ID A0A1U7ZUL9_NELNU Unreviewed; 531 AA.
AC A0A1U7ZUL9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tRNA-5-taurinomethyluridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011953};
DE EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN Name=LOC104597469 {ECO:0000313|RefSeq:XP_010257320.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010257320.1};
RN [1] {ECO:0000313|RefSeq:XP_010257320.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_010257320.1; XM_010259018.2.
DR AlphaFoldDB; A0A1U7ZUL9; -.
DR STRING; 4432.A0A1U7ZUL9; -.
DR GeneID; 104597469; -.
DR KEGG; nnu:104597469; -.
DR eggNOG; KOG2805; Eukaryota.
DR InParanoid; A0A1U7ZUL9; -.
DR OrthoDB; 231303at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061708; F:tRNA-5-taurinomethyluridine 2-sulfurtransferase; IEA:UniProtKB-EC.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 2.30.30.280; Adenine nucleotide alpha hydrolases-like domains; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR InterPro; IPR046885; MnmA-like_C.
DR InterPro; IPR046884; MnmA-like_central.
DR InterPro; IPR023382; MnmA-like_central_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR NCBIfam; TIGR00420; trmU; 1.
DR PANTHER; PTHR43052; -; 1.
DR PANTHER; PTHR43052:SF1; TRNA-5-TAURINOMETHYLURIDINE 2-SULFURTRANSFERASE; 1.
DR Pfam; PF03054; tRNA_Me_trans; 1.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 288..350
FT /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT /evidence="ECO:0000259|Pfam:PF20259"
FT DOMAIN 360..440
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
SQ SEQUENCE 531 AA; 60060 MW; E1F2CD42A970069B CRC64;
MQRAMAALPL LNLLSLQNPN IKYSLSLFSL KTARSRFSNP RNVTRCLSVS AAEHKLSLGL
KSNTVLEPYL SCSMPGKRLK VAVLLSGGVD SSVALRLLHA AGHSCTAFYL KIWFQEDFEN
FWSACPWEED LEYVKAVCDQ VEVPLEVVHL TDEYWDNVVS YIIQEYRYGR TPNPDVLCNT
RIKFGAFLDA ISNMEFDYVA SGHYANVIHP CTDQKDGPSI LELSEDKVKD QTYFLSHLSQ
AQLKRLLFPL GCISKNEVRK LAAKLELPNR DRKDSQGICF LGKIKFSEFI AKHIGEMEGI
LLEAETGDFL GKHHGFWFYT IGQRQGLRLP GGPWYVVEKD VKNNVVFVSR NYYSFDKRRR
RFRVGSLKWL AGLPPDQFNK LQCKVRHGPG FYDCSLIMET GEDGDRTSAV VHLSEDDQGL
AAGQFAAFYQ GKTCIGSGVI LECWDSQGFP VCAKALQIAR MEDKSKLGKP VKIKVNPENS
LKSSEITDKV ELNGKSLNSE DITLDKSKQS SQGIFNVNWF QKLREKWLQV F
//
