ID A7TQ07_VANPO Unreviewed; 468 AA.
AC A7TQ07;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=20S-pre-rRNA D-site endonuclease NOB1 {ECO:0000256|PIRNR:PIRNR037125};
GN ORFNames=Kpol_473p15 {ECO:0000313|EMBL:EDO15656.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO15656.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480450; EDO15656.1; -; Genomic_DNA.
DR RefSeq; XP_001643514.1; XM_001643464.1.
DR AlphaFoldDB; A7TQ07; -.
DR STRING; 436907.A7TQ07; -.
DR GeneID; 5543750; -.
DR KEGG; vpo:Kpol_473p15; -.
DR eggNOG; KOG2463; Eukaryota.
DR HOGENOM; CLU_024666_2_1_1; -.
DR InParanoid; A7TQ07; -.
DR OMA; GYELECE; -.
DR OrthoDB; 5473723at2759; -.
DR PhylomeDB; A7TQ07; -.
DR Proteomes; UP000000267; 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; IPR002716; PIN_dom.
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 SMART; SM00670; PINc; 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:UP000000267};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037125}.
FT DOMAIN 11..116
FT /note="PIN"
FT /evidence="ECO:0000259|SMART:SM00670"
FT REGION 125..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
SQ SEQUENCE 468 AA; 53060 MW; 4B76A9BA70BA742C CRC64;
MSSDSNTAHV KALVLDATPL ITQSYTHYQR YAKSFYTTPT VFQEIKDAQA RKNLEIWQSL
GTLNLRHPNQ DSIATVSKFA KLTGDFQVLS ANDIHILALA YELETELNKG DWRLRKVPGE
SLDHLGISDT VEHIKEDQGK EDKESVPKEE GGEKKKKKTR RGGKKQRAKR EAEAQVEAES
QPQVQQDKED DEEVITQVEA KVETEVVVPK VEKENEELGE EYGEEDDDGD WITPDNLTEM
IIKDSGEDTT GSRGVEASEQ ERNNALDLPS NQVALATGDF AVQNVALQLN LNLMNFMSGL
RIKRLRNYML RCHACFKLLP LPKDGKAKHF CPSCGLQNTL LRCAVSVDSE TGKITPHLKS
NFQWINRGNV YSIASPLSKN SQKKYGKKGY IHSKPQYQEV ILREDQKEYS QLMKQEEWTN
RHNEKVLDNW IGGGSADNYM SPFAITGLKH HSVKVNRGRY VNSVRRKK
//
