CTU1_CANAL
ID CTU1_CANAL Reviewed; 395 AA.
AC Q5AML2; A0A1D8PLC0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 1 {ECO:0000255|HAMAP-Rule:MF_03053};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_03053};
DE AltName: Full=Cytoplasmic tRNA adenylyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Name=NCS6 {ECO:0000255|HAMAP-Rule:MF_03053};
GN Synonyms=CTU1 {ECO:0000255|HAMAP-Rule:MF_03053};
GN OrderedLocusNames=CAALFM_C401500WA; ORFNames=CaO19.12104, CaO19.4634;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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:0000255|HAMAP-
CC Rule:MF_03053}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053}.
CC -!- SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03053}.
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DR EMBL; CP017626; AOW28931.1; -; Genomic_DNA.
DR RefSeq; XP_722706.2; XM_717613.2.
DR AlphaFoldDB; Q5AML2; -.
DR SMR; Q5AML2; -.
DR BioGRID; 1218528; 1.
DR STRING; 237561.Q5AML2; -.
DR GeneID; 3635617; -.
DR KEGG; cal:CAALFM_C401500WA; -.
DR CGD; CAL0000179269; orf19.12104.
DR VEuPathDB; FungiDB:C4_01500W_A; -.
DR eggNOG; KOG2840; Eukaryota.
DR HOGENOM; CLU_026481_1_3_1; -.
DR InParanoid; Q5AML2; -.
DR OrthoDB; 860739at2759; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q5AML2; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR Gene3D; 3.40.50.620; -; 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:SF12; PTHR11807:SF12; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR Pfam; PF16503; zn-ribbon_14; 1.
DR PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR PROSITE; PS01263; UPF0021; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..395
FT /note="Cytoplasmic tRNA 2-thiolation protein 1"
FT /id="PRO_0000368258"
FT REGION 297..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 44412 MW; BDDFD029803F1925 CRC64;
MPESTNTIIN SSVKKIKLSA LCELCHGRKA VMKRPKNLMK LCKECFYNIF ETEIHNTIIS
NDLFYRGEKI AIGASGGKDS TVLASILKTL NERYDYGLNL VLLSIDEGIK GYRDDSLATV
KRNQKQYDMP LEIVSYKDLY NWSMDEIVAC AGIRSSCTYC GVLRRQALDR GAEKLGIKHV
VTGHNADDVA ETVLMNLLRG DVARLESSTN IMTTSAGSPI KRSKPFKYTY QKEIVLYAHY
KKLDYFSTEC TYAPEAFRGT ARELLKSLES IRPSCIMDII YSGEHLVLAP KKQKRKTVAY
KNKNKNKKKS NSEQEEQEKQ EQEVNPDGSI SLNRNGIKKD GNTCEKCGYL SSNKICKACM
LLNGLEINRA KVTIDNNSAI DGAAKLTKKL EQLSF
