ID   CTL1_YEAST              Reviewed;         320 AA.
AC   Q03220;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-NOV-2008, entry version 57.
DE   RecName: Full=Polynucleotide 5'-triphosphatase;
DE            EC=3.1.3.33;
DE   AltName: Full=mRNA 5'-triphosphatase;
DE            Short=TPase;
GN   Name=CTL1; OrderedLocusNames=YMR180C; ORFNames=YM8010.10C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313268; 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.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=99238414; 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
RT   capping enzyme.";
RL   Nucleic Acids Res. 27:2181-2188(1999).
CC   -!- FUNCTION: Probably involved in an RNA processing event other than
CC       mRNA capping. Releases gamma-phosphate from the 5'-end of RNA to
CC       produce a diphosphate terminus.
CC   -!- CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H(2)O = a
CC       polynucleotide + phosphate.
CC   -!- COFACTOR: Magnesium and/or manganese. Specific for polynucleotide
CC       RNA in the presence of magnesium, but becomes specific for
CC       nucleotide triphosphates in the presence of manganese.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the fungal TPase family.
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DR   EMBL; Z49808; CAA89913.1; -; Genomic_DNA.
DR   EMBL; AY693065; AAT93084.1; -; Genomic_DNA.
DR   PIR; S55127; S55127.
DR   RefSeq; NP_013905.1; -.
DR   HSSP; O13297; 1D8I.
DR   DIP; DIP:1776N; -.
DR   IntAct; Q03220; -.
DR   Ensembl; YMR180C; Saccharomyces cerevisiae.
DR   GeneID; 855218; -.
DR   GenomeReviews; Z71257_GR; YMR180C.
DR   KEGG; sce:YMR180C; -.
DR   NMPDR; fig|4932.3.peg.4956; -.
DR   CYGD; YMR180c; -.
DR   SGD; S000004792; CTL1.
DR   HOGENOM; Q03220; -.
DR   LinkHub; Q03220; -.
DR   NextBio; 978732; -.
DR   GermOnline; YMR180C; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:InterPro.
DR   GO; GO:0006370; P:mRNA capping; IEA:InterPro.
DR   InterPro; IPR004206; mRNA_triPase.
DR   Pfam; PF02940; mRNA_triPase; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Hydrolase; mRNA processing; Nucleus.
FT   CHAIN         1    320       Polynucleotide 5'-triphosphatase.
FT                                /FTId=PRO_0000210120.
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
//