ID A0A1E3I212_9TREE Unreviewed; 794 AA.
AC A0A1E3I212;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=L203_05431 {ECO:0000313|EMBL:ODN82622.1};
OS Cryptococcus depauperatus CBS 7841.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN82622.1, ECO:0000313|Proteomes:UP000094043};
RN [1] {ECO:0000313|EMBL:ODN82622.1, ECO:0000313|Proteomes:UP000094043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN82622.1,
RC ECO:0000313|Proteomes:UP000094043};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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|RuleBase:RU361234};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004672}.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC {ECO:0000256|ARBA:ARBA00010190}.
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:ODN82622.1}.
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DR EMBL; AWGK01000025; ODN82622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3I212; -.
DR STRING; 1295531.A0A1E3I212; -.
DR VEuPathDB; FungiDB:L203_05431; -.
DR OrthoDB; 605at2759; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000094043; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd01414; SAICAR_synt_Sc; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR001636; SAICAR_synth.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR NCBIfam; TIGR00081; purC; 1.
DR NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR43700; PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE; 1.
DR PANTHER; PTHR43700:SF1; PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE; 1.
DR Pfam; PF01259; SAICAR_synt; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU361234};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000094043}.
FT DOMAIN 488..758
FT /note="SAICAR synthetase/ADE2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01259"
FT REGION 426..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 87718 MW; BB47A5BBF63DE6F2 CRC64;
MVTKEGHSIK LSAEAEAQYG QIIRGVQEVT SGEIIRKVLS EGRVVKAYWG SATTGRPHIA
YCVPLLKIAD FLAAGVHVKV LLADLHAFLD ASKSSLETVK HRVKYYSILL QAVFSALGVP
TDKLEFITGT SYQLSPEYTL DVYKFHALTT TREAEHAGAD VVKESESPLM SSLLYPGLQA
LDEQYLDVDF QFGGVDQRKI FMYAATFLPR LGYAKRAHLM NAMVPGLSGG KMSSSDPKSK
IDFLDTPANI KSKIKAAICP PGQVEGNGVL AFIKTVLVPI QKLRIEHAQS KGETPPVGEG
SFTLPDAPEG TIFSIPRTEE HGGNVHVSSY EELEEIYKAE KLHPDDLKGS VRDALIHFLE
PIRKAFDEDK EWQEIERLAY PSTSVTPVAA ELKKLASLFS LDHTKKKDVR SKPPTEEERA
VLRALKEKEK AKKATATTAD EGTTPSTPST SNITSNQLAQ SSKDALISAN IAVSRCVTST
NLPKLKLLAK GKVRDIYALP GVENEDKLLF VATDRMSAFD VIMNNGIPAK GITLTTLSLF
WFDKLKDVIP NHVLCPSPSS CFSTPAQTWE QFPRSLDEYR DQLEGRSMIV KRCEVVKIEA
IVRGYITGSA WTEYKKSQTV HGIKMPIGLV ESQKLPNPLF TPSTKADQGE HDENIHPEKV
KDICGSELAT QIEEVAIKLY SVAADYAQER GLILADTKFE FGLLPDPTNP NKPTLILIDE
VLTPDSSRYW SAVDYTPGKP QASFDKQYLR DWLSKEGLNG KDGVTLPKDV VSETKRKYEE
TRDRVMNSSI SQKS
//
