ID W3WVH3_PESFW Unreviewed; 407 AA.
AC W3WVH3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=PFICI_09935 {ECO:0000313|EMBL:ETS77873.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS77873.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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; KI912115; ETS77873.1; -; Genomic_DNA.
DR RefSeq; XP_007836707.1; XM_007838516.1.
DR AlphaFoldDB; W3WVH3; -.
DR STRING; 1229662.W3WVH3; -.
DR GeneID; 19274948; -.
DR KEGG; pfy:PFICI_09935; -.
DR eggNOG; KOG2840; Eukaryota.
DR HOGENOM; CLU_026481_1_3_1; -.
DR InParanoid; W3WVH3; -.
DR OMA; KPVRGIC; -.
DR OrthoDB; 5483984at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000030651; 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 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000030651};
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 53..233
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT DOMAIN 375..405
FT /note="Cytoplasmic tRNA 2-thiolation protein 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16503"
FT REGION 324..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR004976-51"
SQ SEQUENCE 407 AA; 44533 MW; 38FC466D4B8ABE97 CRC64;
MAPALCAICK TQRAMIKRPK NHQKLCKSCF IQIFEDEVHH TITSSRLFYP GEKVAIGASG
GKDSTVLASV LKTLNERYDY GLDLVLLSID EGIKGYRDDS LETVKRNAVQ YDMPLKIVGY
DELYGWTMDQ VVETIGKKGN CTYCGVFRRQ ALDRGSKMLG IKHVVTGHNA DDVAETILMN
LLRGDLSRLS RSTSIVTGSD ASEVKRSKPL KYAYEKEIVL YAHHKKLDYF STECLYSPEA
FRGSARSLIK NLEKVRPSAI LDVVRSGEDM ARLVPGQAAD ACGCKGKTAT AAKAAEEESV
GGCGSAVGRG AGGEMAIMEK QLRENEKAEE ADLETEVTVP KAPAPAQRHD RSKQNITGPA
GNSVSVPLRP KQKLGTCERC GYMSSQKLCQ ACMLLDGLNK NRPEISI
//
