CTU2_ASPFC
ID CTU2_ASPFC Reviewed; 364 AA.
AC B0Y1E7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN Name=ncs2; Synonyms=ctu2; ORFNames=AFUB_060070;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499597; EDP51977.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y1E7; -.
DR EnsemblFungi; EDP51977; EDP51977; AFUB_060070.
DR HOGENOM; CLU_024534_3_0_1; -.
DR PhylomeDB; B0Y1E7; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000001699; 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; tRNA processing.
FT CHAIN 1..364
FT /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT /id="PRO_0000369288"
SQ SEQUENCE 364 AA; 40517 MW; A28AA421A457E4A7 CRC64;
MQVCWFERFG GGNQLLTVLS SSRTCYARFV NFKVFKRMEN YRLRRNMPRT GPCKLLLPLS
CGISSSVLLH ILNAQIQHEL AKSHPSPGFD LHLLVIEPSS ISHSSLSYDE GFELLQQTFP
LHSFTRIPLH SIFELDPELQ EVISQFSKDG FVDDTGLSAK ERLDAFRASI PTSTSKVDVD
YILITRLVVA FAKKIACRGV LWGDTDTRLA AKTLANVAKG RGSSLTWQVC DGMSPFGVEF
NFPLRDLFKA EVDNYASFFP ELTRIIIPDE PPSENVLTKN LSIDELMMRY VQTQGEKYPG
VMANVTRTAS KLQASLMPAN VPQCSFCGAF MLNSGNNDGG DTTGASRALE LCYACIRSRP
ELTC