of the versatile nitrogen fixer Azorhizobium caulinodans
RT   ORS571.";
RL   BMC Genomics 9:271-271(2008).
RN   [4] {ECO:0000313|EMBL:BAF89617.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=19542345; DOI=10.1128/AEM.00398-09;
RA   Tsukada S., Aono T., Akiba N., Lee KB., Liu CT., Toyazaki H., Oyaizu H.;
RT   "Comparative genome-wide transcriptional profiling of Azorhizobium
RT   caulinodans ORS571 grown under free-living and symbiotic conditions.";
RL   Appl. Environ. Microbiol. 75:5037-5046(2009).
RN   [5] {ECO:0000313|EMBL:BAF89617.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=20382809; DOI=10.1128/AEM.00238-10;
RA   Akiba N., Aono T., Toyazaki H., Sato S., Oyaizu H.;
RT   "phrR-like gene praR of Azorhizobium caulinodans ORS571 is essential for
RT   symbiosis with Sesbania rostrata and is involved in expression of reb
RT   genes.";
RL   Appl. Environ. Microbiol. 76:3475-3485(2010).
RN   [6] {ECO:0000313|EMBL:BAF89617.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=21571889; DOI=10.1128/AEM.02327-10;
RA   Liu CT., Lee KB., Wang YS., Peng MH., Lee KT., Suzuki S., Suzuki T.,
RA   Oyaizu H.;
RT   "Involvement of the azorhizobial chromosome partition gene (parA) in the
RT   onset of bacteroid differentiation during Sesbania rostrata stem nodule
RT   development.";
RL   Appl. Environ. Microbiol. 77:4371-4382(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_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; AP009384; BAF89617.1; -; Genomic_DNA.
DR   RefSeq; WP_012172142.1; NC_009937.1.
DR   AlphaFoldDB; A8IFI5; -.
DR   STRING; 438753.AZC_3619; -.
DR   KEGG; azc:AZC_3619; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_0_3_5; -.
DR   Proteomes; UP000000270; 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; 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; 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|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02006}; Reference proteome {ECO:0000313|Proteomes:UP000000270};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          378..412
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           256..260
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         196
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         200
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
FT   BINDING         259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02006"
SQ   SEQUENCE   437 AA;  48071 MW;  8882BDB2F2420971 CRC64;
     MTTLRSDFLR TLQERGYIHQ CSDLERLDAK ASEGPITAYI GFDATASSLH AGHLLSIMML
     RTLQRTGHRP IALMGGGTTK IGDPSGKDEA RKMLTDAQIN ENIASIRKVF ARFLDFEGSP
     KGYARFARAV DGKWNEEPRL LPAIMENNAN WLDELKYIPL LREVGPHFTI NRMLTFDSVK
     LRLEREQPLT FLEFNYMILQ AYDFVELNKR HGCTLQMGGS DQWGNIVNGM ELGRRMHGAD
     LFALTTPLLT TSSGAKMGKT AGGAVWLDAA LLSPYEYWQY WRNTGDADVE RFLKLFTELP
     LDEIARLAAL GGQEINHAKD VLATEATALL HGRAAAEEAK ATARATFEEG ALSTNLPTIE
     IPAADLKAGL AANSAFVTAG LVPSTSEARR QIKSGGLKVN DATVTDEKLV LGERDLTAEG
     VIKLSMGKKK HVLVRPV
//
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