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Database: UniProt
Entry: A0A1Y2CWC5_9FUNG
LinkDB: A0A1Y2CWC5_9FUNG
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ID   A0A1Y2CWC5_9FUNG        Unreviewed;       461 AA.
AC   A0A1Y2CWC5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   08-OCT-2025, entry version 18.
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=BCR33DRAFT_762119 {ECO:0000313|EMBL:ORY51339.1};
OS   Rhizoclosmatium globosum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC   Chytriomycetaceae; Rhizoclosmatium.
OX   NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY51339.1, ECO:0000313|Proteomes:UP000193642};
RN   [1] {ECO:0000313|EMBL:ORY51339.1, ECO:0000313|Proteomes:UP000193642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL800 {ECO:0000313|EMBL:ORY51339.1,
RC   ECO:0000313|Proteomes:UP000193642};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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). 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:ORY51339.1}.
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DR   EMBL; MCGO01000005; ORY51339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2CWC5; -.
DR   STRING; 329046.A0A1Y2CWC5; -.
DR   OrthoDB; 25129at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000193642; 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:UP000193642};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03054}.
SQ   SEQUENCE   461 AA;  49593 MW;  0BC4456B157EE581 CRC64;
     MPLCAKCVRD GNSDRASVIA TRGSEYCADC FKVDMFGRFT KAYTTKESLL PRGEPVCVAW
     SGGLSSSLLV HYMNSFLNKN FKQNVSPRFS AVYVCVVDYS CLLSEEKQQI VNQEIEAMQS
     IAEGYNFNFK RIPLESAFTN ENGDLDSTLV ADLTSPEILQ LKFESYSTSK TSTATPISRT
     LDLFASFKST PAANPTTAVT LLNTLTTRLL RRAASTYNCT TLMTGSNAST IAAQIVTQTA
     LGGGFNLPNE ISLEYKVPNT DIVTFRPIRD LLFGEVEKLV ELDEIAQFPG VAGMAEGLFG
     GVVGSVGTEG ASVAKMTIQD LAASFVKGLQ KDFPQSVSTV TRTAFKVQTG ANAPGLDVCL
     LCSNPIQPNS QNWRASHTTS RLDDIPDIIK NEDGTVVEAP KKASEVPATG AADLLLCYAC
     QHVGRDVKVK EKLVLPGGDW FLGAKKDCFV GNGCCDSGVS D
//
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