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CTU2_CAEEL
ID   CTU2_CAEEL              Reviewed;         349 AA.
AC   Q19906;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Cytoplasmic tRNA 2-thiolation protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
DE   AltName: Full=Thiolation of uridine in tRNA protein 2 {ECO:0000255|HAMAP-Rule:MF_03054};
GN   Name=tut-2 {ECO:0000255|HAMAP-Rule:MF_03054}; ORFNames=F29F11.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=18391219; DOI=10.1073/pnas.0709404105;
RA   Dewez M., Bauer F., Dieu M., Raes M., Vandenhaute J., Hermand D.;
RT   "The conserved wobble uridine tRNA thiolase Ctu1-Ctu2 is required to
RT   maintain genome integrity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5459-5464(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 tut-1/ctu-1 that ligates sulfur from
CC       thiocarboxylated urm-1 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; Z73974; CAA98270.2; -; Genomic_DNA.
DR   PIR; E89195; E89195.
DR   PIR; T21554; T21554.
DR   RefSeq; NP_505729.1; NM_073328.5.
DR   AlphaFoldDB; Q19906; -.
DR   SMR; Q19906; -.
DR   STRING; 6239.F29F11.3; -.
DR   EPD; Q19906; -.
DR   PaxDb; Q19906; -.
DR   PeptideAtlas; Q19906; -.
DR   EnsemblMetazoa; F29F11.3.1; F29F11.3.1; WBGene00009256.
DR   GeneID; 179483; -.
DR   KEGG; cel:CELE_F29F11.3; -.
DR   UCSC; F29F11.3; c. elegans.
DR   CTD; 179483; -.
DR   WormBase; F29F11.3; CE23690; WBGene00009256; tut-2.
DR   eggNOG; KOG2594; Eukaryota.
DR   GeneTree; ENSGT00390000008797; -.
DR   HOGENOM; CLU_024534_0_0_1; -.
DR   InParanoid; Q19906; -.
DR   OMA; YVRHKFR; -.
DR   OrthoDB; 1442062at2759; -.
DR   PhylomeDB; Q19906; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q19906; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00009256; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IBA:GO_Central.
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:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Reference proteome; tRNA processing.
FT   CHAIN           1..349
FT                   /note="Cytoplasmic tRNA 2-thiolation protein 2"
FT                   /id="PRO_0000369266"
SQ   SEQUENCE   349 AA;  39412 MW;  6D4957F8BAEAF152 CRC64;
     MELGNFVTDL NGKKCVKCDK DAKFTGVDPK KAWYCQECFV QMVRNKFRSS LSKKKIYKDA
     DARDTLIVFD GTLSGTFLLH QINDALKQIT YKRLMVKPTV LVLVSLTEDT EIQMVIKRIQ
     EIKKSVLENV RWVVAHLACS MYDEDFKLKE NECNGVEKIS DYNQLIASCS VPTYRKELER
     VLKEKCLQKI ACSMGILKCM VPDHADDLGR LAIDQLCLGR GGSISTLVTV TDKRPDFMLI
     RPLCDISKKE LAVYNYLCDI DKHCIHIAQQ NNQQKSVQTL TDAFICTLEN EKFYSTINTV
     LSTAAKIHNT SIGKDDSKCS FCNVEVADSV CSTCSAIREC TGDLLTLLF
 
 
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