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Database: UniProt
Entry: M2UF73_COCH5
LinkDB: M2UF73_COCH5
Original site: M2UF73_COCH5 
ID   M2UF73_COCH5            Unreviewed;       475 AA.
AC   M2UF73;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=20S-pre-rRNA D-site endonuclease NOB1 {ECO:0000256|PIRNR:PIRNR037125};
GN   ORFNames=COCHEDRAFT_1174140 {ECO:0000313|EMBL:EMD92331.1};
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD92331.1, ECO:0000313|Proteomes:UP000016936};
RN   [1] {ECO:0000313|EMBL:EMD92331.1, ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
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).
RN   [2] {ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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; KB445575; EMD92331.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2UF73; -.
DR   STRING; 701091.M2UF73; -.
DR   eggNOG; KOG2463; Eukaryota.
DR   HOGENOM; CLU_024666_2_0_1; -.
DR   OMA; GYELECE; -.
DR   Proteomes; UP000016936; 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:UP000016936};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037125}.
FT   DOMAIN          15..106
FT                   /note="Ribonuclease PIN"
FT                   /evidence="ECO:0000259|Pfam:PF17146"
FT   DOMAIN          324..395
FT                   /note="Nin one binding (NOB1) Zn-ribbon-like"
FT                   /evidence="ECO:0000259|Pfam:PF08772"
FT   REGION          126..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         334
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
SQ   SEQUENCE   475 AA;  52674 MW;  D623DC3AB9219618 CRC64;
     MEPTSSTQQK PIHSLVLDTG PLIKNIISIS TLINSAEELY TTPDILREVR DEATRSRVQT
     TLVPFLKIRT PSPASYDAVV EFSKKTGDHA VLSKQDLGIL ALAYEVHCEK NGGTWGLREV
     PKGEVKRRPE DIERERAEKT ERERLAKEAA ESGGEENLES QTVEKVEEKV EEKVQEQVQE
     QLQEQLGEQG LIEKSAAVEV SSANIHVEQN AELAVTPEHT AQQEPSEAPP QEPLENEMSS
     LSITQQPTPP TTDSEAADSD SDGDWITPTN LSAHQAADSN LQPHVQTASK PPQLDLATMT
     TDHAMQNVLL QLNLTLLSPS LQRIKTVTSK IHRCHACFLL TKEMTRQFCP RCGQPTLQRV
     SCSTNAKGEF RIHLSKTYTY NKRGDRYSIP KPIAGTANTK WKEGSGGGKG GWGRELILAE
     DQKEFLKVKE EGRRRKARDA LDEDFLPGIL TGERVEKNGK VRVGAGRDVN AKKRS
//
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