CET1_SCHPO
ID CET1_SCHPO Reviewed; 303 AA.
AC Q9P6Q6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=mRNA-capping enzyme subunit beta;
DE EC=3.6.1.74 {ECO:0000250|UniProtKB:O13297};
DE AltName: Full=mRNA 5'-phosphatase;
DE AltName: Full=mRNA 5'-triphosphate monophosphatase;
GN Name=pct1; ORFNames=SPAC644.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12788946; DOI=10.1074/jbc.m303060200;
RA Hausmann S., Pei Y., Shuman S.;
RT "Homodimeric quaternary structure is required for the in vivo function and
RT thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe
RT RNA triphosphatases.";
RL J. Biol. Chem. 278:30487-30496(2003).
CC -!- FUNCTION: First step of mRNA capping. Converts the 5'-triphosphate end
CC of a nascent mRNA chain into a diphosphate end.
CC {ECO:0000269|PubMed:12788946}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end
CC diphospho-ribonucleoside in mRNA + H(+) + phosphate;
CC Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74;
CC Evidence={ECO:0000250|UniProtKB:O13297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005;
CC Evidence={ECO:0000250|UniProtKB:O13297};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O13297};
CC -!- SUBUNIT: Heterodimer. The mRNA-capping enzyme is composed of two
CC separate chains alpha and beta, respectively a mRNA guanylyltransferase
CC and an mRNA 5'-triphosphate monophosphatase.
CC {ECO:0000269|PubMed:12788946}.
CC -!- INTERACTION:
CC Q9P6Q6; Q96WV9: cdk9; NbExp=2; IntAct=EBI-443547, EBI-443557;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fungal TPase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB90131.1; -; Genomic_DNA.
DR RefSeq; NP_593872.1; NM_001019302.2.
DR PDB; 4PN0; X-ray; 2.60 A; A/B/C/D=1-303.
DR PDB; 4PN1; X-ray; 2.80 A; A/B/C/D=1-303.
DR PDBsum; 4PN0; -.
DR PDBsum; 4PN1; -.
DR AlphaFoldDB; Q9P6Q6; -.
DR SMR; Q9P6Q6; -.
DR BioGRID; 280085; 9.
DR IntAct; Q9P6Q6; 2.
DR STRING; 4896.SPAC644.04.1; -.
DR MaxQB; Q9P6Q6; -.
DR PaxDb; Q9P6Q6; -.
DR EnsemblFungi; SPAC644.04.1; SPAC644.04.1:pep; SPAC644.04.
DR GeneID; 2543671; -.
DR KEGG; spo:SPAC644.04; -.
DR PomBase; SPAC644.04; pct1.
DR VEuPathDB; FungiDB:SPAC644.04; -.
DR eggNOG; ENOG502RZAX; Eukaryota.
DR HOGENOM; CLU_018004_0_0_1; -.
DR InParanoid; Q9P6Q6; -.
DR OMA; CPNDAFD; -.
DR PhylomeDB; Q9P6Q6; -.
DR PRO; PR:Q9P6Q6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; ISS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IDA:PomBase.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IPI:PomBase.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISO:PomBase.
DR GO; GO:0009452; P:7-methylguanosine RNA capping; IDA:PomBase.
DR GO; GO:0098507; P:polynucleotide 5' dephosphorylation; IDA:PomBase.
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 3D-structure; Hydrolase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome.
FT CHAIN 1..303
FT /note="mRNA-capping enzyme subunit beta"
FT /id="PRO_0000210117"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:4PN0"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:4PN0"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4PN0"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:4PN0"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 147..159
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 179..194
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 201..211
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 222..234
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 237..245
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4PN0"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:4PN0"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:4PN0"
FT HELIX 282..299
FT /evidence="ECO:0007829|PDB:4PN0"
SQ SEQUENCE 303 AA; 35444 MW; 51A5A112CE927AED CRC64;
MDLKGLLHEE NELPSIEKRK IDENAVEHDK VERKRTKSVA VPKIEMNFLN KPIVPDTTKV
ISNFLTHYLI TEPVEHVEIE AKLGTLIDLE TQNRFEFPVM NETILNPEFN LRTRFESDMT
ASEHKYLNEF LNQAFRDSQK PGRLPFAYKH TKQVDLFYET EDNSRDKIRV SKNQSDNQVL
ACVKKRRVAD LFLYCPNDAF DIRISISDEL PVSMPSGNQQ PSLTRLKDRV GYVHQEIKID
LTKTTQNDPV YDTTERHELE VEFGNIADLR DRAQKAKDGM EAPLFRRVQL FMDNVRILRR
EHS
