ID A0A094D0S5_9PEZI Unreviewed; 482 AA.
AC A0A094D0S5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE RecName: Full=20S-pre-rRNA D-site endonuclease NOB1 {ECO:0000256|PIRNR:PIRNR037125};
GN ORFNames=V497_04050 {ECO:0000313|EMBL:KFY59839.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY59839.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY59839.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFY59839.1}.
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DR EMBL; JPJZ01000853; KFY59839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094D0S5; -.
DR STRING; 1420910.A0A094D0S5; -.
DR HOGENOM; CLU_024666_2_0_1; -.
DR OrthoDB; 5473723at2759; -.
DR Proteomes; UP000029268; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037125}.
FT DOMAIN 12..103
FT /note="Ribonuclease PIN"
FT /evidence="ECO:0000259|Pfam:PF17146"
FT DOMAIN 334..405
FT /note="Nin one binding (NOB1) Zn-ribbon-like"
FT /evidence="ECO:0000259|Pfam:PF08772"
FT REGION 114..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..276
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
SQ SEQUENCE 482 AA; 52291 MW; FDFD3CA787456656 CRC64;
MATPAPKLTH TLVLDAAPII TNTPPISTLL SQSEELYTVP QVLDEIRDVA ARSRMETTLL
PFLKLRTPRP ASVKAVTDFA RRTGDLEVLS RPDVLVLALS YELECERNGG DWRLRSLPGQ
KRLNGAPPGS VAEGGEGEKV EGDKVEGGDK VEEKEEKEEV KEVKPIIETR GAWGTKIPTA
EPVVVEAKEE AAKDIEVPAV DAAVPVEEAA VPEVKTEEPA AESTEAPVEE TTETKAAEES
LAALSLTPSD EPSADAPEVV EEASEDSAED EDDEGGWITP SNIKKVQAKE VAGPTAQEPE
VKTMQVACIT SDFAMQNVLL RMNLNLLSPT LTRVRQLKTW VLRCHACFSV TKDMSKQFCS
RCGKPTLLRV SCSTDKDGTF KVHLKKNKQW STRGNVYSIP KPVAGSANTR AGGGGKGGWG
QTLILAEDQK EYVQATERAR RTKERDLMDE DYLPGLLSGN RRGAGGRPQV GAGRNVNSKK
RH
//
