ID A0A163JKS8_ABSGL Unreviewed; 610 AA.
AC A0A163JKS8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Enhancer of mRNA-decapping protein 3 {ECO:0000256|ARBA:ARBA00015797};
GN Name=ABSGL_05719.1 scaffold 7421 {ECO:0000313|EMBL:SAM00053.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM00053.1};
RN [1] {ECO:0000313|EMBL:SAM00053.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM00053.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}.
CC -!- SIMILARITY: Belongs to the EDC3 family.
CC {ECO:0000256|ARBA:ARBA00006610}.
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; LT553105; SAM00053.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JKS8; -.
DR STRING; 4829.A0A163JKS8; -.
DR InParanoid; A0A163JKS8; -.
DR OMA; KNRDDEC; -.
DR OrthoDB; 1409462at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR Gene3D; 2.30.30.100; -; 1.
DR Gene3D; 3.40.50.10260; YjeF N-terminal domain; 1.
DR InterPro; IPR025762; DFDF.
DR InterPro; IPR019050; FDF_dom.
DR InterPro; IPR025609; Lsm14-like_N.
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 SMART; SM01271; LSM14; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT DOMAIN 249..285
FT /note="DFDF"
FT /evidence="ECO:0000259|PROSITE:PS51512"
FT DOMAIN 368..588
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51385"
FT REGION 122..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 74..103
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 122..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 68420 MW; D5EA7DC85EE802F6 CRC64;
MAEAFIGFHV SLTLHSGIKL DGTVAHIEST TQQMTLKDVT LFFPGQTPHH TPIYGVVGSD
IADLQILPTS KNTLPQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQSSIVSTV QQPSIVSTVQ
QPSNVSTVQQ PSNVSTAQQQ QQQQQQKQQR QQQLSSTVNS HTHSIIVHEE ETDRLDNRTN
HSQSTRTTIV YSYDDINVPD RSLPQKQQHS TRARKTEKDI KPTKSMSCTT DRKLNKQHTK
HQRQSTDWAN EDVNRFKEEE FDFQANLDMF DKAKVFAEIQ EIDETASENL LVTLNRLPQA
LARKKQVNLL PSENVLESTP VEGGGNESDI ESEGSGDRQQ RTTMRKKEVA IVTALDGTPC
PVVSPLQMAH AEHECTSVIG MNEDQMVENG SRGTFEVVVK ILDNRKLIND NPRPLVLILV
GNCKNGAYGL STARRLYNHG HRVIVAMVTG ESPACMVTDR QKFMYERIGG TIVSGIRGLS
QVHEQPDLVV DAMLGSQTKL VDLQEERATY LSICDMIQWT HTKNTAPILS IDYPSGVDAS
TGQNHHPMHH IQPQWTVCLG APKSGCISAK VTGDLYMVDL GYPRLCWKKV GLKKFALPWG
ASFVVELKYL
//