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Database: UniProt
Entry: K1WR11_MARBU
LinkDB: K1WR11_MARBU
Original site: K1WR11_MARBU 
ID   K1WR11_MARBU            Unreviewed;       675 AA.
AC   K1WR11;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   RecName: Full=Enhancer of mRNA-decapping protein 3 {ECO:0000256|ARBA:ARBA00015797};
GN   ORFNames=MBM_07018 {ECO:0000313|EMBL:EKD14807.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD14807.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD14807.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD14807.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}.
CC   -!- SIMILARITY: Belongs to the EDC3 family.
CC       {ECO:0000256|ARBA:ARBA00006610}.
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DR   EMBL; JH921444; EKD14807.1; -; Genomic_DNA.
DR   RefSeq; XP_007294907.1; XM_007294845.1.
DR   AlphaFoldDB; K1WR11; -.
DR   STRING; 1072389.K1WR11; -.
DR   GeneID; 18762953; -.
DR   KEGG; mbe:MBM_07018; -.
DR   eggNOG; KOG2585; Eukaryota.
DR   HOGENOM; CLU_024328_0_0_1; -.
DR   InParanoid; K1WR11; -.
DR   OMA; AWRKYGT; -.
DR   OrthoDB; 1409462at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR   InterPro; IPR025762; DFDF.
DR   InterPro; IPR019050; FDF_dom.
DR   InterPro; IPR004443; YjeF_N_dom.
DR   InterPro; IPR036652; YjeF_N_dom_sf.
DR   PANTHER; PTHR13612:SF0; ENHANCER OF MRNA-DECAPPING PROTEIN 3; 1.
DR   PANTHER; PTHR13612; UNCHARACTERIZED; 1.
DR   Pfam; PF09532; FDF; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   SMART; SM01199; FDF; 1.
DR   SUPFAM; SSF64153; YjeF N-terminal domain-like; 1.
DR   PROSITE; PS51512; DFDF; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..675
FT                   /note="Enhancer of mRNA-decapping protein 3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003854622"
FT   DOMAIN          243..279
FT                   /note="DFDF"
FT                   /evidence="ECO:0000259|PROSITE:PS51512"
FT   DOMAIN          408..648
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51385"
FT   REGION          88..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  72974 MW;  F9746C55AB405A35 CRC64;
     MSNTFIGLTM LVTLSAPPGA QLRGVVITCP ANGKFVPEFT INASEIVELV EATNENAQLP
     RQPPPRPTPA AAPELKTFED PAILSMSKIP AGTTPANSQR PSIPAQWSAK STEPDDSART
     ATGRESRPKA LRELTPAATL VEPMQKMRVK VKPHDDDVVA IPVIEELDGE AEIVPEQPVA
     KARTRRGRKN RKPREEVVDE NTNSKGWRQT PLLEPTTSFQ PFATLKRKNR LKGGKVEESG
     WATEDATDVQ EMGDFDFVGS LAKFDKHTVF NQIQAEDSIA EEDRLVSHNR LPKAKPGTAG
     GKNLHYTENV LEAPIGGVKS TAWKSEAGES GEERASQLGS GSGRRSRRTE RVERAESKFS
     LSRRPVSRKG SVVNHPARSV SIPIAAAKPS FFLVPSNGRC ETISALQMLN LENIADHELG
     LSEEMMTENA GRGIAEVALS ALNIGGRGLT QGKTSIVPTI VVFAGNSKSG LRAVAAGRQI
     RNHGFNVIVC VLGLERETEL LVGLRRQIKV FRGFGGKILT KIELLEYVKT LESPLELIID
     GLLGLTISFE ELRTGDQASA YELIAWANRS TARVLAIDVP TGVDPTSGKV SIVDGRQLYI
     HADFVVSMGA PKKGLLEAMS LGEGIADEDS TGWQLFVADI GLGPAAWKKG GTRVRKGVEF
     EGSWVLQMRF QGGGE
//
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