CTL1_YEAST
ID CTL1_YEAST Reviewed; 320 AA.
AC Q03220; D6W003;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Polynucleotide 5'-triphosphatase;
DE EC=3.1.3.33 {ECO:0000269|PubMed:10219091};
DE AltName: Full=mRNA 5'-triphosphatase;
DE Short=TPase;
GN Name=CTL1; OrderedLocusNames=YMR180C; ORFNames=YM8010.10C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP CHARACTERIZATION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10219091; DOI=10.1093/nar/27.10.2181;
RA Rodriguez C.R., Takagi T., Cho E.J., Buratowski S.;
RT "A Saccharomyces cerevisiae RNA 5'-triphosphatase related to mRNA capping
RT enzyme.";
RL Nucleic Acids Res. 27:2181-2188(1999).
CC -!- FUNCTION: Probably involved in an RNA processing event other than mRNA
CC capping. Releases gamma-phosphate from the 5'-end of RNA to produce a
CC diphosphate terminus. {ECO:0000269|PubMed:10219091}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a
CC 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate;
CC Xref=Rhea:RHEA:11008, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13942,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:138276, ChEBI:CHEBI:138288; EC=3.1.3.33;
CC Evidence={ECO:0000269|PubMed:10219091};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11009;
CC Evidence={ECO:0000305|PubMed:10219091};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Magnesium and/or manganese. Specific for polynucleotide RNA in the
CC presence of magnesium, but becomes specific for nucleotide
CC triphosphates in the presence of manganese.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10219091}. Nucleus
CC {ECO:0000269|PubMed:10219091}.
CC -!- SIMILARITY: Belongs to the fungal TPase family. {ECO:0000305}.
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DR EMBL; Z49808; CAA89913.1; -; Genomic_DNA.
DR EMBL; AY693065; AAT93084.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10077.1; -; Genomic_DNA.
DR PIR; S55127; S55127.
DR RefSeq; NP_013905.1; NM_001182686.1.
DR AlphaFoldDB; Q03220; -.
DR SMR; Q03220; -.
DR BioGRID; 35358; 77.
DR DIP; DIP-1776N; -.
DR IntAct; Q03220; 1.
DR MINT; Q03220; -.
DR STRING; 4932.YMR180C; -.
DR MaxQB; Q03220; -.
DR PaxDb; Q03220; -.
DR PRIDE; Q03220; -.
DR EnsemblFungi; YMR180C_mRNA; YMR180C; YMR180C.
DR GeneID; 855218; -.
DR KEGG; sce:YMR180C; -.
DR SGD; S000004792; CTL1.
DR VEuPathDB; FungiDB:YMR180C; -.
DR HOGENOM; CLU_075385_0_0_1; -.
DR OMA; ANDREKF; -.
DR BioCyc; YEAST:G3O-32868-MON; -.
DR BRENDA; 3.6.1.74; 984.
DR ChiTaRS; CTL1; yeast.
DR PRO; PR:Q03220; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03220; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IDA:SGD.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0098507; P:polynucleotide 5' dephosphorylation; IBA:GO_Central.
DR CDD; cd07470; CYTH-like_mRNA_RTPase; 1.
DR Gene3D; 3.20.100.10; -; 1.
DR InterPro; IPR040343; Cet1/Ctl1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR004206; mRNA_triPase_Cet1.
DR InterPro; IPR037009; mRNA_triPase_Cet1_sf.
DR PANTHER; PTHR28118; PTHR28118; 1.
DR Pfam; PF02940; mRNA_triPase; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..320
FT /note="Polynucleotide 5'-triphosphatase"
FT /id="PRO_0000210120"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 36974 MW; 82EFBDF3E100B57B CRC64;
MSDQPETPSN SRNSHENVGA KKADANVASK FRSLHISETT KPLTSTRALY KTTRNNSRGA
TEFHKHVCKL AWKYLACIDK SSISHIEIEM KFGVITDKRT HRRMTPHNKP FIVQNRNGRL
VSNVPEQMFS SFQELLRSKS ENPSKCAPRV VKQVQKYTKD SIYNCNNASK VGKLTSWRCS
EDLRNKELKL TYIKKVRVKD FLIRYPQSSL DAKISISLEV PEYETSAAFR NGFILQRTKS
RSTYTFNDKM PLHLDLTKVT TTRRNSHQYT SHEVEVEMDP IFKETISAND REKFNEYMCS
FLNASDLIRK AAERDNMLTT
