位置:首页 > 蛋白库 > MCES_DEBHA
MCES_DEBHA
ID   MCES_DEBHA              Reviewed;         524 AA.
AC   Q6BMH4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=mRNA cap guanine-N7 methyltransferase;
DE            EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
DE   AltName: Full=mRNA (guanine-N(7))-methyltransferase;
DE   AltName: Full=mRNA cap methyltransferase;
GN   Name=ABD1; OrderedLocusNames=DEHA2F05434g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC         S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC         COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC         ChEBI:CHEBI:167617; EC=2.1.1.56;
CC         Evidence={ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-
CC         ProRule:PRU00895};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00895}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382138; CAG88922.2; -; Genomic_DNA.
DR   RefSeq; XP_460598.2; XM_460598.2.
DR   AlphaFoldDB; Q6BMH4; -.
DR   SMR; Q6BMH4; -.
DR   STRING; 4959.XP_460598.2; -.
DR   EnsemblFungi; CAG88922; CAG88922; DEHA2F05434g.
DR   GeneID; 2903540; -.
DR   KEGG; dha:DEHA2F05434g; -.
DR   VEuPathDB; FungiDB:DEHA2F05434g; -.
DR   eggNOG; KOG1975; Eukaryota.
DR   HOGENOM; CLU_020346_2_0_1; -.
DR   InParanoid; Q6BMH4; -.
DR   OMA; FSFHYMF; -.
DR   OrthoDB; 1390749at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR   InterPro; IPR016899; mRNA_G-N7_MeTrfase_euk.
DR   InterPro; IPR039753; RG7MT1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12189; PTHR12189; 1.
DR   Pfam; PF03291; Pox_MCEL; 1.
DR   PIRSF; PIRSF028762; ABD1; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51562; RNA_CAP0_MT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW   Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..524
FT                   /note="mRNA cap guanine-N7 methyltransferase"
FT                   /id="PRO_0000303908"
FT   DOMAIN          173..524
FT                   /note="mRNA cap 0 methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         223..224
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   BINDING         227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   BINDING         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   BINDING         319
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43148"
FT   BINDING         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43148"
FT   BINDING         354
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O43148"
FT   SITE            254
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            260
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            285
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            353
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            446
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            514
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
SQ   SEQUENCE   524 AA;  59331 MW;  F062DD77414E822E CRC64;
     MSDKEAGVAS SLGSNSPINK DEVDVKNTEE HSKQESKSDI NKPPLKKIKA DDGIDISDSF
     SRRENKGNNK VISSVYNDEN KKTPAWMKSK TTDKYDKYGS RSTPIATPTA PVNNPDERYS
     KYMTNSVNSN DRVRRPPTET TSSQYDKKRA HDEAEDDVVA PYSNLAVANP SSNLYQTFQS
     HINNREGKDI NSIVRSHYNQ RTQQSKFQGS RTKSPIYKLR NFNNAIKYIL LGNWVKPNPD
     SNRPTVILDL CCGKGGDLNK CEFVSVDQYI GIDISDASIK EAFSRYSRNK ARFIPQTAES
     KKERDTRRYN FEACFATGDC FSSSIPEILE PNFPGIIDGL FPVDCVSLQF AMHYAFETEE
     KVHQLLTNVT KSLRAGGTLI GTIPSSDFIR DKIVNRAFID QENRKFGNDL YSVTFHKDPP
     DEGVFRPPFG NGYNYSLKDA IDDVPEYVVP FEVFRGLCEE YGLVLKYKKN FIDIFNQEIP
     KYFSKLNKNL IEGMKRSDGK YGAEGLEKEA VGFYIGFVFE KLGN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024