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Database: UniProt
Entry: U4L3F0_PYROM
LinkDB: U4L3F0_PYROM
Original site: U4L3F0_PYROM 
ID   U4L3F0_PYROM            Unreviewed;       438 AA.
AC   U4L3F0;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=20S-pre-rRNA D-site endonuclease NOB1 {ECO:0000256|PIRNR:PIRNR037125};
GN   ORFNames=PCON_06430 {ECO:0000313|EMBL:CCX06843.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX06843.1};
RN   [1] {ECO:0000313|EMBL:CCX06843.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX06843.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX06843.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
CC   -!- FUNCTION: Required for the synthesis of 40S ribosome subunits. Has a
CC       role in processing 20S pre-rRNA into the mature 18S rRNA, where it is
CC       required for cleavage at the 3' end of the mature 18S rRNA (D-site).
CC       Accompanies the 20S pre-rRNA from the nucleus to the cytoplasm.
CC       {ECO:0000256|PIRNR:PIRNR037125}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|PIRNR:PIRNR037125}.
CC   -!- SIMILARITY: Belongs to the NOB1 family. {ECO:0000256|ARBA:ARBA00005858,
CC       ECO:0000256|PIRNR:PIRNR037125}.
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DR   EMBL; HF935319; CCX06843.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4L3F0; -.
DR   STRING; 1076935.U4L3F0; -.
DR   eggNOG; KOG2463; Eukaryota.
DR   OMA; GYELECE; -.
DR   OrthoDB; 5473723at2759; -.
DR   Proteomes; UP000018144; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:InterPro.
DR   CDD; cd09876; PIN_Nob1-like; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 6.20.210.10; Nin one binding (NOB1), Zn-ribbon-like; 1.
DR   InterPro; IPR039907; NOB1.
DR   InterPro; IPR017117; Nob1_euk.
DR   InterPro; IPR036283; NOB1_Zf-like_sf.
DR   InterPro; IPR014881; NOB1_Zn-bd.
DR   InterPro; IPR033411; Ribonuclease_PIN.
DR   PANTHER; PTHR12814; RNA-BINDING PROTEIN NOB1; 1.
DR   PANTHER; PTHR12814:SF2; RNA-BINDING PROTEIN NOB1; 1.
DR   Pfam; PF08772; NOB1_Zn_bind; 1.
DR   Pfam; PF17146; PIN_6; 1.
DR   PIRSF; PIRSF037125; D-site_20S_pre-rRNA_nuclease; 1.
DR   SUPFAM; SSF144206; NOB1 zinc finger-like; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000313|EMBL:CCX06843.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR037125}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037125};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037125}.
FT   DOMAIN          20..111
FT                   /note="Ribonuclease PIN"
FT                   /evidence="ECO:0000259|Pfam:PF17146"
FT   DOMAIN          291..365
FT                   /note="Nin one binding (NOB1) Zn-ribbon-like"
FT                   /evidence="ECO:0000259|Pfam:PF08772"
FT   REGION          124..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
SQ   SEQUENCE   438 AA;  48292 MW;  911C863AB1596C7C CRC64;
     MAALAAPTTG TTKEKLATYL VIDTGPIVSS AASPSYYLSS ADRIFTTPAV IAEIKDEASR
     SRWETIWKPF VEVRSPKPNS LKVVAEFAKK TGDYRVLSAT DMGLIALGYE LELEVAGGDW
     RLREAPGKEC KGPKPEGWGW EGKIVGEAPK KEEEKKKDEE PKEEEKSSAA VEEVAEQLEA
     TTLETTPVES PSTEEAATAY EDHQQPEGMV ETTDEPTEEV AESNEDSEDD DSDGWITPSN
     LHRHMHPTPK ASTAAVVEKL TVAIATVDFA MQNTLLQMNL HLLSPTSLIR IKNVRSTVLR
     CHACFFVIKH PTATSHFCPR CGSGDTLRRV GCSTDANGVF KLHLKKNFQH NVRGNVFAIP
     KPVAGTCSMK GVPDAPVLRE DQKEYTRAVK WESYRKEKDL MDQDYLPNIL SGTRRRGSAI
     RVGAGRGKNP NQVGRKRK
//
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