ID M2ZS70_PSEFD Unreviewed; 411 AA.
AC M2ZS70;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=20S-pre-rRNA D-site endonuclease NOB1 {ECO:0000256|PIRNR:PIRNR037125};
GN ORFNames=MYCFIDRAFT_87066 {ECO:0000313|EMBL:EME81879.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME81879.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME81879.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME81879.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446559; EME81879.1; -; Genomic_DNA.
DR RefSeq; XP_007927404.1; XM_007929213.1.
DR AlphaFoldDB; M2ZS70; -.
DR STRING; 383855.M2ZS70; -.
DR GeneID; 19342528; -.
DR KEGG; pfj:MYCFIDRAFT_87066; -.
DR eggNOG; KOG2463; Eukaryota.
DR HOGENOM; CLU_024666_2_0_1; -.
DR OrthoDB; 5473723at2759; -.
DR Proteomes; UP000016932; 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:UP000016932};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037125}.
FT DOMAIN 10..101
FT /note="Ribonuclease PIN"
FT /evidence="ECO:0000259|Pfam:PF17146"
FT DOMAIN 264..335
FT /note="Nin one binding (NOB1) Zn-ribbon-like"
FT /evidence="ECO:0000259|Pfam:PF08772"
FT REGION 110..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
SQ SEQUENCE 411 AA; 44887 MW; 016599D592D3326E CRC64;
MAMEKPVNIV VLDTGAIIKN EPPVSTLLSQ AETLVTVPAI ISEIKDAATR SRVETTLKPF
LTIRSPNPNS IRFVTDFARK TGDLSVLSKP DIQIIALTYE LECERNGGDW RLRRIPGQKG
LNGAPPKKGE AQTDNVVDAA VDAVPQPKSE EESTAQNVAT AAEPTGKASQ EDANPALAQS
DLAEQLQSAS ITETAEDIAE QRSPKGWITP SNLKKKQAED AAASTTQTPE PKTMQVGVLT
SDFAMQNVIL QMNLNLLSPS MSRVKHLKTY VLRCHACFNV SKALDKQFCP RCGQPSLTRV
SCSTDANGQF KLHLKKNMQW NNRGNKFSVP KPVHGSANGR IKGGGKDGWG HELILAEDQK
EYQEAAKREK RQKERSLMDE DYLPSILTGD RGKSGGRPKV GAGRNVNSRR R
//
