ID A0A899G0J9_9ASCO Unreviewed; 426 AA.
AC A0A899G0J9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Name=NCS2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN Synonyms=CTU2 {ECO:0000256|HAMAP-Rule:MF_03054};
GN ORFNames=MERGE_002172 {ECO:0000313|EMBL:QSL64868.1};
OS Pneumocystis wakefieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=38082 {ECO:0000313|EMBL:QSL64868.1, ECO:0000313|Proteomes:UP000663699};
RN [1] {ECO:0000313|EMBL:QSL64868.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2A {ECO:0000313|EMBL:QSL64868.1};
RA Cisse O.H., Ma L., Dekker J., Khil P., Jo J., Brenchley J., Blair R.,
RA Pahar B., Chabe M., Van Rompay K.A., Keesler R., Sukura A., Hirsch V.,
RA Kutty G., Liu Y., Peng L., Chen J., Song J., Weissenbacher-Lang C., Xu J.,
RA Upham N.S., Stajich J.E., Cuomo C.A., Cushion M.T., Kovacs J.A.;
RT "Genomes of multiple members of Pneumocystis genus reveal paths to human
RT pathogen Pneumocystis jirovecii.";
RL Submitted (JUN-2020) 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 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: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; CP054535; QSL64868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A899G0J9; -.
DR OrthoDB; 25129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000663699; Chromosome 4.
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:UP000663699};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
SQ SEQUENCE 426 AA; 49177 MW; 7D2A97D3F5F2BE6F CRC64;
MGCEDGCKKV KKYTGNGHPE HSSMCGRCKE KESSFFSKTE AFCSHCFTIY IKRKFHKTLE
SFFKDDASFK NNKALIAISE GTSLALINFF SENSDKFKFK KCFSTLDFIH IEEDGAMKEV
SNSSYISEKI NEMLPGSLFF IVNLKNYILN SDENIKLFWD KMSDSLLGSQ ISKDSVGSLN
DLLSPLPSTT SRMDTLKRIR NNIIYNFAEK NGYNVIIFGD TVSSIASKII SEAAKGRGYS
IPWETRGKIK HLYDIWLLRP MKDILRKEVY YFLEINGIQH TKKFYHKATT IDELVDQYFD
DLEKNNPTFL FTVAKTSSKL QVPEIKNTKE HSDSKLCFIC QMPKENNIND WLKKITLDKA
DISNVINTEI NQDYENYVNK TKDLCYGCFI MLRGSKSELI LPYFEKGNIN CIRNPKDEVL
REYLID
//
