ID B9QAD0_TOXGV Unreviewed; 1596 AA.
AC B9QAD0; A0A0F7V8Z9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=tRNA-5-taurinomethyluridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011953};
DE EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN ORFNames=BN1205_093240 {ECO:0000313|EMBL:CEL77233.1}, TGVEG_309110
GN {ECO:0000313|EMBL:ESS34705.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS34705.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|EMBL:ESS34705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS34705.1};
RA Paulsen I.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ESS34705.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS34705.1};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEL77233.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:CEL77233.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for
CC the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of
CC mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble
CC position. ATP is required to activate the C2 atom of the wobble base.
CC {ECO:0000256|ARBA:ARBA00003986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-
CC cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A +
CC AMP + diphosphate + H(+) + L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726,
CC Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963,
CC ChEBI:CHEBI:87171, ChEBI:CHEBI:87172, ChEBI:CHEBI:456215;
CC EC=2.8.1.14; Evidence={ECO:0000256|ARBA:ARBA00000897};
CC -!- SIMILARITY: Belongs to the MnmA/TRMU family.
CC {ECO:0000256|ARBA:ARBA00006191}.
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DR EMBL; LN714501; CEL77233.1; -; Genomic_DNA.
DR EMBL; AAYL02000053; ESS34705.1; -; Genomic_DNA.
DR STRING; 432359.B9QAD0; -.
DR PaxDb; 5811-TGME49_109110; -.
DR EnsemblProtists; ESS34705; ESS34705; TGVEG_309110.
DR VEuPathDB; ToxoDB:TGVEG_309110; -.
DR eggNOG; KOG2805; Eukaryota.
DR OMA; DNIQWIS; -.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 3.90.1010.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR046885; MnmA-like_C.
DR InterPro; IPR046884; MnmA-like_central.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR PANTHER; PTHR43052; -; 1.
DR PANTHER; PTHR43052:SF1; TRNA-5-TAURINOMETHYLURIDINE 2-SULFURTRANSFERASE; 1.
DR Pfam; PF03054; tRNA_Me_trans; 2.
DR Pfam; PF20258; tRNA_Me_trans_C; 1.
DR Pfam; PF20259; tRNA_Me_trans_M; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Methyltransferase {ECO:0000313|EMBL:CEL77233.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ESS34705.1}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1596
FT /note="tRNA-5-taurinomethyluridine 2-sulfurtransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010109068"
FT DOMAIN 1114..1152
FT /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT /evidence="ECO:0000259|Pfam:PF20259"
FT DOMAIN 1541..1577
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
FT REGION 48..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..639
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1596 AA; 173358 MW; 9A8E80157EE30BAA CRC64;
MFLSSLGGCK SLSAVLFLLL FVLDPRQASP LATSVASAAG SSAWLPAALP RSSGVRPPDQ
SRRLGRSAPR GNADNLQQLP SQNGVRRRRS VSWARGLPAL FRAAADEGTE GGTRSDPRED
DACSLLPSSH RPSWQLRGDA AGASLNEKSG KTRRRSGSHP WVRSVAKHRF PRWTYTSLSH
HRGVPCASLL PHRCGFCPSS SFLNSARFCP VIGEDTAVRG VLAGGDGVWS HVVSGSAARC
DAGRPRQEKA GVAGRKRPHT AVFFISNFAP CGASTSSRDC FANSAEDRRG APVGPPLSPS
LRSLSRSSLC SLSRSSLRSS ARDPFSPATP LASSGSLPPR MRELLSELRR QKDLHAVFEK
LVSFASSVPL YPARDASAVS SRASTASPPS PPRPVPSASL SPAPPPKATE TSGRADDRLL
PPAQLLQQPR REASEEADEE GDSPEAWERV AGCAALVRIR VCLRRVLSPK REGESRACSV
FREADVREEP QQGALASLSV AASSSSGASC HDVEGAKKER RELRREDRDG EDERRRWELR
VDLRGWSDSL VVRAWLAILV VGLNNAAPDT VLALSTDDIL REAGLMPSST PSGGKGHKDT
VKETQGEPEK QTEEGEDGHR EAEEEAEEAE EEAEEEEEEE KERKGSKRES EEERLQEGEE
RLREEETRKC REEEKRRLVV PQGLEFMLRS IQRQVREQLS RLAEEEKNGG APDGKVRKSK
TDRDASRDLT GETRTRTDEN GVQRSVFHRC RSDAETEADS HHVSSSLSSS LPPSQPHLSS
PSSSSLSSSS SPSSSSSSSS SAAPDLFAST TETCEEKREL RRSAASSPPQ VAVLLSGGVD
SSVSLCLLQQ RGFAPQAFFI KVWLPELLLV SRHLNRLLDS GLAPAAAGGC GWERDLLFAD
QVCRQARVPL EVLPLQEAYW EGVVQQMLDE ARQGLTPNPD WWCNQRVKFG AFLDLLDGRE
TRFSARRIAG ESEGENEKEE ADMPFLRNSS RWTGAVASGH YARVVPAAET SRRSEEGEDT
EDRDEDGEED RGDKERGSEE ERRTRLFRGK DRRKDQSYFL SGLSQRQLRR LVTPVGDMEK
VEVRRLAAAL DLPTARRQDS QGLCFLGNLS LSFFFRHFLG SSTGPVLHFP SCLALGSHDG
LWNFTVGQRK GVTPCIDVAR VRRLSSLPDS SLTPHAASVD SEGSEEQTAR AGDSRRRQAR
APPGKPTKAS ATGQGRQAAD DEERRLLEAK CHRDGDDSCL RSANHTVRGR LECTDNADRP
DGRVPVLSEG NEAPSSSSCS SSAEADEGQE EGGDRQSRLS SSSFAACLSG SPQNLFEPAN
PFSRTGLGAA SLAGRWVVAA KHPPSNALFV VSEKEMKAAA AVAESVGYSL DVLAAGPGVR
TLGDSQTYLL ALLLTLQQKF LRVDNIQWIS HPPCAACNAE EQPVSRDPSF LGTLLGSRDP
RARLRGDEKS LETADEFAFL RWALEGSRDK RPRLYDVQVR HAAGTACAAI HRRVRLCLFP
PERRSPSFLS PSAVSEESGG RRKESRAPFG PSRVETSAGS SGAWTAWIEL AEPDEGLAPG
QIAAIYEGEE CLGAGRISAR QGQMAVEAAL RSAGLN
//
