ID A0A4Y9ZAZ3_9AGAM Unreviewed; 507 AA.
AC A0A4Y9ZAZ3;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 08-OCT-2025, entry version 14.
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=EVG20_g1846 {ECO:0000313|EMBL:TFY71157.1};
OS Dentipellis fragilis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Dentipellis.
OX NCBI_TaxID=205917 {ECO:0000313|EMBL:TFY71157.1, ECO:0000313|Proteomes:UP000298327};
RN [1] {ECO:0000313|EMBL:TFY71157.1, ECO:0000313|Proteomes:UP000298327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105465 {ECO:0000313|EMBL:TFY71157.1,
RC ECO:0000313|Proteomes:UP000298327};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Dentipellis fragilis.";
RL Submitted (FEB-2019) 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:TFY71157.1}.
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DR EMBL; SEOQ01000064; TFY71157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9ZAZ3; -.
DR STRING; 205917.A0A4Y9ZAZ3; -.
DR OrthoDB; 25129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000298327; 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 CDD; cd01986; AANH-like; 1.
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:UP000298327};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
SQ SEQUENCE 507 AA; 55701 MW; 4D11ABCA2C2D0280 CRC64;
MSSCGNPVAD PEALMPRKSK LDKSRMCVRC KETPGNIVIR HAVYCKDCFA PLVQIKFRRS
FEPHVNRKPD GPRKLALKPS GDLLVGFSGG LGSTVLLDLV HRTYLDESAM KTETGGKAHP
RKGKVWKNIH VCYVEICDAF PGIRDRTEEV RQAVNRYEGF EFVPLRIQDA FDAKWWKRVS
GDTLSGDLDV DLTSEDLYMS PSSSTSSPLS SLQACLQSLP TPTAVASSIS TLTRLLLLYT
AHSTGSSHLI LGTSLTSLSI ALISSISQGG GFTVPQEAQE EWTPFGSEPA SGEEPWAGDV
RVIRPLREIG MKECAAWAWW NHLPVVGKEK LPGMRQTIGG LTKDFIVGLE KDFPSTVSTI
ARTVGKLAPK EDAGGRCIFC ERAAQSTVQE WKSRISIRSL SESSHSADDD KERRLTPLLC
YFCHTTLTSR SSRSAASTKP AAPVVNPKVP LPVWVSWHFT HNVNQALAEN GHAENSKVAA
EDNEVWQRKP LGQDAMKAAV SEFLLEE
//
