ID A0A1V2L8J4_CYBFA Unreviewed; 434 AA.
AC A0A1V2L8J4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-OCT-2025, entry version 24.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Name=NCS2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Synonyms=CTU2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN ORFNames=BON22_1949 {ECO:0000313|EMBL:ONH68219.1};
OS Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Phaffomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=36022 {ECO:0000313|EMBL:ONH68219.1, ECO:0000313|Proteomes:UP000189513};
RN [1] {ECO:0000313|Proteomes:UP000189513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
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). May act by
CC forming a heterodimer with NCS6 that ligates sulfur from
CC thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
CC Prior mcm(5) tRNA modification by the elongator complex is required for
CC 2-thiolation. May also be involved in protein urmylation.
CC {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03054}.
CC -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03054}.
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:ONH68219.1}.
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DR EMBL; MPUK01000003; ONH68219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2L8J4; -.
DR STRING; 36022.A0A1V2L8J4; -.
DR VEuPathDB; FungiDB:BON22_1949; -.
DR OMA; KQRKQMM; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000189513; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:TreeGrafter.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:TreeGrafter.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_03054; CTU2; 1.
DR InterPro; IPR019407; CTU2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR20882; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 2; 1.
DR PANTHER; PTHR20882:SF14; CYTOPLASMIC TRNA 2-THIOLATION PROTEIN 2; 1.
DR Pfam; PF10288; CTU2; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03054};
KW Reference proteome {ECO:0000313|Proteomes:UP000189513};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
SQ SEQUENCE 434 AA; 49473 MW; 8982D099ED1390D8 CRC64;
MTSESTRVCS RCKTEPAVIL SRKELFCGSC FIRFISGKQR RHMGGDKFKV RFGTNIIREN
VVFPCSFGKS SLVLLDIIFQ QFNEQLKNPR VWIGFHLDVV FVDDGEVSGY KNDVKEIIED
IKKEYDTERF PVSFTIIPID AYSQGKQMKR ILITPEFETL MNQMFQGEAK TVTEMLRIAP
NRASRDDLQK VVIQELIMSH VIEQGATALI WGHNMSSLAG QVLALTVKGR GSEIHRHLTD
YKDEIAGKEI DVIHPLRDVS QGEVEKFIKF RKLEKLLLIS TQDSSKLMNK QKTVDEVVLQ
YYDTVDTADD NIVSTVVRTG AKLAEPKNYD GVKCIVCGGK IYNDPKVWLR DITYHGHRGP
ETELEKELLK EWEANQKING VIADSDDFET RSMCYGCIVT VGGHAKSTIT WPVRTEMAQK
KEILDEFVID EEDD
//