ID A0A0V1L0N7_9BILA Unreviewed; 920 AA.
AC A0A0V1L0N7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=tRNA-5-taurinomethyluridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011953};
DE EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN ORFNames=T02_3861 {ECO:0000313|EMBL:KRZ52638.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ52638.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ52638.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ52638.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRZ52638.1}.
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DR EMBL; JYDW01000187; KRZ52638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L0N7; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0061708; F:tRNA-5-taurinomethyluridine 2-sulfurtransferase; IEA:UniProtKB-EC.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR019424; 7TM_GPCR_Srsx.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR046885; MnmA-like_C.
DR InterPro; IPR009622; NDUFAF4.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR NCBIfam; TIGR00420; trmU; 1.
DR PANTHER; PTHR11933:SF5; MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1; 1.
DR PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 1.
DR Pfam; PF10320; 7TM_GPCR_Srsx; 1.
DR Pfam; PF03054; tRNA_Me_trans; 1.
DR Pfam; PF20258; tRNA_Me_trans_C; 1.
DR Pfam; PF06784; UPF0240; 1.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 604..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 723..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 811..837
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 622..870
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 920 AA; 105118 MW; 9B6883B127ED7F8B CRC64;
MKASVRQLSI HIFKLLSDAM GKVLSSAYRS ALNVGVDRRA ELLINKMKNG DCPPVAAPRY
PSEEKRIQQL NENYPEMESM IHSKNAELHE NLKKLSVTRS VSFVESSQSS SSRMLPRKAI
CADKQLKFGI VEPPREKVPP GKIQLSKFLE LMNEVQNSGV DVQLLAEQYG LREFDLKQTM
KYFGAFHEGT QEIYLPPLKL DELDSFGEKV ETVDEFELKR IGPSLINILM KVQKSSAWTE
NMFKSVACAI SGGIDSAVAA YLLKARGFDV IGVFMKNWDL IEEFGYCCSD KDLLDAQKVC
RHLKIPFHEV HFINEYWDDV FTNLLDGYVV GKTPNPDILC NRLIKFDLFF SYCMHTLKVD
AVATGHYARS SFGRFLENFS PEKNAKLFRP TDKLKDQTYF LCQIPQASLR RTMFPLANWL
KKDVRVMAER IGMGWLNAKK ESYGICMIGK RNFKDFISDY VMTKKGFFVD VDSQKKVGEH
EGSVQTLQPY WIEEQEPEVL KESRKLKCEF KYQHVLRSTS CIVKKLPSEL GLQVELKHPV
RAISAGQYAI FYNDQDECLG GAEIASTKPF WPELVSLMDM FVVNVSMLEE ALALKNMIAN
QVNLIPYFAI GIGFVTLLLN MGGYVAMSLE KTVRKEKKYL LIRLMNLSYS VFGLGLITYG
FCLIHVRSAE KMPFITQKRC FLINMLLDFS LHLVTDVNLF TAVDRCLAVA VPKFYIHVFK
PKLINVITVL IVIHTGVLNI VGYFYTSNDL QLFCAFSTRT SRYYSSKVRI QSNILLCLTV
LLYIFLIILI HRKIRLLKRN GMNISKARKE MNVRLLMTLF MSIATYSATI IVGSIVISLS
LEEPNLIDSM LLSRYSLIAY FCGILHFLLI VISMDEFRTL LRRTYLRFTI SKLSKVGVAL
SVQVQKPVRS VAETVELRQQ
//
