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Database: UniProt
Entry: A0A093HA98_STRCA
LinkDB: A0A093HA98_STRCA
Original site: A0A093HA98_STRCA 
ID   A0A093HA98_STRCA        Unreviewed;       396 AA.
AC   A0A093HA98;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=Mitochondrial tRNA-specific 2-thiouridylase 1 {ECO:0000256|ARBA:ARBA00018888};
DE            EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
DE   Flags: Fragment;
GN   ORFNames=N308_10074 {ECO:0000313|EMBL:KFV76320.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV76320.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV76320.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV76320.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KL205899; KFV76320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093HA98; -.
DR   STRING; 441894.ENSSCUP00000001085; -.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
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   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; PTHR11933:SF5; MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1; 1.
DR   PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 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:UP000053584};
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          211..273
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          284..364
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
FT   REGION          376..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV76320.1"
FT   NON_TER         396
FT                   /evidence="ECO:0000313|EMBL:KFV76320.1"
SQ   SEQUENCE   396 AA;  45488 MW;  C2528A0F101DD36A CRC64;
     GYQVTGVFMK NWDPLDEQGA CCIDKDCEDA YRVCQKLDIP FHQVSYVKEY WNEVFSDLLK
     EYELGRTPNP DIVCNKHIKF NYFLHYALDN LGADAMATGH YARTSLEEEE VFQQKHIKRP
     QGLFRNRFEV RNTVKLLQGA DLFKDQTFFL SQISQAALRK TIFPLGDLTK SFVKKIAAEH
     GLHHVLKKKE ACHPFPFQST GICFIGERNF EKFLLEYLEP QPGNFVSIED KKVMGTHKGW
     FLYTIGQRAR LAGLKDAWFV VDKDVSTGDI FVAPSTDHPA LYRDLLRTNR VHWIAEEPPA
     ELIRDKMMEC HFRCRHQMAL VPCVLTLNQD GSVWVTLVKP ERALTPGQFA VFYKGDECLG
     SGKILRLGPS VYTLKQGKNR EEGAKKEETD KIEPAT
//
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