ID A0A1G3C2J5_9BACT Unreviewed; 402 AA. AC A0A1G3C2J5; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 05-JUL-2017, entry version 6. 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 ORFNames=A3H23_03960 {ECO:0000313|EMBL:OHC01680.1}; OS Planctomycetes bacterium RIFCSPLOWO2_12_FULL_40_19. OC Bacteria; Planctomycetes. OX NCBI_TaxID=1801983 {ECO:0000313|EMBL:OHC01680.1, ECO:0000313|Proteomes:UP000177189}; RN [1] {ECO:0000313|EMBL:OHC01680.1, ECO:0000313|Proteomes:UP000177189} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27774985; DOI=10.1038/ncomms13219; RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J., RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., RA Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected RT biogeochemical processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a CC two-step reaction: tyrosine is first activated by ATP to form Tyr- CC AMP and then transferred to the acceptor end of tRNA(Tyr). CC {ECO:0000256|HAMAP-Rule:MF_02007, ECO:0000256|SAAS:SAAS00724248}. CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP + CC diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000256|HAMAP- CC Rule:MF_02007, ECO:0000256|SAAS:SAAS00777173}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02007, CC ECO:0000256|SAAS:SAAS00724244}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007, CC ECO:0000256|SAAS:SAAS00724257}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. TyrS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02007, CC ECO:0000256|SAAS:SAAS00724250}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02007}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OHC01680.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MHZA01000143; OHC01680.1; -; Genomic_DNA. DR Proteomes; UP000177189; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR CDD; cd00805; TyrRS_core; 1. DR Gene3D; 3.10.290.10; -; 1. DR Gene3D; 3.40.50.620; -; 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; IPR002307; Tyr-tRNA-ligase. DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type. DR InterPro; IPR024108; Tyr-tRNA-ligase_bac_2. DR PANTHER; PTHR11766; PTHR11766; 1. DR PANTHER; PTHR11766:SF5; PTHR11766:SF5; 1. DR Pfam; PF01479; S4; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR SMART; SM00363; S4; 1. DR TIGRFAMs; TIGR00234; tyrS; 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|HAMAP-Rule:MF_02007, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777199}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02007, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777290}; KW Complete proteome {ECO:0000313|Proteomes:UP000177189}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007, KW ECO:0000256|SAAS:SAAS00724231}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02007, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777344, KW ECO:0000313|EMBL:OHC01680.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02007, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777134}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02007, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00777336}; KW RNA-binding {ECO:0000256|SAAS:SAAS00724237}. FT DOMAIN 340 401 S4 RNA-binding. {ECO:0000259|PROSITE: FT PS50889}. FT MOTIF 231 235 "KMSKS" region. {ECO:0000256|HAMAP-Rule: FT MF_02007}. FT BINDING 234 234 ATP. {ECO:0000256|HAMAP-Rule:MF_02007}. SQ SEQUENCE 402 AA; 46011 MW; B6B0EE7A5FD54886 CRC64; MFKGIDEQLN IIKRGVVEII REDELIERLY RSIKTKTPLR AKLGLDPTAP DIHIGNAIPI HKLRNFQELG HTAVLIIGDY TAIVGDPSGV NKTRPQLSHE DILKNTRTYL DQIGKILDID KTEIRYNSEW FKEMKFTDVI TLASKMTVAR MMERDDFSKR YTSKVPISLH EFIYPLMQGY DSIMVRSDVE IGGTDQIFSL LVGRDLQRDK NIEPQVALTT PLLEGIDGNK KMSKSLDNYI GIYEDPKEIF GKTMRIGDDL MRKYFELATD MTVEEIDSAL KGHPRQAKIV LGKAIVRRYY NEETAREVAE EFDRVFKEHK LPDNIPQVKL PSDECQNHKI WIVRLLVLSG FAATNGEARR LISQGGVSIN NNVLTDPACE VEMETDMILR VGKRRFARIV MN //