ID A0A2Z6REA5_9GLOM Unreviewed; 543 AA.
AC A0A2Z6REA5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|RuleBase:RU361234};
DE EC=6.1.1.1 {ECO:0000256|RuleBase:RU361234};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|RuleBase:RU361234};
GN ORFNames=RCL2_001952800 {ECO:0000313|EMBL:GES92764.1}, RclHR1_04000017
GN {ECO:0000313|EMBL:GBC00936.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBC00936.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBC00936.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBC00936.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GES92764.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HR1 {ECO:0000313|EMBL:GES92764.1};
RA Maeda T., Kobayashi Y., Nakagawa T., Ezawa T., Yamaguchi K., Bino T.,
RA Nishimoto Y., Shigenobu S., Kawaguchi M.;
RT "Conservation and host-specific expression of non-tandemly repeated
RT heterogenous ribosome RNA gene in arbuscular mycorrhizal fungi.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
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:ARBA00034238};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10221;
CC Evidence={ECO:0000256|ARBA:ARBA00034238};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU361234}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBC00936.1}.
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; BEXD01003336; GBC00936.1; -; Genomic_DNA.
DR EMBL; BLAL01000216; GES92764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6REA5; -.
DR STRING; 94130.A0A2Z6REA5; -.
DR Proteomes; UP000247702; Unassembled WGS sequence.
DR Proteomes; UP000615446; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd02799; tRNA_bind_EMAP-II_like; 1.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR11586; TRNA-AMINOACYLATION COFACTOR ARC1 FAMILY MEMBER; 1.
DR PANTHER; PTHR11586:SF33; TYROSINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU361234};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361234};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361234};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361234}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU361234};
KW Reference proteome {ECO:0000313|Proteomes:UP000247702};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 377..482
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
SQ SEQUENCE 543 AA; 60408 MW; 818F21AB78A91D04 CRC64;
MSVSCMSPEQ KYELITRNLQ EVLGREEILK ILNERDLKLY WGTAPTGKPH IGYFVPMSKI
ADFLTAGVEV TILLADIHAF LDNMKAPLDL VKFRTKYYEV LIKALLESIG VPIEKLKFII
GSSYQLTEKY SMDNYRLCAT VTEHDAKKAG AEVVKQVESA LLSGLLYPGL QALDEEYLGV
DAQFGGVDQR KIFVFAEKYL PHLGYKKRAH LMNKMVPGLA GSKMSSSDPD SKIDLLDDAD
VVSRKLKKAF CEEGNIDDNG ILSFVESVLF PLRSLNGKTP SFLIKRDEKW GGNVNYTSYQ
SLKDDFRDKK VHPGDLKAAA TEAINNLLEP IRKRWKDDPE LQKLTKQAYP EIEKIVKKKE
SKKHNQAPSG NGGKSIDVSR LDIRVAKIIK AELHENNPKS YVSTVDVGDA SGNPRTVVSG
LASYIPLEQM QGRYVLAVCN LKPSKFQGIE SCAMLLAASS SDDKTIELLD PPAGSEIGET
VIFEGYGSVE RDGEILNPKN KIFEKVAENF KINEEGIATF KDIPFKTSKG DVTVKTLKEG
TIR
//
