ID A0A4U5VCA5_COLLU Unreviewed; 511 AA.
AC A0A4U5VCA5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-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=CTU2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Synonyms=NCS2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN ORFNames=D9C73_020163 {ECO:0000313|EMBL:TKS85180.1};
OS Collichthys lucidus (Big head croaker) (Sciaena lucida).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Collichthys.
OX NCBI_TaxID=240159 {ECO:0000313|EMBL:TKS85180.1, ECO:0000313|Proteomes:UP000298787};
RN [1] {ECO:0000313|EMBL:TKS85180.1, ECO:0000313|Proteomes:UP000298787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JT15FE1705JMU {ECO:0000313|EMBL:TKS85180.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TKS85180.1};
RA Cai M., Xiao S.;
RT "Genome Assembly of Collichthys lucidus.";
RL Submitted (JAN-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 CTU1/ATPBD3 that ligates sulfur from
CC thiocarboxylated URM1 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}.
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DR EMBL; CM014094; TKS85180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5VCA5; -.
DR STRING; 240159.A0A4U5VCA5; -.
DR OrthoDB; 25129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000298787; Chromosome 17.
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:UP000298787};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
FT REGION 181..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 55882 MW; 1018CD2EC07B8917 CRC64;
MCQVDEDYHD QLEHADAPSV SKKCAKCKEA TAAVVIRAGD TYCRDCFKEY FIHKFRAMLG
KNRIIFPGEK VLLAVSGGPS SCSMLSQVQE GLSQNAHKKL RFLPGIVYID EGGAVGQSVE
ERRRTVAELR ALFRATGFPF HIVPLEQVLD LPGSVVTVAP SPSEQPASAY KAAVDHFIQS
DGGSRLTPQE EQETSHPDVQ ESHTQSLQQL IGSAKTLTAR EDLLSTLRHH VLVHTARTEG
YSKVMLGDNC TRLAVKLLTS ISLGRGAQLA QDTGFSDSRY GDIILVRPMR DYSAKEIAYY
NRMFTVSSVF IPGLDTMATD KASIQRLTES FVTKLQAGFP STVSTIYRTS EKLQTVCRSS
STADLFDRCL LCMCALDTAV EDASAFKATQ ISEKLSQTKS PGAPRTKTQR QIQAPVESES
TAPSRQCCSS GGENCGRAAA GGGGCCSSAK LSETTNLKSL MCYSCQLTIK DMTSVERLPQ
YILSEAQRRQ RRSQMREEIS EFLLDEGDGG D
//
