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Database: UniProt
Entry: A0A0F0I143_ASPPU
LinkDB: A0A0F0I143_ASPPU
Original site: A0A0F0I143_ASPPU 
ID   A0A0F0I143_ASPPU        Unreviewed;      1101 AA.
AC   A0A0F0I143;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DUF814 domain protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=P875_00042348 {ECO:0000313|EMBL:KJK61464.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61464.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK61464.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NEMF family.
CC       {ECO:0000256|ARBA:ARBA00008318}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJK61464.1}.
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DR   EMBL; JZEE01000675; KJK61464.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I143; -.
DR   STRING; 1403190.A0A0F0I143; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProt.
DR   Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR   InterPro; IPR021846; NFACT-C.
DR   InterPro; IPR008532; NFACT_RNA-bd.
DR   PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR   PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR   Pfam; PF11923; NFACT-C; 1.
DR   Pfam; PF05670; NFACT-R_1; 1.
DR   Pfam; PF05833; NFACT_N; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          545..658
FT                   /note="NFACT RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF05670"
FT   DOMAIN          954..1068
FT                   /note="NFACT protein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11923"
FT   REGION          250..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          335..366
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        271..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..464
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..739
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..786
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..808
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        824..854
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..888
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1101 AA;  121680 MW;  482F64D8179F8E0A CRC64;
     MKQRFSSLDV KVISQELASE IVNLRVSNIY DLSSRIFLFK LAKPDHRKQL IVDSGFRCHV
     TQYSRATASM PSPFVTRMRK FLRSRRITSV KQIGTDRIID ISFSDGMYHM FLEFFAGGNI
     IITDREHNIL ALYRQVSVSE GEEARVGIQY TVTNKQNYHG IPEITLDRIR ETLEKAKALF
     AREDGAPKKS KKKNADVLRK ALSQGFPEYP PLLLDHAFAT KQIDPATPLD KVLQDEGLLQ
     EVNGVLQEAQ NENTRLSTQE SHPGYIVAKE DNRSVSQSTT ENEKPSETGN LLYEDFHPFK
     PRQFEGKPGI SILEFPSLNA TVDEYFSSIE TQKLESRLTE REEAAKRKLD AVRQEHEKKI
     GALKEQQELH IRKASAVEDN VYRVQEAMDA VNGLIAQGMD WVEIARLIEM EQSRGNPVAR
     IIKLPLKLHE NTITLLLGEA GDEQDEGDEL FSSDESEESE DEQDNSQQPP SVLTIDIDLG
     ISPWANAKQY YEQKKQAAVK EQRTAQSSTK ALKSHEKKVT EDLKRGMKKE KQTLRQTRQP
     FWFEKFLFFI SSEGYLVLGG RDAMQSELLY RRHLKKGDIF VHADLEGARP MIVKNRSKDP
     NAPIPPSTLS QAGNLCVATS SAWDSKAVMS AWWVQANQIT KTAEVGGLLP MGDFLVKGEK
     NFLAPSQLVL GFGVTFQISK DSLKNHKTHF VDEPEAPEPT TEGGHEQAGE STQGSEQQQE
     TEEAHKPSLD PKEQAEEQSS DSENELDNAD SLPARNPLQR GPSESPHTEA VQEGEKDTGS
     DGEEVADRPE EQADALDEEE AEAASADAPA EDESEHRLSA TARQSPRKGK SPDSSEAGQQ
     APGKNSTAKA TNAKQAPPPT RGKKGKAKKA AAKYADQDDE DRELALRLLG ANKGKASKAA
     AAAEVKANRE KEAEAQKKRR QAQHERAAEA ERRRQALLEE GGDDYDEETA AAEAADLEWI
     PALIGTPRPE DEILAAIPVC APWSALSRYR YKVKLQPGTV KKGKAVKEIL GRWVAETTTG
     KVKKEYAEEA GISIADAEKL RAREGDVIKA WKETEIINSV PVGKVRIMLG AGGGGSDSKG
     KGKGGGSGSK GGKGGKGGKK K
//
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