ID A0A2G5TJ26_9PELO Unreviewed; 349 AA.
AC A0A2G5TJ26;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
DE AltName: Full=Thiolation of uridine in tRNA protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Name=Cni-tut-2 {ECO:0000313|EMBL:PIC27006.1};
GN Synonyms=Cnig_chr_V.g19399 {ECO:0000313|EMBL:PIC27006.1}, tut-2
GN {ECO:0000256|HAMAP-Rule:MF_03054};
GN ORFNames=B9Z55_019399 {ECO:0000313|EMBL:PIC27006.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC27006.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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 tut-1/ctu-1 that ligates sulfur from
CC thiocarboxylated urm-1 onto the uridine of tRNAs at wobble position.
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:PIC27006.1}.
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DR EMBL; PDUG01000005; PIC27006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5TJ26; -.
DR OrthoDB; 25129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000230233; Chromosome V.
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 FunFam; 3.40.50.620:FF:000431; Cytoplasmic tRNA 2-thiolation protein 2; 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03054};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
SQ SEQUENCE 349 AA; 39633 MW; 7617FD444C172E8A CRC64;
MNSNNFTSDL NGKTCVKCDK EAKFTGVDPK KAWYCQGCFI QMVRNKFRSA LSKKKIYKDA
DARDTLVVYD GSPSGTFLLN QIDDALKQIT YKRLMVKPTV LVLVSETEEP EIQQVIKRVA
EIKENFLENV NWFIAHIASC LYDEPLELKE FECNGVEKIT AYKSLLASCS VPTYKKELER
MLKEKCLQKL AESLKVTKCM VTDDADDLGR LALDQLCLGR GGSLSSLVTV ADKRNDFMII
RPLCDLSKRE ISIYNYLCKI DDHYIQFSHT QSQEKSVQTL TDAFIRTLED EKFYSTINTV
LSTASKIHNT NGKDGSRCSM CYVEVAEFHC ETCSAIRNSC SENLDNIFS
//
