ID A0A179FS71_METCM Unreviewed; 390 AA.
AC A0A179FS71;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 10-JUN-2026, entry version 28.
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=VFPPC_04476 {ECO:0000313|EMBL:OAQ68207.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ68207.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ68207.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ68207.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on Phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAQ68207.1}.
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DR EMBL; LSBJ02000003; OAQ68207.1; -; Genomic_DNA.
DR RefSeq; XP_018145057.1; XM_018283823.1.
DR AlphaFoldDB; A0A179FS71; -.
DR STRING; 1380566.A0A179FS71; -.
DR GeneID; 28847817; -.
DR KEGG; pchm:VFPPC_04476; -.
DR OrthoDB; 25129at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000078397; Unassembled WGS sequence.
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:UP000078397};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03054}.
SQ SEQUENCE 390 AA; 42915 MW; 4972668E6036105E CRC64;
MAPATGISKP CRRCAKPDAP YELRNDPTCR DCFVEYVEQK GGRRLGAVAR DTRAPGRPGP
RRYLGGLSFG PSSTVMMQIL DVSAKFHSSK KSSPAFEPLV IHIDTDLSHS ADQKDTPAQK
LLAKYRERFP NVSFECVHLS KIWSVKTLDW SALNVAGDDT EGTDVDRLRK FFDSLPSMTS
KADILRLFIR HLLLDLALER SYTALLLGHS TSALAALTLA EVANGRGFAV PWQINDGPFT
VCKYSASADS SGEREVSQVQ MPIYYPLREV FKHELKIYLD LMPSVKDLMP DSDSTASNIV
SHKDLSIAEV MERYFDSVEG PYSGIVANVV RTTGKLDKAT SGSFCHMCGM TLDEQGDSRW
AGELGDDVDA PEGGVRTARL CYGCKRSING
//
