ID A0A9W8CRN6_9FUNG Unreviewed; 470 AA.
AC A0A9W8CRN6;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Name=CTU2 {ECO:0000256|HAMAP-Rule:MF_03054,
GN ECO:0000313|EMBL:KAJ1721303.1};
GN Synonyms=NCS2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN ORFNames=LPJ53_004157 {ECO:0000313|EMBL:KAJ1721303.1};
OS Coemansia erecta.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=147472 {ECO:0000313|EMBL:KAJ1721303.1, ECO:0000313|Proteomes:UP001149813};
RN [1] {ECO:0000313|EMBL:KAJ1721303.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 32514 {ECO:0000313|EMBL:KAJ1721303.1};
RA Reynolds N.K., Stajich J.E., Barry K., Grigoriev I.V., Crous P.,
RA Smith M.E.;
RT "Phylogenomic reconstructions and comparative analyses of Kickxellomycotina
RT fungi.";
RL Submitted (JUL-2022) 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:KAJ1721303.1}.
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DR EMBL; JANBOJ010000181; KAJ1721303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W8CRN6; -.
DR OrthoDB; 25129at2759; -.
DR Proteomes; UP001149813; 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:UP001149813};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
SQ SEQUENCE 470 AA; 51516 MW; E0657CBB9EF01F1D CRC64;
MCDVDTPEHK QPLDTRLERK RVPGKCIKCK TAKPNVTIRG CLYCKPCFVS ASIVKFRGAL
KKSNSRIDAQ RRQQNGVSEP QRLMVALSGG PSSTAMLHLV VDYQQSVTQR SGDFVQPPYA
DIVVGHIDES ALFDVAEGAV RSIADGRTFC EASLEDIFSA SADRDVLLQI VRASMASEQQ
QQNGGGFCAQ IIRNSDNNTP PRERLRQLFS ALDSDTSRES LLDAIRTFLL VRLARAHHCS
VLLLGDSATR IATRVVSLTS CGRGFSLPFE IAPESSWFDG VTMIRPMRDF IAKEVAFFNR
WAGYTSVVVP TFTTGAPVHA SIDRLSETFV VGLDRDFAST VSTVCRTVQK LEPRADALAA
CPCIVCGMPA EPDAQDWRSR LTVGQAAAPA LSSAGFDISS HLCYSCQNIL HFSESGDRGG
LVLPGFCVER IRDHAVSRPS ASSDAEQHEA LRRQVEQFFL NSDDEDDDCE
//
