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CEF1_MAGO7
ID   CEF1_MAGO7              Reviewed;         773 AA.
AC   Q52G60; A4RKP8; G4MZK9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Pre-mRNA-splicing factor CEF1;
GN   Name=CEF1; ORFNames=MGG_01426;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Involved in pre-mRNA splicing and cell cycle control.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC   -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
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DR   EMBL; CM001232; EHA54568.1; -; Genomic_DNA.
DR   RefSeq; XP_003714375.1; XM_003714327.1.
DR   PDB; 6JUI; X-ray; 2.40 A; A=1-106.
DR   PDBsum; 6JUI; -.
DR   AlphaFoldDB; Q52G60; -.
DR   SMR; Q52G60; -.
DR   STRING; 318829.MGG_01426T0; -.
DR   EnsemblFungi; MGG_01426T0; MGG_01426T0; MGG_01426.
DR   GeneID; 2679320; -.
DR   KEGG; mgr:MGG_01426; -.
DR   VEuPathDB; FungiDB:MGG_01426; -.
DR   eggNOG; KOG0050; Eukaryota.
DR   HOGENOM; CLU_009082_0_0_1; -.
DR   InParanoid; Q52G60; -.
DR   OMA; PFRTQRE; -.
DR   OrthoDB; 975557at2759; -.
DR   PHI-base; PHI:2991; -.
DR   Proteomes; UP000009058; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR021786; Cdc5p/Cef1_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   Pfam; PF11831; Myb_Cef; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51294; HTH_MYB; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; DNA-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Reference proteome; Repeat; Spliceosome.
FT   CHAIN           1..773
FT                   /note="Pre-mRNA-splicing factor CEF1"
FT                   /id="PRO_0000197102"
FT   DOMAIN          1..56
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          57..106
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        29..52
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        80..102
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          114..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          156..203
FT                   /evidence="ECO:0000255"
FT   COILED          648..754
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        132..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           11..24
FT                   /evidence="ECO:0007829|PDB:6JUI"
FT   HELIX           29..34
FT                   /evidence="ECO:0007829|PDB:6JUI"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:6JUI"
FT   HELIX           41..50
FT                   /evidence="ECO:0007829|PDB:6JUI"
FT   HELIX           63..75
FT                   /evidence="ECO:0007829|PDB:6JUI"
FT   TURN            81..86
FT                   /evidence="ECO:0007829|PDB:6JUI"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:6JUI"
FT   HELIX           91..106
FT                   /evidence="ECO:0007829|PDB:6JUI"
SQ   SEQUENCE   773 AA;  86096 MW;  438298C909F8B579 CRC64;
     MPVVKGGVWT NIEDEILKAS VSKYGLNQWA RVSSLLARKT PKQCKARWNE WLDPSIRKIE
     WSKDEDEKLL HLAKLMPTQW RTIAPIVGRT ANQCLERYQK LLDEAEQKEA AAALGLTGTG
     EASAPTADSV RRLRPGEIDP DPETKPAKAD TVDLDEDEKE MLSEARARLA NTQGKKAKRK
     ARERQQEESR RLAALQKRRE LKTAGINVKV TTRKPGQMDY NADIPFEQKP APGFYDTSEE
     LARNERERAA FDPKKVQLAT KRKGDQDEDA DRKRRKNDKE GSQSASLQEA LKAGRMQKMR
     EAEQSSKRRA LVLPEPQVGE GELEDIVKMG MIGERAGQMA RESENDATRG LVGSYSSLNT
     GAPIRTPRAP EQEDHIANEI RNIRALQETQ SSLLGGENTP LHEGVASTGF DGVAPRKQVM
     STPNPLATPM RSGANGMGMT PGGPGATPRA PGQTPLRTPR DGFSLNSVGD EVASRQQLLK
     GLAALPKPKE TEWDLELPED QMEVDAAEAL EEDASERDRR EREIREAQEA LERRRRTQVM
     QRDLPRPAVV DIDLFLKHAD SIPDPSQSMV AREAAMLMAN DAIKFPAAGV KPARSSKVQV
     EQVDDAALAE ARLQVLVEAG SAPKPEDVQK AWDREKSNSL LLGLACYDDD EEEEQVAIMR
     AALEEVQQSI VSSAEKGNKL EKKLNLHHGG YKQRAEMLRK KIGEASEALS KANDALSAFK
     TLAVSEEITI TRRLEALREE VAYVSRRERE AQELYRRIRE ESDHMPVVTN GYH
 
 
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