ID A0A150VCK1_9PEZI Unreviewed; 448 AA.
AC A0A150VCK1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ribosome biogenesis protein NOP53 {ECO:0000256|ARBA:ARBA00018339, ECO:0000256|PIRNR:PIRNR017302};
GN ORFNames=M433DRAFT_141240 {ECO:0000313|EMBL:KYG48210.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48210.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG48210.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG48210.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- FUNCTION: May play a role in ribosome biogenesis.
CC {ECO:0000256|PIRNR:PIRNR017302}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|PIRNR:PIRNR017302}. Nucleus, nucleoplasm
CC {ECO:0000256|PIRNR:PIRNR017302}.
CC -!- SIMILARITY: Belongs to the NOP53 family.
CC {ECO:0000256|ARBA:ARBA00008838, ECO:0000256|PIRNR:PIRNR017302}.
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:KYG48210.1}.
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DR EMBL; JPDO01000054; KYG48210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VCK1; -.
DR STRING; 766039.A0A150VCK1; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR011687; Nop53/GLTSCR2.
DR PANTHER; PTHR14211; GLIOMA SUPPRESSOR CANDIDATE REGION GENE 2; 1.
DR PANTHER; PTHR14211:SF7; RIBOSOME BIOGENESIS PROTEIN NOP53; 1.
DR Pfam; PF07767; Nop53; 1.
DR PIRSF; PIRSF017302; Gltscr2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR017302};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517,
KW ECO:0000256|PIRNR:PIRNR017302}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..258
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 164..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 50971 MW; F4E764E56B6DD030 CRC64;
MDEPTITAPA SYGQPSRKGK KAWRKNVDIS DIQSGLETVR EEIIATGGVI AEKAADELFT
TDVIGDVGLV KRPGVTKWLK CDEILAQRSP VLGLTGRKKR KSGEGNLNAT PMSSKRYKRG
DYVPYKEVQR LRAVADNVNG AVEIDEPSIM QDLWAETETT RDPSLNYLDE TRSKKEPKTL
KHAPKSLTAS GKMVPSVRKP EAGKSYNPLV GDWAALLERE GAAAVEAEIE RLRFEADAAE
KEARAAAEAA KVEQQEREEL ASDYESAWES EWEGFQSGTE CNEVFTQKPP RRKTVAEKNK
IKARKEREAL ERRIRKDRER AAQEKRIQQI AREISAREKA RNRRSSSALM RSNNSDSSES
DDGVEPALQK RRFGKLPIPE PPLEVVLPDE LQDSLRRLKP EGDLLTDRYR NLLVNGKLEV
RKRRDKEQYK QARKFRTEKW SYKDWKLR
//
