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Database: UniProt
Entry: W6MXX8_9ASCO
LinkDB: W6MXX8_9ASCO
Original site: W6MXX8_9ASCO 
ID   W6MXX8_9ASCO            Unreviewed;       365 AA.
AC   W6MXX8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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};
GN   Name=NCS6 {ECO:0000256|HAMAP-Rule:MF_03053};
GN   Synonyms=CTU1 {ECO:0000256|HAMAP-Rule:MF_03053};
GN   ORFNames=KUCA_T00005653001 {ECO:0000313|EMBL:CDK29660.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK29660.1};
RN   [1] {ECO:0000313|EMBL:CDK29660.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29660.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK29660.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29660.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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. Prior mcm(5) tRNA
CC       modification by the elongator complex is required for 2-thiolation. May
CC       also be involved in protein urmylation. {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   EMBL; HG793131; CDK29660.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MXX8; -.
DR   STRING; 1382522.W6MXX8; -.
DR   HOGENOM; CLU_026481_1_0_1; -.
DR   OrthoDB; 5483984at2759; -.
DR   UniPathway; UPA00988; -.
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   InterPro; IPR020554; UPF0021_CS.
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.
DR   PROSITE; PS01263; UPF0021; 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   RNA-binding {ECO:0000256|HAMAP-Rule:MF_03053};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03053};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03053}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_03053}.
FT   DOMAIN          60..242
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   DOMAIN          311..341
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16503"
FT   BINDING         64..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT   BINDING         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
SQ   SEQUENCE   365 AA;  40952 MW;  56990EE8D781090C CRC64;
     MSTARVPRAK ILCELCHDRK AIMKRPKNLQ KICKECFYHV FETEIHNTII DANLFQRGEK
     VAIGASGGKD STVLASVLKT LNERYDYGLE LVLLSIDEGI VGYRDDSLAT VKRNQKQYDM
     HLEIVSYKDL FKWSMDEIVA CAGVRSSCTY CGVMRRQALD RGATKLGISH VVTGHNADDM
     AETVLMNLLR GDTGRLEKSV NILTESSGSP VKRSKPFKYT YQKEIVLYAH YKKLDYFSTE
     CTYAPEAFRG TARVLLKNLE AVRPSCIIDI IRSGEQLKLR PKKQRMRVSA VAQEVEVKRD
     GSVSLKPESS NTCERCGYLS NNRICQACFL LEGLEKNRAK VLIEGGNTAI AGAAKITREL
     EALSF
//
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