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Database: UniProt
Entry: A0A0K0DVZ7_STRER
LinkDB: A0A0K0DVZ7_STRER
Original site: A0A0K0DVZ7_STRER 
ID   A0A0K0DVZ7_STRER        Unreviewed;       356 AA.
AC   A0A0K0DVZ7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000256|HAMAP-Rule:MF_03053};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_03053};
DE   AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000256|HAMAP-Rule:MF_03053};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000141300.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000141300.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC       wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds
CC       tRNAs and probably acts by catalyzing adenylation of tRNAs, an
CC       intermediate required for 2-thiolation. It is unclear whether it acts
CC       as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1
CC       onto the uridine of tRNAs at wobble position. {ECO:0000256|HAMAP-
CC       Rule:MF_03053}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03053}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053}.
CC   -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03053}.
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DR   AlphaFoldDB; A0A0K0DVZ7; -.
DR   STRING; 6248.A0A0K0DVZ7; -.
DR   WBParaSite; SSTP_0000141300.1; SSTP_0000141300.1; SSTP_0000141300.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01993; Alpha_ANH_like_II; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_03053; CTU1; 1.
DR   InterPro; IPR032442; CTU1_C.
DR   InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011063; TilS/TtcA_N.
DR   InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR   NCBIfam; TIGR00269; TIGR00269 family protein; 1.
DR   PANTHER; PTHR11807; ATPASES OF THE PP SUPERFAMILY-RELATED; 1.
DR   PANTHER; PTHR11807:SF12; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 1; 1.
DR   Pfam; PF01171; ATP_bind_3; 1.
DR   Pfam; PF16503; zn-ribbon_14; 1.
DR   PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR004976-51};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004976-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_03053};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03053}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_03053};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_03053}.
FT   DOMAIN          49..241
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   DOMAIN          279..307
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16503"
FT   BINDING         53..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
SQ   SEQUENCE   356 AA;  40623 MW;  26AE1C8259AB1A76 CRC64;
     MKCTNCEEKP KVKAAKTGQL FCDKCFTNWF EKDVHETIIK CELFKRDEKI AIGASGGKDS
     IVLSHIMKRL NDRYDYGLNF YLICIDEGIK GYRDFSIESV IQSEKELSIP LIILSYKDLY
     GWTMDDIVAK IGKKNNCTFC GVFRRQALDR GAQKIKANKL LTGHNADDLA ETVYLNVLRG
     DTARLQRCGA NITGSEDSLP RAKPLKYSYE KDIVMYAYFN KLKYFSTECI YSPNAFRGNV
     RTLIKDLEAI RPRTIMDLIR SAEELTLKDD VTVPDLLLCQ RCGYISSQKI CKACLLLTGL
     ENDDPNIGIT KKKKWKAEIK IEEDKFNTDK EKKLNLCSSK DEDKSACECA KQSLDF
//
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