CTU2_AJECN
ID CTU2_AJECN Reviewed; 359 AA.
AC A6QYX4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN Name=NCS2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN Synonyms=CTU2 {ECO:0000255|HAMAP-Rule:MF_03054}; ORFNames=HCAG_02581;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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: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; CH476656; EDN05978.1; -; Genomic_DNA.
DR RefSeq; XP_001542410.1; XM_001542360.1.
DR AlphaFoldDB; A6QYX4; -.
DR STRING; 339724.A6QYX4; -.
DR EnsemblFungi; EDN05978; EDN05978; HCAG_02581.
DR GeneID; 5449353; -.
DR KEGG; aje:HCAG_02581; -.
DR VEuPathDB; FungiDB:HCAG_02581; -.
DR HOGENOM; CLU_024534_3_0_1; -.
DR OMA; GKLCYGC; -.
DR OrthoDB; 1442062at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000009297; Unassembled 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..359
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000369285"
SQ SEQUENCE 359 AA; 39965 MW; EE4BFE6E5E3334C6 CRC64;
MTLDSRYGGE VYGGSKVVKR MEKYRPQNAP KNRQRKLLLP LSYGISSSTL LHILNLQLER
QISSGLGRRA YDIHVLNIGT CEQSDSHRLG LFREAYPLHT YTQVPLHSIF KHDTTIKDVI
SEYGGPEFAD DPSKTDQERL DIFRLSLSTA TARADIDGIL LTRLVVAIAK EQDCDGILWG
DSDTRLASKA LSNVAKGRGF SVPWDVCDGM SPWGIQFNFP MRDLFKFELS TYASLALPKS
LNVVDSERPS VDNLSNKNMS IEDLLAHYVE TQGQKYPGVM ANIVRTINKL QPQSADTDHK
CMLCGMPVDY SGEDPAIIGG QGSSQYTLQD WRERPVAGTL CYGCARTRLD LVPPRSVSS