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CTU2_CAEBR
ID   CTU2_CAEBR              Reviewed;         349 AA.
AC   A8X8I6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 47.
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=CBG09667;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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; HE600998; CAP28947.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8X8I6; -.
DR   STRING; 6238.CBG09667; -.
DR   EnsemblMetazoa; CBG09667.1; CBG09667.1; WBGene00031222.
DR   WormBase; CBG09667; CBP31444; WBGene00031222; Cbr-tut-2.
DR   eggNOG; KOG2594; Eukaryota.
DR   HOGENOM; CLU_024534_0_0_1; -.
DR   InParanoid; A8X8I6; -.
DR   OMA; YVRHKFR; -.
DR   OrthoDB; 1442062at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000008549; Chromosome V.
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.
DR   Pfam; PF10288; CTU2; 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_0000369265"
SQ   SEQUENCE   349 AA;  39892 MW;  C592811053ABDA28 CRC64;
     MNFNNFTSDL NGKTCVKCEK EAKFTGVDPK KAWYCQECFI QMVRNKFRSA LSKKKIYKEA
     DARDTLVVYD GSPSGTFLLN QIDDALKQIT YKRLMVKPTV LVLVSESEEP EIQQVIKRVA
     EIKKNFLENV NWFIAHIAFC LYDEPSELKE FECNGIEKIT AYKYLLASCS VPTYKKELER
     MLKEKCLQKL AESLKVTKCM VTDDADDLGR LALDQLCLGR GGSLSSLVTV AEKRNDFMII
     RPLCDLSKRE ISIYNYLCKI DDHYIQFSHT QSQEKSVQTL TDAFIRTLED EKFYSTINTV
     LSTASKIHNT NGKDGSRCSM CYVEVAEFQC ETCSAVRNSC SENLNIIFS
 
 
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