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Database: UniProt
Entry: A0A1X0SBU9_RHIZD
LinkDB: A0A1X0SBU9_RHIZD
Original site: A0A1X0SBU9_RHIZD 
ID   A0A1X0SBU9_RHIZD        Unreviewed;      1060 AA.
AC   A0A1X0SBU9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DUF814-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BCV71DRAFT_194285 {ECO:0000313|EMBL:ORE21618.1};
OS   Rhizopus microsporus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=58291 {ECO:0000313|EMBL:ORE21618.1, ECO:0000313|Proteomes:UP000242381};
RN   [1] {ECO:0000313|EMBL:ORE21618.1, ECO:0000313|Proteomes:UP000242381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11559 {ECO:0000313|EMBL:ORE21618.1,
RC   ECO:0000313|Proteomes:UP000242381};
RX   PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA   Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA   Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT   "Lipid metabolic changes in an early divergent fungus govern the
RT   establishment of a mutualistic symbiosis with endobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC   -!- SIMILARITY: Belongs to the NEMF family.
CC       {ECO:0000256|ARBA:ARBA00008318}.
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DR   EMBL; KV921276; ORE21618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0SBU9; -.
DR   VEuPathDB; FungiDB:BCV72DRAFT_224377; -.
DR   OMA; MFLEFFA; -.
DR   Proteomes; UP000242381; 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   NCBIfam; NF041120; RqcH_arch; 1.
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:UP000242381}.
FT   DOMAIN          504..617
FT                   /note="NFACT RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF05670"
FT   DOMAIN          953..1044
FT                   /note="NFACT protein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11923"
FT   REGION          652..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          315..342
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          459..486
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        652..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..706
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..724
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..810
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..840
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..866
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..929
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  119892 MW;  4D61D487468ACF11 CRC64;
     MKQRFNALDV RSTVMNLRER LIGIRLQNVY DVNAKTFLFK FAKPDDKELV LVESGTRIHT
     TQFSREKSDM PSPFCAKLRK CLRTRRLTNV RQLGVDRIVD FEFAGGEKSL GYHIICEFYA
     SGNIILTDHE YRILALLRTV QPTETLKMAV GEIYNIKSVL TDFKKVDSNQ LKEALSAAGP
     KDNLKKILNI KFEYGPAMVE HIIMESELDP NMKVASDFDT SENSPMMHAL LEGFKKADDM
     IQSTKNAVPR GYIILMDDKK PSDDKEDAME IYDEFHPFLY KQFTHRKFKE YPTFDMAVDE
     FFSSIEAQKL ELKTRKQEEA ALKKLEAVKQ EQEKRVESLL NQQLTNTRKA ELIELNLQYV
     DAAITIIRNA VASQMDWQDL NDLVKEEKRR GNPIALLIDT LKLDTNQITL ILTDPDYHEE
     SEDEDEEEKP KEIFKVDVDI GLTAFANARK YYEQKKSTAS KHEKTIEASA KALKSAERKI
     RQDLKETKIT ATINKIRKPF WFEKFMWFIS TEGYLVIAGR DMQQNEMLVK RYLSKDDVYV
     HADLHGAASV VVKNKPQANG QPIPPSTLYQ AGIMSVCQSK AWDSKIVTSA YWVYPDQVSK
     SAPTGEYLTT GSFMIRGKKN FLPPVQLVYG FGYLFKLDES SIGNHVKPAK ENDLSTEYDN
     DVLEPEQSAK VDSIEETDKS DAAEKSKEAE PNASSGISIS NSEKSVNEED GSSDDDDSDD
     SNSSSSSDDE SAFPDTKLQS LPVSNNENVP DASKYALDEY GHDSDEYQTS SAPDSDKAQA
     KKRFITAKER RLMKKQNATE ITEEIRLKQQ KQQQKQQNNG KQKQQAPAKP SVTTPPSSTR
     GRKGKAKKIK EKYADQDEEE RQLRMELLGS NKGPQPKGKK AKREAKAKAE KAALEKERAR
     KEAEEKARLA QSQKEEEAEN DGSLEVGEEK DSDVIRQLLK EENITMLEAD EIANLSALDS
     LTGNPLPEDI LHFAIPVCAP YPAIQKYKYK VKLTPGSLKR GKAVKQAQSV FLALSDASAR
     EKELIKGVAD MENINTMMSK VKVSAPNLET SKRKKGSGRK
//
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