CTU2_CULQU
ID CTU2_CULQU Reviewed; 425 AA.
AC B0X911;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN ORFNames=CPIJ015900;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) 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/CTU1 that ligates sulfur from
CC thiocarboxylated URM1 onto the uridine of tRNAs at wobble position.
CC {ECO:0000255|HAMAP-Rule:MF_03054}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054}.
CC -!- SIMILARITY: Belongs to the CTU2/NCS2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03054}.
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DR EMBL; DS232513; EDS42917.1; -; Genomic_DNA.
DR RefSeq; XP_001866133.1; XM_001866098.1.
DR AlphaFoldDB; B0X911; -.
DR STRING; 7176.CPIJ015900-PA; -.
DR GeneID; 6049355; -.
DR KEGG; cqu:CpipJ_CPIJ015900; -.
DR VEuPathDB; VectorBase:CPIJ015900; -.
DR VEuPathDB; VectorBase:CQUJHB002905; -.
DR eggNOG; KOG2594; Eukaryota.
DR HOGENOM; CLU_024534_2_1_1; -.
DR InParanoid; B0X911; -.
DR OMA; YVRHKFR; -.
DR OrthoDB; 1442062at2759; -.
DR PhylomeDB; B0X911; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000002320; Partially assembled WGS sequence.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
DR GO; GO:0034227; P:tRNA thio-modification; ISS:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_03054; CTU2; 1.
DR InterPro; IPR019407; CTU2.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR20882; PTHR20882; 1.
DR Pfam; PF10288; CTU2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; tRNA processing.
FT CHAIN 1..425
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000369269"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47986 MW; EAD7F257CA424809 CRC64;
MCSIVEDDFG DEGGAHTMKE ESPAPAISAT TDGEELCRKC TVNPSVLKLN LKEPQCRECF
LHYVRHKFRA SLGATKIVRR GSRVLVVFSG SAENVVMLDM IRYGLQQESF KKLRIEPVVV
FVSEDHVGRE DGERVGVVQE KVRILKQFEF RSYFSVIGAK ECVAVEDSDL LERYSEERAR
FNKILSGFKS ATSKQDFIVQ NRKQTLKVIA KRLDCPYVFL SDIGLDLAKT LLSNVALGRG
RSLALDIAFC DDRDEQHKII RPMRDLNPDE IENYLKHADN ELSYITLEDP FKDKPSLQNL
TCKFVDGLQR TYPSTVSTVF RTGDKMSCET VKPTAENDDD QDLLSLFDQS LRLNSSSTSV
RCKFCHSALD FHGSTTLFAT EFSRMVSSRI NVELSHEAIV ESSKRMEEDA RRRVNGEEVD
GGEGS