ID V5F9G2_BYSSN Unreviewed; 430 AA.
AC V5F9G2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=PVAR5_1380 {ECO:0000313|EMBL:GAD92784.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92784.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD92784.1}.
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DR EMBL; BAUL01000038; GAD92784.1; -; Genomic_DNA.
DR AlphaFoldDB; V5F9G2; -.
DR eggNOG; KOG2840; Eukaryota.
DR HOGENOM; CLU_026481_1_3_1; -.
DR InParanoid; V5F9G2; -.
DR OrthoDB; 5483984at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000018001; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03053};
KW Reference proteome {ECO:0000313|Proteomes:UP000018001};
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 54..233
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT DOMAIN 371..401
FT /note="Cytoplasmic tRNA 2-thiolation protein 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16503"
FT REGION 282..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 47282 MW; 650AE0A72BF2C38C CRC64;
MPPSVCFHCK EARAVIIRPK NRHKLCRSCF LHVFETEIHE TITSTSLFQR GERVAIGASG
GKDSTVLASV LKTLNERYDY GLDLVLLSID EGIKGYRDDS LETVKRNAQQ YDMPLEIVGY
DELYGWTMDQ VVAQVGKKGN CTYCGVFRRQ ALDRGAARLD IKHVVTGHNA DDVAETVMMN
LLRGDLPRLS RGTSIVTDSD ASEIKRSKPL KYAYEKEIVL YAHHKKLDYF STECIYSPEA
FRGSARTLIK DLEKIRPSSI LDIVRSGEDM ALLVPPEVAG TRKCMSGSSA SAEADDYSTG
GCGSQNGRSS GGEMAEMEKQ LAADEAAREN ETEITLPLSD QPSTAAVPLK KKKVTGTKAK
GVKPLKLQKM GKCERCGYLS SQKVCKACAL LEGLNKNRPK TSIELAVGVE EEESSTTLMR
QMESVELTSG
//
