YSH1_DEBHA
ID YSH1_DEBHA Reviewed; 815 AA.
AC Q6BMW3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Endoribonuclease YSH1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein YSH1;
GN Name=YSH1; OrderedLocusNames=DEHA2F02134g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the cleavage factor I (CF I) involved in pre-
CC mRNA 3'-end processing. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR382138; CAG88764.2; -; Genomic_DNA.
DR RefSeq; XP_460457.2; XM_460457.1.
DR AlphaFoldDB; Q6BMW3; -.
DR SMR; Q6BMW3; -.
DR STRING; 4959.XP_460457.2; -.
DR EnsemblFungi; CAG88764; CAG88764; DEHA2F02134g.
DR GeneID; 2903960; -.
DR KEGG; dha:DEHA2F02134g; -.
DR VEuPathDB; FungiDB:DEHA2F02134g; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q6BMW3; -.
DR OMA; VMIPRRC; -.
DR OrthoDB; 218195at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR021718; CPSF73-100_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF11718; CPSF73-100_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM01098; CPSF73-100_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..815
FT /note="Endoribonuclease YSH1"
FT /id="PRO_0000238901"
FT REGION 521..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 815 AA; 90791 MW; B14BEC235B694923 CRC64;
MTVDSQPADG TDDFKFFGLG GCNEVGRSCH IIEYKNKVIM LDAGVHPGLQ GLSSLPFYDE
YDLSKVDILL VSHFHLDHAA SLPYVMQHTN FNGRVFMTHA TKAIYRWLLS DFVKVTSIGG
GSDARLNNSD PNANTGSSNL YTDDDLMRSF DRIETIDYHS TIELDGIRFT AYHAGHVLGA
CMYFIEIGGL KVLFTGDYSS EEDRHLQVAE VPPIKPDILI TESTFGTATH EPRLEKETRM
TNIIHSTLLK GGRILMPVFA LGRAQELLLI LEEYWSLNDD LQNINIYYAS SLARKCMAVY
QTYTNIMNDS IRLTTSATNS SKKQNPFQFK FIKSIKNLDK FQDFGPCVVV ASPGMLQNGV
SRELLERWAP DPKNAVIMTG YSVEGTMAKD LLTEPHTIQS AMNSDMTIPR RLSIEEISFA
AHVDFQQNAS FIEKVNPSKI ILVHGESNPM GRLKSALLSK YASRKGTEQE VKVFNPRNCD
EVTIGIKGLK VAKVLGTLAE EQLSYLKKEI STQIKKDNVK IEELSDDNMD KETMPESDEK
ADKESEDTKN DIDKNNDENA NEKNIISTGK ALSGVLVSKD FDLNLLQLQD LHEFTQLSTS
IVKSKINLKI NADISLMKWH LEQMFGFISI LADDEETWEC VIMDMIDISV EKNNSQSAGG
LLINVEWVND NLMADSLADS VIAILYSIDS SPASVKLTSK SCSHSHNKVK EEVDDDAMIE
STPPPEKNAH ANSEISSRIH RITSLLKAQF GDSLKTAAGE EGKKATIVIG KNEAKIDYLN
LTVDCNSRVL RDRIENIIKR GCGLAAPLSQ YEKTT
