ID A0A1L9N454_ASPTC Unreviewed; 1539 AA.
AC A0A1L9N454;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=MIF4G domain-containing protein {ECO:0000259|SMART:SM00543};
GN ORFNames=ASPTUDRAFT_122971 {ECO:0000313|EMBL:OJI84066.1};
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI84066.1, ECO:0000313|Proteomes:UP000184304};
RN [1] {ECO:0000313|Proteomes:UP000184304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000256|ARBA:ARBA00005775}.
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DR EMBL; KV878203; OJI84066.1; -; Genomic_DNA.
DR STRING; 767770.A0A1L9N454; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_122971; -.
DR OMA; PRGGPNM; -.
DR Proteomes; UP000184304; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR Gene3D; 1.25.40.180; -; 1.
DR Gene3D; 1.20.970.30; eIF4G, eIF4E-binding domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR022745; eIF4G1_eIF4E-bd.
DR InterPro; IPR036211; eIF4G_eIF4E-bd_sf.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1.
DR Pfam; PF12152; eIF_4G1; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101489; Eukaryotic initiation factor 4f subunit eIF4g, eIF4e-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000184304}.
FT DOMAIN 1108..1347
FT /note="MIF4G"
FT /evidence="ECO:0000259|SMART:SM00543"
FT REGION 1..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1539 AA; 164680 MW; 9C79A822C8BA3115 CRC64;
MSSIPPKSGL QPQGQSTSTQ AASSAHTSSP SVGGKSSPQA PVPTPSSTST TAPRSYANAT
KKSATDSTAA PVTVGGQSQH GKSTTASPVS GKPMQQSQTP GVTIVNGAPA PASQGDHTRK
PSVTITSAGT SGYIPNGGQT GRPNSLQFGF AANQQSSPNM GNPAVLANQP QSGLGVTPPM
NPRVTSPQTS PSPIPQPASS GGRPPPSSYQ SQGNVPNFGS FGDSGDNQQM RPAPQAPLGP
GAQSTHLRRE SSQSTHSDMS NHMGGGPGGR GGYHHQGGRG RGFSQSSYQG QIPYSPNASF
RSTPNQPRGG PNMAPQFPNQ PRPMPFPNSP HQASRSPALA NAHPATPQMN QVPMAHPQMA
PQPYYGQPMP PQPVRPHPLQ KPARRGGALN RKKGTSRAPV PPRSSATHSP HITLPPNLAP
ESGHFERYLT MMKSKQGYPT FDPNYGFYPG YNMSGVPYMP PSPQPRPGIP YNPQAPYMQN
QYPVQPAAQA TALSRSPSHS NDRPGSSLGQ GQPPAGAPGP AHAHNASRSS NSPAPQKSSF
VIPTAKKNAV VIKDPGSGAV KTFEKAPASP ARVTPSPVKI ATPTSTPPPR TGSSADHTRT
DSKSTKTDEE KKKELRDAVH QKIEQDRIEK EEAERRKAEE EAAQKKKEEE EEAARKKAEE
DAAQKKKEEE EAAQKKAADE EAARKGLEDL SLKDKPAETK AEEPSKPAAA PAPADDDDID
YDAIEREMAE IEAKERAAEE AYYAKKKAEK EEKERKEKEE LEAYEANMKN AEREAEALEE
ARAKKREEES KDKDLFASLK KGGFPATEAS TPGDSGAATP ASDMSMGPPA KPASANKREK
PAALKLETAK AVEPPQPSAA MKALHSARFV EDLSKITYPE SIASPNPALN ASAPADRKFH
YNKEFLLQFQ SVFKEKPSID WDARVRETVG DSDSSRPQSA RTPMMGGRNS SRPGAAPFQM
GNFGQAPSRS NLPPGTTSAE RFAMSNAART SSMGNPFGNF GRPGLGIGAP GLSRTNSASA
MHPGMPSSPR VGSSNRSGTR TGSKRDKQNA KKEEEMAKSM PLTAGMEVKA LQVSSTGWKP
RSIGQAPAAA AAGPTPAGSA YMPPDMVQRK VKAALNKMTP ENFDRIAGQL LEIVSQSKDE
TDGRTLRQVI QLTFEKATDE AHWASIYAKF CKRMLESMSA EIKDENIHDK NGNVVAGGSL
FRKYLLNRCQ EEFERGWKVN LPPKPEGETE EAAMMSDEYY KAAAAKRRGL GLVKFIGELY
KLGMLTERIM HECVKKLVDY EGMPDEAEVE SLTSLLRTIG ASLDVSEKGH AFMNAYFHRI
GLMIQTPGLP SRLRFMLMDI VDLRSARWQS KDADKGPKTI QQIREEAARA QQEAEMERLR
QQANRGSRPG LGRGDARSYS GYGNQAPPQD FASSKVGSDD LRRLRTSRQT NQPMSFGPSS
MLGSRSNSGR KNLGPGGNLV RGSDDSAASS RTGTPTGKKE DKEAASSINA FSALASLEDR
DNMATSPPSN PTSPLLTKSQ PAVERRPSKT PSKDGEEAS
//
